|
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 ... |
121-621 |
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: 796.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 121 GLDFSSTIVKHAPISLLVFlhkigQSGslrswpathipwwwsrsmtpwaLELSATSSIQDCGQENHHAPVPPQPDDLSIV 200
Cdd:cd05927 67 GPEAIEYILNHAEISIVFC-----DAG----------------------VKVYSLEEFEKLGKKNKVPPPPPKPEDLATI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 201 CFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSD 280
Cdd:cd05927 120 CYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 281 DMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLGGCVRMI 358
Cdd:cd05927 200 DIKALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 359 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWA--CKGEGEIC 436
Cdd:cd05927 280 LTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVC 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 437 VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVH 516
Cdd:cd05927 360 IRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 517 GDSLKAFLVGIVVPDPEVMPSWA-QKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNG 595
Cdd:cd05927 440 GDSLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENG 519
|
490 500
....*....|....*....|....*.
gi 795413665 596 LLTPTLKAKRPELREYFKKQIEELYS 621
Cdd:cd05927 520 LLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
182-621 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 585.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwAPtcADVHISYLPLAHMFERMVQSVV 261
Cdd:PLN02736 208 GRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF--YP--SDVHISYLPLAHIYERVNQIVM 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 262 YCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGiiRNDS-I 338
Cdd:PLN02736 284 LHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQALENG--KNPSpM 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 339 WDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL 418
Cdd:PLN02736 362 WDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 419 VDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYV 495
Cdd:PLN02736 442 VDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 496 APEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKESGL 574
Cdd:PLN02736 522 APEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQL 601
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 795413665 575 HSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 621
Cdd:PLN02736 602 RGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
193-621 |
2.77e-145 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 434.14 E-value: 2.77e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFfQ 272
Cdd:COG1022 181 KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSFLPLAHVFERTVSYYALAAGATVAF-A 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 273 GDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLLEFA---AKRKQAEVRSGiiRNDSIW-------- 339
Cdd:COG1022 256 ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavGRRYARARLAG--KSPSLLlrlkhala 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 DELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLV 419
Cdd:COG1022 334 DKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKIA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEK 499
Cdd:COG1022 413 E-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQP 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 500 IENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKesGLHSFE 578
Cdd:COG1022 482 IENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEVDRANA--GLSRAE 558
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 795413665 579 QVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 621
Cdd:COG1022 559 QIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
194-608 |
8.06e-140 |
|
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: 414.69 E-value: 8.06e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFE-RMVQSVVYCHGGRVGFFQ 272
Cdd:cd05907 86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFAS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 273 gDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqaslG 352
Cdd:cd05907 162 -SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------G 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 353 GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgE 432
Cdd:cd05907 211 GRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------D 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 433 GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQ 512
Cdd:cd05907 279 GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 513 IYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIEG-TYADLCTSKDLKKAILEDMVRLGKEsgLHSFEQVKAIHIHSDMFS 591
Cdd:cd05907 359 AVVIGDGRP-FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFT 435
|
410
....*....|....*..
gi 795413665 592 VQNGLLTPTLKAKRPEL 608
Cdd:cd05907 436 IENGELTPTLKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
192-605 |
8.96e-137 |
|
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: 408.91 E-value: 8.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 192 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAHMFERMVQSVVYCHGGRVGFf 271
Cdd:cd17639 85 GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD--DRYLAYLPLAHIFELAAENVCLYRGGTIGY- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 272 qGDIRLLSDDMKALC--------PTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGIirnDS-IWD 340
Cdd:cd17639 162 -GSPRTLTDKSKRGCkgdltefkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GTpLLD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 341 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVD 420
Cdd:cd17639 238 ELVFKKVRAALGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 421 VEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPE 498
Cdd:cd17639 317 WEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 499 KIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYADLCTSKDLKKAILEDMVRLGKESGLHSF 577
Cdd:cd17639 397 KLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAGLEKF 476
|
410 420
....*....|....*....|....*...
gi 795413665 578 EQVKAIHIHSDMFSVQNGLLTPTLKAKR 605
Cdd:cd17639 477 EIPQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
193-620 |
2.06e-123 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 379.75 E-value: 2.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTES-QWAPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFF 271
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSaNAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFW 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 272 QGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGI--IRNDSIWDELFFNKI 347
Cdd:PLN02614 301 RGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDKLVFNKV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 348 QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNY 426
Cdd:PLN02614 381 KQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESVPEMEY 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 427 --WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIY 504
Cdd:PLN02614 461 daLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIY 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 505 IRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIH 584
Cdd:PLN02614 540 GEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIH 619
|
410 420 430
....*....|....*....|....*....|....*.
gi 795413665 585 IHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 620
Cdd:PLN02614 620 LDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
182-620 |
6.77e-121 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 373.00 E-value: 6.77e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWapTCADVHISYLPLAHMFERMVQ 258
Cdd:PLN02430 207 GKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDKM--THDDVYLSFLPLAHILDRMIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 259 SVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRND 336
Cdd:PLN02430 285 EYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLAWMNRGYSHKK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 337 S--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPC 413
Cdd:PLN02430 365 AspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVY 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 414 NHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQ 491
Cdd:PLN02430 445 NELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQ 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 492 GEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKE 571
Cdd:PLN02430 524 GEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEK 603
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 795413665 572 SGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 620
Cdd:PLN02430 604 NKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
182-621 |
8.49e-121 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 373.02 E-value: 8.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTESqwAPTCADVHISYLPLAHMFERMVQ 258
Cdd:PLN02861 208 GSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDR--VATEEDSYFSYLPLAHVYDQVIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 259 SVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRND 336
Cdd:PLN02861 285 TYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 337 S--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLP 412
Cdd:PLN02861 365 AspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMT 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 413 CNHIKLVDVEELNYWACKG--EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLA 490
Cdd:PLN02861 444 TIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLS 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 491 QGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGK 570
Cdd:PLN02861 523 QGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGK 602
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 795413665 571 ESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 621
Cdd:PLN02861 603 KLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
164-621 |
3.56e-108 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 341.33 E-value: 3.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 164 SMTPWALelSATSSIQDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTesqwaPTCA--D 241
Cdd:PLN02387 221 GSSNWTV--SSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVV-----PKLGknD 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 242 VHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIRLLSD-----------DMKALCPTIFPVVPRLLNRMYDKIFSQANT 310
Cdd:PLN02387 294 VYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 311 P--LKRWLLEFAAKRKQAEVR------SGIIRndSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVY 382
Cdd:PLN02387 372 KggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIG 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 383 EGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEA--L 457
Cdd:PLN02387 450 QGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykV 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 458 DSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVM 535
Cdd:PLN02387 530 DERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQAL 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 536 PSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKK 614
Cdd:PLN02387 610 EKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKD 689
|
....*..
