|
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 ... |
101-678 |
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: 890.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 101 QPYKWISYKQVSDRAEYLGSCLLHKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADI 180
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 181 PVVICDTpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICF 260
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 261 TSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDM 340
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 KALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAIISKFNEVKNGIIRRDSLWDKLVFSKIQGSLGGKVRLMIT 418
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 419 GAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFS--VNNEGEICIK 496
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 497 GNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGE 576
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 577 SLRSFLIGVVVPDPDSLPSFAA-KIGVKGSFEELCKNQCVKEAILEDLQKIGKEGGLKSFEQVKSIFVHPEPFTIENGLL 655
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAAsKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|...
gi 58218988 656 TPTLKAKRVELAKFFQTQIKSLY 678
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
71-681 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 698.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 71 FSDAKTLYENFQRGLAVSDNGPCLGYRKPNQ----PYKWISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWV 146
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 147 ISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICdTPQKATMLVENVEKglTPGLKTIILMDPFDDDLMKRGEKC 226
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 227 GVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEpiFQPTsdDVTISYLP 306
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYPS--DVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 307 LAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKT--PLKKFLLNLAiiskFN 384
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKEsgGLKERLFNAA----YN 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 385 EVKNGIIRRDS---LWDKLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWT 461
Cdd:PLN02736 347 AKKQALENGKNpspMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 462 AGHVGTPVACNFVKLEDVADMNYFSVNN---EGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIV 538
Cdd:PLN02736 427 SGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKII 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 539 DRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVK-GSFEELCKNQCVKE 617
Cdd:PLN02736 507 DRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRA 586
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58218988 618 AILEDLQKIGKEGGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYESI 681
Cdd:PLN02736 587 AVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-679 |
1.21e-180 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 526.59 E-value: 1.21e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 72 SDAKTLYENFQRGLAVSDNGPCLGYrKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELA 151
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALRE-KEDGIWQSLTWAEFAERVRALAAGLLALGVK--PGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 152 CYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTPQKATMLVENVEKglTPGLKTIILMDPfdddlmkRGEKCGVEML 231
Cdd:COG1022 85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLDP-------RGLRDDPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 232 SLHDAENIGKENF------KKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYL 305
Cdd:COG1022 156 SLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 306 PLAHMFERLVQGILFSCGGKIGFfQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAI---I 380
Cdd:COG1022 232 PLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAkaEEAGGLKRKLFRWALavgR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 381 SKFNEVKNGiiRRDSLW--------DKLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAaMGCWVFEAYGQTECTGGC 452
Cdd:COG1022 311 RYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 453 SITSPGDWTAGHVGTPVACNFVKLEDvadmnyfsvnnEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPN 532
Cdd:COG1022 388 TVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 533 GTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESlRSFLIGVVVPDPDSLPSFAAKIGVK-GSFEELCK 611
Cdd:COG1022 457 GFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQ 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58218988 612 NQCVKEAILEDLQKIGKegGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYE 679
Cdd:COG1022 536 DPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
72-683 |
2.26e-166 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 492.41 E-value: 2.26e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 72 SDAKTLYENFQRGLAVSDNGPCLGYRKPNQ----PYKWISYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVI 147
Cdd:PLN02430 39 SDITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 148 SELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVV-ICDTPQKATMlveNVEKGLTPGLKTIILMDPFDDDLMKRGEKC 226
Cdd:PLN02430 117 AMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVfVQDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 227 GVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPiFQP--TSDDVTISY 304
Cdd:PLN02430 194 GVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQ-FEDkmTHDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 305 LPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAIISK 382
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 383 FNEVKNGIIRRDS--LWDKLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDW 460
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 461 TA-GHVGTPVACNFVKLEDVADMNY--FSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKI 537
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 538 VDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQCVKE 617
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 618 AILEDLQKIGKEGGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE 683
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKLAE 657
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
101-663 |
8.52e-162 |
|
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: 472.85 E-value: 8.52e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 101 QPYKWISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADI 180
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVE--PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 181 PVVICDTPqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppkpEDLSVICF 260
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 261 TSGTTGDPKGAMLTHENVVSNMAAFLKFLEPifqpTSDDVTISYLPLAHMFE-RLVQGILFSCGGKIGFFQgDIRLLPDD 339
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLPA----TEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 340 MKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIiskfnevkngiirrdslwdklvfskiqgslGGKVRLMITG 419
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 420 AAPISTPVLTFFRAAmGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDvadmnyfsvnnEGEICIKGNN 499
Cdd:cd05907 220 GAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 500 VFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESlR 579
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 580 SFLIGVVVPDPDSLPSFAAKIGVKG-SFEELCKNQCVKEAILEDLQKIGKEggLKSFEQVKSIFVHPEPFTIENGLLTPT 658
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*
gi 58218988 659 LKAKR 663
Cdd:cd05907 445 LKLKR 449
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
90-683 |
3.80e-159 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 474.12 E-value: 3.80e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 90 NGPCLGYR-----KPNQpYKWISYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVISELACYTYSMVAVPLYD 164
Cdd:PLN02614 60 NNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKDEAK--CGIYGANSPEWIISMEACNAHGLYCVPLYD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 165 TLGTEAIIFVINRADIPVVICDTpQKATMLVENVEKGlTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAENIGK-EN 243
Cdd:PLN02614 137 TLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEgKQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 244 FKKPVPpKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQP-TSDDVTISYLPLAHMFERLVQGILFSC 322
Cdd:PLN02614 215 YDLPIK-KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAlTVKDVYLSYLPLAHIFDRVIEECFIQH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 323 GGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTP--LKKFLLNLAIISKFNEVKNGI--IRRDSLWD 398
Cdd:PLN02614 294 GAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 399 KLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDW-TAGHVGTPVACNFVKLE 477
Cdd:PLN02614 374 KLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELdMLGTVGPPVPNVDIRLE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 478 DVADMNYFSVNN--EGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAP 555
Cdd:PLN02614 454 SVPEMEYDALAStpRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAV 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 556 EKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQCVKEAILEDLQKIGKEGGLKSF 635
Cdd:PLN02614 533 ENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGF 612
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 58218988 636 EQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE 683
Cdd:PLN02614 613 EIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTNE 660
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
102-666 |
1.28e-157 |
|
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: 464.38 E-value: 1.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 102 PYKWISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIP 181
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 182 VVICDtpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvpPKPEDLSVICFT 261
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 262 SGTTGDPKGAMLTHENVVSNMAAFLKFLePIFqPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFfqGDIRLLPD--- 338
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRV-PEL-LGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 339 -----DMKALKPTVFPTVPRLLNRVYDKVQNE--AKTPLKKFLLNLAIISKFNEVKNGIirrDS-LWDKLVFSKIQGSLG 410
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKlnPMGGLKRTLFWTAYQSKLKALKEGP---GTpLLDELVFKKVRAALG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 411 GKVRLMITGAAPISTPVLTFFrAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNE 490
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 491 --GEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPV 568
Cdd:cd17639 329 prGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 569 LQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVKGS-FEELCKNQCVKEAILEDLQKIGKEGGLKSFEQVKSIFVHPEP 647
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSeWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*....
gi 58218988 648 FTIENGLLTPTLKAKRVEL 666
Cdd:cd17639 489 WTPENGLVTAAQKLKRKEI 507
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
70-678 |
1.93e-153 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 459.31 E-value: 1.93e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 70 YFSDAKTLYENFQRglavsdngpcLGYRKPNQ----PYKWISYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEW 145
Cdd:PLN02861 48 FFSDAVKKYPNNQM----------LGRRQVTDskvgPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDR--CGIYGSNCPEW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 146 VISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTPQKATMLveNVEKGLTPGLKTIILMDPFDDDLMKRGEK 225
Cdd:PLN02861 116 IIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 226 CGVEMLSLHDAENIGKENFKKPvPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQ-PTSDDVTISY 304
Cdd:PLN02861 194 LGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRvATEEDSYFSY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 305 LPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVY----DKVQneAKTPLKKFLLNLAII 380
Cdd:PLN02861 273 LPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYtgimQKIS--SGGMLRKKLFDFAYN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 381 SKFNEVKNGIIRRDS--LWDKLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCsITSPG 458
Cdd:PLN02861 351 YKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 459 DW--TAGHVGTPVACNFVKLEDVADMNYFSVNN--EGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGT 534
Cdd:PLN02861 430 NVfsMVGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 535 LKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQC 614
Cdd:PLN02861 509 MKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLK 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58218988 615 VKEAILEDLQKIGKEGGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLY 678
Cdd:PLN02861 589 ARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
102-679 |
7.20e-132 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 404.88 E-value: 7.20e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 102 PYKWISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIP 181
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHN--KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 182 VVICDTPQKATmLVENVEKGLTpgLKTIILMDPFDDDLMKRGEK-CGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICF 260
Cdd:PLN02387 181 TVICDSKQLKK-LIDISSQLET--VKRVIYMDDEGVDSDSSLSGsSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 261 TSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIfqpTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFfqGDIRLLPD-- 338
Cdd:PLN02387 258 TSGSTGLPKGVMMTHGNIVATVAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDts 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 339 ---------DMKALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAIISKFNEVKN------GIIRrdSLWDKLV 401
Cdd:PLN02387 333 nkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKkvDAKGGLAKKLFDIAYKRRLAAIEGswfgawGLEK--LLWDALV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 402 FSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVAD 481
Cdd:PLN02387 411 FKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 482 MNYFSVNN---EGEICIKGNNVFKGYLKDPEKTQEV--LDKDG--WLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIA 554
Cdd:PLN02387 491 GGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVS 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 555 PEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVK-GSFEELC-KNQCVKEaILEDLQKIGKEGGL 632
Cdd:PLN02387 571 LGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCeKEEAVKE-VQQSLSKAAKAARL 649
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 58218988 633 KSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYE 679
Cdd:PLN02387 650 EKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
102-548 |
1.82e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 381.28 E-value: 1.82e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 102 PYKWISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIP 181
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVG--KGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 182 VVICDTPQKATMLVENVEKGLTPGLKTIILMDPFDDDLMkrgekcgvemlsLHDAENIGKENFKKPVPPKPEDLSVICFT 261
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 262 SGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVqGIL--FSCGGKIGFFQGDIRLLP-- 337
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSL-GLLgpLLAGATVVLPPGFPALDPaa 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 338 --DDMKALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAIISKFnevkngiirrdslwdklvfskiqgsLGGKVRL 415
Cdd:pfam00501 243 llELIERYKVTVLYGVPTLLNM----------------LLEAGAPKRA-------------------------LLSSLRL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 416 MITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDW---TAGHVGTPVACNFVKLEDVADMNYFSVNNEGE 492
Cdd:pfam00501 282 VLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGE 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 493 ICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLA 548
Cdd:pfam00501 362 LCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
104-679 |
1.23e-103 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 331.17 E-value: 1.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 104 KWISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVV 183
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLT--KGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 184 ICDTpQKATMLVENVEKGLTPGLkTIILMDPFDDDLmkrgEKCGVEMLSLHDAENIGKE---NFKKPVPPKPEDLSVICF 260
Cdd:PTZ00216 198 VCNG-KNVPNLLRLMKSGGMPNT-TIIYLDSLPASV----DTEGCRLVAWTDVVAKGHSagsHHPLNIPENNDDLALIMY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 261 TSGTTGDPKGAMLTHENVVSNMAAF-LKFLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFfqGDIRLLPD- 338
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDt 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 339 ------DMKALKPTVFPTVPRllnrVYDKVQN--EAKTP----LKKFLLNLAIISKFNEVKNGiirRDS-LWDKLVFSKI 405
Cdd:PTZ00216 350 farphgDLTEFRPVFLIGVPR----IFDTIKKavEAKLPpvgsLKRRVFDHAYQSRLRALKEG---KDTpYWNEKVFSAP 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 406 QGSLGGKVRLMITGAAPISTPVLTFFRAAMGCwVFEAYGQTE--CTGGcsITSPGDWTAGHVGTPVACNFVKLEDVADmn 483
Cdd:PTZ00216 423 RAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGG--IQRTGDLEPNAVGQLLKGVEMKLLDTEE-- 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 484 YFSVNN---EGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIEN 560
Cdd:PTZ00216 498 YKHTDTpepRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 561 VYSrSRPVLQ-----VFVHgeSLRSFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQCVKEAILEDLQKIGKEGGLKSF 635
Cdd:PTZ00216 578 LYG-QNELVVpngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSF 654
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 58218988 636 EQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYE 679
Cdd:PTZ00216 655 EIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
101-663 |
8.96e-87 |
|
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: 280.01 E-value: 8.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 101 QPYKWISYKQVSDRAEYLGSCLLHKGYKSsqDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADi 180
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 181 PVVIcdtpqkatmLVENvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppKPEDLSVICF 260
Cdd:cd17640 78 SVAL---------VVEN-----------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 261 TSGTTGDPKGAMLTHENVVSNMAAFLKFLEPifQPTsdDVTISYLPLAHMFERLVQGILFSCGGKIGFfqGDIRLLPDDM 340
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVPP--QPG--DRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 KALKPTVFPTVPRLLNRVYDKVQNE--AKTPLKKFLLNLAIiskfnevkngiirrdslwdklvfskiqgsLGGKVRLMIT 418
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------SGGIFKFGIS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 419 GAAPISTPVLTFFRAAmGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGN 498
Cdd:cd17640 221 GGGALPPHVDTFFEAI-GIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 499 NVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESL 578
Cdd:cd17640 300 QVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 579 RsFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQCVKEAIL---EDLQKIGKEGGLKSFEQVKSIFVHPEPFtIENGLL 655
Cdd:cd17640 380 K-RLGALIVPNFEELEKWAKESGVKLANDRSQLLASKKVLKLyknEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGEM 457
|
....*...
gi 58218988 656 TPTLKAKR 663
Cdd:cd17640 458 TQTMKIKR 465
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
107-670 |
5.34e-80 |
|
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: 263.56 E-value: 5.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICD 186
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 187 TPQKAtmlvENVEKGLTPGLKTIILMdPFD--------DDLMKRGEKCGVEMlslhdaenigkenfkkpvPPKPEDLSVI 258
Cdd:cd05932 86 KLDDW----KAMAPGVPEGLISISLP-PPSaancqyqwDDLIAQHPPLEERP------------------TRFPEQLATL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 259 CFTSGTTGDPKGAMLTHenvvSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFER-LVQGILFScGGKIGFFQGDIRLLP 337
Cdd:cd05932 143 IYTSGTTGQPKGVMLTF----GSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERvFVEGGSLY-GGVLVAFAESLDTFV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 338 DDMKALKPTVFPTVPRLL----NRVYDKVqneaktPLKKF--LLNLAIISKfnevkngIIRRdslwdklvfsKIQGSLG- 410
Cdd:cd05932 218 EDVQRARPTLFFSVPRLWtkfqQGVQDKI------PQQKLnlLLKIPVVNS-------LVKR----------KVLKGLGl 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 411 GKVRLMITGAAPISTPVLTFFRAaMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDvadmnyfsvnnE 490
Cdd:cd05932 275 DQCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------D 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 491 GEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQ 570
Cdd:cd05932 343 GEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEM 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 571 VFVHGESLrSFLIGVVVPDpdslpSFAAKIGVKGSFEELcknqcvKEAILEDLQKIGKEggLKSFEQVKSIFVHPEPFTI 650
Cdd:cd05932 423 VCVIGSGL-PAPLALVVLS-----EEARLRADAFARAEL------EASLRAHLARVNST--LDSHEQLAGIVVVKDPWSI 488
|
570 580
....*....|....*....|
gi 58218988 651 ENGLLTPTLKAKRVELAKFF 670
Cdd:cd05932 489 DNGILTPTLKIKRNVLEKAY 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
98-678 |
2.65e-68 |
|
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: 234.56 E-value: 2.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 98 KPNQPYKWISYKQVSDRAEYLGSCLLHKGYkssqDQF--VGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVI 175
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 176 NRADIPVVICDTPQKATMLVEnVEKGLtPGLKTII-LMDPFD---------DDLMKRGEKcgvemLSLHDAENIGKENfk 245
Cdd:cd05933 77 ETSEANILVVENQKQLQKILQ-IQDKL-PHLKAIIqYKEPLKekepnlyswDEFMELGRS-----IPDEQLDAIISSQ-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 246 kpvppKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVQ---GILFsc 322
Cdd:cd05933 148 -----KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDiwlPIKV-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 323 GGKIGFFQGDIR--LLPDDMKALKPTVFPTVPRLLNRVYDKVQ-NEAK-TPLKKFLLNLA--IISKFNEVKNG----IIR 392
Cdd:cd05933 221 GGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMKaVGAKsGTLKRKIASWAkgVGLETNLKLMGgespSPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 393 RDSLWDKLVFSKIQGSLG-GKVRLMITGAAPISTPVLTFFrAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVAC 471
Cdd:cd05933 301 FYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 472 NFVKLEDVADmnyfsvNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGE 551
Cdd:cd05933 380 CKTKIHNPDA------DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 552 YIAPEKIENVYSRSRPVLQ-VFVHGESlRSFLIGVVV----PDPDS------LPS----FAAKIGVKGS-FEELCKNQC- 614
Cdd:cd05933 454 NVPPVPIEDAVKKELPIISnAMLIGDK-RKFLSMLLTlkceVNPETgepldeLTEeaieFCRKLGSQATrVSEIAGGKDp 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58218988 615 -VKEAILEDLQKIGKEgGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLY 678
Cdd:cd05933 533 kVYEAIEEGIKRVNKK-AISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
106-598 |
3.07e-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: 3.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVG--PGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 dtpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppkpedlSVICFTSGTT 265
Cdd:COG0318 103 ----------------------------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAHMFErLVQGILFS--CGGKI----GFfqgDIRLLPDD 339
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAA----ALGLTPGDVVLVALPLFHVFG-LTVGLLAPllAGATLvllpRF---DPERVLEL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 340 MKALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAiiskfnevkngiirrdsLWDKLVFSkiqgSLggkvRLMITG 419
Cdd:COG0318 185 IERERVTVLFGVPTMLAR----------------LLRHP-----------------EFARYDLS----SL----RLVVSG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 420 AAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTA--GHVGTPVACNFVKLEDvADMNYFSVNNEGEICIKG 497
Cdd:COG0318 224 GAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 498 NNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRPVLQVFV---- 573
Cdd:COG0318 303 PNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvp 380
|
490 500
....*....|....*....|....*...
gi 58218988 574 ---HGESlrsfLIGVVVPDPDSLPSFAA 598
Cdd:COG0318 381 dekWGER----VVAFVVLRPGAELDAEE 404
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
106-656 |
4.69e-68 |
|
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: 233.50 E-value: 4.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGScLLHKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADiPVVIC 185
Cdd:cd17632 68 ITYAELWERVGAVAA-AHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETE-PRLLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQKATMLVENVEKGLTPGlkTIILMD--PFDDDLMK-----RGEKCGVEMLSLHDAENIGKENFKKPVPPKPED---- 254
Cdd:cd17632 146 VSAEHLDLAVEAVLEGGTPP--RLVVFDhrPEVDAHRAalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEpddd 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 255 -LSVICFTSGTTGDPKGAMLTHENVVSnmaAFLKF--LEPIFQPTSddVTISYLPLAHMFERlvqGILFS--CGGKIGFF 329
Cdd:cd17632 224 pLALLIYTSGSTGTPKGAMYTERLVAT---FWLKVssIQDIRPPAS--ITLNFMPMSHIAGR---ISLYGtlARGGTAYF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 330 QG--DIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISkfnEVKNGIirRDSLwdklvfskiqg 407
Cdd:cd17632 296 AAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAE---RVKAEL--RERV----------- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 408 sLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEcTGGCSITspgdwtaGHVGTPVACNFvKLEDVADMNYFSV 487
Cdd:cd17632 360 -LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE-AGAVILD-------GVIVRPPVLDY-KLVDVPELGYFRT 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 488 NN---EGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSR 564
Cdd:cd17632 430 DRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAA 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 565 SRPVLQVFVHGESLRSFLIGVVVPDPDSLpsfaakigVKGSFEELcknqcvKEAILEDLQKIGKEGGLKSFEQVKSIFVH 644
Cdd:cd17632 510 SPLVRQIFVYGNSERAYLLAVVVPTQDAL--------AGEDTARL------RAALAESLQRIAREAGLQSYEIPRDFLIE 575
|
570
....*....|..
gi 58218988 645 PEPFTIENGLLT 656
Cdd:cd17632 576 TEPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
106-663 |
5.05e-65 |
|
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: 224.99 E-value: 5.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPqkatmlvENVEKGLT-----PGLKTIILMDP-----FDDDLMKRGEKCgVEMLSLHDAENIGKenFKKPVPP-KPED 254
Cdd:cd17641 90 EDE-------EQVDKLLEiadriPSVRYVIYCDPrgmrkYDDPRLISFEDV-VALGRALDRRDPGL--YEREVAAgKGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 255 LSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFlepIFQPTSDDVtISYLPLAHMFER---LVQGILfsCGGKIGFFQG 331
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAA---DPLGPGDEY-VSVLPLPWIGEQmysVGQALV--CGFIVNFPEE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 DIRLLPDdMKALKPTVFPTVPRLLNRVYDKVQN--EAKTPLKKFLLNLAIiSKFNEVKNGIIR--RDSLW--------DK 399
Cdd:cd17641 234 PETMMED-LREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMFELGM-KLGLRALDRGKRgrPVSLWlrlaswlaDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 400 LVFSKIQGSLG-GKVRLMITGAAPISTPVLTFFRAaMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKled 478
Cdd:cd17641 312 LLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVR--- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 479 vadmnyfsVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKI 558
Cdd:cd17641 388 --------IDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 559 ENVYSRSRPVLQVFVHGESlRSFLIGVVVPDPDSLPSFAAKIGVK-GSFEELCKNQCVKEAILEDLQKIGKEggLKSFEQ 637
Cdd:cd17641 460 ENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQR 536
|
570 580
....*....|....*....|....*.
gi 58218988 638 VKSIFVHPEPFTIENGLLTPTLKAKR 663
Cdd:cd17641 537 IRRFLLLYKELDADDGELTRTRKVRR 562
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
106-663 |
1.35e-64 |
|
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: 221.16 E-value: 1.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DtpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppKPEDLSVICFTSGTT 265
Cdd:cd05914 86 S----------------------------------------------------------------DEDDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAaFLKFLEPIfqpTSDDVTISYLPLAHMFERLVQGIL-FSCGGKIgFFQGDI---RLLPDDMK 341
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVD-GVKEVVLL---GKGDKILSILPLHHIYPLTFTLLLpLLNGAHV-VFLDKIpsaKIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 342 ALKPTVFPTVPRLLNRVYDKVQNEAKTpLKKFLLNLAIIskfneVKNGIIRrdslwdKLVFSKIQGSLGGKVRLMITGAA 421
Cdd:cd05914 177 QVTPTLGVPVPLVIEKIFKMDIIPKLT-LKKFKFKLAKK-----INNRKIR------KLAFKKVHEAFGGNIKEFVIGGA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 422 PISTPVLTFFRAaMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVacnfvKLEDVADMNYFSVNNEGEICIKGNNVF 501
Cdd:cd05914 245 KINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVI-----DGVEVRIDSPDPATGEGEIIVRGPNVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 502 KGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQ--VFV-HGEsl 578
Cdd:cd05914 319 KGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLEslVVVqEKK-- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 579 rsfLIGVVVPDPDSLPSFAAKIgvkgsfeelcknQCVKEAILED-LQKIGKEggLKSFEQVKSIFVHPEPFTienglLTP 657
Cdd:cd05914 397 ---LVALAYIDPDFLDVKALKQ------------RNIIDAIKWEvRDKVNQK--VPNYKKISKVKIVKEEFE-----KTP 454
|
....*.
gi 58218988 658 TLKAKR 663
Cdd:cd05914 455 KGKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
254-598 |
5.11e-64 |
|
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: 215.61 E-value: 5.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAHMFerlVQGILFSC---GGKIGFFQ 330
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA----SGGLTEGDVFLSTLPLFHIG---GLFGLLGAllaGGTVVLLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 331 G-DIRLLPDDMKALKPTVFPTVPRLLNRvydkvqneaktplkkfllnlaiiskfnevkngiIRRDSLWDKLVFSkiqgSL 409
Cdd:cd04433 74 KfDPEAALELIEREKVTILLGVPTLLAR---------------------------------LLKAPESAGYDLS----SL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 410 ggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWT--AGHVGTPVACNFVKLEDVADmNYFSV 487
Cdd:cd04433 117 ----RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 488 NNEGEICIKGNNVFKGYLKDPEKTQEVlDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKlAQGEYIAPEKIENVYSRSRP 567
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350
....*....|....*....|....*....|....
gi 58218988 568 VLQVFVHG---ESLRSFLIGVVVPDPDSLPSFAA 598
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLRPGADLDAEE 303
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
106-591 |
5.14e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 201.67 E-value: 5.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIG--KGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 dtpQKATMLVENVEKGLTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAENIGKEnfkkpvpPKPEDLSVICFTSGTT 265
Cdd:PRK07656 109 ---LGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPE-------VDPDDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKFLepifQPTSDDVTISYLPLAHMFErLVQGIL--FSCGGKIgffqgdIRLL---PDDM 340
Cdd:PRK07656 179 GRPKGAMLTHRQLLSNAADWAEYL----GLTEGDRYLAANPFFHVFG-YKAGVNapLMRGATI------LPLPvfdPDEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 KAL----KPTVFPTVPRLLNrvydkvqneaktplkkFLLNLAIISKFNevkngiirrdslwdklvFSKIqgslggkvRLM 416
Cdd:PRK07656 248 FRLieteRITVLPGPPTMYN----------------SLLQHPDRSAED-----------------LSSL--------RLA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 417 ITGAAPISTPVLTFFRAAMGCW-VFEAYGQTECTGGCSITSPGD---WTAGHVGTPVACNFVKLEDvADMNYFSVNNEGE 492
Cdd:PRK07656 287 VTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 493 ICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVF 572
Cdd:PRK07656 366 LLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAA 444
|
490
....*....|....*....
gi 58218988 573 VhgeslrsflIGvvVPDPD 591
Cdd:PRK07656 445 V---------IG--VPDER 452
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
106-561 |
9.88e-56 |
|
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: 9.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQKATMLveNVEKGLTPGLKtIILMDPfdddlmkRGEKCGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTT 265
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDK-IIVLDD-------KPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKFLEPIFQptSDDVTISYLPLAHMFErlVQGILFSCggkigfFQGDIRLL-----PDDM 340
Cdd:cd05911 159 GLPKGVCLSHRNLIANLSQVQTFLYGNDG--SNDVILGFLPLYHIYG--LFTTLASL------LNGATVIImpkfdSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 KAL----KPTVFPTVPRLLNRVydkvqneaktplkkfllnlaiiskfneVKNGIIRRDSLwdklvfskiqGSLggkvRLM 416
Cdd:cd05911 229 LDLiekyKITFLYLVPPIAAAL---------------------------AKSPLLDKYDL----------SSL----RVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 417 ITGAAPISTPVLTFFRAAMGCWVF-EAYGQTECTGGCSITSPGDWTAGHVGTPVAcNF-VKLEDVADMNYFSVNNEGEIC 494
Cdd:cd05911 268 LSGGAPLSKELQELLAKRFPNATIkQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEPGEIC 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58218988 495 IKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENV 561
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV 412
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
104-592 |
1.20e-55 |
|
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: 196.63 E-value: 1.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 104 KWISYKQVSDRAEYLGSCLLHKGYKSSqDQfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVV 183
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPG-DR-VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 184 ICDTPqkatmLVENVEKGLTPGLktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkPVPPKPEDLSVICFTSG 263
Cdd:cd05936 101 IVAVS-----FTDLLAAGAPLGE----------------------------------------RVALTPEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 264 TTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPtsDDVTISYLPLAHMFERLVQGILFSC-GGKIGFFQG--DIRLLpDDM 340
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQIKAWLEDLLEG--DDVVLAALPLFHVFGLTVALLLPLAlGATIVLIPRfrPIGVL-KEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 KALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAIISKFNevkngiirrdslwdklvFSKIqgslggkvRLMITGA 420
Cdd:cd05936 213 RKHRVTIFPGVPTMYIA----------------LLNAPEFKKRD-----------------FSSL--------RLCISGG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 421 APISTPVLTFFRAAMGCWVFEAYGQTECT-GGCSITSPGDWTAGHVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGNN 499
Cdd:cd05936 252 APLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELPPGEVGELWVRGPQ 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 500 VFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVHGeslr 579
Cdd:cd05936 331 VMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVVG---- 404
|
490
....*....|...
gi 58218988 580 sfligvvVPDPDS 592
Cdd:cd05936 405 -------VPDPYS 410
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
106-590 |
5.04e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 179.61 E-value: 5.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACytySM---VAVPLYDTLGTEAIIFVINRADIPV 182
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVK--KGDRVAVFDWNSHEYLEAYFAV---PKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 183 VICDT---PqkatmLVENVeKGLTPGLKTIILMDPFDDdlmkrgEKCGVEMLSLHDAENIGKENFKKPvPPKPEDLSVIC 259
Cdd:PRK06187 107 VLVDSefvP-----LLAAI-LPQLPTVRTVIVEGDGPA------APLAPEVGEYEELLAAASDTFDFP-DIDENDAAAML 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 260 FTSGTTGDPKGAMLTHENVVSN---MAAFLKFlepifqpTSDDVTISYLPLAHMFERLVQGILFSCGGKI---GFFqgDI 333
Cdd:PRK06187 174 YTSGTTGHPKGVVLSHRNLFLHslaVCAWLKL-------SRDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 334 RLLPDDMKALKPTVFPTVPRLLNRVydkvqneAKTPLKKFllnlaiiskfnevkngiirRDslwdklvFSKIqgslggkv 413
Cdd:PRK06187 245 ENLLDLIETERVTFFFAVPTIWQML-------LKAPRAYF-------------------VD-------FSSL-------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 414 RLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSP-----GDWT-AGHVGTPVACNFVKLEDvADMNYFSV 487
Cdd:PRK06187 284 RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPedqlpGQWTkRRSAGRPLPGVEARIVD-DDGDELPP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 488 NNE--GEICIKGNNVFKGYLKDPEKTQEVLDkDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRS 565
Cdd:PRK06187 363 DGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGH 440
|
490 500
....*....|....*....|....*
gi 58218988 566 RPVLQVFVhgeslrsflIGvvVPDP 590
Cdd:PRK06187 441 PAVAEVAV---------IG--VPDE 454
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
117-680 |
1.05e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 171.05 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 117 YLGSCLLHKGYKSSQD----QFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVIN---------------- 176
Cdd:PTZ00342 111 YEGKGIPEKKYNEEQNngkfKLLGLYGSNSINWLVADLACMLSGVTTLVMHSKFSIDVIVDILNetklewlcldldlveg 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 177 ----RADIP----VVICDTPQKATMLVENVEKGLT------PGLKT---------------IILMDPFDDD--------- 218
Cdd:PTZ00342 191 llerKNELPhlkkLIILDTLIKSKEININKEEKNNgsnvnnNGNKNnkeeqkgndlsneleDISLGPLEYDkeklekikd 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 219 LMKRGEKCGVEMLSLHDAENIGKENFKKPvPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKflEPIFQPTSD 298
Cdd:PTZ00342 271 LKEKAKKLGISIILFDDMTKNKTTNYKIQ-NEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCK--HSIFKKYNP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 299 DVTISYLPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAK--TPLKKFLLN 376
Cdd:PTZ00342 348 KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLVK 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 377 lAIISKFNEVKNGIIRRdsLWDKL--VFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSI 454
Cdd:PTZ00342 428 -KILSLRKSNNNGGFSK--FLEGIthISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 455 TSPGDWTAGHVGTPVACNfVKLEDVADMNYFSVNN--EGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPN 532
Cdd:PTZ00342 505 QHADDNNTESIGGPISPN-TKYKVRTWETYKATDTlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKN 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 533 GTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGV---------- 602
Cdd:PTZ00342 584 GSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlestginekn 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 603 ---KGSFEELCKN---QCVKEAILEdlqkIGKEGGLKSFEQVKSIFVHPEPFTIENgLLTPTLKAKRVELAK---FFQTQ 673
Cdd:PTZ00342 664 yleKLTDETINNNiyvDYVKGKMLE----VYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKdyaFFIDQ 738
|
....*..
gi 58218988 674 IKSLYES 680
Cdd:PTZ00342 739 VKKIYKN 745
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
106-590 |
6.42e-43 |
|
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: 160.85 E-value: 6.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGyKSSQDQfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIc 185
Cdd:cd17631 21 LTYAELDERVNRLAHALRALG-VAKGDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 dtpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppkpEDLSVICFTSGTT 265
Cdd:cd17631 98 -------------------------------------------------------------------DDLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKFLEPifqpTSDDVTISYLPLAHMFERLVQGI-LFSCGGKI----GFfqgDIRLLPDDM 340
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNALAALDL----GPDDVLLVVAPLFHIGGLGVFTLpTLLRGGTVvilrKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 KALKPTVFPTVPRLLNrvydkvqneaktplkkFLLNLaiiskfnevkngiirrdSLWDKLVFSKiqgslggkVRLMITGA 420
Cdd:cd17631 184 ERHRVTSFFLVPTMIQ----------------ALLQH-----------------PRFATTDLSS--------LRAVIYGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 421 APISTPVLTFFRAAmGCWVFEAYGQTECTGGCSITSPGDW--TAGHVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGN 498
Cdd:cd17631 223 APMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 499 NVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKlAQGEYIAPEKIENVYSRSRPVLQVFVhgesl 578
Cdd:cd17631 301 HVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAV----- 373
|
490
....*....|..
gi 58218988 579 rsflIGvvVPDP 590
Cdd:cd17631 374 ----IG--VPDE 379
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
196-561 |
6.90e-43 |
|
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: 162.02 E-value: 6.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 196 ENVEKgLTPGLKTIILMD--PFDDDLMKRGEKCGvemlslhdaenigKENFKKPVPPKPEDLSVICFTSGTTGDPKGAML 273
Cdd:cd05904 113 ELAEK-LASLALPVVLLDsaEFDSLSFSDLLFEA-------------DEAEPPVVVIKQDDVAALLYSSGTTGRSKGVML 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 274 THENVVSNMAAFLKFLEPifQPTSDDVTISYLPLAHM--FERLVQGILfSCGGKI----GFfqgDIRLLPDDMKALKPTV 347
Cdd:cd05904 179 THRNLIAMVAQFVAGEGS--NSDSEDVFLCVLPMFHIygLSSFALGLL-RLGATVvvmpRF---DLEELLAAIERYKVTH 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 348 FPTVPRLLnrvydkvqneaktplkkfllnLAIiskfneVKNGIIrrdslwDKLVFSKIQGslggkvrlMITGAAPISTPV 427
Cdd:cd05904 253 LPVVPPIV---------------------LAL------VKSPIV------DKYDLSSLRQ--------IMSGAAPLGKEL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 428 LTFFRAAM-GCWVFEAYGQTECTGGCSITSPGDWTAGHVGTP--VACNF-VKLEDVADMNYFSVNNEGEICIKGNNVFKG 503
Cdd:cd05904 292 IEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVgrLVPNVeAKIVDPETGESLPPNQTGELWIRGPSIMKG 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 58218988 504 YLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENV 561
Cdd:cd05904 372 YLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
111-602 |
4.26e-41 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 156.72 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 111 VSDRAEYLGSCLLHKGYK--SSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIcdTP 188
Cdd:cd05909 8 LTYRKLLTGAIALARKLAkmTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL--TS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 189 QKAtmlvenVEKGLTPGLKTIilMDPFD----DDLMKR---GEKCGVEMLSLHDAENIGKENFKKPVppKPEDLSVICFT 261
Cdd:cd05909 86 KQF------IEKLKLHHLFDV--EYDARivylEDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 262 SGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAHMFERLVQGIL-FSCGGKIGFFqgdirllPDdm 340
Cdd:cd05909 156 SGSEGLPKGVVLSHKNLLANVEQITA----IFDPNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVFH-------PN-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 kalkPTVFPTVPRLlnrVYD-KVQNEAKTPLkkFLlnlaiiskfnevkNGIIRRdslWDKLVFSKIqgslggkvRLMITG 419
Cdd:cd05909 223 ----PLDYKKIPEL---IYDkKATILLGTPT--FL-------------RGYARA---AHPEDFSSL--------RLVVAG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 420 AAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPG-DWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGN 498
Cdd:cd05909 270 AEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 499 NVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRP----VLQVFV- 573
Cdd:cd05909 350 NVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEILPedneVAVVSVp 427
|
490 500 510
....*....|....*....|....*....|..
gi 58218988 574 ---HGESLRSFLIGvVVPDPDSLPSFAAKIGV 602
Cdd:cd05909 428 dgrKGEKIVLLTTT-TDTDPSSLNDILKNAGI 458
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
104-590 |
8.01e-41 |
|
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: 155.93 E-value: 8.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 104 KWISYKQVSDRAEYLGSCLLHKGYKSsQDQfVGIFAQNRPEWVISELACYTYSMVAVPLyDTLGTEAII-FVINRADIPV 182
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKK-GDR-VAIALPNGLEFVVAFLAAARAGAVVAPL-NPAYKKAEFeFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 183 VIcdTPQKATMLVENVEKGLTPGLKTIILmDPFDDDLMKRGEKcgvemLSLHDAeniGKENFKKPVPPKPEDLSVICFTS 262
Cdd:cd05926 90 VL--TPKGELGPASRAASKLGLAILELAL-DVGVLIRAPSAES-----LSNLLA---DKKNAKSEGVPLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 263 GTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAHmferlVQGIL------FSCGGKIgffqgdirLL 336
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNITN----TYKLTPDDRTLVVMPLFH-----VHGLVasllstLAAGGSV--------VL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 337 P---------DDMKALKPTVFPTVPRLLnrvydkvqneaktplkKFLLNlaiiskfNEVKNGIIRRdslwdklvfskiqg 407
Cdd:cd05926 222 PprfsastfwPDVRDYNATWYTAVPTIH----------------QILLN-------RPEPNPESPP-------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 408 slgGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGgcSITS----PGDWTAGHVGTPVACNFVKLEDvaDMN 483
Cdd:cd05926 265 ---PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH--QMTSnplpPGPRKPGSVGKPVGVEVRILDE--DGE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 484 YFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYS 563
Cdd:cd05926 338 ILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLL 416
|
490 500
....*....|....*....|....*..
gi 58218988 564 RSRPVLQVFVHGeslrsfligvvVPDP 590
Cdd:cd05926 417 SHPAVLEAVAFG-----------VPDE 432
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
106-594 |
1.27e-39 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 153.45 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLlhKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd17642 45 YSYAEYLEMSVRLAEAL--KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DtpQKATMLVENVEKGLtPGLKTIILMDPFDDdlmKRGEKCGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTT 265
Cdd:cd17642 123 S--KKGLQKVLNVQKKL-KIIKTIIILDSKED---YKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVsnmAAFLKFLEPIF--QPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGF-FQGDIRLLPDDMKA 342
Cdd:cd17642 197 GLPKGVQLTHKNIV---ARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmYKFEEELFLRSLQD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 343 LKPTVFPTVPrllnrvydkvqneaktPLKKFLLNLAIISKFNEvkngiirrdslwdklvfskiqgslgGKVRLMITGAAP 422
Cdd:cd17642 274 YKVQSALLVP----------------TLFAFFAKSTLVDKYDL-------------------------SNLHEIASGGAP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 423 ISTPV---------LTFFRaamgcwvfEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEI 493
Cdd:cd17642 313 LSKEVgeavakrfkLPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGEL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 494 CIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENVysrsrpVLQvfv 573
Cdd:cd17642 385 CVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESI------LLQ--- 454
|
490 500
....*....|....*....|...
gi 58218988 574 HGESLRSFLIGvvVPDPDS--LP 594
Cdd:cd17642 455 HPKIFDAGVAG--IPDEDAgeLP 475
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
254-591 |
2.67e-39 |
|
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: 150.52 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYLPLAHMfERLVQGILFS--CGGKI---GF 328
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA----WRWTEDDVLLHVLPLHHV-HGLVNALLCPlfAGASVeflPK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 329 FQGDIRLLPDDMKALkpTVFPTVPRLLNRVYDkvQNEAKTPLKKFllnlaiiskfnevkngiIRRDSLwdklvfskiqgs 408
Cdd:cd05941 165 FDPKEVAISRLMPSI--TVFMGVPTIYTRLLQ--YYEAHFTDPQF-----------------ARAAAA------------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 409 lgGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECtgGCSITSP--GDWTAGHVGTPVACNFVKLEDVADMNYFS 486
Cdd:cd05941 212 --ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEI--GMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 487 VNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKK-NIFKlAQGEYIAPEKIENVYSRS 565
Cdd:cd05941 288 RGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAH 366
|
330 340
....*....|....*....|....*.
gi 58218988 566 RPVLQVFVHGeslrsfligvvVPDPD 591
Cdd:cd05941 367 PGVSECAVIG-----------VPDPD 381
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
235-571 |
3.02e-37 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 146.95 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 235 DAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQ-PTSDDVTISYLPLAHMFER 313
Cdd:PRK08751 190 EALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKlEEGCEVVITALPLYHIFAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 314 LVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFpTVPRLLNRVYDKVQNeakTPLkkfllnlaiiskfnevkngiirr 393
Cdd:PRK08751 270 TANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRF-TAFTGVNTLFNGLLN---TPG----------------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 394 dslWDKLVFSKIQGSLGGkvrlmitGAApISTPVLTFFRAAMGCWVFEAYGQTECTGGCSItSPGDWTA--GHVGTPVAC 471
Cdd:PRK08751 323 ---FDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACI-NPLTLKEynGSIGLPIPS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 472 NFVKLEDVADmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGE 551
Cdd:PRK08751 391 TDACIKDDAG-TVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGF 468
|
330 340
....*....|....*....|
gi 58218988 552 YIAPEKIENVYSRSRPVLQV 571
Cdd:PRK08751 469 NVYPNEIEDVIAMMPGVLEV 488
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
231-590 |
2.45e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 144.14 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 231 LSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDdVTISYLPLAHM 310
Cdd:PRK05677 185 VKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCE-ILIAPLPLYHI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 311 FerlvqGILFSCGGKigffqgdirllpddMKALKPTVFPTVPRLLNRVydkVQNEAKTPLKKFL-LNlaiiSKFNEVKNg 389
Cdd:PRK05677 264 Y-----AFTFHCMAM--------------MLIGNHNILISNPRDLPAM---VKELGKWKFSGFVgLN----TLFVALCN- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 390 iirrDSLWDKLVFSKIQGSLGGKVRLMITGAApistpvltFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPV 469
Cdd:PRK05677 317 ----NEAFRKLDFSALKLTLSGGMALQLATAE--------RWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 470 ACNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQ 549
Cdd:PRK05677 385 PSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVS 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 58218988 550 GEYIAPEKIENVYSRSRPVLQVFV-------HGESLRSFligvVVPDP 590
Cdd:PRK05677 463 GFNVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF----VVVKP 506
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
231-593 |
5.02e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 143.27 E-value: 5.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 231 LSLHDAENIGKE-NFKKPVPpKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISyLPLAH 309
Cdd:PRK08974 184 ISFRSALHKGRRmQYVKPEL-VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTA-LPLYH 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 310 MFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKP---TVFPTVPRLLNRVydkVQNEaktplkkfllnlaiisKFNEV 386
Cdd:PRK08974 262 IFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKypfTAITGVNTLFNAL---LNNE----------------EFQEL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 387 KngiirrdslwdklvFSKIqgslggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECT---GGCSITSPGdwTAG 463
Cdd:PRK08974 323 D--------------FSSL--------KLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 464 HVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKN 543
Cdd:PRK08974 379 SIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKD 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 58218988 544 IFkLAQGEYIAPEKIENVYSRSRPVLQVF-------VHGESLRSFligvVVPDPDSL 593
Cdd:PRK08974 457 MI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIF----VVKKDPSL 508
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
232-544 |
1.40e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 142.06 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 232 SLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMA---AFLKFLepifqPTSDDVTISYLPLA 308
Cdd:PRK05605 198 TLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGL-----GDGPERVLAALPMF 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 309 HMFE-RLVQGILFSCGGKIGFF-QGDIRLLPDDMKALKPTVFPTVPRLlnrvYDKVQNEAKtplkkfllnlaiiskfnev 386
Cdd:PRK05605 273 HAYGlTLCLTLAVSIGGELVLLpAPDIDLILDAMKKHPPTWLPGVPPL----YEKIAEAAE------------------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 387 KNGIirrdslwdklvfskiqgSLGGkVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctggcsiTSP--------G 458
Cdd:PRK05605 330 ERGV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTE-------TSPiivgnpmsD 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 459 DWTAGHVGTPVACNFVKledVADMNYFSVN----NEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGT 534
Cdd:PRK05605 385 DRRPGYVGVPFPDTEVR---IVDPEDPDETmpdgEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGF 460
|
330
....*....|
gi 58218988 535 LKIVDRKKNI 544
Cdd:PRK05605 461 IRIVDRIKEL 470
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
246-591 |
6.80e-35 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 139.77 E-value: 6.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 246 KPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQ-PTSDD--VTISYLPLAHMFERLVQGIL-FS 321
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEkKPRPDqlNFVCALPLYHIFALTVCGLLgMR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 322 CGGkIGFFQGDIRLLPDDMKALKP---TVFPTVPRLLNRvydkvqneaktplkkfLLNlaiiskfnevkngiirrDSLWD 398
Cdd:PRK07059 277 TGG-RNILIPNPRDIPGFIKELKKyqvHIFPAVNTLYNA----------------LLN-----------------NPDFD 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 399 KLVFSKIQGSLGGkvrlmitGAApISTPVLTFFRAAMGCWVFEAYGQTEcTGGCSITSPGDWTA--GHVGTPVACNFVKL 476
Cdd:PRK07059 323 KLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSE-TSPVATCNPVDATEfsGTIGLPLPSTEVSI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 477 EDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPE 556
Cdd:PRK07059 394 RD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGFNVYPN 471
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 58218988 557 KIENVYSRSRPVLQVFV------H-GESLRSFligVVVPDPD 591
Cdd:PRK07059 472 EIEEVVASHPGVLEVAAvgvpdeHsGEAVKLF---VVKKDPA 510
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
108-592 |
1.37e-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: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 108 YKQVSDRAEYLgscllhKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDt 187
Cdd:TIGR01923 6 DCEAAHLAKAL------KAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 188 pqkatmlvenvekgltpglktiilmDPFdddlmkrgEKCGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGD 267
Cdd:TIGR01923 79 -------------------------SLL--------EEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 268 PKGAMLTHEN-VVSNMAAFLKFlePIfqpTSDDVTISYLPLAHMFErlvQGILFSC---GGKIGFFQGDIRLLpDDMKAL 343
Cdd:TIGR01923 126 PKAVPHTFRNhYASAVGSKENL--GF---TEDDNWLLSLPLYHISG---LSILFRWlieGATLRIVDKFNQLL-EMIANE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 344 KPTVFPTVPRLLNRVYDKVQNEakTPLKKFLLnlaiiskfnevkngiirrdslwdklvfskiqgslggkvrlmitGAAPI 423
Cdd:TIGR01923 197 RVTHISLVPTQLNRLLDEGGHN--ENLRKILL-------------------------------------------GGSAI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 424 STPVLtffRAAM--GCWVFEAYGQTE-CTGGCSITSPGDWTAGHVGTPVACNFVKLEdVADMNyfsvnNEGEICIKGNNV 500
Cdd:TIGR01923 232 PAPLI---EEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIK-VDNKE-----GHGEIMVKGANL 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 501 FKGYLkDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVfvhgeslrs 580
Cdd:TIGR01923 303 MKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEA--------- 371
|
490
....*....|..
gi 58218988 581 fligVVVPDPDS 592
Cdd:TIGR01923 372 ----VVVPKPDA 379
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
143-601 |
1.59e-33 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 135.00 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 143 PEWVISELACYTYSMVAVPLyDTLGTEAII--FVINrADIPVVICDtPQKATMLVENVEKGLTPGLKTIilmdpfDDDlm 220
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPL-NTAYTLAELdyFIGD-AEPALVVCD-PANFAWLSKIAAAAGAPHVETL------DAD-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 221 KRGekcgvemlSLHDAENIGKENFKkPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAflkfLEPIFQPTSDDV 300
Cdd:PRK07514 133 GTG--------SLLEAAAAAPDDFE-TVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALT----LVDYWRFTPDDV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 301 TISYLPLAHMFERLV--QGILFScGGKIGFFQgdiRLLPDDMKALKP--TVFPTVP----RLLnrvydkvQNEAKTPlkk 372
Cdd:PRK07514 200 LIHALPIFHTHGLFVatNVALLA-GASMIFLP---KFDPDAVLALMPraTVMMGVPtfytRLL-------QEPRLTR--- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 373 fllnlaiiskfnevkngiirrdslwdklvfskiqgSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctgGC 452
Cdd:PRK07514 266 -----------------------------------EAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 453 SITS-P--GDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRW 529
Cdd:PRK07514 308 MNTSnPydGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 530 LPNGTLKIVDRKKNIfkLAQGEY-IAPEKIENVYSRSRPVLQVFVHGESLRSF---LIGVVVPDPDSLPSFAAKIG 601
Cdd:PRK07514 388 DERGYVHIVGRGKDL--IISGGYnVYPKEVEGEIDELPGVVESAVIGVPHPDFgegVTAVVVPKPGAALDEAAILA 461
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-575 |
3.86e-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: 127.78 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSNmAAF----LKFlepifqpTSDDVTISYLPLAHMFErLVQGILfSC---GG 324
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFigerLGL-------TEQDRLCIPVPLFHCFG-SVLGVL-AClthGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 325 KIgffqgdirllpddmkalkptVFPTvprllnRVYD------KVQNEAKTPL----KKF--LLNLAIISKFNEvkngiir 392
Cdd:cd05917 71 TM--------------------VFPS------PSFDplavleAIEKEKCTALhgvpTMFiaELEHPDFDKFDL------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 393 rdslwdklvfskiqgslgGKVRLMITGAAPISTPVLTFFRAAMGCW-VFEAYGQTECTGGCSITSPGD---WTAGHVGTP 468
Cdd:cd05917 118 ------------------SSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 469 VACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLA 548
Cdd:cd05917 180 MPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IR 258
|
330 340
....*....|....*....|....*..
gi 58218988 549 QGEYIAPEKIENVYSRSRPVLQVFVHG 575
Cdd:cd05917 259 GGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
135-561 |
1.28e-31 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 130.23 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 135 VGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDT----PQKATMLVENVEKGL--TPGLKT 208
Cdd:COG0365 67 VAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrGGKVIDLKEKVDEALeeLPSLEH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 209 IILMDPFDDDLMKRGEkcgvemLSLHDAENIGKENFKkPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKF 288
Cdd:COG0365 147 VIVVGRTGADVPMEGD------LDWDELLAAASAEFE-PEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 289 lepIFQPTSDDV--TIS------------YLPLAH-----MFErlvqgilfscgGKIGFFQGDiRLLpDDMKALKPTVF- 348
Cdd:COG0365 220 ---VLDLKPGDVfwCTAdigwatghsyivYGPLLNgatvvLYE-----------GRPDFPDPG-RLW-ELIEKYGVTVFf 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 349 --PTVPRLLNRVYDKvqneaktPLKKFllnlaiiskfnevkngiiRRDSLwdklvfskiqgslggkvRLMITGAAPISTP 426
Cdd:COG0365 284 taPTAIRALMKAGDE-------PLKKY------------------DLSSL-----------------RLLGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 427 VLTFFRAAMGCWVFEAYGQTEcTGGCSITSPGDWT--AGHVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGNN--VFK 502
Cdd:COG0365 322 VWEWWYEAVGVPIVDGWGQTE-TGGIFISNLPGLPvkPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFR 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58218988 503 GYLKDPEKTQEVL--DKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENV 561
Cdd:COG0365 400 GYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESA 459
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
81-559 |
4.16e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 128.17 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 81 FQRGLAVSDNgPCLGYRKPNQPYkwiSYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACytySMV-- 158
Cdd:PLN02246 30 FERLSEFSDR-PCLIDGATGRVY---TYADVELLSRRVAAGLHKLGIR--QGDVVMLLLPNCPEFVLAFLGA---SRRga 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 159 ----AVPLYdtlgTEAIIFVINRAdipvvicdtpQKATMLVEN---VEK----GLTPGLKTIILMDPFDDDLMkrgekcg 227
Cdd:PLN02246 101 vtttANPFY----TPAEIAKQAKA----------SGAKLIITQscyVDKlkglAEDDGVTVVTIDDPPEGCLH------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 228 VEMLSLHDAENIGKENFKkpvppkPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPL 307
Cdd:PLN02246 160 FSELTQADENELPEVEIS------PDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 308 AHMFErlVQGILFsCGGKIG--------FfqgDIRLLPDDMKALKPTVFPTVPRLLnrvydkvqneaktplkkfllnLAI 379
Cdd:PLN02246 234 FHIYS--LNSVLL-CGLRVGaailimpkF---EIGALLELIQRHKVTIAPFVPPIV---------------------LAI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 380 IskfnevKNGIIRRDSLwdklvfskiqgslgGKVRLMITGAAPISTPVLTFFRAAMGCWVF-EAYGQTECTGGCSIT--- 455
Cdd:PLN02246 287 A------KSPVVEKYDL--------------SSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAGPVLAMClaf 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 456 --SPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNG 533
Cdd:PLN02246 347 akEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDD 426
|
490 500
....*....|....*....|....*.
gi 58218988 534 TLKIVDRKKNIFKLaQGEYIAPEKIE 559
Cdd:PLN02246 427 ELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
96-559 |
7.80e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 127.56 E-value: 7.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 96 YRKPNQPYKWiSYKQVSDRAEYLGSCLLHKGYKSSQdqfvgIFAQNRPEW---VISELACYTYSMVAVPLYDTLGTEAII 172
Cdd:PRK06087 41 AVVDNHGASY-TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 173 FVINRADIPVVICDTPQKAT---MLVENVEKGLtPGLKTIILMDpfdddlmkrgeKCGVEMLSLHDAENIGK-ENFKKPV 248
Cdd:PRK06087 115 WVLNKCQAKMFFAPTLFKQTrpvDLILPLQNQL-PQLQQIVGVD-----------KLAPATSSLSLSQIIADyEPLTTAI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 249 PPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEpifqPTSDDVTISYLPLAHmferlvqgilfscggKIGF 328
Cdd:PRK06087 183 TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN----LTWQDVFMMPAPLGH---------------ATGF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 329 FQGDI--------RLLPDDMKAlkptvfPTVPRLLNRvyDKVQ-NEAKTPlkkFLLNLaiiskFNEVKNGIIRRDSLwdk 399
Cdd:PRK06087 244 LHGVTapfligarSVLLDIFTP------DACLALLEQ--QRCTcMLGATP---FIYDL-----LNLLEKQPADLSAL--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 400 lvfskiqgslggkvRLMITGAAPISTPVLtffRAAM--GCWVFEAYGQTECTGGcSITSPGD---WTAGHVGTPVACNFV 474
Cdd:PRK06087 305 --------------RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 475 KLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIA 554
Cdd:PRK06087 367 KVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENIS 444
|
....*
gi 58218988 555 PEKIE 559
Cdd:PRK06087 445 SREVE 449
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
231-611 |
9.22e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 127.63 E-value: 9.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 231 LSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMA---AFLKFLEPIFQP---TSDDVTISY 304
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLqvrACLSQLGPDGQPlmkEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 305 LPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKptvfptvprllnrvydKVQNEAKTPLKKFLLNLAIISKFN 384
Cdd:PRK12492 265 LPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELG----------------KWRFSALLGLNTLFVALMDHPGFK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 385 evkngiirrdslwdKLVFSKIQGSLGGKVRLMITGAAPistpvltfFRAAMGCWVFEAYGQTECTGGCSITSPGDWTA-G 463
Cdd:PRK12492 329 --------------DLDFSALKLTNSGGTALVKATAER--------WEQLTGCTIVEGYGLTETSPVASTNPYGELARlG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 464 HVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKN 543
Cdd:PRK12492 387 TVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKD 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 544 IFkLAQGEYIAPEKIENVysrsrpvlqVFVHGESLRSFLIGVvvpdPDSLPSFAAKIGVKG-----SFEEL---CK 611
Cdd:PRK12492 466 LI-IVSGFNVYPNEIEDV---------VMAHPKVANCAAIGV----PDERSGEAVKLFVVArdpglSVEELkayCK 527
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
75-575 |
3.26e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 125.66 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 75 KTLYENFQRGLAVSDNGPCLGYRKPNQPYkwiSYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVISELACYT 154
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGVQPGDR--VGIWAPNCAEWLLTQFATAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 155 YSMVAVPLYDTLGTEAIIFVINRADIPVVICDTPQKAT----MLVEnVEKGLT------------PGLKTIILMDPFD-- 216
Cdd:PRK12583 93 IGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSdyhaMLQE-LLPGLAegqpgalacerlPELRGVVSLAPAPpp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 217 -----DDLMKRGEkcGVEMLSLHDAEnigkenfkkpVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAaflkFLEP 291
Cdd:PRK12583 172 gflawHELQARGE--TVSREALAERQ----------ASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGY----FVAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 292 IFQPTSDDVTISYLPLAHMFerlvqGILFSCGGKIGffQGDIRLLPDDmkALKPTVfptvprllnrVYDKVQNEAKTPLk 371
Cdd:PRK12583 236 SLGLTEHDRLCVPVPLYHCF-----GMVLANLGCMT--VGACLVYPNE--AFDPLA----------TLQAVEEERCTAL- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 372 kFLLNLAIISKFNEVKNGIIRRDSLwdklvfskiqgslggkvRLMITGAAPISTPVLTFFRAAMGCW-VFEAYGQTECTG 450
Cdd:PRK12583 296 -YGVPTMFIAELDHPQRGNFDLSSL-----------------RTGIMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETSP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 451 GCSITSPGD------WTAGHVGTPVACNFVKledvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTG 524
Cdd:PRK12583 358 VSLQTTAADdlerrvETVGRTQPHLEVKVVD----PDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 58218988 525 DIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVHG 575
Cdd:PRK12583 434 DLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
254-561 |
3.78e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 125.48 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPifQPTSDDVTISYLPLAHMFErlVQGILFSC----GGKIGFF 329
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGP--EMIGQVVTLGLIPFFHIYG--ITGICCATlrnkGKVVVMS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 330 QGDIRLLPDDMKALKPTVFPTVPrllnrvydkvqneaktPLkkfLLNLaiiskfneVKNGIIrrdslwDKLVFSKIqgsl 409
Cdd:PLN02330 261 RFELRTFLNALITQEVSFAPIVP----------------PI---ILNL--------VKNPIV------EEFDLSKL---- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 410 ggKVRLMITGAAPISTPVLTFFRAAM-GCWVFEAYGQTECTggCSITSPGDWTAGH-------VGTPVACNFVKLEDVAD 481
Cdd:PLN02330 304 --KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 482 MNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENV 561
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
107-598 |
1.44e-29 |
|
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: 122.10 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLHKGYKSsqDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRAdipvvicd 186
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 187 tpqKATMLVenvekglTPGLktiilmdpfdddlmkrgekcgvemlslhdaenigkenFKKPVP-PKPEDLSVICFTSGTT 265
Cdd:cd05903 73 ---KAKVFV-------VPER-------------------------------------FRQFDPaAMPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKFLEPifqpTSDDVTISYLPLAHMferlvqgilfscggkIGFFQGdirllpddmkALKP 345
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAERLGL----GPGDVFLVASPMAHQ---------------TGFVYG----------FTLP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 346 TVFPTvPRLLNRVYD-----KVQNE-------AKTPLKKFLLNLAiiskfnevkngiirrdslwdklvfsKIQGSLGGKV 413
Cdd:cd05903 157 LLLGA-PVVLQDIWDpdkalALMREhgvtfmmGATPFLTDLLNAV-------------------------EEAGEPLSRL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 414 RLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGC-SITSPGDWTAGHV-GTPVACNFVKLEDvADMNYFSVNNEG 491
Cdd:cd05903 211 RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVtSITPAPEDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 492 EICIKGNNVFKGYLKDPEKTQEVLDkDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQV 571
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEA 367
|
490 500 510
....*....|....*....|....*....|
gi 58218988 572 FVHG---ESLRSFLIGVVVPDPDSLPSFAA 598
Cdd:cd05903 368 AVVAlpdERLGERACAVVVTKSGALLTFDE 397
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
106-575 |
2.13e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 122.66 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSSQDQfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYELNVKKGER-IAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQKATMLVENVEKGLTPglkTIILMDPFDddlmkrgekcgvemlsLHDAENIGKEnfkkpvPPKPEDLSVICFTSGTT 265
Cdd:PRK06839 107 EKTFQNMALSMQKVSYVQR---VISITSLKE----------------IEDRKIDNFV------EKNESASFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENV----VSNMAAFlkflepifQPTSDDVTISYLPLAHmferlVQGI-LFS-----CGGKI---GFFQGD 332
Cdd:PRK06839 162 GKPKGAVLTQENMfwnaLNNTFAI--------DLTMHDRSIVLLPLFH-----IGGIgLFAfptlfAGGVIivpRKFEPT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 333 --IRLLPDDmkalKPTVFPTVPRLLNRvydkvqneaktplkkfllnlaiiskfnevkngiIRRDSLWDKLVFSKiqgslg 410
Cdd:PRK06839 229 kaLSMIEKH----KVTVVMGVPTIHQA---------------------------------LINCSKFETTNLQS------ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 411 gkVRLMITGAAPISTPVLTFFRAaMGCWVFEAYGQTECTGGCSITSPGDW--TAGHVGTPVACNFVKLEDvADMNYFSVN 488
Cdd:PRK06839 266 --VRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 489 NEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPV 568
Cdd:PRK06839 342 EVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDV 419
|
....*..