gi 795413665 615 QIEELYS 621
Cdd:PLN02387 690 DLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
186-490 |
1.32e-90 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 286.52 E-value: 1.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 186 HHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFER-MVQSVVYCH 264
Cdd:pfam00501 146 PPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 265 GGRVGFFQGDIRL----LSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGiirndsiwd 340
Cdd:pfam00501 226 GATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS--------- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 341 elffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIK 417
Cdd:pfam00501 279 --------------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVK 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795413665 418 LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLA 490
Cdd:pfam00501 345 IVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
183-620 |
6.05e-85 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 279.94 E-value: 6.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 183 QENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTESQWAPTCADVHISYLPLAHMFERMVQSVV 261
Cdd:PTZ00216 252 GSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIF 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 262 YCHGGRVGFfqGDIRLLSD-------DMKALCPTIFPVVPRLLNRMydKIFSQANTP----LKRWLLEFAAKRKQAEVRS 330
Cdd:PTZ00216 332 LARGALIGF--GSPRTLTDtfarphgDLTEFRPVFLIGVPRIFDTI--KKAVEAKLPpvgsLKRRVFDHAYQSRLRALKE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 331 GiiRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVG 408
Cdd:PTZ00216 408 G--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVG 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 409 APLPCNHIKLVDVEELNYwACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHI 486
Cdd:PTZ00216 483 QLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKAL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 487 FKLAQGEYVAPEKIENIYIRSQPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAIL 562
Cdd:PTZ00216 562 AKNCLGEYIALEALEALYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKAT 639
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 563 EDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 620
Cdd:PTZ00216 640 ESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
194-606 |
1.33e-73 |
|
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: 243.81 E-value: 1.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFfqG 273
Cdd:cd17640 87 SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--T 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQ--ANTPLKRWLLEFAAkrkqaevrsgiirndsiwdelffnkiqasL 351
Cdd:cd17640 161 SIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL-----------------------------S 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 352 GGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG 431
Cdd:cd17640 212 GGIFKFGISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 432 EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVA 511
Cdd:cd17640 291 KGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIE 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 512 QIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGI---EGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSD 588
Cdd:cd17640 371 QIMVVGQDQK-RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEE 449
|
410
....*....|....*...
gi 795413665 589 MFsVQNGLLTPTLKAKRP 606
Cdd:cd17640 450 PF-IENGEMTQTMKIKRN 466
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
189-598 |
8.56e-64 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 220.79 E-value: 8.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTESQWAPTCADVHISYLPLAHMFERMVQSVVYCHGGrV 268
Cdd:cd17632 217 RPEPDDDPLALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-T 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 GFFQG--DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPLKRWL-----LEFAAKRKQAEVRsgiirndsiwde 341
Cdd:cd17632 293 AYFAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadAETLAERVKAELR------------ 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 342 lffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLVDV 421
Cdd:cd17632 357 ------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDV 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 422 EELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPE 498
Cdd:cd17632 422 PELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 499 KIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMpswaqkrgiegtyaDLCTSKDLKKAILEDMVRLGKESGLHSFE 578
Cdd:cd17632 502 RLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------------AGEDTARLRAALAESLQRIAREAGLQSYE 567
|
410 420
....*....|....*....|
gi 795413665 579 QVKAIHIHSDMFSVQNGLLT 598
Cdd:cd17632 568 IPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
176-605 |
8.99e-64 |
|
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: 218.88 E-value: 8.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 176 SSIQDCGQENHHAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHISYLPLAHM 252
Cdd:cd05932 119 DDLIAQHPPLEERP-TRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGiehIGTEEN-------DRMLSYLPLAHV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 253 FERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLL----NRMYDKIFSQAntpLKRWLlefaakrkQAEV 328
Cdd:cd05932 191 TERVFVEGGSLYGGVLVAFAESLDTFVEDVQRARPTLFFSVPRLWtkfqQGVQDKIPQQK---LNLLL--------KIPV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 329 RSGIIRndsiwdelffNKIQASLG-GCVRMIVTGAAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV 407
Cdd:cd05932 260 VNSLVK----------RKVLKGLGlDQCRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 408 GAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIF 487
Cdd:cd05932 329 GNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 488 KLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEvmpswAQKRGIEGTYADLCTSkdlKKAILEDMvr 567
Cdd:cd05932 398 KTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA-PLALVVLSEE-----ARLRADAFARAELEAS---LRAHLARV-- 466
|
410 420 430
....*....|....*....|....*....|....*...
gi 795413665 568 lgkESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKR 605
Cdd:cd05932 467 ---NSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
193-620 |
1.31e-60 |
|
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: 212.22 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFERMVQS-VVYCHGGRVGFF 271
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 272 QGDIR--LLSDDMKALCPTIFPVVPRLLNRMYDKI---FSQAnTPLKRWLLEFAaKRKQAEV-------RSGIIRNDSIW 339
Cdd:cd05933 228 QPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESPSPLFYRLA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 DELFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIK 417
Cdd:cd05933 306 KKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 418 LVDVEelnywaCKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAP 497
Cdd:cd05933 384 IHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPP 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 498 EKIENIYIRSQP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKRGIEGTY-ADLCTSKDLK-- 558
Cdd:cd05933 458 VPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAGGKDPKvy 535
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795413665 559 KAILEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 620
Cdd:cd05933 536 EAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
200-618 |
1.02e-56 |
|
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: 198.11 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 200 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFErMVQSVVYC--HGGRV----GFfqg 273
Cdd:COG0318 105 ILYTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFG-LTVGLLAPllAGATLvllpRF--- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 DIRLLSDDMKALCPTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiwdelffnkiqaslgg 353
Cdd:COG0318 177 DPERVLELIERERVTVLFGVPTMLARLLR-----------------HPEFARYDLSS----------------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 354 cVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDVE--ELnywAC 429
Cdd:COG0318 217 -LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVDEDgrEL---PP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 430 KGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQP 509
Cdd:COG0318 293 GEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 510 VAQIYV-------HGDSLKAFlvgiVVPDPEvmpswaqkrgiegtyADLcTSKDLKKAILEdmvRLGKesglhsFEQVKA 582
Cdd:COG0318 371 VAEAAVvgvpdekWGERVVAF----VVLRPG---------------AEL-DAEELRAFLRE---RLAR------YKVPRR 421
|
410 420 430
....*....|....*....|....*....|....*.
gi 795413665 583 IHIHSDMfsvqngLLTPTLKAKRPELREYFKKQIEE 618
Cdd:COG0318 422 VEFVDEL------PRTASGKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
196-533 |
6.17e-56 |
|
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: 192.50 E-value: 6.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFerMVQSVVYC--HGGRVGFFQG 273
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 -DIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwllefaakRKQAEVRSgiiRNDSiwdelffnkiqaslg 352
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLARL----------------------LKAPESAG---YDLS--------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 353 gCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDVEElNYWACK 430
Cdd:cd04433 115 -SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 431 GEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPV 510
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|...