gi 58218988 569 LQVFVHG 575
Cdd:PRK06839 420 YEVAVVG 426
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
106-590 |
2.66e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 120.86 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSSQdqFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGD--RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgVEMLslhdaenigkenfkkpvppkpedlsvicFTSGTT 265
Cdd:cd05934 82 DP----------------------------------------ASIL----------------------------YTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYLPLAHMfERLVQGIL--FSCGGKIGffqgdirLLP------ 337
Cdd:cd05934 94 GPPKGVVITHANLTFAGYYSARR----FGLGEDDVYLTVLPLFHI-NAQAVSVLaaLSVGATLV-------LLPrfsasr 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 338 --DDMKALKPTVFPTVPRLLNRVYdkvqneaKTPlkkfllnlaiiskfnevkngiirrDSLWDKlvfskiqgslGGKVRL 415
Cdd:cd05934 162 fwSDVRRYGATVTNYLGAMLSYLL-------AQP------------------------PSPDDR----------AHRLRA 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 416 miTGAAPISTPVLTFFRAAMGCWVFEAYGQTEctGGCSITSPGDWTA--GHVGTPVACNFVKLEDvADMNYFSVNNEGEI 493
Cdd:cd05934 201 --AYGAPNPPELHEEFEERFGVRLLEGYGMTE--TIVGVIGPRDEPRrpGSIGRPAPGYEVRIVD-DDGQELPAGEPGEL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 494 CIKGNN---VFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKlAQGEYIAPEKIENVYSRSRPVLQ 570
Cdd:cd05934 276 VIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVRE 353
|
490 500
....*....|....*....|
gi 58218988 571 VFVHGeslrsfligvvVPDP 590
Cdd:cd05934 354 AAVVA-----------VPDE 362
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
254-575 |
6.97e-29 |
|
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: 117.99 E-value: 6.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAHMFerlvqgilfscGGKIGFFQGDI 333
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD----CADLTEDDRYLIINPFFHTF-----------GYKAGIVACLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 334 R---LLP----DDMKALKP------TVFPTVPRLLNRVYDKvqneakTPLKKFLLNlaiiskfnevkngiirrdslwdkl 400
Cdd:cd17638 66 TgatVVPvavfDVDAILEAiereriTVLPGPPTLFQSLLDH------PGRKKFDLS------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 401 vfskiqgslggKVRLMITGAAPISTPVLTFFRAAMGC-WVFEAYGQTECtGGCSITSPGD---WTAGHVGTPVACNFVKL 476
Cdd:cd17638 116 -----------SLRAAVTGAATVPVELVRRMRSELGFeTVLTAYGLTEA-GVATMCRPGDdaeTVATTCGRACPGFEVRI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 477 EDvadmnyfsvnnEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPE 556
Cdd:cd17638 184 AD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPA 251
|
330
....*....|....*....
gi 58218988 557 KIENVYSRSRPVLQVFVHG 575
Cdd:cd17638 252 EVEGALAEHPGVAQVAVIG 270
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
135-592 |
1.25e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 120.48 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 135 VGIFAQNRPEWVISELACYTYSMVAVPLYdTLGTEA-IIFVINRADIPVVICDT---PQKATMLVENVekgltPGLKTII 210
Cdd:PRK06188 65 VALLSLNRPEVLMAIGAAQLAGLRRTALH-PLGSLDdHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 211 LMDPFDD--DLMKRGEKCGVEMLSLHDAenigkenfkkpvppkPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKF 288
Cdd:PRK06188 139 TLGPVPDgvDLLAAAAKFGPAPLVAAAL---------------PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 289 LEPIFQPTSDDVTisylPLAHMFERLVQGILFScGGKIGFFQG-DIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEak 367
Cdd:PRK06188 204 WEWPADPRFLMCT----PLSHAGGAFFLPTLLR-GGTVIVLAKfDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLR-- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 368 tplkkfllnlaiiskfnevkngiiRRDslwdklvFSKIQgslggkvrLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTE 447
Cdd:PRK06188 277 ------------------------TRD-------LSSLE--------TVYYGASPMSPVRLAEAIERFGPIFAQYYGQTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 448 CTGGCSITSPGDWTAGHV------GTPVACNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWL 521
Cdd:PRK06188 318 APMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 522 HTGDIGRWLPNGTLKIVDRKK--------NIFklaqgeyiaPEKIENVYSRSRPVLQVFV-------HGESLRsfliGVV 586
Cdd:PRK06188 396 HTGDVAREDEDGFYYIVDRKKdmivtggfNVF---------PREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVV 462
|
....*.
gi 58218988 587 VPDPDS 592
Cdd:PRK06188 463 VLRPGA 468
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
107-590 |
1.31e-27 |
|
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: 117.35 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEwvisELACYtY---SMVAV--PLYDTLGTEAIIFVINRADIP 181
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVK--PGDRVATLAWNTHR----HLELY-YavpGMGAVlhTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 182 VVICDtpqkATM--LVENVeKGLTPGLKTIILMDPFDDDLMKRGEKcgvemlsLHDAEN-IGKENFKKPVPPKPE-DLSV 257
Cdd:cd12119 100 VVFVD----RDFlpLLEAI-APRLPTVEHVVVMTDDAAMPEPAGVG-------VLAYEElLAAESPEYDWPDFDEnTAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 258 ICFTSGTTGDPKGAMLTHENVVSN-MAAflkfLEPIFQPTSD-DVtisYLPLAHMFERLVQGILFSCggkigFFQGDIRL 335
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHRSLVLHaMAA----LLTDGLGLSEsDV---VLPVVPMFHVNAWGLPYAA-----AMVGAKLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 336 LPDD----------MKALKPTV---FPTVPRLLnrvydkvqneaktplkkfllnlaiiskFNEVKNGIIRRDSLWdklvf 402
Cdd:cd12119 236 LPGPyldpaslaelIEREGVTFaagVPTVWQGL---------------------------LDHLEANGRDLSSLR----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 403 skiqgslggkvRLMITGAAPISTPVLTFfrAAMGCWVFEAYGQTE-CTGGCSITSPGDWTAGHV----------GTPVAC 471
Cdd:cd12119 284 -----------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPVPG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 472 NFVKLED----VADMNYFSVnneGEICIKGNNVFKGYLKDPEKTQEvLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKL 547
Cdd:cd12119 351 VELRIVDddgrELPWDGKAV---GELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKS 426
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 58218988 548 AqGEYIAPEKIENVYSRSRPVLQVFVhgeslrsflIGvvVPDP 590
Cdd:cd12119 427 G-GEWISSVELENAIMAHPAVAEAAV---------IG--VPHP 457
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
106-598 |
1.49e-27 |
|
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: 116.09 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGykSSQDQFVGIFAQNRPEWVISELACY----TYsmvaVPLYDTLGTEAIIFVINRADIP 181
Cdd:cd05930 13 LTYAELDARANRLARYLRERG--VGPGDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 182 VVICDtpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppkPEDLSVICFT 261
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 262 SGTTGDPKGAMLTHENVVSnmaaFLKFLEPIFQPTSDDVTISYLPLAhmFERLVQGIL--FSCGGKI----GFFQGDIRL 335
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFS--FDVSVWEIFgaLLAGATLvvlpEEVRKDPEA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 336 LPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLkkfllnlaiiskfnevkngiirrdslwdklvfskiqgslggkvRL 415
Cdd:cd05930 176 LADLLAEEGITVLHLTPSLLRLLLQELELAALPSL-------------------------------------------RL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 416 MITGAAPISTPVLT-FFRAAMGCWVFEAYGQTECTGGCSIT--SPGDWTAGHV--GTPVACNFVKLEDvADMNYFSVNNE 490
Cdd:cd05930 213 VLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 491 GEICIKGNNVFKGYLKDPEKTQEV-----LDKDGWLH-TGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSR 564
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLA 370
|
490 500 510
....*....|....*....|....*....|....*..
gi 58218988 565 SRPVLQVFV---HGESLRSFLIGVVVPDPDSLPSFAA 598
Cdd:cd05930 371 HPGVREAAVvarEDGDGEKRLVAYVVPDEGGELDEEE 407
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
249-589 |
1.66e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 119.26 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 249 PPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAflkfLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGF 328
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQ----ISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 329 FQGDirllPDDMKALKPTVFptvprllnrvydkvQNEAK----TPlkKFLlnlaiiskfnevknGIIRRDSLWDKLVFSK 404
Cdd:PRK08633 854 YHPD----PTDALGIAKLVA--------------KHRATillgTP--TFL--------------RLYLRNKKLHPLMFAS 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 405 IqgslggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSP-----GDWT-----AGHVGTPVACNFV 474
Cdd:PRK08633 900 L--------RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAV 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 475 KLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVL---DKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGE 551
Cdd:PRK08633 972 RIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GE 1050
|
330 340 350
....*....|....*....|....*....|....*...
gi 58218988 552 YIAPEKIENvysrsrpVLQVFVHGESLRsfLIGVVVPD 589
Cdd:PRK08633 1051 MVPLGAVEE-------ELAKALGGEEVV--FAVTAVPD 1079
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
75-610 |
3.14e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 116.45 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 75 KTLYENFQRGLAVSDNGPCLGYRKPNqpYKWiSYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVISELACYT 154
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQG--LRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQFATAK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 155 YSMVAV---PLYDTLGTEaiiFVINRADIPVVIC-----DT----------PQKATMLVENVEKGLTPGLKTIIL----- 211
Cdd:PRK08315 91 IGAILVtinPAYRLSELE---YALNQSGCKALIAadgfkDSdyvamlyelaPELATCEPGQLQSARLPELRRVIFlgdek 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 212 ---MDPFDDdLMKRGEKCGVE-------MLSLHDAENIGkenfkkpvppkpedlsvicFTSGTTGDPKGAMLTHENVVSN 281
Cdd:PRK08315 168 hpgMLNFDE-LLALGRAVDDAelaarqaTLDPDDPINIQ-------------------YTSGTTGFPKGATLTHRNILNN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 282 ---MAAFLKFlepifqpTSDD-VTISyLPLAHMFErLVQGIL--FSCGGKIgffqgdirllpddmkalkptVFPtvprll 355
Cdd:PRK08315 228 gyfIGEAMKL-------TEEDrLCIP-VPLYHCFG-MVLGNLacVTHGATM--------------------VYP------ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 356 NRVYD------KVQNEAKTPL----KKFL--LNLAIISKFNevkngiirrdslwdklvFSkiqgSLggkvRLMITGAAPI 423
Cdd:PRK08315 273 GEGFDplatlaAVEEERCTALygvpTMFIaeLDHPDFARFD-----------------LS----SL----RTGIMAGSPC 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 424 STPVLTFFRAAMGC-WVFEAYGQTECTGGCSITSPGD------WTAGHVGTPVAcnfVKLEDVADMNYFSVNNEGEICIK 496
Cdd:PRK08315 328 PIEVMKRVIDKMHMsEVTIAYGMTETSPVSTQTRTDDplekrvTTVGRALPHLE---VKIVDPETGETVPRGEQGELCTR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 497 GNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVHGe 576
Cdd:PRK08315 405 GYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG- 482
|
570 580 590
....*....|....*....|....*....|....
gi 58218988 577 slrsfligvvVPDPdslpsfaaKIGvkgsfEELC 610
Cdd:PRK08315 483 ----------VPDE--------KYG-----EEVC 493
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
158-542 |
1.38e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 115.05 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 158 VAVPLYDTLGTEAIIFVINRADIPVVIC-------DTPQKATMLVENVekgltPGLKTIILMDPFDD--------DLMKR 222
Cdd:PRK07529 108 IANPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtDIWQKVAEVLAAL-----PELRTVVEVDLARYlpgpkrlaVPLIR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 223 GeKCGVEMLSLHD--AENIGKENFKKPvPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSN--MAAFLKFLEPifqptsD 298
Cdd:PRK07529 183 R-KAHARILDFDAelARQPGDRLFSGR-PIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANawLGALLLGLGP------G 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 299 DVTISYLPLAHMFERLVQGIL-FSCGGKIGFF--QG--DIRLLPDDMK---ALKPTVFPTVPRLLNRVydkvqneAKTPL 370
Cdd:PRK07529 255 DTVFCGLPLFHVNALLVTGLApLARGAHVVLAtpQGyrGPGVIANFWKiveRYRINFLSGVPTVYAAL-------LQVPV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 371 kkfllNLAIISkfnevkngiirrdslwdklvfskiqgSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTG 450
Cdd:PRK07529 328 -----DGHDIS--------------------------SL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATC 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 451 GCSITSP-GDWTAGHVGTPVACNFVKLEDV-ADMNYFS---VNNEGEICIKGNNVFKGYLkDPEKTQEVLDKDGWLHTGD 525
Cdd:PRK07529 373 VSSVNPPdGERRIGSVGLRLPYQRVRVVILdDAGRYLRdcaVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGD 451
|
410
....*....|....*..
gi 58218988 526 IGRWLPNGTLKIVDRKK 542
Cdd:PRK07529 452 LGRIDADGYFWLTGRAK 468
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
158-601 |
1.81e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 113.30 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 158 VAVPLYDTLGTEAIIFVINRADIPVVICDTPqkatmLVENVEKGLTpglktiilmDPFDDDLmkrgekcgvemlsLHDAE 237
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG-----AADRLRDALP---------ASPDPGT-------------VLDAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 238 NI-GKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPifqpTSDDVTISYLPLAHMFERLVQ 316
Cdd:cd05922 101 GIrAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI----TADDRALTVLPLSYDYGLSVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 317 GILFSCGGKIgFFQGDIRL---LPDDMKALKPTVFPTVP---RLLNRV-YDKvqneAKTPLKKFLLNLaiiskfnevkng 389
Cdd:cd05922 177 NTHLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPstyAMLTRLgFDP----AKLPSLRYLTQA------------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 390 iirrdslwdklvfskiqgslGGKVRlmitgAAPISTpvltfFRAAMGCW-VFEAYGQTECTGGCSITSPG--DWTAGHVG 466
Cdd:cd05922 240 --------------------GGRLP-----QETIAR-----LRELLPGAqVYVMYGQTEATRRMTYLPPEriLEKPGSIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 467 TPVA-CNFVKLEDvaDMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIF 545
Cdd:cd05922 290 LAIPgGEFEILDD--DGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMI 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58218988 546 KLAqGEYIAPEKIENVySRSRPVLQVFV-------HGESLRSFLIGVVVPDPDSLPSFAAKIG 601
Cdd:cd05922 368 KLF-GNRISPTEIEAA-ARSIGLIIEAAavglpdpLGEKLALFVTAPDKIDPKDVLRSLAERL 428
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
74-682 |
3.35e-26 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 115.34 E-value: 3.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 74 AKTLYENFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKSSqdQFVGIFAQNRPEWVISELACY 153
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 154 TYSMVAVPLYDTLGTeaIIFVINRADIPVVICDTPQKATMLVENVEKgltpgLKTIILMDPF---DDDLMKRgeKCGVEM 230
Cdd:PTZ00297 504 LYGFTTLPLVGKGST--MRTLIDEHKIKVVFADRNSVAAILTCRSRK-----LETVVYTHSFydeDDHAVAR--DLNITL 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 231 LSLHDAENIGKenfKKPVPPKP--EDLSVICFTSGTTGDPKGAML-----THENVVSNMAAFLKflePIFQPTS--DDVT 301
Cdd:PTZ00297 575 IPYEFVEQKGR---LCPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDISTLVM---TGVLPSSfkKHLM 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 302 ISYLPLAHMFERLVQGILFSCGGKIGffQGDIRLLPDDMKALKPTVFPTVPRLL--NRVYDKVQNEAKTPLKKFLLNLAI 379
Cdd:PTZ00297 649 VHFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFstSRLQLSRANERYSAVYSWLFERAF 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 380 isKFNEVKNGIIRRDSLWDKLVFSK-IQGSLGGKVRLMITGAAPISTPV-----LTFFRAAMGCWVFeaygQTECTGGCS 453
Cdd:PTZ00297 727 --QLRSRLINIHRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----FLPSEGVFC 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 454 ITspgdwtaghvGTPVACNFVKLEDVADMNyfSVNNEGEICI--KGnnvfkgylkDPEKTQEVLDKdgwlhtgdigrWLP 531
Cdd:PTZ00297 801 VD----------GTPAPSLQVDLEPFDEPS--DGAGIGQLVLakKG---------EPRRTLPIAAQ-----------WKR 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 532 NGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSfLIGVVVPDPDSLP-----SFAAKIGVKGSf 606
Cdd:PTZ00297 849 DRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfewrqSHCMGEGGGPA- 926
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 607 EELCKNQCVKEA---ILEDLQKIGKEGGLKSfEQVKSiFVHPEP--FTIENGLLTPTLKAKRVELAKFFQTQIKSLYESI 681
Cdd:PTZ00297 927 RQLGWTELVAYAsslLTADFACIAKENGLHP-SNVPE-YVHLHPhaFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYSDV 1004
|
.
gi 58218988 682 E 682
Cdd:PTZ00297 1005 E 1005
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
107-573 |
5.44e-26 |
|
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: 110.82 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLHKGyKSSQDQFVGIFAQNRPEWVISELACY----TYsmvaVPLYDTLGTEAIIFVINRADIPV 182
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAG-GVGPGDRVAVLLERSAELVVAILAVLkagaAY----VPLDPAYPAERLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 183 VICDTPQKATMlvenVEKGLTPGLKTIILMDPFDDdlmkrgekCGVEMLSlhdaenigkenfkkPVPPKPEDLSVICFTS 262
Cdd:TIGR01733 76 LLTDSALASRL----AGLVLPVILLDPLELAALDD--------APAPPPP--------------DAPSGPDDLAYVIYTS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 263 GTTGDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYLPLAhmFERLVQGILFScggkigFFQGDIRLLPDDmKA 342
Cdd:TIGR01733 130 GSTGRPKGVVVTHRSLVNLLAWLARR----YGLDPDDRVLQFASLS--FDASVEEIFGA------LLAGATLVVPPE-DE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 343 LKPTvfptvPRLLNRVYDKVQneaktplkkfllnlaiISKFNEVKngiirrdSLWDKLVFSKIQGSLGgkVRLMITGAAP 422
Cdd:TIGR01733 197 ERDD-----AALLAALIAEHP----------------VTVLNLTP-------SLLALLAAALPPALAS--LRLVILGGEA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 423 ISTPVLTFFRAAMG-CWVFEAYGQTECTGGCSITS-PGDWTAGHV----GTPVACNFVKLEDvADMNYFSVNNEGEICIK 496
Cdd:TIGR01733 247 LTPALVDRWRARGPgARLINLYGPTETTVWSTATLvDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 497 GNNVFKGYLKDPEKTQEVL--------DKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENVYSRSRPV 568
Cdd:TIGR01733 326 GPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGV 404
|
....*
gi 58218988 569 LQVFV 573
Cdd:TIGR01733 405 REAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
250-598 |
5.72e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 109.37 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 250 PKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPifqpTSDDVTISYLPLAHMferlvqgilfscggkIGFF 329
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGL----GADDVILMASPMAHQ---------------TGFM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 330 QGdiRLLPDDMKA---LKPTVFPTvprllnRVYDKVQNE------AKTPlkkFLLNLAiiskfNEVKNGiiRRDSlwdkl 400
Cdd:PRK13295 255 YG--LMMPVMLGAtavLQDIWDPA------RAAELIRTEgvtftmASTP---FLTDLT-----RAVKES--GRPV----- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 401 vfskiqGSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECtGGCSITSPGD---WTAGHVGTPVACNFVKLE 477
Cdd:PRK13295 312 ------SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTEN-GAVTLTKLDDpdeRASTTDGCPLPGVEVRVV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 478 DvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEvlDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEK 557
Cdd:PRK13295 381 D-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVE 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 58218988 558 IENVYSRSRPVLQVFVHG---ESLRSFLIGVVVPDPDSLPSFAA 598
Cdd:PRK13295 457 IEALLYRHPAIAQVAIVAypdERLGERACAFVVPRPGQSLDFEE 500
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-625 |
6.18e-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: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 82 QRGLAVSDNGPCLGYRKPnqpykWISYKQVSDRAEYLGSCLLHKGYksSQDQFVGIFAQNRPEWVISELACYTYSMVAVP 161
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDR-----RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 162 LYDTLGTEAIIFVINRADIPVVICDTPqkatmlvenvekgltpglktiilmdpFD-DDLMKRGEKcgvemlslhdaenig 240
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLFVDRE--------------------------FEyEDLLAEGDP--------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 241 keNFKkPVPPKPE-DLSVICFTSGTTGDPKGAMLTHE----NVVSNMAAFLKFLEPIFQPTsddvtisyLPLAHM----F 311
Cdd:cd12118 123 --DFE-WIPPADEwDPIALNYTSGTTGRPKGVVYHHRgaylNALANILEWEMKQHPVYLWT--------LPMFHCngwcF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 312 erlVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNrvydkvqneaktplkkFLLNLAiiskfnevkngii 391
Cdd:cd12118 192 ---PWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLN----------------MLANAP------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 392 rrdslwdklvfSKIQGSLGGKVRLMITGAAPistPVLTFFRA-AMGCWVFEAYGQTECTGGCSItspGDWTAGHVGTPVA 470
Cdd:cd12118 240 -----------PSDARPLPHRVHVMTAGAPP---PAAVLAKMeELGFDVTHVYGLTETYGPATV---CAWKPEWDELPTE 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 471 ----------CNFVKLE--DVADMNYF-SVNNE----GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNG 533
Cdd:cd12118 303 erarlkarqgVRYVGLEevDVLDPETMkPVPRDgktiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDG 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 534 TLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVhgeslrsfligVVVPDP---DSLPSFAA-KIGVKGSFEEL 609
Cdd:cd12118 382 YIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAV-----------VARPDEkwgEVPCAFVElKEGAKVTEEEI 449
|
570 580
....*....|....*....|....
gi 58218988 610 ---CKNQ-----CVKEAILEDLQK 625
Cdd:cd12118 450 iafCREHlagfmVPKTVVFGELPK 473
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
229-583 |
7.76e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 109.35 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 229 EMLSLHDAENIGKE-NFKKPVPPKPE-DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQptSDDVTISYLP 306
Cdd:PRK06710 180 ESETIHLWNSVEKEvNTGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKE--GEEVVLGVLP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 307 LAHMF-ERLVQGILFSCGGKIGFF-QGDIRLLPDDMKALKPTVFPTVPRLLNRvydkvqneaktplkkfLLNLAIISKFN 384
Cdd:PRK06710 258 FFHVYgMTAVMNLSIMQGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIA----------------LLNSPLLKEYD 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 385 EvkngiirrdslwdklvfskiqgslgGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTggcSIT-SPGDW--- 460
Cdd:PRK06710 322 I-------------------------SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESS---PVThSNFLWekr 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 461 TAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDR 540
Cdd:PRK06710 374 VPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDR 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 58218988 541 KKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFV-------HGESLRSFLI 583
Cdd:PRK06710 453 KKDMI-VASGFNVYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
196-561 |
2.17e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 108.01 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 196 ENVEKGLTPGLKTIILMDPFDDDlMKRGEKCGVEMLSLHDAENIgkenfkkPVPP-KPEDLSVICFTSGTTGDPKGAMLT 274
Cdd:PLN02574 148 ENVEKLSPLGVPVIGVPENYDFD-SKRIEFPKFYELIKEDFDFV-------PKPViKQDDVAAIMYSSGTTGASKGVVLT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 275 HENVVSNMAAFLKFLEPIFQ-PTSDDVTISYLPLAHMF--ERLVQGILfSCGGKIGFFQgdiRLLPDDM-KAL---KPTV 347
Cdd:PLN02574 220 HRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIYglSLFVVGLL-SLGSTIVVMR---RFDASDMvKVIdrfKVTH 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 348 FPTVPRLLNRVYDKVQNEAKTPLKKfllnlaiiskfnevkngiirrdslwdklvfskiqgslggkVRLMITGAAPISTPV 427
Cdd:PLN02574 296 FPVVPPILMALTKKAKGVCGEVLKS----------------------------------------LKQVSCGAAPLSGKF 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 428 LTFFRAAMGCWVF-EAYGQTECT--GGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGY 504
Cdd:PLN02574 336 IQDFVQTLPHVDFiQGYGMTESTavGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGY 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 58218988 505 LKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENV 561
Cdd:PLN02574 416 LNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAV 471
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
106-583 |
2.25e-24 |
|
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: 106.41 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDR--VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppkpEDLSVICFTSGTT 265
Cdd:cd05935 80 GSEL---------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYLPLAHM--FERLVQGILFSCGGKIGFFQGDIRLLPDDMKAL 343
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVW----TGLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 344 KPTVFPTVPRLLNRVYDKVQNEAktplkkfllnlaiiskfnevkngiirRDslWDKLVfskiqgSLGGkvrlmitGAAPI 423
Cdd:cd05935 173 KVTFWTNIPTMLVDLLATPEFKT--------------------------RD--LSSLK------VLTG-------GGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 424 STPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKG 503
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 504 YLKDPEKTQEVLDKDG---WLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRPVLQVFV------- 573
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|
gi 58218988 574 HGESLRSFLI 583
Cdd:cd05935 371 VGEEVKAFIV 380
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
74-591 |
4.09e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 106.97 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 74 AKTLYENfqrgLAVSDNgpclgyRKPNQPYKW-----ISYKQVSDRAEYLGSCLLHKGYKSSQDQfVGIFAQNRPEWVIS 148
Cdd:PRK08314 9 ETSLFHN----LEVSAR------RYPDKTAIVfygraISYRELLEEAERLAGYLQQECGVRKGDR-VLLYMQNSPQFVIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 149 ELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICdtpqkATMLVENVEKGL-TPGLKTIIL---MDPFDDDlmkRGE 224
Cdd:PRK08314 78 YYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV-----GSELAPKVAPAVgNLRLRHVIVaqySDYLPAE---PEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 225 KCGVEMLSLHDAENIG-------KENFKKPVPPKP-----EDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFlepi 292
Cdd:PRK08314 150 AVPAWLRAEPPLQALApggvvawKEALAAGLAPPPhtagpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 293 FQPTSDDVTISYLPLAHmferlVQGILFSCGGKIgFFQGDIRLLPD-DMKAlkptvfptVPRLLNRVYDKVQNEAKTPLK 371
Cdd:PRK08314 226 SNSTPESVVLAVLPLFH-----VTGMVHSMNAPI-YAGATVVLMPRwDREA--------AARLIERYRVTHWTNIPTMVV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 372 KFLLNlaiiskfnevkNGIIRRD--SLWdklvfskiqgSLGGkvrlmitGAAPISTPVLTFFRAAMGCWVFEAYGQTEcT 449
Cdd:PRK08314 292 DFLAS-----------PGLAERDlsSLR----------YIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTE-T 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 450 GGCSITSPGDWTA-GHVGTPV------ACNFVKLEDVAdmnyfsVNNEGEICIKGNNVFKGYLKDPEKTQEV---LDKDG 519
Cdd:PRK08314 343 MAQTHSNPPDRPKlQCLGIPTfgvdarVIDPETLEELP------PGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKR 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58218988 520 WLHTGDIGRWLPNGTLKIVDRKKNIFKlAQGEYIAPEKIENVYSRSRPVLQVFV-------HGESLRSfligVVVPDPD 591
Cdd:PRK08314 417 FFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKA----VVVLRPE 490
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
250-591 |
5.36e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 105.84 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 250 PKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAflkfLEPIFQPTSDDVTISYLPLAHMfERLVQGILFSC--GGKig 327
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDA----LAEAWQWTADDVLVHGLPLFHV-HGLVLGVLGPLriGNR-- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 328 fFQGDIRLLPD---DMKALKPTVFPTVPRLLNRVydkvqneAKTPlkkfllnlaiiskfnevkngiirrdslwdklvfsK 404
Cdd:PRK07787 198 -FVHTGRPTPEayaQALSEGGTLYFGVPTVWSRI-------AADP----------------------------------E 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 405 IQGSLGGkVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVaDMNY 484
Cdd:PRK07787 236 AARALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDE-DGGP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 485 FSVNNE--GEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDR------KKNIFKLAQGEyiape 556
Cdd:PRK07787 314 VPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE----- 388
|
330 340 350
....*....|....*....|....*....|....*
gi 58218988 557 kIENVYSRSRPVLQVFVHGEslrsfligvvvPDPD 591
Cdd:PRK07787 389 -IETALLGHPGVREAAVVGV-----------PDDD 411
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
106-561 |
8.58e-24 |
|
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: 105.49 E-value: 8.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSsqDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQKAtmlvenvekgLTPGLKTIILMDPfdddlmkrgekcgvemlslHDAENIGKENFkkPVPPKPEDLSVICFTSGTT 265
Cdd:cd17655 101 QSHLQP----------PIAFIGLIDLLDE-------------------DTIYHEESENL--EPVSKSDDLAYVIYTSGST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKFlepIFQPTSDDVtISYLPLAhmFERLVQGILFS--CGGKIgffqgdirllpddmkal 343
Cdd:cd17655 150 GKPKGVMIEHRGVVNLVEWANKV---IYQGEHLRV-ALFASIS--FDASVTEIFASllSGNTL----------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 344 kptvfptvprllnRVYDKVQNEAKTPLKKFllnlaiiskFNEVKNGIIRRDSLWDKLVfSKIQGSLGGKVRLMITGAAPI 423
Cdd:cd17655 207 -------------YIVRKETVLDGQALTQY---------IRQNRITIIDLTPAHLKLL-DAADDSEGLSLKHLIVGGEAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 424 STPVLTFF--RAAMGCWVFEAYGQTECTGGCSI--TSPGDWTAGHV--GTPVACNFVKLEDvADMNYFSVNNEGEICIKG 497
Cdd:cd17655 264 STELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGG 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 498 NNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENV 561
Cdd:cd17655 343 EGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEAR 411
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
250-562 |
2.56e-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: 102.81 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 250 PKPEDLSVICFTSGTTGDPKGAMLTHEN----VVS---NMAAflkflepifqpTSDDVTISYLPLAH------MFERLVQ 316
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNhwwsAIGsalNLGL-----------TEDDNWLCALPLFHisglsiLMRSVIY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 317 GILFSCGGKIgffqgDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLnlaiiskfnevkngiirrdsl 396
Cdd:cd05912 143 GMTVYLVDKF-----DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL--------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 397 wdklvfskiqgslggkvrlmitGAAPISTPVLTFFRAaMGCWVFEAYGQTEcTGGCSIT-SPGDWTA--GHVGTPVACNF 473
Cdd:cd05912 197 ----------------------GGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTlSPEDALNkiGSAGKPLFPVE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 474 VKLEDvadmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYI 553
Cdd:cd05912 253 LKIED----DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENI 326
|
....*....
gi 58218988 554 APEKIENVY 562
Cdd:cd05912 327 YPAEIEEVL 335
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
141-590 |
2.70e-23 |
|
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: 103.19 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 141 NRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTpqkatmlvenvekgltpglktiilmdpfdddlm 220
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 221 krgekcgvemlslhdaenigkenfkkpvppkpEDLSVICFTSGTTGDPKGAMLTHENVVSNM--AAFLKFLEP--IFQPT 296
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIptAAYWLGLRPddIHWNI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 297 SDDVTISYLPLAHMFERLVQGILFSCGGKiGFfqgDIRLLPDDMKALKPTVF---PTVPRLLnrvydkvqneaktplkkf 373
Cdd:cd05972 129 ADPGWAKGAWSSFFGPWLLGATVFVYEGP-RF---DAERILELLERYGVTSFcgpPTAYRML------------------ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 374 llnlaiiskfnevkngiIRRDSlwDKLVFSKiqgslggkVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCS 453
Cdd:cd05972 187 -----------------IKQDL--SSYKFSH--------LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 454 ITSPGDWTAGHVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGNNV--FKGYLKDPEKTQEVLdKDGWLHTGDIGRWLP 531
Cdd:cd05972 240 NFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDE 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 58218988 532 NGTLKIVDRKKNIFKlAQGEYIAPEKIENVYSRSRPVLQVFVhgeslrsfligVVVPDP 590
Cdd:cd05972 318 DGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAV-----------VGSPDP 364
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
254-670 |
5.88e-23 |
|
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: 100.48 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLepifQPTSDDVTISYLPLAHM--FERLVQGILfsCGGKIGFFQG 331
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL----GFGGGDSWLLSLPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 DiRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAktPLKKFllnlaiiskfnevkngiirrdslwdKLVFSkiqgslgg 411
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPA--ALKSL-------------------------RAVLL-------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 412 kvrlmitGAAPISTPVLTFFrAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPvacnfvkLEDVAdmnyFSVNNEG 491
Cdd:cd17630 119 -------GGAPIPPELLERA-ADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVL-------LPGRE----LRIVEDG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 492 EICIKGNNVFKGYLKDPEktQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQV 571
Cdd:cd17630 180 EIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 572 FVHGESLRSF---LIGVVVPDPDSLPsfaakigvkgsfEELckNQCVKeailedlQKIGKegglksFEQVKSIFVHPEPf 648
Cdd:cd17630 257 FVVGVPDEELgqrPVAVIVGRGPADP------------AEL--RAWLK-------DKLAR------FKLPKRIYPVPEL- 308
|
410 420
....*....|....*....|..
gi 58218988 649 tiengLLTPTLKAKRVELAKFF 670
Cdd:cd17630 309 -----PRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
251-593 |
7.07e-23 |
|
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: 102.62 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 251 KPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEpiFQPTSD---------DVTIsylplAHMFERLVQGilfs 321
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG--LTSESRvlqfasytfDVSI-----LEIFTTLAAG---- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 322 cggkigffqG-------DIRL--LPDDMKALKPT-VF--PTVPRLLNRvydkvqneAKTPLKKFLLnLAiiskfNE-VKN 388
Cdd:cd05918 173 ---------GclcipseEDRLndLAGFINRLRVTwAFltPSVARLLDP--------EDVPSLRTLV-LG-----GEaLTQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 389 GIIRRdslWdklvfskiqgslGGKVRLMItgaapistpvltffraamgcwvfeAYGQTECTGGCSITSPG-DWTAGHVGT 467
Cdd:cd05918 230 SDVDT---W------------ADRVRLIN------------------------AYGPAECTIAATVSPVVpSTDPRNIGR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 468 PVACNF--VkleDVADMNYFS-VNNEGEICIKGNNVFKGYLKDPEKTQEVLDKD-GWLH------------TGDIGRWLP 531
Cdd:cd05918 271 PLGATCwvV---DPDNHDRLVpIGAVGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNP 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58218988 532 NGTLKIVDRKKNIFKLaQGEYIAPEKIENVYSRSRP-----VLQVFVH-GESLRSFLIGVVVPDPDSL 593
Cdd:cd05918 348 DGSLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSSS 414
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
104-577 |
1.19e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 101.96 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 104 KWISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVV 183
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 184 ICDtpqkatmlvenvekgltpglktiilmDPFDDdlmKRGEKCGVEMLSLHDAEnigkenfKKPVPPKPE----DLSVIC 259
Cdd:PRK03640 104 ITD--------------------------DDFEA---KLIPGISVKFAELMNGP-------KEEAEIQEEfdldEVATIM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 260 FTSGTTGDPKGAMLTHEN-----VVS--NMAAflkflepifqpTSDDVTISYLPLAH------MFERLVQGIlfscggki 326
Cdd:PRK03640 148 YTSGTTGKPKGVIQTYGNhwwsaVGSalNLGL-----------TEDDCWLAAVPIFHisglsiLMRSVIYGM-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 327 gffqgDIRLLP--------DDMKALKPTVFPTVPRLLNRVYDKVQneaktplkkfllnlaiiskfnevkngiirrdslwd 398
Cdd:PRK03640 209 -----RVVLVEkfdaekinKLLQTGGVTIISVVSTMLQRLLERLG----------------------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 399 klvfskiQGSLGGKVRLMITGAAPISTPVLTFFRAAmGCWVFEAYGQTECtggCS--ITSPGDWTA---GHVGTPVACNF 473
Cdd:PRK03640 249 -------EGTYPSSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTET---ASqiVTLSPEDALtklGSAGKPLFPCE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 474 VKLEDvaDMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYI 553
Cdd:PRK03640 318 LKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENI 393
|
490 500
....*....|....*....|....
gi 58218988 554 APEKIENVYSRSRPVLQVFVHGES 577
Cdd:PRK03640 394 YPAEIEEVLLSHPGVAEAGVVGVP 417
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
249-600 |
2.35e-22 |
|
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: 100.46 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 249 PPKPEDLSVICFTSGTTGDPKGAMLTHENV---VSNMAAFLK---------FLEPIFqptsdDVTIsylplahmferlvq 316
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVlnyVSQPPARLDvgpgsrvaqVLSIAF-----DACI-------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 317 GILFS--CGGKIGFFQGDIRLLPDDMKALkpTVFPTVPRLLnrvydkvqneaktplkkfllnlaiiskfnevknGIIRRD 394
Cdd:cd17653 162 GEIFStlCNGGTLVLADPSDPFAHVARTV--DALMSTPSIL---------------------------------STLSPQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 395 SLwdklvfskiqgslgGKVRLMITGAAPISTPVLTffRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFV 474
Cdd:cd17653 207 DF--------------PNLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 475 KLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE----VLDKDGWLH--TGDIGRWLPNGTLKIVDRKKNIFKLa 548
Cdd:cd17653 271 YILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV- 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 58218988 549 QGEYIAPEKIENVYSRSRPVLQ---VFVHGEslrsFLIGVVVP---DPDSLPSFAAKI 600
Cdd:cd17653 349 RGFRINLEEIEEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
106-592 |
5.01e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 100.24 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYkSSQDQfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGV-GFGDR-VLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPqkATMLVENVeKGLTPGLKTIILM-DPFDDDLMkrgekcGVEMLSLHDAEnigkenfkkPVPPK--PEDL-SVICFT 261
Cdd:PRK07786 121 EAA--LAPVATAV-RDIVPLLSTVVVAgGSSDDSVL------GYEDLLAEAGP---------AHAPVdiPNDSpALIMYT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 262 SGTTGDPKGAMLTHENVVSNMAAFLKFLEpifQPTSDDVTISYLPLAHmferlVQGIlfscGGKIGFFQGDIRLLPDDMK 341
Cdd:PRK07786 183 SGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFH-----IAGI----GSMLPGLLLGAPTVIYPLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 342 ALKPTvfptvprllnRVYDKVQNEAKTplkkfllnlaiiskfnevknGIIRRDSLWDKLVFSKIQGSLGGKVRLMITGAA 421
Cdd:PRK07786 251 AFDPG----------QLLDVLEAEKVT--------------------GIFLVPAQWQAVCAEQQARPRDLALRVLSWGAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 422 PISTPVL-----TFFRAAmgcwVFEAYGQTEctggcsiTSP------GD---WTAGHVGTPVACNFVKLEDvADMNYFSV 487
Cdd:PRK07786 301 PASDTLLrqmaaTFPEAQ----ILAAFGQTE-------MSPvtcmllGEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 488 NNEGEICIKGNNVFKGYLKDPEKTQEVLDkDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRP 567
Cdd:PRK07786 369 GEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPD 446
|
490 500
....*....|....*....|....*...
gi 58218988 568 VLQVFVHGESLRSF---LIGVVVPDPDS 592
Cdd:PRK07786 447 IVEVAVIGRADEKWgevPVAVAAVRNDD 474
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
107-590 |
9.50e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 99.24 E-value: 9.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLHKGYKSSqDQfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICD 186
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKG-DR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 187 TPqkatmLVENVEKGLTPGLktiilMDPFDDDLMKRGEKCGVEMLSLHDAENIGkENFKKPVPPKPEDLSVICFTSGTTG 266
Cdd:PRK08316 116 PA-----LAPTAEAALALLP-----VDTLILSLVLGGREAPGGWLDFADWAEAG-SVAEPDVELADDDLAQILYTSGTES 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 267 DPKGAMLTHENV----VSNMAAfLKFlepifqpTSDDVTISYLPLAHMFERLV-QGILFSCGGKIGFFQG-DIRLLPDDM 340
Cdd:PRK08316 185 LPKGAMLTHRALiaeyVSCIVA-GDM-------SADDIPLHALPLYHCAQLDVfLGPYLYVGATNVILDApDPELILRTI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 KALKPTVF---PTV-PRLLNRvydkvqneaktPLkkfllnlaiiskFNevkngiiRRDslwdklvfskiQGSLggkvRLM 416
Cdd:PRK08316 257 EAERITSFfapPTVwISLLRH-----------PD------------FD-------TRD-----------LSSL----RKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 417 ITGAAPISTPVLTFFRAAM-GCWVFEAYGQTECTGGCSITSPGDWT--AGHVGTPVAcnFV--KLEDvADMNYFSVNNEG 491
Cdd:PRK08316 292 YYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEEHLrrPGSAGRPVL--NVetRVVD-DDGNDVAPGEVG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 492 EICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRPVLQV 571
Cdd:PRK08316 369 EIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEV 446
|
490
....*....|....*....
gi 58218988 572 FVhgeslrsflIGvvVPDP 590
Cdd:PRK08316 447 AV---------IG--LPDP 454
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-559 |
1.02e-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: 97.17 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSN---MAAFLKFlepifqpTSDDVTISYLPLAHMFERLVQGILFscggkigF 328
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNawmLALNSLF-------DPDDVLLCGLPLFHVNGSVVTLLTP-------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 329 FQGDIRLLPDDMKALKPTVFPTVPRLLNRVydKVQNEAKTPlkkfllnlAIISKFNEVKngiIRRDSlwdklvfskiqGS 408
Cdd:cd05944 67 ASGAHVVLAGPAGYRNPGLFDNFWKLVERY--RITSLSTVP--------TVYAALLQVP---VNADI-----------SS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 409 LggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSP-GDWTAGHVGTPVACNFVKL--EDvADMNYF 485
Cdd:cd05944 123 L----RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIkvLD-GVGRLL 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58218988 486 ---SVNNEGEICIKGNNVFKGYLKDpEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIE 559
Cdd:cd05944 198 rdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIE 272
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
106-535 |
1.10e-21 |
|
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: 100.70 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSsqDQFVGIFAQNRPEWVISELA------CYtysmvaVPLYDTLGTEAIIFVINRAD 179
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 180 IPVVICDTpqkatmlvenvekgltpglktiilmdpfddDLMKRGEKCGVEMLSLhDAENIGKENFKKP-VPPKPEDLSVI 258
Cdd:COG1020 574 ARLVLTQS------------------------------ALAARLPELGVPVLAL-DALALAAEPATNPpVPVTPDDLAYV 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 259 CFTSGTTGDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYLPLAH---MFErlvqgiLFS---CGGKIGFFQGD 332
Cdd:COG1020 623 IYTSGSTGRPKGVMVEHRALVNLLAWMQRR----YGLGPGDRVLQFASLSFdasVWE------IFGallSGATLVLAPPE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 333 IRLLPDDMKAL----KPTVFPTVPRLLNRvydkvqneaktplkkfLLnlaiiskfnevkngiirrDSLWDKLvfskiqgs 408
Cdd:COG1020 693 ARRDPAALAELlarhRVTVLNLTPSLLRA----------------LL------------------DAAPEAL-------- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 409 lgGKVRLMITG--AAPISTpVLTFFRAAMGCWVFEAYGQTECTGGCSI--TSPGDWTAGHV--GTPVAcN---FV---KL 476
Cdd:COG1020 731 --PSLRLVLVGgeALPPEL-VRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIA-NtrvYVldaHL 806
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 477 EDVAdmnyfsVNNEGEICIKGNNVFKGYLKDPEKTQEV-----LDKDG--WLHTGDIGRWLPNGTL 535
Cdd:COG1020 807 QPVP------VGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
105-598 |
1.21e-21 |
|
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: 98.52 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 105 WISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVI 184
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVG--PGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 185 CDTPqkatmlvenvekgltpglktiiLMDPFDDDLMkrgekcgVEMLSLHDAENIGKEnfkKPVPPKPEDLSVICFTSGT 264
Cdd:cd12116 90 TDDA----------------------LPDRLPAGLP-------VLLLALAAAAAAPAA---PRTPVSPDDLAYVIYTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 265 TGDPKGAMLTHENVVSnmaaFLKFLEPIFQPTSDD----VT-----IS----YLPLahmferlvqgilfSCGGKIGFFQG 331
Cdd:cd12116 138 TGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDrllaVTtyafdISllelLLPL-------------LAGARVVIAPR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 DIRLLPDDMKALKPTVFPTVprllnrvydkVQneaKTPlkkfllnlaiiskfnevkngiirrdSLWDKLVFSKIQGSLGg 411
Cdd:cd12116 201 ETQRDPEALARLIEAHSITV----------MQ---ATP-------------------------ATWRMLLDAGWQGRAG- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 412 kVRLMITGAA-PistPVLTFFRAAMGCWVFEAYGQTECT--GGCSITSPGDwTAGHVGTPVACNFVKLEDvADMNYFSVN 488
Cdd:cd12116 242 -LTALCGGEAlP---PDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 489 NEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLH-------TGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENV 561
Cdd:cd12116 316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAA 394
|
490 500 510
....*....|....*....|....*....|....*....
gi 58218988 562 YSRSRPVLQ--VFVHGESLRSFLIGVVVPDPDSLPSFAA 598
Cdd:cd12116 395 LAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAA 433
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
158-590 |
2.87e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 97.83 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 158 VAVPLYDTLGTEAIIFVINRADIPVVICdTPQKATMLVENVEKGLTPgLKTIILMD---PFDDDLMKRGEKCGVEMLSLH 234
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVT-SAQFYPMYRQIQQEDATP-LRHICLTRvalPADDGVSSFTQLKAQQPATLC 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 235 DAenigkenfkkpVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVsnMAAFLKFLEPIFqpTSDDVTISYLPLAHM-FER 313
Cdd:PRK08008 166 YA-----------PPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL--RDDDVYLTVMPAFHIdCQC 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 314 LVQGILFSCGGKIGF--------FQGDIRllpdDMKALKPTVFPTVPRLLnRVYDKVQNEAKTPLKK--FLLNLAiiskf 383
Cdd:PRK08008 231 TAAMAAFSAGATFVLlekysaraFWGQVC----KYRATITECIPMMIRTL-MVQPPSANDRQHCLREvmFYLNLS----- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 384 NEVKNGIIRRdslwdklvFskiqgslggKVRLmitgaapistpvltffraamgcwvFEAYGQTECTGGCSITSPGD---W 460
Cdd:PRK08008 301 DQEKDAFEER--------F---------GVRL------------------------LTSYGMTETIVGIIGDRPGDkrrW 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 461 TAghVGTPVACNFVKLEDvADMNYFSVNNEGEICIKG---NNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKI 537
Cdd:PRK08008 340 PS--IGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYF 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 58218988 538 VDRKKNIFKLAqGEYIAPEKIENVYSrSRPVLQVFVhgeslrsfLIGvvVPDP 590
Cdd:PRK08008 417 VDRRCNMIKRG-GENVSCVELENIIA-THPKIQDIV--------VVG--IKDS 457
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
105-570 |
4.82e-21 |
|
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: 97.31 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 105 WISYKQVSDRAEYLGSCLLHKGYKSSQdqfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAII---FVINRADIP 181
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVGKPGDR---VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAErlaAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 182 VVICDTPQKATmLVENVEKGLTPGLKTIILMDPFDDDLMKRGEkcgvemlslhdaenigkenfkkPVPPKPEDLSVICFT 261
Cdd:cd05931 101 VVLTTAAALAA-VRAFAASRPAAGTPRLLVVDLLPDTSAADWP----------------------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 262 SGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAH-MfeRLVQGILFSCggkigFFQGDIRLLPddm 340
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM--GLIGGLLTPL-----YSGGPSVLMS--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 kalkPTVFPTVP----RLLNRV-----------YD----KVQNEAKTPlkkflLNLaiiskfnevkngiirrdslwdklv 401
Cdd:cd05931 224 ----PAAFLRRPlrwlRLISRYratisaapnfaYDlcvrRVRDEDLEG-----LDL------------------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 402 fskiqgslgGKVRLMITGAAPISTPVLTFFRAAMGCW------VFEAYGQTECT----------GGCSITSPGDWTAGHV 465
Cdd:cd05931 271 ---------SSWRVALNGAEPVRPATLRRFAEAFAPFgfrpeaFRPSYGLAEATlfvsggppgtGPVVLRVDRDALAGRA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 466 -----GTPVACNFVKL-EDVADMNYFSVNNE----------GEICIKGNNVFKGYLKDPEKTQEV------LDKDGWLHT 523
Cdd:cd05931 342 vavaaDDPAARELVSCgRPLPDQEVRIVDPEtgrelpdgevGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRT 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 58218988 524 GDIGRwLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRPVLQ 570
Cdd:cd05931 422 GDLGF-LHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPALR 466
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
252-590 |
9.06e-21 |
|
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: 95.78 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSnmaaFLKFLEPIFQPTSDDVTISYLPLAhmFERLVQGILFS-CGGkigffq 330
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDLYPAlASG------ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 331 GDIRLLPDDMKALKPTVFPTVPRL-LNRVYdkvqneaKTPlkkfllnlaiiskfnevkngiirrdSLWDKLVFSK--IQG 407
Cdd:cd05945 164 ATLVPVPRDATADPKQLFRFLAEHgITVWV-------STP-------------------------SFAAMCLLSPtfTPE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 408 SLGGkVRLMITGAAPISTPVL-TFFRAAMGCWVFEAYGQTECTGGCSITspgDWT----AGH----VGTPVACNFVKLED 478
Cdd:cd05945 212 SLPS-LRHFLFCGEVLPHKTArALQQRFPDARIYNTYGPTEATVAVTYI---EVTpevlDGYdrlpIGYAKPGAKLVILD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 479 vADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKD---GWLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAP 555
Cdd:cd05945 288 -EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIEL 365
|
330 340 350
....*....|....*....|....*....|....*....
gi 58218988 556 EKIENVYSRSRPVLQVFV----HGESlRSFLIGVVVPDP 590
Cdd:cd05945 366 EEIEAALRQVPGVKEAVVvpkyKGEK-VTELIAFVVPKP 403
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
253-563 |
2.22e-20 |
|
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: 93.09 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 253 EDLSVICFTSGTTGDPKGAMLTHENVVsnmAAFLKFLEPIFQPTSDDVTISYLPLAHMFERL-VQGILFSCGGKIGFfqG 331
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFF---AVPDILQKEGLNWVVGDVTYLPLPATHIGGLWwILTCLIHGGLCVTG--G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 DIRLLPDDMKAL---KPTVFPTVPRLLNrvydKVQNEAKTPLKkfllnlaiiskfnEVKngiirrdslwdklvfskiqgs 408
Cdd:cd17635 76 ENTTYKSLFKILttnAVTTTCLVPTLLS----KLVSELKSANA-------------TVP--------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 409 lggKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSI-TSPGDWTAGHVGTPVACNFVKLEDVADMNYFSv 487
Cdd:cd17635 118 ---SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPS- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 488 NNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYS 563
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAE 267
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
125-561 |
4.76e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 93.72 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 125 KGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADiPVVIcdtpqkatmlvenvekgltp 204
Cdd:PRK09088 40 RRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE-PRLL-------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 205 glktiilmdpFDDDLMKRGEKCGVEMLSLHDAENIGKENFKKPVPPkpEDLSVICFTSGTTGDPKGAMLTHENVVSNMAA 284
Cdd:PRK09088 99 ----------LGDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERNLQQTAHN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 285 FLKFlepifqpTSDDVTISYLPLAHMFErlVQGILFSC------GGKI----GFFQG-DIRLLPDdmKALKPTVFPTVPR 353
Cdd:PRK09088 167 FGVL-------GRVDAHSSFLCDAPMFH--IIGLITSVrpvlavGGSIlvsnGFEPKrTLGRLGD--PALGITHYFCVPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 354 LLNRvydkvqneaktplkkfllnlaiiskfnevkngiIRRDSLWDklvfskiqGSLGGKVRLMITGAAPISTPVLTFFRA 433
Cdd:PRK09088 236 MAQA---------------------------------FRAQPGFD--------AAALRHLTALFTGGAPHAAEDILGWLD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 434 AmGCWVFEAYGQTEctGGCSITSPGDWT-----AGHVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDP 508
Cdd:PRK09088 275 D-GIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRP 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 58218988 509 EKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENV 561
Cdd:PRK09088 351 QATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAV 402
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
251-596 |
1.57e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.64 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 251 KPEDlSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAHMfERLVQGIL--FSCGGKIgf 328
Cdd:PRK05852 175 RPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIIT----GYRLSPRDATVAVMPLYHG-HGLIAALLatLASGGAV-- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 329 fqgdirLLP-----------DDMKALKPTVFPTVPrllnrvydkvqneaktPLKKFLLNLAIISKFnevkngiirrdslw 397
Cdd:PRK05852 247 ------LLPargrfsahtfwDDIKAVGATWYTAVP----------------TIHQILLERAATEPS-------------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 398 dklvfskiqGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGgcSITSPGDWTAGHVGTPVACNFVKLE 477
Cdd:PRK05852 291 ---------GRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATH--QVTTTQIEGIGQTENPVVSTGLVGR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 478 DVA--------DMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAq 549
Cdd:PRK05852 360 STGaqirivgsDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG- 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 550 GEYIAPEKIENVYSRSRPVLQVFV-------HGESLRSFLI--GVVVPDPDSLPSF 596
Cdd:PRK05852 438 GEKISPERVEGVLASHPNVMEAAVfgvpdqlYGEAVAAVIVprESAPPTAEELVQF 493
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
135-590 |
1.97e-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: 92.17 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 135 VGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTpqkatmlvenvEKGLTpglktiilmdp 214
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIA-----------EDNIP----------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 215 fdDDLMKRGEKCGVE--MLSLHDAENIGKENFKK--------------PVPPKPEDLSVICFTSGTTGDPKgaMLTHEN- 277
Cdd:cd05970 133 --EEIEKAAPECPSKpkLVWVGDPVPEGWIDFRKliknaspdferptaNSYPCGEDILLVYFSSGTTGMPK--MVEHDFt 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 278 -----VVSnmAAFLKFLEPifqptsDDVtisYLPLAHM-FERLVQGILFS---CGGKIGFFQGDiRLLPDDM--KALK-- 344
Cdd:cd05970 209 yplghIVT--AKYWQNVRE------GGL---HLTVADTgWGKAVWGKIYGqwiAGAAVFVYDYD-KFDPKALleKLSKyg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 345 PTVF---PTVPRLLNRvydkvqneaktplkkfllnlAIISKFNevkngiirrdslwdklvFSKIqgslggkvRLMITGAA 421
Cdd:cd05970 277 VTTFcapPTIYRFLIR--------------------EDLSRYD-----------------LSSL--------RYCTTAGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 422 PISTPVLTFFRAAMGCWVFEAYGQTECTgGCSITSPG-DWTAGHVGTPVACNFVKLEDvADMNYFSVNNEGEICI---KG 497
Cdd:cd05970 312 ALNPEVFNTFKEKTGIKLMEGFGQTETT-LTIATFPWmEPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEIVIrtsKG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 498 NNV--FKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKlAQGEYIAPEKIENVYSRSRPVLQVFVHG 575
Cdd:cd05970 390 KPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
490
....*....|....*
gi 58218988 576 eslrsfligvvVPDP 590
Cdd:cd05970 468 -----------VPDP 471
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
252-569 |
2.70e-19 |
|
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: 91.78 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEpifqPTSDDVTISYLPLAHmferlvqgilfscggKIGFFQG 331
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE----WKTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 DIRLLPDDMKA-LKPT-VFPTVPRL-LNRVYDKVQNEAKTP--LKKFLLNLAIISKFNEvkngiirrdslWDKlvfskiq 406
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPILwLKKASEHKATIVSSPnfGYKYFLKTLKPEKAND-----------WDL------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 407 gslgGKVRLMITGAAPISTPVLTFFRAAMGCW------VFEAYGQTECTGGCSI-------------------------- 454
Cdd:cd05908 228 ----SSIRMILNGAEPIDYELCHEFLDHMSKYglkrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepev 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 455 --TSPGDWTAGHVGTPVACNFVKLEDVADmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGrWLPN 532
Cdd:cd05908 304 dkKDSECLTFVEVGKPIDETDIRICDEDN-KILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRN 381
|
330 340 350
....*....|....*....|....*....|....*..