gi 795413665 511 AQIYVHGdslkaflvgivVPDPE 533
Cdd:cd04433 271 AEAAVVG-----------VPDPE 282
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
194-571 |
1.01e-53 |
|
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: 193.02 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwAPTcaDVHISYLPLAHMFERM---VQSVVycHGGRVGF 270
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL--GPG--DEYVSVLPLPWIGEQMysvGQALV--CGFIVNF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 271 FQgDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWL--------LEFAAKRKQAEVRSGIIRNDS-IW 339
Cdd:cd17641 231 PE-EPETMMEDLREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwLA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 DELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNHIK 417
Cdd:cd17641 310 DALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEVR 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 418 LVDVeelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAP 497
Cdd:cd17641 388 IDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSP 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795413665 498 EKIENIYIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKE 571
Cdd:cd17641 457 QFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
194-605 |
4.53e-53 |
|
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: 188.42 E-value: 4.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGRVGF 270
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGvkeVVLLGKG-------DKILSILPLHHIYPLTFTLLLPLLNGAHVV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 271 FQGDI---RLLSDDMKALCPTIfpVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKrkqaevrsgIIRNDSIWdELFFNKI 347
Cdd:cd05914 161 FLDKIpsaKIIALAFAQVTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 348 QASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPlpcnhIKLVDVEELNYW 427
Cdd:cd05914 229 HEAFGGNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 428 ACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRS 507
Cdd:cd05914 303 PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNM 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 508 QPVA--QIYVHGDSLKAflvgIVVPDPEVMPSWAQKRgiegtyadlctsKDLKKAILEDmVRLGKESGLHSFEQVKAIHI 585
Cdd:cd05914 383 PFVLesLVVVQEKKLVA----LAYIDPDFLDVKALKQ------------RNIIDAIKWE-VRDKVNQKVPNYKKISKVKI 445
|
410 420
....*....|....*....|
gi 795413665 586 HSDMFSVqngllTPTLKAKR 605
Cdd:cd05914 446 VKEEFEK-----TPKGKIKR 460
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
188-525 |
2.07e-49 |
|
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: 178.53 E-value: 2.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAHMFErmvQSVVYCHGGR 267
Cdd:cd05936 118 ERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGD--DVVLAALPLFHVFG---LTVALLLPLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGFFQ------GDIRLLsDDMKALCPTIFPVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaEVRSGIirndsiwde 341
Cdd:cd05936 193 LGATIvliprfRPIGVL-KEIRKHRVTIFPGVPTMYIA----------------LLNAPEFKK--RDFSSL--------- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 342 lffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVD 420
Cdd:cd05936 245 --------------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 421 vEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKI 500
Cdd:cd05936 311 -DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREV 387
|
330 340 350
....*....|....*....|....*....|..
gi 795413665 501 ENIYIRSQPVAQIYV-------HGDSLKAFLV 525
Cdd:cd05936 388 EEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
181-525 |
8.76e-46 |
|
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: 168.93 E-value: 8.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 181 CGQENHHAPVPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFS---GFLKVTESQwaptcADVHISYLPLAHMF-- 253
Cdd:cd05911 130 LGEEDEDLPPPLKdgKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSqvqTFLYGNDGS-----NDVILGFLPLYHIYgl 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 254 ERMVQSVVYchGGRV----GFFqgdirllSDDMKALCP----TIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkq 325
Cdd:cd05911 205 FTTLASLLN--GATViimpKFD-------SELFLDLIEkykiTFLYLVPPIAAAL-------AKSPL------------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 326 aevrsgiirndsiwdelfFNKIQASlggCVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTS 404
Cdd:cd05911 256 ------------------LDKYDLS---SLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 405 GHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK 484
Cdd:cd05911 315 GSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 795413665 485 HIFKLaQGEYVAPEKIENIyIRSQP------VAQIY--VHGDSLKAFLV 525
Cdd:cd05911 395 ELIKY-KGFQVAPAELEAV-LLEHPgvadaaVIGIPdeVSGELPRAYVV 441
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
193-542 |
1.81e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 168.93 E-value: 1.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTESqwaptcaDVHISYLPLAHMFERMVqSVVYC--HGGR 267
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG-------DRYLAANPFFHVFGYKA-GVNAPlmRGAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VgffqgdIRLLS---DDMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiirndsiwd 340
Cdd:PRK07656 236 I------LPLPVfdpDEVFRLIeterITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS---------- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 341 elffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCNHI 416
Cdd:PRK07656 283 --------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVEN 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 417 KLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYV 495
Cdd:PRK07656 349 KIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNV 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 795413665 496 APEKIENIYIRSQPVAQIYV-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 542
Cdd:PRK07656 426 YPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAYVVlkpGAELTEEELI-AYCREH 481
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
194-621 |
4.93e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 159.11 E-value: 4.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNV------VADFSGFLKvtesqWAPtcaDVHISYLPLAHMFERMVQSVVYCHGGR 267
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK-----YNP---KTHLSYLPISHIYERVIAYLSFMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLlefaAKRKQAEVRSGIIRNDSIWDELFFN 345
Cdd:PTZ00342 375 INIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFSKFLEGITH 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 346 ---KIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLVD 420
Cdd:PTZ00342 451 issKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVRT 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 421 VEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKI 500
Cdd:PTZ00342 530 WETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDML 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 501 ENIYIRSQPVAQIYVHG-DSLKAFLvGIVVPDPEVM------PSWAQKRGI-EGTYADLCTSKDLKKAILEDMVR----- 567
Cdd:PTZ00342 610 NNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYVDYVKgkmle 688
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 795413665 568 LGKESGLHSFEQVKAIHIHSDMFSVQNgLLTPTLKAKRPEL-REY--FKKQIEELYS 621
Cdd:PTZ00342 689 VYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVfKDYafFIDQVKKIYK 744
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
182-532 |
1.71e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 154.96 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTES-QWapTCADVHISYLPLAHMFERMVqsv 260
Cdd:PRK06187 154 AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWlKL--SRDDVYLVIVPMFHVHAWGL--- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 vychgGRVGFFQG---------DIRLLSDDMKALCPTIFPVVPRLLNRMydkifSQANTPLKRWLlefaakrkqaevrSG 331
Cdd:PRK06187 226 -----PYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQML-----LKAPRAYFVDF-------------SS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 332 IirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH----- 406
Cdd:PRK06187 283 L-----------------------RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtkrr 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 407 -VGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRK 483
Cdd:PRK06187 340 sAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRI 417
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 795413665 484 KHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 532
Cdd:PRK06187 418 KDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
196-536 |
1.72e-38 |
|
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: 147.44 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHISYLPLAHmfermVQSVV-------YChGGRV 268
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAAN----VRALVDAWRWTEDDVLLHVLPLHH-----VHGLVnallcplFA-GASV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 ---GFFQGDIRLLSDDMKALcpTIFPVVPRllnrMYDKIFS--QANTPLKRWLLEFAAKRkqaevrsgiirndsiwdelf 343
Cdd:cd05941 160 eflPKFDPKEVAISRLMPSI--TVFMGVPT----IYTRLLQyyEAHFTDPQFARAAAAER-------------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 344 fnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDV 421
Cdd:cd05941 214 -----------LRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 422 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK-HIFKlAQGEYVAPEKI 500
Cdd:cd05941 281 ETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEI 359
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 795413665 501 ENIyIRSQP-VAQIYVHGDSLKAF---LVGIVVPDPEVMP 536
Cdd:cd05941 360 ERV-LLAHPgVSECAVIGVPDPDWgerVVAVVVLRAGAAA 398
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
180-503 |
4.08e-38 |
|
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: 147.77 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 180 DCGQENHHAPVPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTcaDVHISYLPLAHMFermv 257
Cdd:cd05904 141 LLFEADEAEPPVVVikQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE--DVFLCVLPMFHIY---- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 258 qsvvychgGRVGFFQGDIRL-----------LSDDMKALCP---TIFPVVPrllnrmydkifsqantPLkrwlleFAAKR 323
Cdd:cd05904 215 --------GLSSFALGLLRLgatvvvmprfdLEELLAAIERykvTHLPVVP----------------PI------VLALV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 324 KQAEVRSGIIRndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP--- 399
Cdd:cd05904 265 KSPIVDKYDLS---------------SL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApek 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 400 GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKV 479
Cdd:cd05904 326 DRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFI 405
|
330 340
....*....|....*....|....
gi 795413665 480 IDRKKHIFKLaQGEYVAPEKIENI 503
Cdd:cd05904 406 VDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
195-532 |
1.51e-36 |
|
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: 141.98 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvteSQWAPTCADVHISYLPLAHMFE-RMVQSVVYCHGGRV----G 269
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNAL----AALDLGPDDVLLVVAPLFHIGGlGVFTLPTLLRGGTVvilrK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 270 FFQGDIRLLSDDMKAlcpTIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsgiirndsiWDELFFnkiqA 349
Cdd:cd17631 174 FDPETVLDLIERHRV---TSFFLVPTMIQAL-------LQHPR--------------------------FATTDL----S 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 350 SLggcvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYW 427
Cdd:cd17631 214 SL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVD-PDGREV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 428 ACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIyirs 507
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDV---- 361
|
330 340
....*....|....*....|....*
gi 795413665 508 qpvaqIYVHGDSLKAFLVGivVPDP 532
Cdd:cd17631 362 -----LYEHPAVAEVAVIG--VPDE 379
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
167-531 |
2.00e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 140.91 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 167 PWAlELSATSSIQDCGQENHHAPvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQ-WAPTCAD---V 242
Cdd:PRK05605 195 PWE-TLVDAAIGGDGSDVSHPRP---TPDDVALILYTSGTTGKPKGAQLTHRNLFAN------AAQGKaWVPGLGDgpeR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 243 HISYLPLAHMFE-RMVQSV-VYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmYDKIfsqantplkrwlLEFA 320
Cdd:PRK05605 265 VLAALPMFHAYGlTLCLTLaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAA 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 321 AKRkqaevrsGIirndsiwdelffnkiqaSLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFT 397
Cdd:PRK05605 329 EER-------GV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 398 TpgDWTSGHVGAPLPCNHIKLVDVEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGT 476
Cdd:PRK05605 384 D--DRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGF 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 795413665 477 LKVIDRKKHIFkLAQGEYVAPEKIENIyirsqpVAQiyvHGDSLKAFLVGIVVPD 531
Cdd:PRK05605 461 IRIVDRIKELI-ITGGFNVYPAEVEEV------LRE---HPGVEDAAVVGLPRED 505
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
190-503 |
1.81e-34 |
|
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: 137.08 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 190 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwaPTCADVHISYLPLAHMFermvqsvvychggrvG 269
Cdd:cd05909 142 APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------G 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 270 FFQGDIRLLSDDMKALC---PTIFPVVPRLLnrmYDK----IFSqanTPLkrwLLEFAAKRKQAEVRSGIirndsiwdel 342
Cdd:cd05909 203 LTGCLWLPLLSGIKVVFhpnPLDYKKIPELI---YDKkatiLLG---TPT---FLRGYARAAHPEDFSSL---------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 343 ffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDV 421
Cdd:cd05909 264 -------------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 422 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIE 501
Cdd:cd05909 331 ETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIE 408
|
..
gi 795413665 502 NI 503
Cdd:cd05909 409 DI 410
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
182-525 |
5.60e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 136.43 E-value: 5.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCaDVHISYLPLAHM----FERMV 257
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGC-EILIAPLPLYHIyaftFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 258 QSVVYCHGgrvgffqgdiRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPlkrwlleFAAkrkqaevrsgiIRNDS 337
Cdd:PRK05677 273 MMLIGNHN----------ILISN------PRDLPAMVKELGKWKFSGFVGLNTL-------FVA-----------LCNNE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 338 IWDELFFNKIQASLGGcvRMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIK 417
Cdd:PRK05677 319 AFRKLDFSALKLTLSG--GMALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCK 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 418 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAP 497
Cdd:PRK05677 391 VID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYP 468
|
330 340 350
....*....|....*....|....*....|....*.
gi 795413665 498 EKIENIyIRSQP----VAQIYV----HGDSLKAFLV 525
Cdd:PRK05677 469 NELEDV-LAALPgvlqCAAIGVpdekSGEAIKVFVV 503
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
190-525 |
1.89e-32 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 132.10 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 190 VPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkVTESQWA--PTCADVH---ISYLPLAHMFERMVQSVVY 262
Cdd:PRK08974 199 VKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN------LEQAKAAygPLLHPGKelvVTALPLYHIFALTVNCLLF 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 263 CHGGrvgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirNDSIWDEL 342
Cdd:PRK08974 273 IELG------GQNLLITN------PRDIPGFVKELKKYPFTAITGVNTLFNALL------------------NNEEFQEL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 343 FFNKIQASLGGcvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLV 419
Cdd:PRK08974 323 DFSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEK 499
Cdd:PRK08974 393 D-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNE 469
|
330 340 350
....*....|....*....|....*....|...
gi 795413665 500 IENIYIRSQPVAQIY-------VHGDSLKAFLV 525
Cdd:PRK08974 470 IEDVVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
182-532 |
2.46e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 131.54 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflkvTESQWAPTCA------DVHISYLPLAHMFER 255
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQ-----QAHQWLAGTGkleegcEVVITALPLYHIFAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 256 MVQSVVYCHGGrvgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWLlefaakrkqaevrsgiirN 335
Cdd:PRK08751 270 TANGLVFMKIG------GCNHLISN------PRDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------N 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 336 DSIWDELFFNKIQASLGGcvRMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPCN 414
Cdd:PRK08751 320 TPGFDQIDFSSLKMTLGG--GMAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPST 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 415 HIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEY 494
Cdd:PRK08751 392 DACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFN 469
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 795413665 495 VAPEKIENIYIRSQPVAQIYVHG----DSLKAFLVGIVVPDP 532
Cdd:PRK08751 470 VYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
191-610 |
4.00e-31 |
|
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: 127.04 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 191 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFERMVQ--SVVYChGGRV 268
Cdd:cd05926 145 VPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNT----YKLTPDDRTLVVMPLFHVHGLVASllSTLAA-GGSV 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 ----GFfqgDIRLLSDDMKALCPTIFPVVPRLLnrmydKIfsqantplkrwLLEFAAKRKQAEvrsgiirndsiwdelfF 344
Cdd:cd05926 220 vlppRF---SASTFWPDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESP----------------P 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 345 NKIqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPlpcNHIKLVDV 421
Cdd:cd05926 265 PKL--------RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKP---VGVEVRIL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 422 EElnywacKGE-------GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEY 494
Cdd:cd05926 333 DE------DGEilppgvvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 495 VAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDP---EVMPSWAQKRgiEGTYADlctskdlKKAILEDMvrlgkE 571
Cdd:cd05926 406 ISPLEVDGVLLSHPAVLEAVAFG-----------VPDEkygEEVAAAVVLR--EGASVT-------EEELRAFC-----R 460
|
410 420 430
....*....|....*....|....*....|....*....