gi 58218988 533 GTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVL 569
Cdd:cd05908 382 GRLVITGREKDII-FVNGQNVYPHDIERIAEELEGVE 417
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
248-542 |
3.69e-19 |
|
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: 91.57 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 248 VPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAflkfLEPIFQPTSDDVTISYLPLAHmferlVQGILFscggkIG 327
Cdd:cd05906 162 PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG----KIQHNGLTPQDVFLNWVPLDH-----VGGLVE-----LH 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 328 FFqgDIRLLPDDMKALKPTVFPTVPRLLNRVyDKVQnEAKTPLKKFLLNLaIISKFNEVKngiirrDSLWDklvfskiqg 407
Cdd:cd05906 228 LR--AVYLGCQQVHVPTEEILADPLRWLDLI-DRYR-VTITWAPNFAFAL-LNDLLEEIE------DGTWD--------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 408 sLGGkVRLMITGAAPISTPVL--------------TFFRAAmgcwvfeaYGQTECTGGCSITSP---GDWTAGH----VG 466
Cdd:cd05906 288 -LSS-LRYLVNAGEAVVAKTIrrllrllepyglppDAIRPA--------FGMTETCSGVIYSRSfptYDHSQALefvsLG 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 467 TPVACNFVKLEDVADmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGrWLPNGTLKIVDRKK 542
Cdd:cd05906 358 RPIPGVSMRIVDDEG-QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
254-590 |
6.99e-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: 88.48 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVV-SNMAaflkfLEPIFQPTSDDVTISYLPLAHmferlVQGI-----LFSCGGK-- 325
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANLQ-----LIHAMGLTEADVYLNMLPLFH-----IAGLnlalaTFHAGGAnv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 326 -IGFFQGDIRLlpDDMKALKPTVFPTVPRLLNRVYDKVqneAKTPLKkfLLNLAIISkfnevknGI-----IRRdslWDK 399
Cdd:cd17637 71 vMEKFDPAEAL--ELIEEEKVTLMGSFPPILSNLLDAA---EKSGVD--LSSLRHVL-------GLdapetIQR---FEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 400 lvfskiqgslggkvrlmITGAapistpvlTFfraamgcWVfeAYGQTEcTGGCSITSPGDWTAGHVGTPVACNFVKLEDV 479
Cdd:cd17637 134 -----------------TTGA--------TF-------WS--LYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVDD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 480 ADmNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRK--KNIFKlAQGEYIAPEK 557
Cdd:cd17637 179 ND-RPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAE 255
|
330 340 350
....*....|....*....|....*....|...
gi 58218988 558 IENVYSRSRPVLQVFVHGeslrsfligvvVPDP 590
Cdd:cd17637 256 VEKVILEHPAIAEVCVIG-----------VPDP 277
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
247-598 |
7.77e-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: 90.10 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 247 PVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSnmaaFLKFLEPIFQPTSDDVTISYLPLAhmFERLVQGIL--FSCGG 324
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 325 KIGFFQGDIRLLPDDMKALKPTvfptvpRLLNRVYdkvqneAKTPLKKFLLNLAiiskfnevkngiirrdslwdklvfsK 404
Cdd:cd17651 204 TLVLPPEEVRTDPPALAAWLDE------QRISRVF------LPTVALRALAEHG-------------------------R 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 405 IQGSLGGKVRLMITGAAPISTPVLT--FFRAAMGCWVFEAYGQTECTGGCSITSPGD---WTA-GHVGTPVACNFVKLED 478
Cdd:cd17651 247 PLGVRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 479 vADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIVDRKKNIFKLaQGEY 552
Cdd:cd17651 327 -AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 58218988 553 IAPEKIENVYSRSRPVLQVFVHGESLRS---FLIGVVVPDPDSLPSFAA 598
Cdd:cd17651 405 IELGEIEAALARHPGVREAVVLAREDRPgekRLVAYVVGDPEAPVDAAE 453
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
177-559 |
8.00e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 90.44 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 177 RADIPVVICDTPQKATMLvenvekgltpGLKTIILMDPFD---DDLMKRGEKcGVEMLSLHDAENIgkenfkKPVPPKPE 253
Cdd:PRK07768 90 RTDLAVWAEDTLRVIGMI----------GAKAVVVGEPFLaaaPVLEEKGIR-VLTVADLLAADPI------DPVETGED 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEpiFQPTSdDVTISYLPLAH-MferlvqgilfscgGKIGFFqgd 332
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE--FDVET-DVMVSWLPLFHdM-------------GMVGFL--- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 333 irllpddmkalkptvfpTVPRLLNRVYDKVqneakTPLkKFLlnlaiiskfnevkngiiRRDSLWDKLVfSKIQG----- 407
Cdd:PRK07768 214 -----------------TVPMYFGAELVKV-----TPM-DFL-----------------RDPLLWAELI-SKYRGtmtaa 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 408 -----SLGGK---------------VRLMITGAAPISTPVLTFFRAAMGCW------VFEAYGQTECTGGCSITSPGD-- 459
Cdd:PRK07768 253 pnfayALLARrlrrqakpgafdlssLRFALNGAEPIDPADVEDLLDAGARFglrpeaILPAYGMAEATLAVSFSPCGAgl 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 460 ---------WTAGHVGTPVACN----FVKL-------------EDVADMNYFSVnneGEICIKGNNVFKGYLkDPEKTQE 513
Cdd:PRK07768 333 vvdevdadlLAALRRAVPATKGntrrLATLgpplpglevrvvdEDGQVLPPRGV---GVIELRGESVTPGYL-TMDGFIP 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 58218988 514 VLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIE 559
Cdd:PRK07768 409 AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
107-666 |
9.54e-19 |
|
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: 89.41 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICD 186
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLE--KGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 187 tpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppKPEDLSVICFTSGTTG 266
Cdd:cd05971 86 ----------------------------------------------------------------GSDDPALIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 267 DPKGAMLTHENVVSNMAAfLKFLEPIFQPTSD---------------DVTISYL----P-LAHMFERLvqgilfscggki 326
Cdd:cd05971 102 PPKGALHAHRVLLGHLPG-VQFPFNLFPRDGDlywtpadwawiggllDVLLPSLyfgvPvLAHRMTKF------------ 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 327 gffqgDIRLLPDDMKALKPT-VF--PTVPRLLNRVYDkvqneaktPLKKFLLNLAIISkfnevkngiirrdslwdklvfs 403
Cdd:cd05971 169 -----DPKAALDLMSRYGVTtAFlpPTALKMMRQQGE--------QLKHAQVKLRAIA---------------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 404 kiqgslggkvrlmiTGAAPISTPVLTFFRAAMGCWVFEAYGQTEC---TGGCSITSPGDwtAGHVGTPVACNFVKLEDvA 480
Cdd:cd05971 214 --------------TGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-D 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 481 DMNYFSVNNEGEICIK--GNNVFKGYLKDPEKTqEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKI 558
Cdd:cd05971 277 NGTPLPPGEVGEIAVElpDPVAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEI 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 559 ENVYSRSRPVLQVFVHGeslrsfligvvVPDPDSLPSFAAKIGVKGSFEElcknqcvKEAILEDLQkigkegglksfEQV 638
Cdd:cd05971 355 EECLLKHPAVLMAAVVG-----------IPDPIRGEIVKAFVVLNPGETP-------SDALAREIQ-----------ELV 405
|
570 580 590
....*....|....*....|....*....|..
gi 58218988 639 KSIF-VHPEPFTIE--NGL-LTPTLKAKRVEL 666
Cdd:cd05971 406 KTRLaAHEYPREIEfvNELpRTATGKIRRREL 437
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
92-656 |
1.17e-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: 89.80 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 92 PCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLhkGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPL---YDTLGT 168
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLL--DLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 169 E-------------AIIFV-----INRADIPVVICDTPQKATmlvenveKGLTPGLKTIilmdPFDDDLMKRGekcGVEM 230
Cdd:cd05921 90 DlaklkhlfellkpGLVFAqdaapFARALAAIFPLGTPLVVS-------RNAVAGRGAI----SFAELAATPP---TAAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 231 LSLHDAenIGkenfkkpvppkPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKfLEPIFQPtSDDVTISYLPLAHM 310
Cdd:cd05921 156 DAAFAA--VG-----------PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQ-TYPFFGE-EPPVLVDWLPWNHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 311 FE-----RLV---QGILFSCGGK--IGFFQGDIRllpdDMKALKPTVFPTVPRLLNRVYDKVQNEAkTPLKKFLLNLAII 380
Cdd:cd05921 221 FGgnhnfNLVlynGGTLYIDDGKpmPGGFEETLR----NLREISPTVYFNVPAGWEMLVAALEKDE-ALRRRFFKRLKLM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 381 skfneVKNGIIRRDSLWDKLVFSKIQgSLGGKVRlMITGaapistpvltffraamgcwvfeaYGQTECTGGCSITSPGDW 460
Cdd:cd05921 296 -----FYAGAGLSQDVWDRLQALAVA-TVGERIP-MMAG-----------------------LGATETAPTATFTHWPTE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 461 TAGHVGTPVACNFVKLedvadmnyFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWL----PNGTLK 536
Cdd:cd05921 346 RSGLIGLPAPGTELKL--------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLV 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 537 IVDRKKNIFKLAQGEYIA--PEKIENVYSRSRPVLQVFVHGESlRSFLIGVVVPDPDSLPSFAAkiGVKGSFEELCKNQC 614
Cdd:cd05921 418 FDGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACRRLVG--LQEASDAEVLRHAK 494
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 58218988 615 VKEAILEDLQKIGKEGGlKSFEQVKSIFVHPEPFTIENGLLT 656
Cdd:cd05921 495 VRAAFRDRLAALNGEAT-GSSSRIARALLLDEPPSIDKGEIT 535
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
106-593 |
1.77e-18 |
|
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: 89.11 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADI-PVVI 184
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMtAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 185 CDtpqkatmlvenvEKGLTPGLKTIILMDPFDDDLMKRGEkcgvemlslhdAENIGKEnFKKPvPPKPEDLSVICFTSGT 264
Cdd:cd05923 107 AV------------DAQVMDAIFQSGVRVLALSDLVGLGE-----------PESAGPL-IEDP-PREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 265 TGDPKGAMLTH---ENVVSNMA--AFLKFlepifqpTSDDVTISYLPLAHMferlvqgilfscggkIGFFQgdirLLpdd 339
Cdd:cd05923 162 TGLPKGAVIPQraaESRVLFMStqAGLRH-------GRHNVVLGLMPLYHV---------------IGFFA----VL--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 340 MKALKPTVFPTVPRllnrvYDKVQNEaktplkkfllnLAIISKfnEVKNGIIRRDSLWDKLVFSKIQGSLGGK-VRLMIT 418
Cdd:cd05923 213 VAALALDGTYVVVE-----EFDPADA-----------LKLIEQ--ERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 419 GAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADmNYFSVNNEGEICIK-- 496
Cdd:cd05923 275 AGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTGTEMRPGFFSEVRIVRIGGSPD-EALANGEEGELIVAaa 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 497 GNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVHG- 575
Cdd:cd05923 354 ADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGv 431
|
490 500
....*....|....*....|
gi 58218988 576 --ESLRSFLIGVVVPDPDSL 593
Cdd:cd05923 432 adERWGQSVTACVVPREGTL 451
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
190-666 |
7.55e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 87.55 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 190 KATMLV---------ENVEKGLTPGLKTIILMDPFDDDLmkrgekcGVEMLSLHDAENIGKENFKKPVPP---KPEDLSV 257
Cdd:PLN02860 104 RPVMLVtdetcsswyEELQNDRLPSLMWQVFLESPSSSV-------FIFLNSFLTTEMLKQRALGTTELDyawAPDDAVL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 258 ICFTSGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAHMferlvqGILFSC------GGKIGFF-Q 330
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSALIVQSLAKIA----IVGYGEDDVYLHTAPLCHI------GGLSSAlamlmvGACHVLLpK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 331 GDIRLLPDDMKALKPTVFPTVPRLLnrvydkvqneaktplkkfllnlaiiskfnevkngiirRDSLwdKLVFSKIQGSLG 410
Cdd:PLN02860 247 FDAKAALQAIKQHNVTSMITVPAMM-------------------------------------ADLI--SLTRKSMTWKVF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 411 GKVRLMITGAAPISTPVL-----TFFRAAmgcwVFEAYGQTE-C--------------TGGCSITSPGDWTAGHVGTPV- 469
Cdd:PLN02860 288 PSVRKILNGGGSLSSRLLpdakkLFPNAK----LFSAYGMTEaCssltfmtlhdptleSPKQTLQTVNQTKSSSVHQPQg 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 470 -----ACNFVKLEDVADmnyfSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNI 544
Cdd:PLN02860 364 vcvgkPAPHVELKIGLD----ESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDR 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 545 FKlAQGEYIAPEKIENVYSRSRPVLQVFVHG---ESLRSFLIGVVVPDPDSLPSFAAKIGVKGSFeELCKnqcvkeailE 621
Cdd:PLN02860 440 IK-TGGENVYPEEVEAVLSQHPGVASVVVVGvpdSRLTEMVVACVRLRDGWIWSDNEKENAKKNL-TLSS---------E 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 58218988 622 DLQKIGKEGGLKSFEQVKSIFVHPEPFTienglLTPTLKAKRVEL 666
Cdd:PLN02860 509 TLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEV 548
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
92-656 |
1.12e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 87.02 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 92 PCLGYRKPNQ-PYKWISYKQVSDRAEYLGSCLLHKGYksSQDQFVGIFAQNRPEWVISELACYTYSMVAVPL---YDTLG 167
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 168 TE-------------AIIFV------------INRADIPVVICDtpqkatmlvenvekGLTPGLKTIilmdPFDDDLMKr 222
Cdd:PRK12582 144 HDhaklkhlfdlvkpRVVFAqsgapfaralaaLDLLDVTVVHVT--------------GPGEGIASI----AFADLAAT- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 223 geKCGVEMLSLHDAenIGkenfkkpvppkPEDLSVICFTSGTTGDPKGAMLTHENVVSN--MAAFLKFLEPIFQPTsddV 300
Cdd:PRK12582 205 --PPTAAVAAAIAA--IT-----------PDTVAKYLFTSGSTGMPKAVINTQRMMCANiaMQEQLRPREPDPPPP---V 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 301 TISYLPLAHMF--ERLVQGILFSCG------GK--IGFFQGDIRLLPDdmkaLKPTVFPTVPRLLNRVYDKVQNEAKTpL 370
Cdd:PRK12582 267 SLDWMPWNHTMggNANFNGLLWGGGtlyiddGKplPGMFEETIRNLRE----ISPTVYGNVPAGYAMLAEAMEKDDAL-R 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 371 KKFLLNLAIISKfnevkNGIIRRDSLWDKL--VFSKIQGSlggkvRLmitgaaPISTpvltffraamgcwvfeAYGQTEc 448
Cdd:PRK12582 342 RSFFKNLRLMAY-----GGATLSDDLYERMqaLAVRTTGH-----RI------PFYT----------------GYGATE- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 449 TGGcsITSPGDWTA---GHVGTPVACNFVKLEDVADmNYfsvnnegEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGD 525
Cdd:PRK12582 389 TAP--TTTGTHWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGD 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 526 IGRWL----PNGTLKIVDRKKNIFKLAQGEYIAPEKIE-NVYSRSRPVLQ-VFVHGESlRSFLIGVVVPDPDSLPSFAAK 599
Cdd:PRK12582 459 AARFVdpddPEKGLIFDGRVAEDFKLSTGTWVSVGTLRpDAVAACSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLAGD 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 58218988 600 IGvkGSFEELCKNQCVKEAILEDLQKIGKEGGLKSfEQVKSIFVHPEPFTIENGLLT 656
Cdd:PRK12582 538 PD--AAPEDVVKHPAVLAILREGLSAHNAEAGGSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
249-591 |
1.18e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 86.63 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 249 PPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLkflePIFQP-TSDDVTISYLPlahMF----ERLvqGILFscg 323
Cdd:PRK06178 205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAY----AVAVVgGEDSVFLSFLP---EFwiagENF--GLLF--- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 324 gkigffqgdirllpddmkalkPTVFPTVPRLLNRvYDKVQNEAKTPLKKFLLNLAIISKFNEVKN--GIIRRDslwdklv 401
Cdd:PRK06178 273 ---------------------PLFSGATLVLLAR-WDAVAFMAAVERYRVTRTVMLVDNAVELMDhpRFAEYD------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 402 FSKIQgslggkvrlmitgaapiSTPVLTF-----------FRAAMGCWVFEA-YGQTEcTGGCSITSPGDWTAGH----- 464
Cdd:PRK06178 324 LSSLR-----------------QVRVVSFvkklnpdyrqrWRALTGSVLAEAaWGMTE-THTCDTFTAGFQDDDFdllsq 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 465 ---VGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRK 541
Cdd:PRK06178 386 pvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRR 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 58218988 542 KNIFKLaQGEYIAPEKIENVYSRSRPVLQVFVHGEslrsfligvvvPDPD 591
Cdd:PRK06178 465 KEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVVGR-----------PDPD 502
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
252-561 |
1.43e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.41 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYLPLAHMFErlvqgilFSCGGkigffqg 331
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAYG-------FNSCT------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 dirLLPddMKALKPTVF---PTVPRLLNRVYD--KVQNEAKTPLkkFLLNLAIISKFNE---------VKNGIIRRDSLW 397
Cdd:PRK06334 244 ---LFP--LLSGVPVVFaynPLYPKKIVEMIDeaKVTFLGSTPV--FFDYILKTAKKQEsclpslrfvVIGGDAFKDSLY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 398 DKL--VFSKIQgslggkvrlmitgaapistpvltffraamgcwVFEAYGQTECTGGCSIT---SPGDWTAghVGTPVACN 472
Cdd:PRK06334 317 QEAlkTFPHIQ--------------------------------LRQGYGTTECSPVITINtvnSPKHESC--VGMPIRGM 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 473 FVKLedVADMNYFSVNN--EGEICIKGNNVFKGYL-KDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAq 549
Cdd:PRK06334 363 DVLI--VSEETKVPVSSgeTGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG- 439
|
330
....*....|..
gi 58218988 550 GEYIAPEKIENV 561
Cdd:PRK06334 440 AEMVSLEALESI 451
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
106-599 |
1.94e-17 |
|
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: 85.72 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELA------CYtysmvaVPLYDTLGTEAIIFVINRAD 179
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVG--PGDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 180 IPVVICDTPqkatmlvenvEKGLTPGLKTIILMDPFDDDlmkrgekcgvemlslHDAENIgkenfkkPVPPKPEDLSVIC 259
Cdd:cd12117 95 AKVLLTDRS----------LAGRAGGLEVAVVIDEALDA---------------GPAGNP-------AVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 260 FTSGTTGDPKGAMLTHENVV-----SNMAAFlkflepifqpTSDDVTISYLPL---AHMFErlVQGILFScGGKigffqg 331
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVrlvknTNYVTL----------GPDDRVLQTSPLafdASTFE--IWGALLN-GAR------ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 dIRLLPDDmkalkptvfptVPRLLNRVYDKVQNEAKTPLkkFLlnlaIISKFNevkngiirrdslwdkLVFSKIQGSLGG 411
Cdd:cd12117 204 -LVLAPKG-----------TLLDPDALGALIAEEGVTVL--WL----TAALFN---------------QLADEDPECFAG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 412 kVRLMITGAAPISTP-VLTFFRAAMGCWVFEAYGQTECTG---GCSITsPGDWTAGHV--GTPVACNFVKLEDvADMNYF 485
Cdd:cd12117 251 -LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTTfttSHVVT-ELDEVAGSIpiGRPIANTRVYVLD-EDGRPV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 486 SVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIE 559
Cdd:cd12117 328 PPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 58218988 560 NVYSRSRPVLQVFV---HGESLRSFLIGVVVP----DPDSLPSFAAK 599
Cdd:cd12117 407 AALRAHPGVREAVVvvrEDAGGDKRLVAYVVAegalDAAELRAFLRE 453
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
105-590 |
7.11e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 84.23 E-value: 7.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 105 WISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEwviselacytysMV----AVPL----YDTLGT----EAII 172
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIG--RGDTVAVLLPNIPA------------MVeahfGVPMagavLNTLNTrldaASIA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 173 FVINRADIPVVICDtPQKATMLVENVEkgLTPGLKtIILMDpFDDDLMKRGEKCGVemLSLHDAENIGKENFKkPVPPKP 252
Cdd:PRK08162 109 FMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPK-PLVID-VDDPEYPGGRFIGA--LDYEAFLASGDPDFA-WTLPAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 253 E-DLSVICFTSGTTGDPKGAMLTHE----NVVSNMAAFLKFLEPIFQPTsddvtisyLPLAHmferlVQGILF------S 321
Cdd:PRK08162 181 EwDAIALNYTSGTTGNPKGVVYHHRgaylNALSNILAWGMPKHPVYLWT--------LPMFH-----CNGWCFpwtvaaR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 322 CGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNrvydkvqneaktplkkfllnlAIISKFNEVKNGIirrdslwdklv 401
Cdd:PRK08162 248 AGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLS---------------------ALINAPAEWRAGI----------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 402 fskiqgslGGKVRLMITGAAPISTpVLTFFrAAMGCWVFEAYGQTECTGGCSITspgDWTAGHVGTPVA----------C 471
Cdd:PRK08162 296 --------DHPVHAMVAGAAPPAA-VIAKM-EEIGFDLTHVYGLTETYGPATVC---AWQPEWDALPLDeraqlkarqgV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 472 NFVKLED--VAD---MNYFSVNNE--GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNI 544
Cdd:PRK08162 363 RYPLQEGvtVLDpdtMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 58218988 545 FkLAQGEYIAPEKIENVYSRSRPVLQVFVhgeslrsfligVVVPDP 590
Cdd:PRK08162 442 I-ISGGENISSIEVEDVLYRHPAVLVAAV-----------VAKPDP 475
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
97-656 |
8.28e-17 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 84.16 E-value: 8.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 97 RKPNQPYKWISYKQVSDRAEYLGSCLLHKGYksSQDQFVGIFAQNRPEWVISELACYTYSMVAVPL---YDTLG------ 167
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGL--SAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdfgkl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 168 -------TEAIIFVINRA------------DIPVVicdtpqkatmlvenVEKGLTPGLKTIilmdPFDDdLMKRGEKCGV 228
Cdd:PRK08180 139 rhvlellTPGLVFADDGAafaralaavvpaDVEVV--------------AVRGAVPGRAAT----PFAA-LLATPPTAAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 229 EmlSLHDAenIGkenfkkpvppkPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAA------FLKFLEPifqptsddVTI 302
Cdd:PRK08180 200 D--AAHAA--VG-----------PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMlaqtfpFLAEEPP--------VLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 303 SYLPLAHMFE-----RLV---QGILFSCGGK--IGFFQGDIRLLpddmKALKPTVFPTVPRLLnrvydkvqnEAKTPLkk 372
Cdd:PRK08180 257 DWLPWNHTFGgnhnlGIVlynGGTLYIDDGKptPGGFDETLRNL----REISPTVYFNVPKGW---------EMLVPA-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 373 fllnlaiiskfnevkngiIRRDSLWDKLVFSKiqgslggkVRLMITGAAPISTPVLT----FFRAAMG--CWVFEAYGQT 446
Cdd:PRK08180 322 ------------------LERDAALRRRFFSR--------LKLLFYAGAALSQDVWDrldrVAEATCGerIRMMTGLGMT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 447 ECTGGCSITSPGDWTAGHVGTPVACNFVKLedvadmnyfsVNNEG--EICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTG 524
Cdd:PRK08180 376 ETAPSATFTTGPLSRAGNIGLPAPGCEVKL----------VPVGGklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 525 DIGRWL----PNGTLKIVDRKKNIFKLAQGEYIA--PEKIENVySRSRPVLQ-VFVHGESlRSFLIGVVVPDPDSLPSFA 597
Cdd:PRK08180 446 DAVRFVdpadPERGLMFDGRIAEDFKLSSGTWVSvgPLRARAV-SAGAPLVQdVVITGHD-RDEIGLLVFPNLDACRRLA 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 58218988 598 AkIGVKGSFEELCKNQCVKEAILEDLQKIGKEGGlKSFEQVKSIFVHPEPFTIENGLLT 656
Cdd:PRK08180 524 G-LLADASLAEVLAHPAVRAAFRERLARLNAQAT-GSSTRVARALLLDEPPSLDAGEIT 580
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
135-591 |
1.54e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 83.19 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 135 VGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTPQKATMlvenveKGLTPGLKTIILMDP 214
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELL------DGLDPGVRVINVDSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 215 FDDDLmkrgekcgvemLSLHDAENIGkenfkkPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAflkfLEPIFQ 294
Cdd:PRK07867 131 AWADE-----------LAAHRDAEPP------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVM----LAQRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 295 PTSDDVTISYLPLAHMfERLVQG--ILFSCGGKIGF---FQGDiRLLPdDMKALKPTVFPTVPRLLNRVY--DKVQNEAK 367
Cdd:PRK07867 190 LGPDDVCYVSMPLFHS-NAVMAGwaVALAAGASIALrrkFSAS-GFLP-DVRRYGATYANYVGKPLSYVLatPERPDDAD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 368 TPLKkfllnlaiISKFNEVKNGIIRRdslwdklvfskiqgslggkvrlmitgaapistpvltfFRAAMGCWVFEAYGQTE 447
Cdd:PRK07867 267 NPLR--------IVYGNEGAPGDIAR-------------------------------------FARRFGCVVVDGFGSTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 448 ctGGCSITSPGDWTAGHVGTPVACnfVKLEDVA----------DMNYFSVNNE--GEIC-IKGNNVFKGYLKDPEKTQEV 514
Cdd:PRK07867 302 --GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedADGRLLNADEaiGELVnTAGPGGFEGYYNDPEADAER 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58218988 515 LdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENVYSRSRPVLQVFVHGeslrsfligvvVPDPD 591
Cdd:PRK07867 378 M-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPDPV 441
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
106-575 |
2.60e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.52 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLlHKGYKSSQDQFVGIFAQNRPEWVISELAcyTYSMVAV--PLYDTLGTEAIIFVINRADIPVV 183
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFA--VACMGAVfnPLNKQLMNDQIVHIINHAEDEVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 184 ICD---TPQKATMLVEnvekglTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAENIGKENFKKPVPPKpEDLSVICF 260
Cdd:PRK05620 116 VADprlAEQLGEILKE------CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPELDE-TTAAAICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 261 TSGTTGDPKGAMLTHENVvsnmaaflkFLEPIFQPTSDDVTI----SYL---PLAHMferLVQGILFScggkiGFFQGdi 333
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSL---------YLQSLSLRTTDSLAVthgeSFLccvPIYHV---LSWGVPLA-----AFMSG-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 334 rllpddmkalKPTVFP----TVPRLlnrvydkvqneAKTplkkfllnlaIISKFNEVKNGIirrDSLWDKLVFSKIQG-- 407
Cdd:PRK05620 250 ----------TPLVFPgpdlSAPTL-----------AKI----------IATAMPRVAHGV---PTLWIQLMVHYLKNpp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 408 ---SLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHvgTPVACNFVKLEDVADMNY 484
Cdd:PRK05620 296 ermSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGE--ARWAYRVSQGRFPASLEY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 485 FSVN----------NEGEICIKGNNVFKGYLKDP----------------EKTQEVLDKDGWLHTGDIGRWLPNGTLKIV 538
Cdd:PRK05620 370 RIVNdgqvmestdrNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIH 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 58218988 539 DRKKNIFKlAQGEYIAPEKIENVYSRSRPVLQVFVHG 575
Cdd:PRK05620 450 DRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
106-595 |
2.96e-16 |
|
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: 81.74 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLlhKGYKSSQDQFVGIFAQNRPEWVISELACytysmvavplydtlgteaiifvINRADIPVVIc 185
Cdd:cd05919 11 VTYGQLHDGANRLGSAL--RNLGVSSGDRVLLLMLDSPELVQLFLGC----------------------LARGAIAVVI- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 dtpqkatmlveNVEkgLTPGLKTIILMDpfdddlmkrgekCGVEMLSLHDaenigkenfkkpvppkpEDLSVICFTSGTT 265
Cdd:cd05919 66 -----------NPL--LHPDDYAYIARD------------CEARLVVTSA-----------------DDIAYLLYSSGTT 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKflePIFQPTSDDVTISylpLAHMF--ERLVQGILF--SCGGKIGFFQGdiRLLPDDMK 341
Cdd:cd05919 104 GPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFfgYGLGNSLWFplAVGASAVLNPG--WPTAERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 342 AL----KPTVFPTVPRLLNRVYDKvqneaktplkkfllnlaiiskfnevknGIIRRDSLWDklvfskiqgslggkVRLMI 417
Cdd:cd05919 176 ATlarfRPTVLYGVPTFYANLLDS---------------------------CAGSPDALRS--------------LRLCV 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 418 TGAAPISTPVLTFFRAAMGCWVFEAYGQTEcTGGCSITS-PGDWTAGHVGTPVACNFVKLEDvADMNYFSVNNEGEICIK 496
Cdd:cd05919 215 SAGEALPRGLGERWMEHFGGPILDGIGATE-VGHIFLSNrPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVR 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 497 GNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRPVLQVFV--- 573
Cdd:cd05919 293 GPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvav 370
|
490 500
....*....|....*....|....*.
gi 58218988 574 ---HGES-LRSFligvVVPDPDSLPS 595
Cdd:cd05919 371 pesTGLSrLTAF----VVLKSPAAPQ 392
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
249-573 |
5.55e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 81.43 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 249 PPKPEDLSV-ICFTSGTTGDPKGAMLTHEnvvsnmAAFLKFLEP--IFQPTSDDVTISYLPLAHmferlVQGILFS---- 321
Cdd:PLN02479 190 PPADEWQSIaLGYTSGTTASPKGVVLHHR------GAYLMALSNalIWGMNEGAVYLWTLPMFH-----CNGWCFTwtla 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 322 --CGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFllnlaiiskfnevkngiirrdslwdk 399
Cdd:PLN02479 259 alCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRV-------------------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 400 lvfskiqgslggkVRLMITGAAPisTPVLTFFRAAMGCWVFEAYGQTECTGGCSITS-PGDWTAGHVGTPVACN------ 472
Cdd:PLN02479 313 -------------VHVMTAGAAP--PPSVLFAMSEKGFRVTHTYGLSETYGPSTVCAwKPEWDSLPPEEQARLNarqgvr 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 473 FVKLE--DVAD---MNYFSVNNE--GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIF 545
Cdd:PLN02479 378 YIGLEglDVVDtktMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII 456
|
330 340
....*....|....*....|....*...
gi 58218988 546 kLAQGEYIAPEKIENVYSRSRPVLQVFV 573
Cdd:PLN02479 457 -ISGGENISSLEVENVVYTHPAVLEASV 483
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
252-589 |
8.51e-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: 80.20 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEpifqptSDDVTISYLPLAHM--------FER--LVQGILFS 321
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYE------LDSFPVRLLQMASFsfdvfagdFARslLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 322 CGGKIGFfqgDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQneaktplkkfllnlaiiskfnevkngiirrdslWDKLV 401
Cdd:cd17650 166 CPDEVKL---DPAALYDLILKSRITLMESTPALIRPVMAYVY---------------------------------RNGLD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 402 FSKIqgslggkvRLMITGA--APISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGH-----VGTPVACNFV 474
Cdd:cd17650 210 LSAM--------RLLIVGSdgCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 475 KLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGW------LHTGDIGRWLPNGTLKIVDRKKNIFKLa 548
Cdd:cd17650 282 YVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI- 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 58218988 549 QGEYIAPEKIENVYSRSRPVLQVFV---HGESLRSFLIGVVVPD 589
Cdd:cd17650 360 RGFRIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
247-598 |
1.66e-15 |
|
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: 79.62 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 247 PVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAhmFERLVQGI--LFSCGG 324
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR----RFAVGPDDRVLALSSLS--FDLSVYDIfgALSAGA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 325 KIgffqgdirLLPDDMKALKP------------TVFPTVPRLLNRVYDKVQNEAKTPLKkflLNLAIISkfnevknGiir 392
Cdd:cd12114 194 TL--------VLPDEARRRDPahwaelierhgvTLWNSVPALLEMLLDVLEAAQALLPS---LRLVLLS-------G--- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 393 rDslWdklvfskIQGSLGGKVRLMITGAAPIStpvltffraaMGcwvfeayGQTECtggcSITS--------PGDWTAGH 464
Cdd:cd12114 253 -D--W-------IPLDLPARLRALAPDARLIS----------LG-------GATEA----SIWSiyhpidevPPDWRSIP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 465 VGTPVAcnfvkledvaDMNYFSVNN---------EGEICIKGNNVFKGYLKDPEKTQE--VLDKDG--WLHTGDIGRWLP 531
Cdd:cd12114 302 YGRPLA----------NQRYRVLDPrgrdcpdwvPGELWIGGRGVALGYLGDPELTAArfVTHPDGerLYRTGDLGRYRP 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58218988 532 NGTLKIVDRKKNIFKLaQGEYIAPEKIENVYSRSRPVLQ--VFVHGESLRSFLIGVVVPDPDSLPSFAA 598
Cdd:cd12114 372 DGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTPIAPD 439
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
106-567 |
1.81e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 80.78 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGScLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK06814 659 LTYRKLLTGAFVLGR-KLKKNTP--PGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTP--QKATM--LVENVEKGLTpglktIILMDPFdddlmKRGEKCGVEMLSLhdaenIGKENFKKPVP-PKPEDLSVICF 260
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEFGIR-----IIYLEDV-----RAQIGLADKIKGL-----LAGRFPLVYFCnRDPDDPAVILF 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 261 TSGTTGDPKGAMLTHENVVSNMA---AFLKFlepifqpTSDDVTISYLPLAHMFerlvqgilfscggkiGFFQGdiRLLP 337
Cdd:PRK06814 801 TSGSEGTPKGVVLSHRNLLANRAqvaARIDF-------SPEDKVFNALPVFHSF---------------GLTGG--LVLP 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 338 ddMKALKPTVF-PT------VPRLlnrVYDkvqneaktplkkflLNLAIISKFNEVKNGIIRRDSLWDklvFSKIqgslg 410
Cdd:PRK06814 857 --LLSGVKVFLyPSplhyriIPEL---IYD--------------TNATILFGTDTFLNGYARYAHPYD---FRSL----- 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 411 gkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVAdmnyfSVNNE 490
Cdd:PRK06814 910 ---RYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVP-----GIDEG 981
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58218988 491 GEICIKGNNVFKGYLKdPEKtQEVLD--KDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRP 567
Cdd:PRK06814 982 GRLFVRGPNVMLGYLR-AEN-PGVLEppADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEELAAELWP 1057
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
234-590 |
2.78e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 79.31 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 234 HDAENIGKENFKKPVPPKPEDLSVIC---FTSGTTGDPKGAMLTHEN---VVSNMAAFLkflepifQP--TSDDVTISYL 305
Cdd:PRK07470 141 LDYEALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQmafVITNHLADL-------MPgtTEQDASLVVA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 306 PLAHM--FERLVQgilFSCGGKIGFFQGDiRLLPDDMKAL----KPTVFPTVPRLLNRVydkVQNEAktplkkfllnlai 379
Cdd:PRK07470 214 PLSHGagIHQLCQ---VARGAATVLLPSE-RFDPAEVWALverhRVTNLFTVPTILKML---VEHPA------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 380 iskfnevkngIIRRDslwdklvfskiQGSLggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGgcSIT---- 455
Cdd:PRK07470 274 ----------VDRYD-----------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTG--NITvlpp 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 456 ---SPGDWTAGHVGTpvaCNF------VKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDI 526
Cdd:PRK07470 327 alhDAEDGPDARIGT---CGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDL 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58218988 527 GRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVHGeslrsfligvvVPDP 590
Cdd:PRK07470 402 GHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPDP 453
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
107-573 |
3.11e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 79.29 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLhkGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICD 186
Cdd:PLN03102 41 TWPQTYDRCCRLAASLI--SLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 187 TP-----QKATMLVENVEKGLTPGLKTIILMD----PFDDD-----LMKRGEKCG---VEMLSLHDAENigkenfkkpvp 249
Cdd:PLN03102 119 RSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSEEldyecLIQRGEPTPslvARMFRIQDEHD----------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 250 pkPEDLSvicFTSGTTGDPKGAMLTHEnvvsnmAAFLKFLEPI--FQPTSDDVTISYLPLAHmferlVQGILFSCG-GKI 326
Cdd:PLN03102 188 --PISLN---YTSGTTADPKGVVISHR------GAYLSTLSAIigWEMGTCPVYLWTLPMFH-----CNGWTFTWGtAAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 327 GFFQGDIRLLpddmkalkptvfpTVPRllnrVYDKVQneaktplkkfLLNLAIISKFNEVKNGIIRRDSLwdklvfskIQ 406
Cdd:PLN03102 252 GGTSVCMRHV-------------TAPE----IYKNIE----------MHNVTHMCCVPTVFNILLKGNSL--------DL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 407 GSLGGKVRLMITGAAPISTPVLTFFRaaMGCWVFEAYGQTECTGGCSITSPGD-WT------AGHVGTPVACNFVKLEDV 479
Cdd:PLN03102 297 SPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLADV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 480 ADMNYFSVNNE-------GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEY 552
Cdd:PLN03102 375 DVKNKETQESVprdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGEN 452
|
490 500
....*....|....*....|.
gi 58218988 553 IAPEKIENVYSRSRPVLQVFV 573
Cdd:PLN03102 453 ISSVEVENVLYKYPKVLETAV 473
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
248-594 |
7.22e-15 |
|
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: 77.70 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 248 VPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAaflkFLEPIFQPTSDDVTISYLPLAhmFERLVQGIL--FSCGGK 325
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLL----WMQDEYPLGPGDRVLQKTPLS--FDVSVWELFwpLVAGAR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 326 IGFFQ----GDIRLLPDDMKALKPTVFPTVPRLLnRVydkvqneaktplkkfLLNLAiiskfnevkngiirRDSLWDKLv 401
Cdd:cd17646 207 LVVARpgghRDPAYLAALIREHGVTTCHFVPSML-RV---------------FLAEP--------------AAGSCASL- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 402 fskiqgslggkvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCS-ITSPGDWTAGHV--GTPVACNFVKLED 478
Cdd:cd17646 256 ------------RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYVLD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 479 vADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG----WLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEY 552
Cdd:cd17646 324 -DALRPVPVGVPGELYLGGVQLARGYLGRPALTAErfVPDPFGpgsrMYRTGDLARWRPDGALEFLGRSDDQVKI-RGFR 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 58218988 553 IAPEKIENVYSRSRPVLQVFV---HGESLRSFLIGVVVPDPDSLP 594
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPAAGAAG 446
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
247-591 |
1.38e-14 |
|
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: 76.65 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 247 PVPPkPEDLS---VICFTSGTTGDPKGAMLTHENVVSN-----MAAFLkflepiFQPTSDDVTISYLPLAHMF-ERLVQG 317
Cdd:cd05929 117 PETP-IEDEAagwKMLYSGGTTGRPKGIKRGLPGGPPDndtlmAAALG------FGPGADSVYLSPAPLYHAApFRWSMT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 318 ILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVydkvqneAKTPlkkfllnlaiiskfNEVKNgiiRRDslw 397
Cdd:cd05929 190 ALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRL-------LKLP--------------EAVRN---AYD--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 398 dklvFSKIQGslggkvrlMITGAAPISTPVltffRAAMGCW----VFEAYGQTECTGGCSITSPgDWTA--GHVGTPVAC 471
Cdd:cd05929 243 ----LSSLKR--------VIHAAAPCPPWV----KEQWIDWggpiIWEYYGGTEGQGLTIINGE-EWLThpGSVGRAVLG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 472 NfVKLEDvADMNYFSVNNEGEICIKGNNVFKgYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGE 551
Cdd:cd05929 306 K-VHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGV 381
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 58218988 552 YIAPEKIENVYSRSRPVLQVFVHGeslrsfligvvVPDPD 591
Cdd:cd05929 382 NIYPQEIENALIAHPKVLDAAVVG-----------VPDEE 410
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
106-594 |
1.58e-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: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DtpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppkPEDLSVICFTSGTT 265
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVsnmaAFLKFLEPIFqpTSDDVT-------ISY-LPLAHMFERLvqgilfSCGGKIgFFQGDIRLLP 337
Cdd:cd12115 118 GRPKGVAIEHRNAA----AFLQWAAAAF--SAEELAgvlastsICFdLSVFELFGPL------ATGGKV-VLADNVLALP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 338 DDMKALKPTVFPTVP----RLLNrvYDKVQNEAKTplkkflLNLAiiskfnevknGiirrDSLWDKLVfSKIQGSLGGKV 413
Cdd:cd12115 185 DLPAAAEVTLINTVPsaaaELLR--HDALPASVRV------VNLA----------G----EPLPRDLV-QRLYARLQVER 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 414 rlmitgaapistpvltffraamgcwVFEAYGQTECTG---GCSITsPGDWTAGHVGTPVACNFVKLEDvADMNYFSVNNE 490
Cdd:cd12115 242 -------------------------VVNLYGPSEDTTystVAPVP-PGASGEVSIGRPLANTQAYVLD-RALQPVPLGVP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 491 GEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENVYSR 564
Cdd:cd12115 295 GELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRS 373
|
490 500 510
....*....|....*....|....*....|...
gi 58218988 565 SRPVLQ--VFVHGESLRS-FLIGVVVPDPDSLP 594
Cdd:cd12115 374 IPGVREavVVAIGDAAGErRLVAYIVAEPGAAG 406
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
106-612 |
2.12e-14 |
|
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: 76.25 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLyDTLGTEAiifvinraDIPVVIC 185
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPV-NTLLTPD--------DYAYYLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTpqKATMLVenVEKGLTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAENIGKE-NFKKPVPPKPEDLSVICFTSGT 264
Cdd:cd05959 99 DS--RARVVV--VSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEaEQLKPAATHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 265 TGDPKGAMLTHEN--VVSNMAAflkflEPIFQPTSDDVTISYLPLAHMFErLVQGILF--SCGGKIGFFQGdiRLLPDDM 340
Cdd:cd05959 175 TGRPKGVVHLHADiyWTAELYA-----RNVLGIREDDVCFSAAKLFFAYG-LGNSLTFplSVGATTVLMPE--RPTPAAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 341 KAL----KPTVFPTVPRLLNRvydkvqneaktplkkfLLNlaiiskfnevkngiirrDSLWDKLVFSKIqgslggkvRLM 416
Cdd:cd05959 247 FKRirryRPTVFFGVPTLYAA----------------MLA-----------------APNLPSRDLSSL--------RLC 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 417 ITGAAPISTPVLTFFRAAMGCWVFEAYGQTE-----CTggcsiTSPGDWTAGHVGTPVACNFVKL-----EDVADmnyfs 486
Cdd:cd05959 286 VSAGEALPAEVGERWKARFGLDILDGIGSTEmlhifLS-----NRPGRVRYGTTGKPVPGYEVELrdedgGDVAD----- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 487 vNNEGEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKlAQGEYIAPEKIENVYSRSR 566
Cdd:cd05959 356 -GEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHP 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 58218988 567 PVLQVFVHGESLRSFLI---GVVVPDPDSLPSFAAKIGVKgsfeELCKN 612
Cdd:cd05959 433 AVLEAAVVGVEDEDGLTkpkAFVVLRPGYEDSEALEEELK----EFVKD 477
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
251-595 |
3.03e-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: 75.55 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 251 KPEDLSVICFTSGTTGDPKGAMLTHENVVSnmaaFLKFLEPIFQPTSDDVTISYLPLAhmFERLVQGILFS-CGGkigff 329
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVN----LSHGLIKEYGITSSDRVLQFASIA--FDVAAEEIYVTlLSG----- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 330 qGDIRLLPDDMkalkptvFPTVPRLLnrvyDKVQNEAKTplkkfLLNLAiiskfnevkngiirrDSLWDKLVFSKIQGSL 409
Cdd:cd17644 173 -ATLVLRPEEM-------RSSLEDFV----QYIQQWQLT-----VLSLP---------------PAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 410 GG--KVRLMITGAAPISTPVLTFFRAAMGCWV--FEAYGQTECTGGCSITSPGDWTAGH-----VGTPVACNFVKLEDvA 480
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 481 DMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLH--------TGDIGRWLPNGTLKIVDRKKNIFKLaQGEY 552
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 58218988 553 IAPEKIENVYSRSRPVLQVFV---HGESLRSFLIGVVVPDPDSLPS 595
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPS 424
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
231-568 |
3.15e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 75.96 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 231 LSLHDAENIGKENFKKPVPPKP-EDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLkflEPIFQPTSDDVTISYLPLAH 309
Cdd:PRK05851 129 VTVHDLATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLN---ARVGLDAATDVGCSWLPLYH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 310 -MferlvqGILFSCGGKIGffQGDIRLLPDdmkalkpTVFPTVP-RLLNRVYDKVQNEAKTPlkkfllNLA--IISKFNe 385
Cdd:PRK05851 206 dM------GLAFLLTAALA--GAPLWLAPT-------TAFSASPfRWLSWLSDSRATLTAAP------NFAynLIGKYA- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 386 vkngiiRRDSLWDKlvfskiqgslgGKVRLMITGAAPISTPVLTFFRAAMGCWVFEA------YGQTECTggCSITSP-- 457
Cdd:PRK05851 264 ------RRVSDVDL-----------GALRVALNGGEPVDCDGFERFATAMAPFGFDAgaaapsYGLAEST--CAVTVPvp 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 458 -------------GDWTAGH--VGTPVACNFVKL---EDVADMNYFSVnneGEICIKGNNVFKGYLKdpektQEVLDKDG 519
Cdd:PRK05851 325 giglrvdevttddGSGARRHavLGNPIPGMEVRIspgDGAAGVAGREI---GEIEIRGASMMSGYLG-----QAPIDPDD 396
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 58218988 520 WLHTGDIGrWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRPV 568
Cdd:PRK05851 397 WFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERVAAQVRGV 443
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
252-589 |
4.54e-14 |
|
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: 75.04 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAflkfLEPIFQPTSDDVTI---SY----------LPLAHmferlvqgi 318
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTlfhSYafdfsvweiwGALLH--------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 319 lfscGGKIGFFQGDIRLLPDDMkalkptvfptvPRLLNRVYDKVQNEAKTPLKKFLLnlaiiskfnEVKNGIIRRDSLwd 398
Cdd:cd17643 159 ----GGRLVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLVE---------AADRDGRDPLAL-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 399 klvfskiqgslggkvRLMITGAAPISTPVLTFFRAAMGCW---VFEAYGQTECTGGCSIT--SPGDW---TAGHVGTPVA 470
Cdd:cd17643 213 ---------------RYVIFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 471 CNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG-----WLHTGDIGRWLPNGTLKIVDRKKN 543
Cdd:cd17643 278 GLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfVANPFGgpgsrMYRTGDLARRLPDGELEYLGRADE 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 58218988 544 IFKLaQGEYIAPEKIENVYSRSRPVLQVFV---HGESLRSFLIGVVVPD 589
Cdd:cd17643 357 QVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVAD 404
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
248-580 |
5.05e-14 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 75.52 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 248 VPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAflkfLEPIFQPTSDDVTISYLPLAHMFErLVQGIL--FSCGGK 325
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQ----IKTIADFTPNDRFMSALPLFHSFG-LTVGLFtpLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 326 IgfFqgdirLLPddmkalKPTVFPTVPRLlnrVYDK---VQNEAKTplkkFLLNLAiiskfnevkngiiRRDSLWDklvF 402
Cdd:PRK08043 435 V--F-----LYP------SPLHYRIVPEL---VYDRnctVLFGTST----FLGNYA-------------RFANPYD---F 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 403 skiqgslgGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVAdm 482
Cdd:PRK08043 479 --------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVP-- 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 483 nyfSVNNEGEICIKGNNVFKGYLK--DP--------EKTQEVLDKdGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEY 552
Cdd:PRK08043 549 ---GIEQGGRLQLKGPNIMNGYLRveKPgvlevptaENARGEMER-GWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEM 623
|
330 340
....*....|....*....|....*...
gi 58218988 553 IAPEKIENVYSRSRPVLQvfvHGESLRS 580
Cdd:PRK08043 624 VSLEMVEQLALGVSPDKQ---HATAIKS 648
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
106-589 |
1.78e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.43 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSsqDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGP--DVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQKATMLVENvekgltpGLKTIILMDPFDddlmkrgekcgveMLSLHDAENigkenfkKPVPPKPEDLSVICFTSGTT 265
Cdd:PRK12467 616 QSHLLAQLPVPA-------GLRSLCLDEPAD-------------LLCGYSGHN-------PEVALDPDNLAYVIYTSGST 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHenvvSNMAAFLKFLEPIFQPTSDDVTISYLPLA------HMFERLVQGilfscggkigffqGDIRLLPDD 339
Cdd:PRK12467 669 GQPKGVAISH----GALANYVCVIAERLQLAADDSMLMVSTFAfdlgvtELFGALASG-------------ATLHLLPPD 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 340 MkALKPTVFptvprllnrvYDKVQNEAKTPLKKFllnlaiiskfnevkngiirrDSLWDKLVFSKIQGSLGGKVRLMITG 419
Cdd:PRK12467 732 C-ARDAEAF----------AALMADQGVTVLKIV--------------------PSHLQALLQASRVALPRPQRALVCGG 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 420 AA-PISTPVLtFFRAAMGCWVFEAYGQTECTGGCSI----TSPGDWTAGHVGTPVACNFVKLEDvADMNYFSVNNEGEIC 494
Cdd:PRK12467 781 EAlQVDLLAR-VRALGPGARLINHYGPTETTVGVSTyelsDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELY 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 495 IKGNNVFKGYLKDPEKTQE--VLDKDG-----WLHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENVYSRSRP 567
Cdd:PRK12467 859 IGGAGLARGYHRRPALTAErfVPDPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPG 937
|
490 500
....*....|....*....|....
gi 58218988 568 VLQVFV--HGESLRSFLIGVVVPD 589
Cdd:PRK12467 938 VREAVVlaQPGDAGLQLVAYLVPA 961
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
247-573 |
2.33e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.60 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 247 PVPPKPEDLSVICFTSGTTGDPKGAMLTHEN-------VVSNMAaflkflepiFQPtSDDVTISyLPLAHmferlV--QG 317
Cdd:PRK09029 129 AVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhlasaegVLSLMP---------FTA-QDSWLLS-LPLFH-----VsgQG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 318 ILF---SCGGKIGFfqGDIRLLPDDMK-----ALKPTvfpTVPRLLNrvydkvQNEAKTPLKKFLLnlaiiskfnevkng 389
Cdd:PRK09029 193 IVWrwlYAGATLVV--RDKQPLEQALAgcthaSLVPT---QLWRLLD------NRSEPLSLKAVLL-------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 390 iirrdslwdklvfskiqgslggkvrlmitGAAPISTpVLTFFRAAMG--CWVfeAYGQTECtgGCSITS-PGDWTAGhVG 466
Cdd:PRK09029 248 -----------------------------GGAAIPV-ELTEQAEQQGirCWC--GYGLTEM--ASTVCAkRADGLAG-VG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 467 TPVACNFVKLEDvadmnyfsvnneGEICIKGNNVFKGYLKDpEKTQEVLDKDGWLHTGDIGRWLpNGTLKIVDRKKNIFk 546
Cdd:PRK09029 293 SPLPGREVKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF- 357
|
330 340
....*....|....*....|....*..
gi 58218988 547 LAQGEYIAPEKIENVYSRSRPVLQVFV 573
Cdd:PRK09029 358 FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
92-595 |
4.71e-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: 71.74 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 92 PCLgyRKPNQPYkwiSYKQVSDRAEYLGSCLLHKGYKSSQDQfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAI 171
Cdd:cd05958 2 TCL--RSPEREW---TYRDLLALANRIANVLVGELGIVPGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 172 IFVINRADIPVVICDTPQKATmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppk 251
Cdd:cd05958 76 AYILDKARITVALCAHALTAS----------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 pEDLSVICFTSGTTGDPKGAMLTHENVvsnMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERlvQGIL---FSCGGKIGF 328
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDP---LASADRYAVNVLRLREDDRFVGSPPLAFTFGL--GGVLlfpFGVGASGVL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 329 FQGDIrllPDDMKAL----KPTVFPTVPRLLNrvydkvqneaktplkkfllnlAIISKFNEvkngiirrdslwdklvfsk 404
Cdd:cd05958 171 LEEAT---PDLLLSAiaryKPTVLFTAPTAYR---------------------AMLAHPDA------------------- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 405 iQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDvADMNY 484
Cdd:cd05958 208 -AGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 485 FSVNNEGEICIKGNNvfkGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSR 564
Cdd:cd05958 286 VPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQ 361
|
490 500 510
....*....|....*....|....*....|....
gi 58218988 565 SRPVLQVFVHGESLRSFLIGV---VVPDPDSLPS 595
Cdd:cd05958 362 HPAVAECAVVGHPDESRGVVVkafVVLRPGVIPG 395
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
252-598 |
5.88e-13 |
|
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: 71.52 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYLPLAhmFERLVQGIL--FSCGGkigff 329
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA----FDVGPGSRVLQFASPS--FDASVWELLmaLLAGA----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 330 qgdiRLlpddmkalkptVFPTVPRLLnrvydkvqneAKTPLKKFLLNLAIiskfNEVkngiirrdSLWDKLVFSKIQGSL 409
Cdd:cd17652 161 ----TL-----------VLAPAEELL----------PGEPLADLLREHRI----THV--------TLPPAALAALPPDDL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 410 GGKVRLMITGAAPisTPVLTFfRAAMGCWVFEAYGQTECTGGCSITSP-GDWTAGHVGTPVACNFVKLEDvADMNYFSVN 488
Cdd:cd17652 204 PDLRTLVVAGEAC--PAELVD-RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 489 NEGEICIKGNNVFKGYLKDPEKTQE--VLDKDGWL-----HTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENV 561
Cdd:cd17652 280 VPGELYIAGAGLARGYLNRPGLTAErfVADPFGAPgsrmyRTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAA 358
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 58218988 562 YSRSRPVLQ--VFVHGESL-RSFLIGVVVPDPDSLPSFAA 598
Cdd:cd17652 359 LTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAE 398
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
441-575 |
1.31e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 70.69 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 441 EAYGQTECTGGCSITSPGDWTA--GHVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLdKD 518
Cdd:PRK06145 295 DAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YG 372
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 58218988 519 GWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVHG 575
Cdd:PRK06145 373 DWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
257-590 |
1.45e-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: 69.25 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 257 VICFTSGTTGDPKGAMLTHENVVSnMAAFLKFLEPIfqpTSDDVTISYLPLAHMFERLVQGILFSCGGKigffqgdirll 336
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLA-QALVLAVLQAI---DEGTVFLNSGPLFHIGTLMFTLATFHAGGT----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 337 pddmkalkpTVFptVPRL-LNRVYDKVQNEAKTplKKFLLnLAIISKFNEVkNGIIRRD--SLWDklvfskiqgslggkV 413
Cdd:cd17636 69 ---------NVF--VRRVdAEEVLELIEAERCT--HAFLL-PPTIDQIVEL-NADGLYDlsSLRS--------------S 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 414 RLMITGAAPISTPVLTFFRAAMGcwvfeaYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDvADMNYFSVNNEGEI 493
Cdd:cd17636 120 PAAPEWNDMATVDTSPWGRKPGG------YGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPDGEVGEI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 494 CIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYsRSRP-VLQVF 572
Cdd:cd17636 193 VARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCL-RQHPaVADAA 269
|
330
....*....|....*...
gi 58218988 573 VhgeslrsflIGvvVPDP 590
Cdd:cd17636 270 V---------IG--VPDP 276
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
252-594 |
2.06e-12 |
|
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: 69.74 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLepiFQPTSDDVTISYLPlAHMFERLVQGILFSCGGkigffqG 331
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERY---FGRDNGDEAVLFFS-NYVFDFFVEQMTLALLN------G 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 DIRLLPDDMKALKPtvfPTVPRLLNRvyDKVQNEAKTPlkkfllnlAIISKFNevkngIIRRDSLwdklvfskiqgslgg 411
Cdd:cd17648 163 QKLVVPPDEMRFDP---DRFYAYINR--EKVTYLSGTP--------SVLQQYD-----LARLPHL--------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 412 kvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTggcsITS------PGDWTAGHVGTPVACNFVKLEDvADMNYF 485
Cdd:cd17648 210 --KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETT----VTNhkrffpGDQRFDKSLGRPVRNTKCYVLN-DAMKRV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 486 SVNNEGEICIKGNNVFKGYLKDPEKTQEVL-------DKDGWL-------HTGDIGRWLPNGTLKIVDRKKNIFKLaQGE 551
Cdd:cd17648 283 PVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqtEQERARgrnarlyKTGDLVRWLPSGELEYLGRNDFQVKI-RGQ 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 58218988 552 YIAPEKIENVYSRSRPVLQVFV--------HGESLRSFLIGVVVPDPDSLP 594
Cdd:cd17648 362 RIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
247-588 |
2.62e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 69.93 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 247 PVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAfLKFLEPIfqpTSDDVTISYLPLahmFerlvqgILFS--CGG 324
Cdd:PRK09274 168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA-LREDYGI---EPGEIDLPTFPL---F------ALFGpaLGM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 325 KigffqgdiRLLPDdMKALKP-TVFPtvprllNRVYDKVQNEAKTPLkkFLlNLAIISKfnevkngiIRRDSLWDKLVFS 403
Cdd:PRK09274 235 T--------SVIPD-MDPTRPaTVDP------AKLFAAIERYGVTNL--FG-SPALLER--------LGRYGEANGIKLP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 404 KiqgslggkVRLMITGAAPISTPVLTFFRAAM--GCWVFEAYGQTECTGGCSITS------PGDWT---AGH-VGTPVAC 471
Cdd:PRK09274 289 S--------LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSIESreilfaTRAATdngAGIcVGRPVDG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 472 NFVKLEDVAD--MNYFS------VNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG--WLHTGDIGRWLPNGTLKIVD 539
Cdd:PRK09274 361 VEVRIIAISDapIPEWDdalrlaTGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCG 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 58218988 540 RKKNIFKLAQGEY--IAPEKIENVYSrsrpvlQVFvhgeslRSFLIGVVVP 588
Cdd:PRK09274 441 RKAHRVETAGGTLytIPCERIFNTHP------GVK------RSALVGVGVP 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
107-561 |
5.30e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 68.62 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLHKGYKSSqDQfVGIFAQNRPEwvisELACYTYSMVAVPLYDTLG----TEAIIFVINRADIPV 182
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLG-DR-VATIAWNTWR----HLEAWYGIMGIGAICHTVNprlfPEQIAWIINHAEDRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 183 VICDTpqkatMLVENVEK--GLTPGLKTIILMDpfDDDLMKR----GEKCGVEMLSLHDAENIGKEnFkkpvppkPEDLS 256
Cdd:PRK06018 115 VITDL-----TFVPILEKiaDKLPSVERYVVLT--DAAHMPQttlkNAVAYEEWIAEADGDFAWKT-F-------DENTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 257 V-ICFTSGTTGDPKGAMLTHE-NVVSNMAAflkfLEPIFQPTSDDVTIsyLPLAHMFERLVQGILFSC---GGKI----- 326
Cdd:PRK06018 180 AgMCYTSGTTGDPKGVLYSHRsNVLHALMA----NNGDALGTSAADTM--LPVVPLFHANSWGIAFSApsmGTKLvmpga 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 327 ---GffqGDIRLLPDDMKALKPTVFPTVPRLLnrvydkVQNEAKTPLKKFLLNLAIIskfnevkngiirrdslwdklvfs 403
Cdd:PRK06018 254 kldG---ASVYELLDTEKVTFTAGVPTVWLML------LQYMEKEGLKLPHLKMVVC----------------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 404 kiqgslGGkvrlmitGAAPIStpVLTFFRAaMGCWVFEAYGQTEctggcsiTSPgdwtAGHVGTpVACNFVKLEDVADMN 483
Cdd:PRK06018 302 ------GG-------SAMPRS--MIKAFED-MGVEVRHAWGMTE-------MSP----LGTLAA-LKPPFSKLPGDARLD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 484 Y--------FSV--------NNE--------GEICIKGNNVFKGYLKdpeKTQEVLDKDGWLHTGDIGRWLPNGTLKIVD 539
Cdd:PRK06018 354 VlqkqgyppFGVemkitddaGKElpwdgktfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITD 430
|
490 500
....*....|....*....|..