gi 795413665 572 SGLHSFEQVKAIHIhsdmfsVQNGLLTPTLKAKRPELRE 610
Cdd:cd05926 461 KHLAAFKVPKKVYF------VDELPKTATGKIQRRKVAE 493
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
188-534 |
6.22e-31 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 127.44 E-value: 6.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKVTE-SQWAPTCAdvhisyLPLAHMFERMVQ 258
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEKKPRpDQLNFVCA------LPLYHIFALTVC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 259 SVVYCHGGRVGFF---QGDIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqaNTPlkrwllEFaakrkqaevrsgiirn 335
Cdd:PRK07059 271 GLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL-------NNP------DF---------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 336 dsiwDELFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLPC 413
Cdd:PRK07059 322 ----DKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 414 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGE 493
Cdd:PRK07059 389 TEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGF 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 795413665 494 YVAPEKIENIyIRSQP----VAQIYVH----GDSLKAFlvgIVVPDPEV 534
Cdd:PRK07059 467 NVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
196-526 |
7.67e-31 |
|
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: 123.38 E-value: 7.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflkvtesQWApTCADVHIS--YL---PLAHMFErmvqsvvYCHGGRVGF 270
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAA--------AWA-DCADLTEDdrYLiinPFFHTFG-------YKAGIVACL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 271 FQGdirllsddmkalcPTIFPV----VPRLLNRMYDKIFSQANTP--LKRWLLEFAAkRKQAEVRSgiirndsiwdelff 344
Cdd:cd17638 65 LTG-------------ATVVPVavfdVDAILEAIERERITVLPGPptLFQSLLDHPG-RKKFDLSS-------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 345 nkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVD 420
Cdd:cd17638 117 ----------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 421 veelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKI 500
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEV 253
|
330 340 350
....*....|....*....|....*....|...
gi 795413665 501 ENIYIRSQPVAQIYV-------HGDSLKAFLVG 526
Cdd:cd17638 254 EGALAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-517 |
4.86e-30 |
|
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: 121.23 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESqwaptcaDVHISYLPLAHMFErMVQSVVYC--HGGRV 268
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTEQ-------DRLCIPVPLFHCFG-SVLGVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 GFFQgdirlLSDDMKAL--------C------PTIFPvvpRLLNRMydkifSQANTPLKRwllefaakrkqaeVRSGIIr 334
Cdd:cd05917 73 VFPS-----PSFDPLAVleaiekekCtalhgvPTMFI---AELEHP-----DFDKFDLSS-------------LRTGIM- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 335 ndsiwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAP 410
Cdd:cd05917 126 --------------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 411 LPCNHIKLVDvEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkL 489
Cdd:cd05917 180 MPHTEAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-I 257
|
330 340
....*....|....*....|....*...
gi 795413665 490 AQGEYVAPEKIENIYIRSQPVAQIYVHG 517
Cdd:cd05917 258 RGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
193-537 |
1.33e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 121.87 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHIS--YLPLAHmfermvqsvvyc 263
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVnllLWMQEAYPLTPGdrvlQFTSFSFDVSVWeiFGALLA------------ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 264 hGGRVGFFQGDIRLLSDDMKALC----PTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsgiirndsiw 339
Cdd:cd05930 159 -GATLVVLPEEVRKDPEALADLLaeegITVLHLTPSLLRLLLQELELAALPSL--------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 delffnkiqaslggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCN 414
Cdd:cd05930 211 ----------------RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 415 HIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA-----LDSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFK 488
Cdd:cd05930 275 RVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVK 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 489 LAqGEYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 537
Cdd:cd05930 354 IR-GYRIELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
196-533 |
1.70e-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: 121.24 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTHGNVVadFSGflKVTESQWAPTCADVHISYLPLAHM---FERMVQSVVycHGGRV---- 268
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLT--FAG--YYSARRFGLGEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 ----GFFQGDIRllsdDMKALCPTIFPVVPRLLnrmydkiFSQANTPlkrwllefaaKRKQAEVRsgiirndsiwdelff 344
Cdd:cd05934 156 rfsaSRFWSDVR----RYGATVTNYLGAMLSYL-------LAQPPSP----------DDRAHRLR--------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 345 nkiqaslggcvrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEel 424
Cdd:cd05934 200 --------------AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 425 NYWACKGE-GEICVR---GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKI 500
Cdd:cd05934 264 GQELPAGEpGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEV 341
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 795413665 501 ENIYIRSQPVAQIYVHG-------DSLKAFlvgIVVPDPE 533
Cdd:cd05934 342 ERAILRHPAVREAAVVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
193-542 |
1.97e-29 |
|
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: 121.40 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTESqwaptcaDVHISYLPLAHMFErmvQSVVY---CHGG 266
Cdd:TIGR01923 109 NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSkenLGFTED-------DNWLLSLPLYHISG---LSILFrwlIEGA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 267 RVGFFQGDIRLLsDDMKALCPTIFPVVPRLLNRMYDKifSQANTPLKRWLLefaakrkqaevrsgiirndsiwdelffnk 346
Cdd:TIGR01923 179 TLRIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNENLRKILL----------------------------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 347 iqaslGGcvrmivtGAAPASptvlgFLRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDVE 422
Cdd:TIGR01923 227 -----GG-------SAIPAP-----LIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 423 ElnywackGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 502
Cdd:TIGR01923 290 E-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIET 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 795413665 503 IYIRSQPVAQIYV--HGDSL-----KAFLVGIVVPDPEVMPSWAQKR 542
Cdd:TIGR01923 361 VLYQHPGIQEAVVvpKPDAEwgqvpVAYIVSESDISQAKLIAYLTEK 407
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
169-484 |
4.45e-29 |
|
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: 121.62 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 169 ALELSATSSIQDCGqENHHAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflKVTESQWAPtcADVHISYLP 248
Cdd:cd05906 143 GIRVLSIEELLDTA-ADHDLP-QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 249 LAHmfermVQSVVYCHggrvgffQGDIRLLSDDMKALCPTIFPVVPRLLNRMyDKiFSQANTplkrWLLEFA-AK-RKQA 326
Cdd:cd05906 217 LDH-----VGGLVELH-------LRAVYLGCQQVHVPTEEILADPLRWLDLI-DR-YRVTIT----WAPNFAfALlNDLL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 327 EVRSgiirnDSIWDelffnkiqasLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP-- 399
Cdd:cd05906 279 EEIE-----DGTWD----------LSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfp 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 400 -GDWTSGH----VGAPLPCNHIKLVDVEElnywACKGEGEIC---VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkW 471
Cdd:cd05906 344 tYDHSQALefvsLGRPIPGVSMRIVDDEG----QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-F 418
|
330
....*....|...