gi 58218988 540 RKKNIFKlAQGEYIAPEKIENV 561
Cdd:PRK06018 431 RSKDVIK-SGGEWISSIDLENL 451
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
260-591 |
1.18e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 67.41 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 260 FTSGTTGDPKG--AMLTHENVVSNMAAFlKFLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFFQgdiRLLP 337
Cdd:PRK13391 161 YSSGTTGRPKGikRPLPEQPPDTPLPLT-AFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME---HFDA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 338 DDMKAL----KPTVFPTVPRLLNRVYdkvqneaKTPlkkfllnlaiiskfNEVKNgiiRRD--SLwdklvfskiqgslgg 411
Cdd:PRK13391 237 EQYLALieeyGVTHTQLVPTMFSRML-------KLP--------------EEVRD---KYDlsSL--------------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 412 kvRLMITGAAPisTPVLTffRAAMGCW----VFEAYGQTECTGGCSITSPgDWTA--GHVGTPVACNFVKLEDvaDMNYF 485
Cdd:PRK13391 278 --EVAIHAAAP--CPPQV--KEQMIDWwgpiIHEYYAATEGLGFTACDSE-EWLAhpGTVGRAMFGDLHILDD--DGAEL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 486 SVNNEGEICIKGNNVFKgYLKDPEKTQEVLDKDG-WLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSR 564
Cdd:PRK13391 349 PPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLIT 426
|
330 340
....*....|....*....|....*..
gi 58218988 565 SRPVLQVFVHGeslrsfligvvVPDPD 591
Cdd:PRK13391 427 HPKVADAAVFG-----------VPNED 442
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
252-600 |
2.01e-11 |
|
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: 66.62 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHenvvSNMAAFLKFLEPIFQPTSDDVTISYLPL----AHmfERLVQGILfsCGGKIg 327
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSH----GPLAAHCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACV- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 328 ffqgdirLLPDDMKALKPtvfptvprllNRVYDKVQNEAKTPLKkflLNLAIISKFNEVkngiIRRDSlwdklvfSKIQG 407
Cdd:cd17649 164 -------VLRPDELWASA----------DELAEMVRELGVTVLD---LPPAYLQQLAEE----ADRTG-------DGRPP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 408 SLggkvRLMITGAAPISTPVLTffRAAM-GCWVFEAYGQTECTggcsITS------PGDWTAGH---VGTPVACNFVKLE 477
Cdd:cd17649 213 SL----RLYIFGGEALSPELLR--RWLKaPVRLFNAYGPTEAT----VTPlvwkceAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 478 DvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG-----WLHTGDIGRWLPNGTLKIVDRKKNIFKLaQG 550
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 58218988 551 EYIAPEKIENVYSRSRPVLQVFVHGES--LRSFLIGVVVP-DPDSLPSFAAKI 600
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLrAAAAQPELRAQL 413
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
106-561 |
2.39e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 66.69 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRAdipvvic 185
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDR--VAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRG------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 dtpqKATMLV--------------ENVEKGLTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAEnigkENFKKPVPPK 251
Cdd:PRK06164 107 ----RARWLVvwpgfkgidfaailAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPA----PPAAAGERAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFT-SGTTGDPKGAMLTHENVVSNMAAFLKFL--EPifqptsDDVTISYLPlahmferlVQGIlFSCGGKIGF 328
Cdd:PRK06164 179 DPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYgyDP------GAVLLAALP--------FCGV-FGFSTLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 329 FQGDIRLLPDDmkalkptVFPTvPRLLNRVYD-KV-----QNEAKTPLkkfllnlaiiskfneVKNGIIRRDSLWDKLV- 401
Cdd:PRK06164 244 LAGGAPLVCEP-------VFDA-ARTARALRRhRVthtfgNDEMLRRI---------------LDTAGERADFPSARLFg 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 402 FSKIQGSLGGKVRLMITGAAPI-----STPVLtffrAAMGCWVFEAYGQTECTGGCSITSPGdwtaghvgtpvacNFVKL 476
Cdd:PRK06164 301 FASFAPALGELAALARARGVPLtglygSSEVQ----ALVALQPATDPVSVRIEGGGRPASPE-------------ARVRA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 477 EDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPE 556
Cdd:PRK06164 364 RDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPA 442
|
....*
gi 58218988 557 KIENV 561
Cdd:PRK06164 443 EIEHA 447
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
201-588 |
2.51e-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: 66.33 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 201 GLTPGLKTIiLMDPFDDD-------LMKRG-------EKCGVEMLS--LHDAEN---IGKenfkkpvpPKPEDLSVICFT 261
Cdd:cd05910 23 GIRRGMRAV-LMVPPGPDffaltfaLFKAGavpvlidPGMGRKNLKqcLQEAEPdafIGI--------PKADEPAAILFT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 262 SGTTGDPKGAMLTHenvvSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVqgilfscggkigffqGDIRLLPDdMK 341
Cdd:cd05910 94 SGSTGTPKGVVYRH----GTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPAL---------------GLTSVIPD-MD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 342 ALKPTvfPTVPRLLnrvydkVQneaktPLKKFLLNLAIISKfnevkngiirrdSLWDKLV-FSKIQGSLGGKVRLMITGA 420
Cdd:cd05910 154 PTRPA--RADPQKL------VG-----AIRQYGVSIVFGSP------------ALLERVArYCAQHGITLPSLRRVLSAG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 421 APISTPVLTFFRAAM--GCWVFEAYGQTECTGGCSI------TSPGDWTAGH----VGTPVACNFVKLEDVADMNYFSVN 488
Cdd:cd05910 209 APVPIALAARLRKMLsdEAEILTPYGATEALPVSSIgsrellATTTAATSGGagtcVGRPIPGVRVRIIEIDDEPIAEWD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 489 NE--------GEICIKGNNVFKGYLKDPEKTQ--EVLDKDG--WLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIape 556
Cdd:cd05910 289 DTlelprgeiGEITVTGPTVTPTYVNRPVATAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLY--- 365
|
410 420 430
....*....|....*....|....*....|...
gi 58218988 557 kienvysrSRPVLQVF-VHGESLRSFLIGVVVP 588
Cdd:cd05910 366 --------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
249-559 |
3.54e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 66.18 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 249 PPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAF----LKFLEPifqptsdDVTISYLPLAH-Mferlvqgilfscg 323
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIshdgLKVRPG-------DRCVSWLPFYHdM------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 324 GKIGFFqgdirllpddmkaLKPtvfptvprLLNRV---YDKVQNEAKTPLkkflLNLAIISKfNEvknGII--------- 391
Cdd:PRK09192 232 GLVGFL-------------LTP--------VATQLsvdYLPTRDFARRPL----QWLDLISR-NR---GTIsysppfgye 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 392 ---RRDSLWDKLVFSKIQGSLGGkvrlmiTGAAPISTPVLTFFRAAMGCWVFEA------YGQTECTGGCSITSPG---- 458
Cdd:PRK09192 283 lcaRRVNSKDLAELDLSCWRVAG------IGADMIRPDVLHQFAEAFAPAGFDDkafmpsYGLAEATLAVSFSPLGsgiv 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 459 ------------------DWTAGHVGTPVAC------NFVKLEDVADmnyfSVNNE---GEICIKGNNVFKGYLKDPEkT 511
Cdd:PRK09192 357 veevdrdrleyqgkavapGAETRRVRTFVNCgkalpgHEIEIRNEAG----MPLPErvvGHICVRGPSLMSGYFRDEE-S 431
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 58218988 512 QEVLDKDGWLHTGDIGrWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIE 559
Cdd:PRK09192 432 QDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
107-664 |
5.31e-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: 65.22 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGSCLLHKGYKSSQDQFVgiFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICd 186
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFV--LSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 187 TPQkatmlvenvekgltpglktiilmdpfdddLMKRGEkcgvemlslhdaenigkenfkkpvppkPEDLSVICFTSGTTG 266
Cdd:cd05969 79 TEE-----------------------------LYERTD---------------------------PEDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 267 DPKGAMLTHENVVSN--MAAFLKFLEP--IFQPTSDDVTISYLpLAHMFERLVQGI-LFSCGGKIgffqgDIRLLPDDMK 341
Cdd:cd05969 103 TPKGVLHVHDAMIFYyfTGKYVLDLHPddIYWCTADPGWVTGT-VYGIWAPWLNGVtNVVYEGRF-----DAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 342 ALKPTVFPTVP---RLLNRVYDKvqneaktPLKKFLLNlaiiskfnevkngiirrdslwdklvfskiqgslggKVRLMIT 418
Cdd:cd05969 177 RVKVTVWYTAPtaiRMLMKEGDE-------LARKYDLS-----------------------------------SLRFIHS 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 419 GAAPISTPVLTFFRAAMGCWVFEAYGQTEcTGGCSITS-PG-DWTAGHVGTPVACnfVKLEDV-ADMNYFSVNNEGEICI 495
Cdd:cd05969 215 VGEPLNPEAIRWGMEVFGVPIHDTWWQTE-TGSIMIANyPCmPIKPGSMGKPLPG--VKAAVVdENGNELPPGTKGILAL 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 496 KGN--NVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRPVLQVFV 573
Cdd:cd05969 292 KPGwpSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGV 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 574 HGeslrsfligvvVPDPDSLPSFAAKIGVKGSFE--ELCKNqcvkEAILEDLQKIGKEGGLKSFEQVKSIfvhpePFTIE 651
Cdd:cd05969 370 IG-----------KPDPLRGEIIKAFISLKEGFEpsDELKE----EIINFVRQKLGAHVAPREIEFVDNL-----PKTRS 429
|
570
....*....|...
gi 58218988 652 NGLLTPTLKAKRV 664
Cdd:cd05969 430 GKIMRRVLKAKEL 442
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
106-559 |
5.66e-11 |
|
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: 65.19 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKssQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVK--KDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTpQKATMLVENvekgltpglKTIILMDpfdDDLMKRGekcgvemlslhDAENIGKENfkkpvppKPEDLSVICFTSGTT 265
Cdd:cd17656 92 QR-HLKSKLSFN---------KSTILLE---DPSISQE-----------DTSNIDYIN-------NSDDLLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHEnvvsNMAAFLKF-LEPIFQPTSDDVtisyLPLAHM-FERLVQGIlFS--CGGkigffqGDIRLLPDDMK 341
Cdd:cd17656 141 GKPKGVQLEHK----NMVNLLHFeREKTNINFSDKV----LQFATCsFDVCYQEI-FStlLSG------GTLYIIREETK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 342 AlkptvfpTVPRLLNRVydkvqneAKTPLKKFLLNLAIIskfnevkngiirrdslwdKLVFSKIQ--GSLGGKVRLMITG 419
Cdd:cd17656 206 R-------DVEQLFDLV-------KRHNIEVVFLPVAFL------------------KFIFSEREfiNRFPTCVKHIITA 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 420 AAP--ISTPVLTFFRAAmGCWVFEAYG--QTECTGGCSITSPGDWTA-GHVGTPVACNFVKLEDvADMNYFSVNNEGEIC 494
Cdd:cd17656 254 GEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQPQGIVGELY 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58218988 495 IKGNNVFKGYLKDPEKTQEVLDKDGW------LHTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIE 559
Cdd:cd17656 332 ISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
105-573 |
9.04e-11 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 64.78 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 105 WISYKQVSDRAEYLGSCLLHKGYKSSqDQfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAI--IFVINRADIPV 182
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRG-DR-VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLehILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 183 VicdtpqKATML--VENVEKGLTPgLKTIILMDPFDDDLMKRGEKCgVEMLSLHDAENigkenfkkPVPPKPEDLSVICF 260
Cdd:PRK06155 124 V------EAALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAGWST-APLPPLDAPAP--------AAAVQPGDTAAILY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 261 TSGTTGDPKGAMLTHENVV---SNMAAFLKFlepifqpTSDDVTISYLPLAH-----MF-------ERLVQGILFSCGGk 325
Cdd:PRK06155 188 TSGTTGPSKGVCCPHAQFYwwgRNSAEDLEI-------GADDVLYTTLPLFHtnalnAFfqallagATYVLEPRFSASG- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 326 igFFqgdirllpDDMKALKPTVFptvprllnrvydkvqneaktplkkFLLNlAIISkfnevkngiirrdslwdkLVFSKI 405
Cdd:PRK06155 260 --FW--------PAVRRHGATVT------------------------YLLG-AMVS------------------ILLSQP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 406 QG--SLGGKVRLMITGAAPIStpVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDwTAGHVGTpVACNFVKleDVADMN 483
Cdd:PRK06155 287 AResDRAHRVRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGR-LAPGFEA--RVVDEH 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 484 YFSV--NNEGEICIKGNNVF---KGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKlAQGEYIAPEKI 558
Cdd:PRK06155 361 DQELpdGEPGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEV 438
|
490
....*....|....*
gi 58218988 559 ENVYSRSRPVLQVFV 573
Cdd:PRK06155 439 EQVLLSHPAVAAAAV 453
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
414-561 |
9.75e-11 |
|
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: 64.78 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 414 RLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctGGCSITSPGD---WTAGHVGTPVaCNF--VKL-----EDVADmn 483
Cdd:COG1021 303 RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--GLVNYTRLDDpeeVILTTQGRPI-SPDdeVRIvdedgNPVPP-- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 484 yfsvNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNifklaQ----GEYIAPEKIE 559
Cdd:COG1021 378 ----GEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-----QinrgGEKIAAEEVE 448
|
..
gi 58218988 560 NV 561
Cdd:COG1021 449 NL 450
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
413-591 |
1.10e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 64.54 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 413 VRLMITGAAPISTPVltffRAAMGCW----VFEAYGQTEcTGGCSITSPGDWTA--GHVGTPVACNFVKLEDvaDMNYFS 486
Cdd:PRK08276 264 LRVAIHAAAPCPVEV----KRAMIDWwgpiIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGEVRILDE--DGNELP 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 487 VNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGrWL-PNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRS 565
Cdd:PRK08276 337 PGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTH 414
|
170 180
....*....|....*....|....*.
gi 58218988 566 RPVLQVFVHGeslrsfligvvVPDPD 591
Cdd:PRK08276 415 PKVADVAVFG-----------VPDEE 429
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
106-278 |
1.42e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 64.14 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSsQDQfVGIFAQNRPEWVISELACYTYSMVAVP------------LYDTLGTEAIIF 173
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP-GDH-VGIYARNRIEYVEAMLGAFKARAVPVNvnyryvedelryLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 174 viNRADIPVVicdtpqkATMLVEnvekglTPGLKTIILMDpfdDDLMKRGEKCGVEmlsLHDAENIGKENfKKPVPPKPE 253
Cdd:PRK07798 107 --EREFAPRV-------AEVLPR------LPKLRTLVVVE---DGSGNDLLPGAVD---YEDALAAGSPE-RDFGERSPD 164
|
170 180
....*....|....*....|....*
gi 58218988 254 DLSVICfTSGTTGDPKGAMLTHENV 278
Cdd:PRK07798 165 DLYLLY-TGGTTGMPKGVMWRQEDI 188
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-547 |
1.57e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.98 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYksSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGV--GPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQKATMLVenvekgltPGlktiilmdpfdddlmkrgekcGVEMLSLHDAENIGKENFKKPVPP-KPEDLSVICFTSGT 264
Cdd:PRK12316 2107 QRHLLERLPL--------PA---------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 265 TGDPKGAMLTHenvvSNMAAFLKFLEPIFQPTSDDVTISYLPLAhmFERLVQGILFS-CGGKIGFFQGDIRLLP----DD 339
Cdd:PRK12316 2158 TGLPKGVAVSH----GALVAHCQAAGERYELSPADCELQFMSFS--FDGAHEQWFHPlLNGARVLIRDDELWDPeqlyDE 2231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 340 MKALKPTVFPTVPRLLNRVYDKVQNEAKTPlkkfllnlaiiskfnevkngiirrdslwdklvfskiqgslggKVRLMITG 419
Cdd:PRK12316 2232 MERHGVTILDFPPVYLQQLAEHAERDGRPP------------------------------------------AVRVYCFG 2269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 420 AAPISTPVLTFFRAAMGC-WVFEAYGQTEctggcSITSPGDWTAGH----------VGTPVACNFVKLEDvADMNYFSVN 488
Cdd:PRK12316 2270 GEAVPAASLRLAWEALRPvYLFNGYGPTE-----AVVTPLLWKCRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPG 2343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58218988 489 NEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLH-------TGDIGRWLPNGTLKIVDRKKNIFKL 547
Cdd:PRK12316 2344 MAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI 2409
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
235-561 |
2.12e-10 |
|
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: 63.60 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 235 DAENIGKENFKkPVPPKPE-DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSddVTISYLPLAHMFER 313
Cdd:cd05915 135 LAYEEALGEEA-DPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFHVNAW 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 314 LVQGILFSCGGKIGFfqgdIRLLPDDmkalkPTVFPTVprllnrVYDKVQNEAKTPlkkfllnlaiiSKFNEVKNGiirR 393
Cdd:cd05915 212 CLPYAATLVGAKQVL----PGPRLDP-----ASLVELF------DGEGVTFTAGVP-----------TVWLALADY---L 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 394 DSlwdklvfskIQGSLGGKVRLMITGAAPistPVLTFFRAAMGCW-VFEAYGQTECTG-GCSI-------TSPGDWTAGH 464
Cdd:cd05915 263 ES---------TGHRLKTLRRLVVGGSAA---PRSLIARFERMGVeVRQGYGLTETSPvVVQNfvkshleSLSEEEKLTL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 465 VGTPVACNFVKLEDVADMNYFSVNNEGE----ICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDR 540
Cdd:cd05915 331 KAKTGLPIPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDR 410
|
330 340
....*....|....*....|.
gi 58218988 541 KKNIFKLAqGEYIAPEKIENV 561
Cdd:cd05915 411 LKDLIKSG-GEWISSVDLENA 430
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
254-560 |
3.12e-10 |
|
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: 63.12 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLAHMFERLVQGIL--FSCGGKIgffqg 331
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAE----VCGLDQDTVYLAVLPAAHNFPLACPGVLgtLLAGGRV----- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 dirLLPDDMKALKptVFPTVPRllnrvyDKVQNEAKTPlkkfllnlAIISKFneVKNGIIRRDSLwdklvfskiqGSLgg 411
Cdd:cd05920 211 ---VLAPDPSPDA--AFPLIER------EGVTVTALVP--------ALVSLW--LDAAASRRADL----------SSL-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 412 kvRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEctGGCSIT---SPGDWTAGHVGTPVAC-NFVKLEDvADMNYFSV 487
Cdd:cd05920 258 --RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYTrldDPDEVIIHTQGRPMSPdDEIRVVD-EEGNPVPP 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58218988 488 NNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIEN 560
Cdd:cd05920 333 GEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN 404
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
106-592 |
3.28e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 63.02 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSsqDQFVGIFAQNRPEWVISELACyTYSMVAVPLYDT-LGTEAIIFVINRADIPVVI 184
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNHRGFVLALYAA-GKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 185 CDtpQKATMLVENVEKGLtPGLKTIIlMDPFDDDLMKRGEKCGVEMLSLHDAENIgkenfkkPVPPKPEdlSVICFTSGT 264
Cdd:PRK07788 152 YD--DEFTDLLSALPPDL-GRLRAWG-GNPDDDEPSGSTDETLDDLIAGSSTAPL-------PKPPKPG--GIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 265 TGDPKGAMLTHENVVSNMAAFLKFLePiFQptSDDVTISYLPLAHMFERLVQGILFSCGGKIGF---FqgDIRLLPDDMK 341
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLLSRV-P-FR--AGETTLLPAPMFHATGWAHLTLAMALGSTVVLrrrF--DPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 342 ALKPTVFPTVPRLLNRVYDKVQNeaktPLKKFLLNlaiiskfnevkngiirrdSLwdKLVFSkiQGSlggkvrlmitgaa 421
Cdd:PRK07788 293 KHKATALVVVPVMLSRILDLGPE----VLAKYDTS------------------SL--KIIFV--SGS------------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 422 PISTPVLTFFRAAMGCWVFEAYGQTECTGgCSITSPGDWTA--GHVGTPVACNFVKLEDvADMNYFSVNNEGEICIKGNN 499
Cdd:PRK07788 334 ALSPELATRALEAFGPVLYNLYGSTEVAF-ATIATPEDLAEapGTVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 500 VFKGYLKDPEKtQEVldkDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFV------ 573
Cdd:PRK07788 412 PFEGYTDGRDK-QII---DGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVigvdde 486
|
490 500
....*....|....*....|
gi 58218988 574 -HGESLRSFligvVVPDPDS 592
Cdd:PRK07788 487 eFGQRLRAF----VVKAPGA 502
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
252-560 |
3.70e-10 |
|
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: 62.57 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 252 PEDLSVICFTSGTTGDPKGAMLTHENVVSnmaaFLKFLEPIFQPTSDDVTISYlplahmferlvqgilfscgGKIGFFQG 331
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVN----LCEWHRPYFGVTPADKSLVY-------------------ASFSFDAS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 332 DIRLLPDDMKALKPTVFPTVPRL-LNRVYDKVQNEAKTPLkkfLLNLAIISKFNEVKNgiirrDSLwdklvfskiqgslg 410
Cdd:cd17645 160 AWEIFPHLTAGAALHVVPSERRLdLDALNDYFNQEGITIS---FLPTGAAEQFMQLDN-----QSL-------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 411 gkvRLMITGAAPISTPVLTFFRaamgcwVFEAYGQTECTggCSITS-PGDWTAGH--VGTPVACNFVKLEDvADMNYFSV 487
Cdd:cd17645 218 ---RVLLTGGDKLKKIERKGYK------LVNNYGPTENT--VVATSfEIDKPYANipIGKPIDNTRVYILD-EALQLQPI 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58218988 488 NNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIEN 560
Cdd:cd17645 286 GVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEP 363
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
256-611 |
5.88e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 256 SVICFTSGTTGDPKGAM--LTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFFQG-D 332
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRfD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 333 IRLLPDDMKALKPTVFPTVPRLLNRVYdKVQNEAKTplkkfllnlaiiskfnevkngiiRRDSlwdklvfskiqgslgGK 412
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLL-KLDADVRT-----------------------RYDV---------------SS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 413 VRLMITGAAPISTPVltffRAAMGCW----VFEAYGQTECTGGCSITSPgDWTA--GHVGTPVACNFVKLEDvaDMNYFS 486
Cdd:PRK13390 272 LRAVIHAAAPCPVDV----KHAMIDWlgpiVYEYYSSTEAHGMTFIDSP-DWLAhpGSVGRSVLGDLHICDD--DGNELP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 487 VNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDG--WLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSR 564
Cdd:PRK13390 345 AGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTM 423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 58218988 565 SRPVLQVFVHGeslrsfligvvVPDPDSLPSFAAKI----GVKGSfEELCK 611
Cdd:PRK13390 424 HPAVHDVAVIG-----------VPDPEMGEQVKAVIqlveGIRGS-DELAR 462
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
169-561 |
3.71e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 59.72 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 169 EAIIFVINRADIPVVICDT---PqkatmLVENVEkGLTPGLKTIILMDpfDDDLMKRGEkcgVEMLSLHDAenIGKENFK 245
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDLtflP-----LVDALA-PQCPNVKGWVAMT--DAAHLPAGS---TPLLCYETL--VGAQDGD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 246 KPVPPKPEDL-SVICFTSGTTGDPKGAMLTHENVVsnMAAFLKFLEPIFQPTSDDVTisyLPLAHMFERLVQGILFSC-- 322
Cdd:PRK07008 168 YDWPRFDENQaSSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFHVNAWGLPYSApl 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 323 -GGKIgffqgdirllpddmkalkptVFPTvPRLLNR-VYDKVQNE-----AKTPLKKFLLnlaiiskFNEVKNGiirrds 395
Cdd:PRK07008 243 tGAKL--------------------VLPG-PDLDGKsLYELIEAErvtfsAGVPTVWLGL-------LNHMREA------ 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 396 lwdKLVFSKIQgslggkvRLMITGAA-PIStpVLTFFRAAMGCWVFEAYGQTEctggcsiTSP----GDWTAGHVGTPVA 470
Cdd:PRK07008 289 ---GLRFSTLR-------RTVIGGSAcPPA--MIRTFEDEYGVEVIHAWGMTE-------MSPlgtlCKLKWKHSQLPLD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 471 CNFVKLEDVA------DMNYfsVNNEG-----------EICIKGNNVFKGYLKdpeKTQEVLDkDGWLHTGDIGRWLPNG 533
Cdd:PRK07008 350 EQRKLLEKQGrviygvDMKI--VGDDGrelpwdgkafgDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADG 423
|
410 420
....*....|....*....|....*...
gi 58218988 534 TLKIVDRKKNIFKlAQGEYIAPEKIENV 561
Cdd:PRK07008 424 FMQITDRSKDVIK-SGGEWISSIDIENV 450
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
248-560 |
3.98e-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: 59.40 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 248 VPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAA---FLKFLEP--IFQPTSDDVTISYLpLAHMFERLVQGilfSC 322
Cdd:cd05928 169 VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVngrYWLDLTAsdIMWNTSDTGWIKSA-WSSLFEPWIQG---AC 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 323 GGKIGFFQGDIRLLPDDMKALKPTVF---PTVPRLLnrvydkVQNEaktpLKKFllnlaiisKFNEVKNgiirrdslwdk 399
Cdd:cd05928 245 VFVHHLPRFDPLVILKTLSSYPITTFcgaPTVYRML------VQQD----LSSY--------KFPSLQH----------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 400 lvfskiqgslggkvrlMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDV 479
Cdd:cd05928 296 ----------------CVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 480 aDMNYFSVNNEGEICIKGNNV-----FKGYLKDPEKTQEVLDKDGWLhTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIA 554
Cdd:cd05928 360 -NGNVLPPGTEGDIGIRVKPIrpfglFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIG 436
|
....*.
gi 58218988 555 PEKIEN 560
Cdd:cd05928 437 PFEVES 442
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
106-279 |
4.40e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 59.52 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSSQDQFvgIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVF--IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 dTPQkatmLVENVEKGLTPGLKTIILMDPFDDDlmkrGEKCgvemLSLHDAENIGKENFKkPVPPKPEDLSVICFTSGTT 265
Cdd:PRK04319 152 -TPA----LLERKPADDLPSLKHVLLVGEDVEE----GPGT----LDFNALMEQASDEFD-IEWTDREDGAILHYTSGST 217
|
170
....*....|....
gi 58218988 266 GDPKGAMLTHENVV 279
Cdd:PRK04319 218 GKPKGVLHVHNAML 231
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
405-593 |
5.10e-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: 59.12 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 405 IQGSLGG---KVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSiTSPGD-WTAGHVGTPVACNFVKLEDVA 480
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 481 DmnyfSVNNEGEICIK-GNN----VFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKlAQGEYIAP 555
Cdd:cd05974 270 G----APATEGEVALDlGDTrpvgLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170 180 190
....*....|....*....|....*....|....*...
gi 58218988 556 EKIENVYSRSRPVLQvfvhgeslrsfliGVVVPDPDSL 593
Cdd:cd05974 344 FELESVLIEHPAVAE-------------AAVVPSPDPV 368
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
414-561 |
5.84e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 58.94 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 414 RLMITGAAPISTPVLtffRAAMGCW---VFEAYGQTEcTGGCSITSPGDWTA--GHVGTPVACNFVKLEDvADMNYFSVN 488
Cdd:PRK12406 274 RHVIHAAAPCPADVK---RAMIEWWgpvIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQG 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58218988 489 NEGEIC--IKGNNVFKgYLKDPEKTQEVlDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENV 561
Cdd:PRK12406 349 EIGEIYsrIAGNPDFT-YHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAV 420
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
100-573 |
1.48e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 57.48 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 100 NQPYKWISYKQVSDRAEYLGSCLLHKGYKSSQdqfvgifaqnrpewviselacytysmvAVPLYDTLGTEAIIFVINRAD 179
Cdd:cd17654 11 TTSDTTVSYADLAEKISNLSNFLRKKFQTEER---------------------------AIGLRCDRGTESPVAILAILF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 180 IPVVIcdTPQKATMLvenvekgltPGLKTIILMDPFDDDLMKRGEKCgVEMLSLHDAenigKENFKKPVPpkpEDLSVIC 259
Cdd:cd17654 64 LGAAY--APIDPASP---------EQRSLTVMKKCHVSYLLQNKELD-NAPLSFTPE----HRHFNIRTD---ECLAYVI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 260 FTSGTTGDPKGAMLTHENVVSNMAAFLKflepIFQPTSDDVTISYLPLahMFERLVQGIL--FSCGGKIGFFQGDIRLLP 337
Cdd:cd17654 125 HTSGTTGTPKIVAVPHKCILPNIQHFRS----LFNITSEDILFLTSPL--TFDPSVVEIFlsLSSGATLLIVPTSVKVLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 338 D-----DMKALKPTVFPTVPRLLNRVYDKVqneaktpLKKFLL----NLAIIskfnevkngiirrdslwdklvfskiqgS 408
Cdd:cd17654 199 SkladiLFKRHRITVLQATPTLFRRFGSQS-------IKSTVLsatsSLRVL---------------------------A 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 409 LGGKvrlmitgAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAG-HVGTPVacnFVKLEDVADMNYFSV 487
Cdd:cd17654 245 LGGE-------PFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPvQLGSPL---LGTVIEVRDQNGSEG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 488 nnEGEICIKGNNVfKGYLKDPEKTQEVLdkdgWLHTGDIGRwLPNGTLKIVDRKKNIFKLAqGEYIAPEKIENVYSRSRP 567
Cdd:cd17654 315 --TGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLIQQVIESCLG 385
|
....*.
gi 58218988 568 VLQVFV 573
Cdd:cd17654 386 VESCAV 391
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
258-581 |
4.71e-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: 55.49 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 258 ICFTSGTTGDPKGAMLTHENvvsnMAAFLKFLEPIFQPTSDDVTISYLPLAH-MFERLVQGILFSCGGKIGFFQGDIRLL 336
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS----WIESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 337 PDDMKALKPTVFPTVPrllnrvydkvqneakTPLKKFLLNLAIISKFNEVKNGiirrDSLWDKLVFSKIQGSLGGKVRLM 416
Cdd:cd17633 81 IRKINQYNATVIYLVP---------------TMLQALARTLEPESKIKSIFSS----GQKLFESTKKKLKNIFPKANLIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 417 ITGAAPIStpvltfFRAamgcwvFEAYGQTEctggcsitspgdwTAGHVGTPVACNFVKLEDVADmnyfsvNNEGEICIK 496
Cdd:cd17633 142 FYGTSELS------FIT------YNFNQESR-------------PPNSVGRPFPNVEIEIRNADG------GEIGKIFVK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 497 GNNVFKGYLKdpektQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVHGE 576
Cdd:cd17633 191 SEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
....*
gi 58218988 577 SLRSF 581
Cdd:cd17633 265 PDARF 269
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
106-592 |
5.05e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 55.92 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGykSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK13382 69 LTWRELDERSDALAAALQALP--IGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DtpQKATMLVENVEKGlTPGLKTIILMDPFDDDLMkrgekcgVEMLSlhdAENIGKEnfkkpVPPKPEDLSVICFTSGTT 265
Cdd:PRK13382 147 D--EEFSATVDRALAD-CPQATRIVAWTDEDHDLT-------VEVLI---AAHAGQR-----PEPTGRKGRVILLTSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFL-----KFLEPIFqptsddvtISyLPLAHM--FERLVQGILFSCggkigffqgDI----R 334
Cdd:PRK13382 209 GTPKGARRSGPGGIGTLKAILdrtpwRAEEPTV--------IV-APMFHAwgFSQLVLAASLAC---------TIvtrrR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 335 LLPDDMKAL----KPTVFPTVPRLLNRVYDKVQneaktplkkfllnlaiiskfnEVKNgiirRDSlwdklvfskiqgslG 410
Cdd:PRK13382 271 FDPEATLDLidrhRATGLAVVPVMFDRIMDLPA---------------------EVRN----RYS--------------G 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 411 GKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTEcTGGCSITSPGDWTAG--HVGTPVACNFVKLEDvADMNYFSVN 488
Cdd:PRK13382 312 RSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE-AGMIATATPADLRAApdTAGRPAEGTEIRILD-QDFREVPTG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 489 NEGEICIKGNNVFKGYlkDPEKTQEVldKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPV 568
Cdd:PRK13382 390 EVGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPDV 464
|
490 500
....*....|....*....|....*..
gi 58218988 569 LQVFVHG---ESLRSFLIGVVVPDPDS 592
Cdd:PRK13382 465 AEAAVIGvddEQYGQRLAAFVVLKPGA 491
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
227-535 |
1.05e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 54.90 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 227 GVEMLSLHDAENIgKENFKKPVPP------KPEDLSVICFTSGTTGDPKGAMLTHENVVSnmaaFLKFLEPIFQ------ 294
Cdd:PRK04813 112 EILGIPVITLDEL-KDIFATGNPYdfdhavKGDDNYYIIFTSGTTGKPKGVQISHDNLVS----FTNWMLEDFAlpegpq 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 295 -----PTSDDVTISYLPLAhmferLVQGilfscggkigffqGDIRLLPDDMKALKPTVFPTVPRLlnrvydKVQNEAKTP 369
Cdd:PRK04813 187 flnqaPYSFDLSVMDLYPT-----LASG-------------GTLVALPKDMTANFKQLFETLPQL------PINVWVSTP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 370 lkKF----LLNlaiiSKFNEVKNgiirrDSLwdklvfskiqgslggkVRLMITGAA-PISTP--VLTFFRAAMgcwVFEA 442
Cdd:PRK04813 243 --SFadmcLLD----PSFNEEHL-----PNL----------------THFLFCGEElPHKTAkkLLERFPSAT---IYNT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 443 YGQTECTGGCS---ITSpgDWTAGHVGTPVAcnFVK-----LEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEV 514
Cdd:PRK04813 293 YGPTEATVAVTsieITD--EMLDQYKRLPIG--YAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEA 368
|
330 340
....*....|....*....|....
gi 58218988 515 L-DKDGW--LHTGDIGRwLPNGTL 535
Cdd:PRK04813 369 FfTFDGQpaYHTGDAGY-LEDGLL 391
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
247-310 |
2.91e-07 |
|
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: 53.45 E-value: 2.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58218988 247 PVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSnMAAFLkflePIFQPTSDDVTISYLPLAHM 310
Cdd:cd05938 138 RAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFL----SLCGVTADDVIYITLPLYHS 196
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
83-275 |
3.08e-07 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 53.65 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 83 RGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKSSqDQfVGIFAQNRPEWVISELACYTYSMVAVPL 162
Cdd:cd05968 69 KWLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKG-DR-VGIYLPMIPEIVPAFLAVARIGGIVVPI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 163 YDTLGTEAI-----------IFVIN---RADIPVVICDTPQKATMLVENVEKGLTP-GLKTIILMDPFDDdlmkrgekcg 227
Cdd:cd05968 147 FSGFGKEAAatrlqdaeakaLITADgftRRGREVNLKEEADKACAQCPTVEKVVVVrHLGNDFTPAKGRD---------- 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 58218988 228 vemLSLHDaenigkenFKKPVPPK-----PEDLSVICFTSGTTGDPKGAMLTH 275
Cdd:cd05968 217 ---LSYDE--------EKETAGDGaerteSEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-611 |
3.34e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.19 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYksSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGV--GPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT 4654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQKATMLVENvekgltpGLKTIILmDPfDDDLMKRGEkcgvemlslHDAEnigkenfkkpVPPKPEDLSVICFTSGTT 265
Cdd:PRK12316 4655 QSHLLQRLPIPD-------GLASLAL-DR-DEDWEGFPA---------HDPA----------VRLHPDNLAYVIYTSGST 4706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVSNMAAFLKFlepiFQPTSDDVTISYLPLAhmFERLVQGIL--FSCGGKIgffqgdirLLPDDMKAL 343
Cdd:PRK12316 4707 GRPKGVAVSHGSLVNHLHATGER----YELTPDDRVLQFMSFS--FDGSHEGLYhpLINGASV--------VIRDDSLWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 344 KPTVFPTVPRllnrvyDKVQNEAKTPlkkfllnlaiiSKFNEVKNGIIRRDSLwdklvfskiqgslgGKVRLMITGAAPI 423
Cdd:PRK12316 4773 PERLYAEIHE------HRVTVLVFPP-----------VYLQQLAEHAERDGEP--------------PSLRVYCFGGEAV 4821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 424 STPVLT-FFRAAMGCWVFEAYGQTECTGGCSI-TSPGDWTAG----HVGTPVACNFVKLEDVAdMNYFSVNNEGEICIKG 497
Cdd:PRK12316 4822 AQASYDlAWRALKPVYLFNGYGPTETTVTVLLwKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGG 4900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 498 NNVFKGYLKDPEKTQE-----VLDKDG--WLHTGDIGRWLPNGTLKIVDR-----KKNIFKLAQGEYIAPEKIENVYSRS 565
Cdd:PRK12316 4901 EGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRvdhqvKIRGFRIELGEIEARLREHPAVREA 4980
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 58218988 566 RPVLQVFVHGESlrsfLIGVVVP-DPDSLPSFAAKIGVKGSFEELCK 611
Cdd:PRK12316 4981 VVIAQEGAVGKQ----LVGYVVPqDPALADADEAQAELRDELKAALR 5023
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
106-601 |
3.77e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.01 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSsqDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVIC 185
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 186 DTPQKATMLVENvekgltpGLKTIILmDPFDDdlmkrgekcgveMLSLHDAENIGkenfkkpVPPKPEDLSVICFTSGTT 265
Cdd:PRK12467 1678 QSHLQARLPLPD-------GLRSLVL-DQEDD------------WLEGYSDSNPA-------VNLAPQNLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 266 GDPKGAMLTHENVVsnmaAFLKFLEPIFQPTSDDVTISYLPLAhmFERLVQGILFSC--GGKIGFFQGDIRLLPDDMKAL 343
Cdd:PRK12467 1731 GRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFWPLinGARLVIAPPGAHRDPEQLIQL 1804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 344 ----KPTVFPTVPRLLNRVYDKVQNEAKtPLKkfllnlaiiskfnevkngiIRRdslwdkLVFskiqgslGGKvrlmitg 419
Cdd:PRK12467 1805 ierqQVTTLHFVPSMLQQLLQMDEQVEH-PLS-------------------LRR------VVC-------GGE------- 1844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 420 AAPISTPVLTFfrAAMG-CWVFEAYGQTECT-----GGCSITSPGDWTAGHVGTPVACNFVKLEDvADMNYFSVNNEGEI 493
Cdd:PRK12467 1845 ALEVEALRPWL--ERLPdTGLFNLYGPTETAvdvthWTCRRKDLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGEL 1921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 494 CIKGNNVFKGYLKDPEKTQE--VLDKDGWL-----HTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIEnVYSRSR 566
Cdd:PRK12467 1922 YLGGVGLARGYLNRPALTAErfVADPFGTVgsrlyRTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIE-ARLREQ 1999
|
490 500 510
....*....|....*....|....*....|....*...
gi 58218988 567 PVLQ---VFVHGESLRSFLIGVVVPDPDSLPSFAAKIG 601
Cdd:PRK12467 2000 GGVReavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
229-570 |
3.96e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 229 EMLSLHDAENIGKENFKKPVPPkPEDLSVICFTSGTTGDPKGAMLTHENVVSN----MAAFLKFLEPifqptsDDVTISY 304
Cdd:PRK05691 143 ELLCVDTLDPALAEAWQEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVANeqliRHGFGIDLNP------DDVIVSW 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 305 LPLAH---MFERLVQGI-------LFSCG----------GKIGFFQGDIRLLPDdmkalkptvFPTvpRLLN-RVydkvq 363
Cdd:PRK05691 216 LPLYHdmgLIGGLLQPIfsgvpcvLMSPAyflerplrwlEAISEYGGTISGGPD---------FAY--RLCSeRV----- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 364 neAKTPLKKflLNLaiiSKFNEVKNGI--IRRDSL---WDKLV---F--SKIQGSLG-GKVRLMITGAAP-ISTPVLTFF 431
Cdd:PRK05691 280 --SESALER--LDL---SRWRVAYSGSepIRQDSLerfAEKFAacgFdpDSFFASYGlAEATLFVSGGRRgQGIPALELD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 432 RAAMGCWVFEAyGQTECTGGCSITSPGDwtAGHVGTPvacnfVKLEDVADmnyfsvNNEGEICIKGNNVFKGYLKDPEKT 511
Cdd:PRK05691 353 AEALARNRAEP-GTGSVLMSCGRSQPGH--AVLIVDP-----QSLEVLGD------NRVGEIWASGPSIAHGYWRNPEAS 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58218988 512 QEV-LDKDG--WLHTGDIGrWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQ 570
Cdd:PRK05691 419 AKTfVEHDGrtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
449-560 |
7.12e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 52.30 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 449 TGGCSItSPGD--WTAGHVGTPVAcnfvkledvadmnyfsVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDI 526
Cdd:PRK10946 354 TQGRPM-SPDDevWVADADGNPLP----------------QGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDL 416
|
90 100 110
....*....|....*....|....*....|....*...
gi 58218988 527 GRWLPNGTLKIVDRKKNifklaQ----GEYIAPEKIEN 560
Cdd:PRK10946 417 VSIDPDGYITVVGREKD-----QinrgGEKIAAEEIEN 449
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
254-591 |
3.17e-06 |
|
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: 50.04 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 254 DLSVICFTSGTTGDPKGAMLTHENVVsNMAAFLKFLEPIFQptsDDVTISYLPLAHmferlvqgilfSCGGKIGFFQGDI 333
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAW-RGGAFFAGSGGALP---SDVLYTCLPLYH-----------STALIVGWSACLA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 334 -------------RLLPDDMKALKPTVFPTVPRLLnrvydkvqneaktplkKFLLNL--AIISKFNEVK----NGIirRD 394
Cdd:cd05940 147 sgatlvirkkfsaSNFWDDIRKYQATIFQYIGELC----------------RYLLNQppKPTERKHKVRmifgNGL--RP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 395 SLWDKLvfskiqgslggKVRLMITGaapistpvltffraamgcwVFEAYGQTECTGGcSITSPG-DWTAGHVGTPVACNF 473
Cdd:cd05940 209 DIWEEF-----------KERFGVPR-------------------IAEFYAATEGNSG-FINFFGkPGAIGRNPSLLRKVA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 474 ----VKLeDVADMNyfSVNNEGEICIKGN--------------NVFKGYLkDPEKTQEVL------DKDGWLHTGDIGRW 529
Cdd:cd05940 258 plalVKY-DLESGE--PIRDAEGRCIKVPrgepgllisrinplEPFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRL 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58218988 530 LPNGTLKIVDRKKNIFKLaQGEYIAPEKIENVYSRSRPVLQVFVHgeslrsfliGVVVPDPD 591
Cdd:cd05940 334 DGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVY---------GVQVPGTD 385
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
395-561 |
4.00e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 50.01 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 395 SLWDKLVFS-KIQGSLGGKVRLMITGAAPISTPVLTFFRAAmGCWVFEAYG--QTECTGGCSITSPGDWT---AGHVGTP 468
Cdd:PRK05857 269 TLLSKLVSElKSANATVPSLRLVGYGGSRAIAADVRFIEAT-GVRTAQVYGlsETGCTALCLPTDDGSIVkieAGAVGRP 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 469 VACNFVKL--EDVADMNYFSVNNE---GEICIKGNNVFKGYLKDPEKTQEVLdKDGWLHTGDIGRWLPNGTLKIVDRKKN 543
Cdd:PRK05857 348 YPGVDVYLaaTDGIGPTAPGAGPSasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSE 426
|
170
....*....|....*...
gi 58218988 544 IFkLAQGEYIAPEKIENV 561
Cdd:PRK05857 427 MI-ICGGVNIAPDEVDRI 443
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
260-318 |
4.49e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 49.94 E-value: 4.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58218988 260 FTSGTTGDPKGAMLTHENVVSN----MAAFlkFLEPIFQPTSDDVTISYLPLAH-MfeRLVQGI 318
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANfeqlMSDY--FGDTGGVPPPDTTVVSWLPFYHdM--GLVLGV 226
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
104-561 |
5.09e-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: 49.88 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 104 KWISYKQVSDRAEYLGSCLLHKGYKSSQDqfVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVV 183
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDR--VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 184 ICDT----PQKATMLVENVEKGLT---PGLKTIILMD----PFDDDlmkrgekcGVEMLSLHDAENIGKENFKkPVPPKP 252
Cdd:cd17634 161 ITADggvrAGRSVPLKKNVDDALNpnvTSVEHVIVLKrtgsDIDWQ--------EGRDLWWRDLIAKASPEHQ-PEAMNA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 253 EDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFlepIFQPTSDDVTISYLPLAHMFER--LVQGILFsCGGKIGFFQ 330
Cdd:cd17634 232 EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKY---VFDYGPGDIYWCTADVGWVTGHsyLLYGPLA-CGATTLLYE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 331 GdirllpddmkalKPtVFPTVPRLlnrvYDKVQNEAKTPLkkFLLNLAIISKFNEVKNGIIRRD--SLwdklvfsKIQGS 408
Cdd:cd17634 308 G------------VP-NWPTPARM----WQVVDKHGVNIL--YTAPTAIRALMAAGDDAIEGTDrsSL-------RILGS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 409 LGgkvrlmitgaAPISTPVLTFFRAAMG---CWVFEAYGQTECTGGCSITSPG--DWTAGHVGTPVACNFVKLEDvADMN 483
Cdd:cd17634 362 VG----------EPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGH 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 484 YFSVNNEGEICIKGN--NVFKGYLKDPEKTQEVLDK--DGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAqGEYIAPEKIE 559
Cdd:cd17634 431 PQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIE 509
|
..
gi 58218988 560 NV 561
Cdd:cd17634 510 SV 511
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
246-544 |
6.66e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 49.34 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 246 KPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMaafLKFLEPIfQPTSDDVTISYLPLAHMFERLVqgILFS--CG 323
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNV---LQVIDAL-EGQEGDRGVSWLPFFHDMGLIT--VLLPalLG 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 324 GKIGFfqgdirllpddmkaLKPTVFPTVP----RLLNRVYDKVQNE-AKTPlkKFLLNLAIIskfnevkNGIIRRDSL-W 397
Cdd:PRK07769 247 HYITF--------------MSPAAFVRRPgrwiRELARKPGGTGGTfSAAP--NFAFEHAAA-------RGLPKDGEPpL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 398 DklvFSKIQGslggkvrlMITGAAPISTPVLTFFRAAMGCWVFE------AYGQTECTGGCSiTSPGD------------ 459
Cdd:PRK07769 304 D---LSNVKG--------LLNGSEPVSPASMRKFNEAFAPYGLPptaikpSYGMAEATLFVS-TTPMDeeptviyvdrde 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 460 WTAGHV-----GTP-----VACNFVKLEDVADMnyfsVNNE----------GEICIKGNNVFKGYLKDPEKTQEVL---- 515
Cdd:PRK07769 372 LNAGRFvevpaDAPnavaqVSAGKVGVSEWAVI----VDPEtaselpdgqiGEIWLHGNNIGTGYWGKPEETAATFqnil 447
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 58218988 516 -------------DKDGWLHTGDIGRWLpNGTLKIVDRKKNI 544
Cdd:PRK07769 448 ksrlseshaegapDDALWVRTGDYGVYF-DGELYITGRVKDL 488
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
260-590 |
1.97e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 47.85 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 260 FTSGTTGDPKGAMLTHENVVSNmaaflkflepiFQPTSDDVTISylplaHMFERLVQGILFSCG---GKIG--FFQGDIR 334
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHS-----------FDCNVHDFHMK-----REDSVLIAGTLVHSLflyGAIStlYVGQTVH 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 335 LLP--------DDMKALKPTVFPTVPRLLNRVYDkvqneaktplkkfllnlaiISKFNEVKNGIIRRDSLWDKLVFSKIQ 406
Cdd:PRK07638 214 LMRkfipnqvlDKLETENISVMYTVPTMLESLYK-------------------ENRVIENKMKIISSGAKWEAEAKEKIK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 407 GSLggkvrlmitgaapistPVLTFFraamgcwvfEAYGQTECTGgCSITSPGDWT--AGHVGTPvaCNFVKLEDV-ADMN 483
Cdd:PRK07638 275 NIF----------------PYAKLY---------EFYGASELSF-VTALVDEESErrPNSVGRP--FHNVQVRICnEAGE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 484 YFSVNNEGEICIKGNNVFKGYLKDPEKTQEvLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYS 563
Cdd:PRK07638 327 EVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLH 404
|
330 340
....*....|....*....|....*..
gi 58218988 564 RsrpvlqvfvHGESLRSFLIGvvVPDP 590
Cdd:PRK07638 405 E---------HPAVDEIVVIG--VPDS 420
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
250-598 |
2.13e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 47.35 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 250 PKPEDLSVICFTSGTTGDPKGAMLTHENVVSnmaaflkflepifqptSDDVTISYL----------PLAHM--FERLVQG 317
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTA----------------SADATHDRLggpgqwllalPAHHIagLQVLVRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 318 ILfscGGKI--------GFfqgDIRLLPDDMKALKPtvfptvprllNRVYDKVqneAKTPLKKFLLNLAIISKFNEvkng 389
Cdd:PRK07824 96 VI---AGSEpveldvsaGF---DPTALPRAVAELGG----------GRRYTSL---VPMQLAKALDDPAATAALAE---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 390 iirrdslwdklvFSKIqgslggkvrlmITGAAPISTPVLTFFRAAmGCWVFEAYGQTECTGGCSitspgdwtagHVGTPV 469
Cdd:PRK07824 153 ------------LDAV-----------LVGGGPAPAPVLDAAAAA-GINVVRTYGMSETSGGCV----------YDGVPL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 470 ACNFVKLEDvadmnyfsvnneGEICIKGNNVFKGY--LKDPEKTQEvldkDGWLHTGDIGRwLPNGTLKIVDRKKNIFKL 547
Cdd:PRK07824 199 DGVRVRVED------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAIST 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 58218988 548 AqGEYIAPEKIENVYSRSRPVLQVFVHG---ESLRSFLIGVVVPDPDSLPSFAA 598
Cdd:PRK07824 262 G-GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEA 314
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
107-598 |
2.82e-05 |
|
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: 47.04 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 107 SYKQVSDRAEYLGScLLHKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICD 186
Cdd:cd05937 7 TYSETYDLVLRYAH-WLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 187 tpqkatmlvenvekgltpglktiilmdpfdddlmkrgekcgvemlslhdaenigkenfkkpvppkPEDLSVICFTSGTTG 266
Cdd:cd05937 86 -----------------------------------------------------------------PDDPAILIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 267 DPKGAmlthenVVSNMAAFL--KFLEPIFQPTSDDVTISYLPLAH-------MFERLVQGILFSCGGKIgffqgDIRLLP 337
Cdd:cd05937 101 LPKAA------AISWRRTLVtsNLLSHDLNLKNGDRTYTCMPLYHgtaaflgACNCLMSGGTLALSRKF-----SASQFW 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 338 DDMKALKPTVFPTVPRLLnrvydkvqneaktplkKFLLNlAIISKFNE---VK----NGIirRDSLWDKLvfskiqgslg 410
Cdd:cd05937 170 KDVRDSGATIIQYVGELC----------------RYLLS-TPPSPYDRdhkVRvawgNGL--RPDIWERF---------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 411 gKVRLMItgaaPIstpvltffraamgcwVFEAYGQTECTGGCSITSPGDWTAGHVG--------------TPVAcnfVKL 476
Cdd:cd05937 221 -RERFNV----PE---------------IGEFYAATEGVFALTNHNVGDFGAGAIGhhglirrwkfenqvVLVK---MDP 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 477 EDvaDMNYFS----------VNNEGEIC--IKGNNV--FKGYLKDPEKTQ-----EVLDK-DGWLHTGDIGRWLPNGTLK 536
Cdd:cd05937 278 ET--DDPIRDpktgfcvrapVGEPGEMLgrVPFKNReaFQGYLHNEDATEsklvrDVFRKgDIYFRTGDLLRQDADGRWY 355
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58218988 537 IVDRKKNIFKLaQGEYIAPEKIENVYSRSRPVLQVFVHgeslrsfliGVVVPDPDSLPSFAA 598
Cdd:cd05937 356 FLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVY---------GVKVPGHDGRAGCAA 407
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
250-590 |
4.72e-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: 46.22 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 250 PKPEDLSVICfTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDV--------TISYL--PLAHMFERLVQGIL 319
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHkaaaaaagTVMFPapPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 320 FSCGGKIgfFQGDIRLLPDDmkalkptVFPTVPR----LLNRVYDKVqneAKtPLkkfllnlaiISKFNEVKNgiirRD- 394
Cdd:cd05924 80 LLGGQTV--VLPDDRFDPEE-------VWRTIEKhkvtSMTIVGDAM---AR-PL---------IDALRDAGP----YDl 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 395 -SLwdklvfskiqgslggkvRLMITGAAPISTPVLTFFRAAM-GCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACN 472
Cdd:cd05924 134 sSL-----------------FAISSGGALLSPEVKQGLLELVpNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 473 FVKLEDvaDMNYFSVNNEGE--ICIKGNnVFKGYLKDPEKTQEVL-DKDG--WLHTGDIGRWLPNGTLKIVDRKKNIFKL 547
Cdd:cd05924 197 TVVLDD--DGRVVPPGSGGVgwIARRGH-IPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINT 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 58218988 548 AqGEYIAPEKIENVYsRSRP-VLQVFVHGeslrsfligvvVPDP 590
Cdd:cd05924 274 G-GEKVFPEEVEEAL-KSHPaVYDVLVVG-----------RPDE 304
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
247-570 |
6.19e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 46.27 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 247 PVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSN---MAAFLKFLEPifqptsDDVTISYLPLAHMFERLVQGILFSCG 323
Cdd:PRK12476 187 PVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNlvqMILSIDLLDR------NTHGVSWLPLYHDMGLSMIGFPAVYG 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 324 GKIGFfqgdirllpddmkaLKPTVFPTVP----RLLNRVYDKVQNEAKTPlkKFLLNLAiiskfneVKNGIIRRDslwDK 399
Cdd:PRK12476 261 GHSTL--------------MSPTAFVRRPqrwiKALSEGSRTGRVVTAAP--NFAYEWA-------AQRGLPAEG---DD 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 400 LVFSKIqgslggkvrLMITGAAPISTPVLTFFRAAMGCW------VFEAYGQTECTGGCSITSPG-----------DWTA 462
Cdd:PRK12476 315 IDLSNV---------VLIIGSEPVSIDAVTTFNKAFAPYglprtaFKPSYGIAEATLFVATIAPDaepsvvyldreQLGA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 463 GHV-----GTPVACNFVKLEDVADMNYFSVNNE-----------GEICIKGNNVFKGYLKDPEKTQEVL----------- 515
Cdd:PRK12476 386 GRAvrvaaDAPNAVAHVSCGQVARSQWAVIVDPdtgaelpdgevGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaeg 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58218988 516 -------DKDGWLHTGDIGRWLpNGTLKIVDRKKNIFKL-AQGEYiaPEKIENVYSRSRPVLQ 570
Cdd:PRK12476 466 shadgaaDDGTWLRTGDLGVYL-DGELYITGRIADLIVIdGRNHY--PQDIEATVAEASPMVR 525
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
443-591 |
3.53e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 43.44 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 443 YGQTECTGGCSITSPGDWTAG--HVGTPVACNFVKLEDvadmnyfsvNNEGEICIKGNNVFKGYLkdpektQEVLDKDGW 520
Cdd:PRK07445 261 YGMTETASQIATLKPDDFLAGnnSSGQVLPHAQITIPA---------NQTGNITIQAQSLALGYY------PQILDSQGI 325
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58218988 521 LHTGDIGRWLPNGTLKIVDRKKNIFkLAQGEYIAPEKIENVYSRSRPVLQVFVHGeslrsfligvvVPDPD 591
Cdd:PRK07445 326 FETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLG-----------LPDPH 384
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
491-598 |
4.62e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 491 GEICIKGNNVFKGYLKDPEKTQEVLDKDGWL------HTGDIGRWLPNGTLKIVDRKKNIFKLaQGEYIAPEKIENVYSR 564
Cdd:PRK10252 803 GDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQA 881
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 58218988 565 SRPVLQVFVH-----------GESLRsfLIGVVVPDPDSLPSFAA 598
Cdd:PRK10252 882 LPDVEQAVTHacvinqaaatgGDARQ--LVGYLVSQSGLPLDTSA 924
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
248-279 |
5.20e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 5.20e-04
10 20 30
....*....|....*....|....*....|..
gi 58218988 248 VPPKPEDLSVICFTSGTTGDPKGAMLTHENVV 279
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
106-309 |
5.90e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 106 ISYKQVSDRAEYLGSCLLHKGYKSSQdqFVGIFAQNRPEWVISELACyTYSMVAVPLYDT-LGTEAIIFVINRADIPVVI 184
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGD--VVALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 185 CDTPqkatmLVENVE--KGLTPGLKTIILMDP-------FDDDLMKRGEKCGVEMLSLHDAenigkenfkkpVPPKpeDL 255
Cdd:PRK08279 140 VGEE-----LVEAFEeaRADLARPPRLWVAGGdtlddpeGYEDLAAAAAGAPTTNPASRSG-----------VTAK--DT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 58218988 256 SVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEpifqPTSDDVTISYLPLAH 309
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
253-584 |
2.02e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 253 EDLSVICFTSGTTGDPKGAMLTHenvvSNMAAFLKFLEPIFQPTSDDVTISYLPLA------HMFERLVQG--ILFSCGG 324
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTH----AALAERLQWMQATYALDDSDVLMQKAPISfdvsvwECFWPLITGcrLVLAGPG 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 325 KigffQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKkfllnlaiiskfnevkngiirrdslwdkLVFSk 404
Cdd:PRK05691 1349 E----HRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLR----------------------------RLFS- 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 405 iqgslGGKVRlmitgAAPISTPVLTFFRAAMgcwVFEAYGQTE---------CTGGCSITSPgdwtaghVGTPVACNFVK 475
Cdd:PRK05691 1396 -----GGEAL-----PAELRNRVLQRLPQVQ---LHNRYGPTEtainvthwqCQAEDGERSP-------IGRPLGNVLCR 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 476 LEDvADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQE--VLDKDG-----WLHTGDIGRWLPNGTLKIVDRKKNIFKLa 548
Cdd:PRK05691 1456 VLD-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfVPDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKL- 1533
|
330 340 350
....*....|....*....|....*....|....*...
gi 58218988 549 QGEYIAPEKIENVYSRSRPVLQ--VFVHGESLRSFLIG 584
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
244-320 |
6.31e-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: 39.72 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58218988 244 FKKPVPPKPEDL---SVICF--TSGTTGDPKGAMLTHENVVSnMAAFLKFLepiFQPTSDDVTISYLPLAHMFERLV--- 315
Cdd:cd05939 90 QSSTEPPSQDDVnfrDKLFYiyTSGTTGLPKAAVIVHSRYYR-IAAGAYYA---FGMRPEDVVYDCLPLYHSAGGIMgvg 165
|
....*
gi 58218988 316 QGILF 320
Cdd:cd05939 166 QALLH 170
|
|
| |