gi 795413665 472 LPAGTLKVIDRKK 484
Cdd:cd05906 419 LDNGNLTITGRTK 431
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
192-515 |
1.48e-28 |
|
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: 118.64 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 192 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvtesQWAPTCADVHISYLPLAHmfermvqsvvycHGGRVGFF 271
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAE----RLGLGPGDVFLVASPMAH------------QTGFVYGF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 272 qgdirllsddmkaLCPTIFPVvPRLLNRMYDK------------IFSQANTPLKRWLLEfaAKRKQAEVRSGIirndsiw 339
Cdd:cd05903 154 -------------TLPLLLGA-PVVLQDIWDPdkalalmrehgvTFMMGATPFLTDLLN--AVEEAGEPLSRL------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 delffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNH 415
Cdd:cd05903 211 ----------------RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 416 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYV 495
Cdd:cd05903 273 IKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENI 349
|
330 340
....*....|....*....|
gi 795413665 496 APEKIENIYIRSQPVAQIYV 515
Cdd:cd05903 350 PVLEVEDLLLGHPGVIEAAV 369
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
188-540 |
2.33e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 119.56 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWA-PTCADVHISYLPLAHMFermvqsvvychgG 266
Cdd:PLN02574 192 KPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIY------------G 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 267 RVGFFQGDIRL-----------LSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKrwllefaakrkqaevrsgi 332
Cdd:PLN02574 259 LSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPILMALTKKAKGVCGEVLK------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 333 irndsiwdelffnkiqaslggCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGA 409
Cdd:PLN02574 320 ---------------------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 410 PLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKL 489
Cdd:PLN02574 379 LAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 795413665 490 aQGEYVAPEKIENIYIrSQP----VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQ 540
Cdd:PLN02574 459 -KGFQIAPADLEAVLI-SHPeiidAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA 511
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
182-525 |
2.51e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 119.54 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTeSQWAP-------TCADVHISYLPLAHMFE 254
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACL-SQLGPdgqplmkEGQEVMIAPLPLYHIYA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 255 RMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkifsqaNTplkrwllEFAAKRKQAEVRSgiir 334
Cdd:PRK12492 273 FTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGL------------NT-------LFVALMDHPGFKD---- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 335 ndsiwdeLFFNKIQASLGGcvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPC 413
Cdd:PRK12492 330 -------LDFSALKLTNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 414 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGE 493
Cdd:PRK12492 395 TALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGF 472
|
330 340 350
....*....|....*....|....*....|....*....
gi 795413665 494 YVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 525
Cdd:PRK12492 473 NVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
195-533 |
2.58e-28 |
|
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: 119.17 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTCAdvHISYLPLAHMFERMVQSVVYCHGGRVGF--- 270
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIfGNQIIPDTA--ILTVIPFHHGFGMFTTLGYLICGFRVVLmyk 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 271 FQGD--IRLLSD---DMKALCPTIFPVVPR--LLNRmYD----KIFSQANTPLKRWLLEFAAKRkqaevrsgiirndsiw 339
Cdd:cd17642 262 FEEElfLRSLQDykvQSALLVPTLFAFFAKstLVDK-YDlsnlHEIASGGAPLSKEVGEAVAKR---------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 delfFNkiqaslggcvrmivtgaapasptvLGFLRaalgcqvyEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLV 419
Cdd:cd17642 325 ----FK------------------------LPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEK 499
Cdd:cd17642 369 DLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAE 447
|
330 340 350
....*....|....*....|....*....|....
gi 795413665 500 IENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDPE 533
Cdd:cd17642 448 LESILLQ---------HPKIFDAGVAGI--PDED 470
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
188-533 |
7.58e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 117.22 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPP-QPDDLSIVCFTSGTTGNPKGAMLTHGN---VVADFSGFLKVtesqwaptcaDVHISYLPLAHMFE--RMVQSV- 260
Cdd:PRK09088 127 ADTPSiPPERVSLILFTSGTSGQPKGVMLSERNlqqTAHNFGVLGRV----------DAHSSFLCDAPMFHiiGLITSVr 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 -VYCHGGRV----GFFQG-DIRLLSDdmKALCPTIFPVVPRLLNRmydkifsqantplkrwllefaakrkqaevrsgiIR 334
Cdd:PRK09088 197 pVLAVGGSIlvsnGFEPKrTLGRLGD--PALGITHYFCVPQMAQA---------------------------------FR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 335 NDSIWDELFFNKIQAslggcvrmIVTGAAP-ASPTVLGFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVG 408
Cdd:PRK09088 242 AQPGFDAAALRHLTA--------LFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 409 APLPCNHIKLVDVEELNYWAckGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIF 487
Cdd:PRK09088 310 IPTPTVQTRVVDDQGNDCPA--GVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 795413665 488 kLAQGEYVAPEKIEniyirsqpvAQIYVHGDSLKAFLVGivVPDPE 533
Cdd:PRK09088 388 -ISGGENVYPAEIE---------AVLADHPGIRECAVVG--MADAQ 421
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
182-532 |
1.90e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 116.51 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHISYLPLAHMFERMVQS-V 260
Cdd:PRK07514 143 AAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN----ALTLVDYWRFTPDDVLIHALPIFHTHGLFVATnV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 VYCHGGRVGFFQgdiRLLSDDMKALCP--TIFPVVPRLLNRMYdkifsqANTPLKRwllEFAAKrkqaevrsgiirndsi 338
Cdd:PRK07514 219 ALLAGASMIFLP---KFDPDAVLALMPraTVMMGVPTFYTRLL------QEPRLTR---EAAAH---------------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 339 wdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNHI 416
Cdd:PRK07514 271 ----------------MRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 417 KLVDVE---ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIfkLAQG 492
Cdd:PRK07514 333 RVTDPEtgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISG 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 795413665 493 EY-VAPEKIENiYIRSQP-VAQIYVHGDSLKAF---LVGIVVPDP 532
Cdd:PRK07514 407 GYnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
188-503 |
2.24e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 116.77 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcaDVHISYLPLAHmfermvqSVVYCHGGR 267
Cdd:PRK06087 180 TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ----DVFMMPAPLGH-------ATGFLHGVT 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGFFQGDIRLLSDDMKAlcptifPVVPRLLNRmyDKI-FSQANTPLkrwllefaakrkqaevrsgiirndsIWDELFFNK 346
Cdd:PRK06087 249 APFLIGARSVLLDIFTP------DACLALLEQ--QRCtCMLGATPF-------------------------IYDLLNLLE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 347 IQASLGGCVRMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDv 421
Cdd:PRK06087 296 KQPADLSALRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 422 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIE 501
Cdd:PRK06087 371 EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVE 449
|
..
gi 795413665 502 NI 503
Cdd:PRK06087 450 DI 451
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
192-540 |
2.31e-27 |
|
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: 114.75 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 192 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTES-QWAPTCADVHISYLPLahmferMVQSVVYchGGR 267
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTEDdNWLCALPLFHISGLSI------LMRSVIY--GMT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLefaakrkqaevrsgiirndsiwdelffnk 346
Cdd:cd05912 146 VYLVDKfDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL----------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 347 iqaslggcvrmivtGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDVEE 423
Cdd:cd05912 197 --------------GGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 424 LNYwackGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENI 503
Cdd:cd05912 261 PPY----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEV 334
|
330 340 350
....*....|....*....|....*....|....*..
gi 795413665 504 YIRSQPVAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 540
Cdd:cd05912 335 LLSHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
184-505 |
1.40e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 113.92 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 184 ENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHISYLPLAHMFErmVQSVVYC 263
Cdd:PLN02246 168 ENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLC 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 264 hGGRVG--------FfqgDIRLLSDDMKALCPTIFPVVPrllnrmydkifsqantPLkrwLLEFAakrKQAEVRSgiirn 335
Cdd:PLN02246 246 -GLRVGaailimpkF---EIGALLELIQRHKVTIAPFVP----------------PI---VLAIA---KSPVVEK----- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 336 dsiwDELffnkiqASlggcVRMIVTGAAPASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGH 406
Cdd:PLN02246 295 ----YDL------SS----IRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 407 VGAPLPCNHIKLVDVE---ELNYWACkgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRK 483
Cdd:PLN02246 358 CGTVVRNAELKIVDPEtgaSLPRNQP---GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRL 434
|
330 340
....*....|....*....|..
gi 795413665 484 KHIFKLaQGEYVAPEKIENIYI 505
Cdd:PLN02246 435 KELIKY-KGFQVAPAELEALLI 455
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-537 |
1.88e-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: 112.92 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 190 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTESQWAPTCADVHISY-LPLAHMFERMVQSVVYCHG 265
Cdd:cd05922 112 HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITADDRALTVLPLSYDYgLSVLNTHLLRGATLVLTND 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 266 GRVGffqgdiRLLSDDMKALCPTIFPVVP---RLLNRMydkIFSQANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdel 342
Cdd:cd05922 192 GVLD------DAFWEDLREHGATGLAGVPstyAMLTRL---GFDPAKLPSLRYLTQAGGRLPQETIAR------------ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 343 ffnkiqaslggcvrmivtgaapasptvlgfLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIklv 419
Cdd:cd05922 251 ------------------------------LRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIPGGEF--- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DVEELNYWACK-GE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFKLAqGEYVA 496
Cdd:cd05922 298 EILDDDGTPTPpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLA-RRDEdGFLFIVGRRDRMIKLF-GNRIS 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 795413665 497 PEKIENIyIRSQP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 537
Cdd:cd05922 376 PTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
187-537 |
1.97e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.78 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 187 HAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtESQWAPTCADVHISYLPLAHMfermvqsvvycHG- 265
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHV-----------HGl 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 266 -----------GRV---GFF--QGDIRLLSDDmkalcPTIFPVVPRllnrMYDKIfsqantplkrwllefAAKRKQAEVR 329
Cdd:PRK07787 185 vlgvlgplrigNRFvhtGRPtpEAYAQALSEG-----GTLYFGVPT----VWSRI---------------AADPEAARAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 330 SGiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA 409
Cdd:PRK07787 241 RG-----------------------ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 410 PLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDR----- 482
Cdd:PRK07787 298 PLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdl 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 795413665 483 -KKHIFKLAQGEyvapekIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 537
Cdd:PRK07787 377 iKSGGYRIGAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
196-515 |
3.43e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 113.15 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHIsyLPLAHMF--ERMVQSVVYCHGGRVGFFQG 273
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTLGL--IPFFHIYgiTGICCATLRNKGKVVVMSRF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 DIRLLSDDMKALCPTIFPVVPrllnrmydkifsqantPLKRWLLEfaakrkqaevrsgiirnDSIWDELFFNKIQaslgg 353
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVP----------------PIILNLVK-----------------NPIVEEFDLSKLK----- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 354 cVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDVEELN 425
Cdd:PLN02330 305 -LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGR 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 426 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYI 505
Cdd:PLN02330 382 SLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILL 460
|
330
....*....|
gi 795413665 506 RSQPVAQIYV 515
Cdd:PLN02330 461 THPSVEDAAV 470
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
170-509 |
1.70e-25 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 109.28 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 170 LELSATSSIQDCGQENHhAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPL 249
Cdd:TIGR01733 96 LDPLELAALDDAPAPPP-PDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 250 AH------MFermvqsVVYCHGGRVgffqgdiRLLSDDMKAlcpTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEfaakr 323
Cdd:TIGR01733 171 SFdasveeIF------GALLAGATL-------VVPPEDEER---DDAALLAALIAEHPVTVLNLTPSLLALLAAA----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 324 kqaevrsgiirndsiwdelffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGD 401
Cdd:TIGR01733 230 ------------------------LPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 402 WTSGHV----GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA-LDSDGWL-------HTGDIG 469
Cdd:TIGR01733 286 DAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLV 364
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 795413665 470 KWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP 509
Cdd:TIGR01733 365 RYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAA-LLRHP 402
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
190-525 |
5.50e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 109.35 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 190 VPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflKVTESQWAPTCAD---VHISYLPLAHMF-ERMVQSVVYCH 264
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN-----TLMGVQWLYNCKEgeeVVLGVLPFFHVYgMTAVMNLSIMQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 265 GGRVGFF-QGDIRLLSDDMKALCPTIFPVVPRLLnrmydkiFSQANTPLkrwllefaakRKQAEVRSgiirndsiwdelf 343
Cdd:PRK06710 275 GYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIY-------IALLNSPL----------LKEYDISS------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 344 fnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHIKL 418
Cdd:PRK06710 325 -----------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEAMI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 419 VDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPE 498
Cdd:PRK06710 390 MSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPR 467
|
330 340 350
....*....|....*....|....*....|....
gi 795413665 499 KIENIYIRSQPVAQIYV-------HGDSLKAFLV 525
Cdd:PRK06710 468 EVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
193-517 |
6.78e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 109.09 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTESqwaptcaDVHISYLPLAHMFErMVQSVVYC--HGGR 267
Cdd:PRK12583 199 DRDDPINIQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLYHCFG-MVLANLGCmtVGAC 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGF----FQGDIRLLSDDMKAlCPTIFPVvPRLLnrmydkiFSQANTPlKRWLLEFAAkrkqaeVRSGIIrndsiwdelf 343
Cdd:PRK12583 271 LVYpneaFDPLATLQAVEEER-CTALYGV-PTMF-------IAELDHP-QRGNFDLSS------LRTGIM---------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 344 fnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAPLPCNHIK 417
Cdd:PRK12583 325 -----------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRTQPHLEVK 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 418 LVDVEELNywACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVA 496
Cdd:PRK12583 386 VVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIY 462
|
330 340
....*....|....*....|.
gi 795413665 497 PEKIENIYIRSQPVAQIYVHG 517
Cdd:PRK12583 463 PREIEEFLFTHPAVADVQVFG 483
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
191-531 |
1.85e-24 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 106.62 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 191 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTESQ----------WAptCADVHISYLplahmfermv 257
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLnyVSQPPArLDVGPGSrvaqvlsiafDA--CIGEIFSTL---------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 258 qsvvyCHGGRVgFFQGDIRLLSDDMKALcpTIFPVVPRLLNRMYDKIFSQantplkrwllefaakrkqaevrsgiirnds 337
Cdd:cd17653 169 -----CNGGTL-VLADPSDPFAHVARTV--DALMSTPSILSTLSPQDFPN------------------------------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 338 iwdelffnkiqaslggcVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNH 415
Cdd:cd17653 211 -----------------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNST 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 416 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKVIDRKKHIFKL 489
Cdd:cd17653 270 CYILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 795413665 490 aQGEYVAPEKIENIYIRSQPVAQ---IYVHGDSLKAFlvgiVVPD 531
Cdd:cd17653 349 -RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
196-533 |
2.28e-24 |
|
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: 104.27 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEsqwaptcADVHISYLPLAHMFERMVQSVVYCHGGR---VG 269
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 270 FFQGDIRL-LSDDMKAlcpTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRSgiIRNdsiwdelffnkiq 348
Cdd:cd17637 74 KFDPAEALeLIEEEKV---TLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 349 aslggcvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWA 428
Cdd:cd17637 119 ----------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 429 CKGE-GEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRK--KHIFKlAQGEYVAPEKIENIyI 505
Cdd:cd17637 184 PAGEtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV-I 260
|
330 340
....*....|....*....|....*....
gi 795413665 506 RSQP-VAQIYVHGdslkaflvgivVPDPE 533
Cdd:cd17637 261 LEHPaIAEVCVIG-----------VPDPK 278
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
195-542 |
2.71e-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: 106.02 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvtESQWAP-TCADVHISYLPLAHM--FERMVQSVVYCHGGRVGFF 271
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQ-----SAVWTGlTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 272 QGDIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnKIQASL 351
Cdd:cd05935 159 RWDRETALELIEKYKVTFWTNIPTMLVDL-------LATP----------------------------------EFKTRD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 352 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG 431
Cdd:cd05935 198 LSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 432 EGEICVRGPNVFKGYLKDPDRTKEALDSDG---WLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQ 508
Cdd:cd05935 278 VGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHP 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 795413665 509 PVAQIYV-------HGDSLKAFLVgiVVP------DPEVMPSWAQKR 542
Cdd:cd05935 357 AI*EVCVisvpderVGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
188-484 |
5.28e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 106.58 E-value: 5.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTESQWAPTcaDVHISYLPLAHMFERMVQSVVYCHGGR 267
Cdd:PRK07529 206 SGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWLGALLLGLGPG--DTVFCGLPLFHVNALLVTGLAPLARGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 ---VGFFQG--DIRLLSDDMK---ALCPTIFPVVPRLLNRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiw 339
Cdd:PRK07529 282 hvvLATPQGyrGPGVIANFWKiveRYRINFLSGVPTVYAAL-------LQVP---------------------------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 delffnkIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKL 418
Cdd:PRK07529 327 -------VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRV 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 419 VDVEEL-NYW--ACKGE-GEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK 484
Cdd:PRK07529 400 VILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
193-533 |
5.35e-24 |
|
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: 105.70 E-value: 5.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvtesqwapTCADVHISYLPL----------AHMFERMVQSVVY 262
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALS----------------TSALAHGRALGLtsesrvlqfaSYTFDVSILEIFT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 263 --CHGG---------RVGFFQGDIRllsdDMKALCPTIFPVVPRLLNRmydkifsqANTPlkrwllefaakrkqaevrsg 331
Cdd:cd05918 168 tlAAGGclcipseedRLNDLAGFIN----RLRVTWAFLTPSVARLLDP--------EDVP-------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 332 iirndsiwdelffnkiqaslggCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAP 410
Cdd:cd05918 216 ----------------------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 411 LPC--------NHIKLVDVeelnywackGE-GEICVRGPNVFKGYLKDPDRTKEA-LDSDGWLH------------TGDI 468
Cdd:cd05918 272 LGAtcwvvdpdNHDRLVPI---------GAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDL 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795413665 469 GKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENiYIRSQP------VAQIYVH-GDSLKAFLVGIVVPDPE 533
Cdd:cd05918 343 VRYNPDGSLEYVGRKDTQVKI-RGQRVELGEIEH-HLRQSLpgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
190-525 |
1.71e-23 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 104.38 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 190 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkvTESQWAPTCADVHISYLPLAHMFermvqsvvychggrvg 269
Cdd:PRK08008 168 PPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYY--SAWQCALRDDDVYLTVMPAFHID---------------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 270 fFQgdirllsddmkalCPTIFPVvprllnrmydkiFSQANTPLkrwLLE-FAAKRKQAEVRsgiirndsiwdelffnKIQ 348
Cdd:PRK08008 228 -CQ-------------CTAAMAA------------FSAGATFV---LLEkYSARAFWGQVC----------------KYR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 349 ASLGGCVRMIVTG--AAPASPT--------VLGFLRAA----------LGCQVYEGYGQTECTAGCTFTTPGD---WTSg 405
Cdd:PRK08008 263 ATITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 406 hVGAPLPCNHIKLVDveELNYWACKGE-GEICVRG---PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVID 481
Cdd:PRK08008 342 -IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVD 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 482 RKKHIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHG--DSL-----KAFLV 525
Cdd:PRK08008 419 RRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
161-496 |
3.33e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 104.19 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 161 WSRSMTPWAlELSATSSIQDCgqENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGFLKVTESq 234
Cdd:PRK08180 180 PGRAATPFA-ALLATPPTAAV--DAAHAAV--GPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPP- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 235 waptcadVHISYLPLAHMF--ERMVQSVVYcHGGR---------VGFFQGDIRLLsddmKALCPTIFPVVPRLlnrmydk 303
Cdd:PRK08180 254 -------VLVDWLPWNHTFggNHNLGIVLY-NGGTlyiddgkptPGGFDETLRNL----REISPTVYFNVPKG------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 304 ifsqantplkrWLLEFAAKRKQAEVRsgiirndsiwdELFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGC 379
Cdd:PRK08180 315 -----------WEMLVPALERDAALR-----------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 380 QVY--EGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEelnywackGEGEICVRGPNVFKGYLKDPDRTKEAL 457
Cdd:PRK08180 365 RIRmmTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAF 436
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 795413665 458 DSDGWLHTGDIGKWL----PAGTLKVIDRKKHIFKLAQGEYVA 496
Cdd:PRK08180 437 DEEGYYRSGDAVRFVdpadPERGLMFDGRIAEDFKLSSGTWVS 479
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
194-534 |
8.12e-23 |
|
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: 101.55 E-value: 8.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPLAhmFERMVQSVVYC--HGGrvgff 271
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDLYPAlaSGA----- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 272 qgdirllsddmkalcpTIFPVvPRLLNRMYDKIFSQ-ANTPLKRWLlefaakrkqaevrsgiiRNDSIWDELF----FNk 346
Cdd:cd05945 165 ----------------TLVPV-PRDATADPKQLFRFlAEHGITVWV-----------------STPSFAAMCLlsptFT- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 347 iQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDv 421
Cdd:cd05945 210 -PESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 422 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD---GWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPE 498
Cdd:cd05945 288 EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELE 366
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 795413665 499 KIENIYIRSQPVAQIYV----HGDSlKAFLVGIVVPDPEV 534
Cdd:cd05945 367 EIEAALRQVPGVKEAVVvpkyKGEK-VTELIAFVVPKPGA 405
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
189-542 |
8.36e-23 |
|
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: 103.78 E-value: 8.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTES----QWAPTCADVHIS--YLPLahmfermvqs 259
Cdd:COG1020 611 PVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGPGdrvlQFASLSFDASVWeiFGAL---------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 260 vvyCHGGRVGFFQGDIRLLSDDMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKRKQAEVRsgiirn 335
Cdd:COG1020 681 ---LSGATLVLAPPEARRDPAALAELLarhrVTVLNLTPSLLRALLD-----------------AAPEALPSLR------ 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 336 dsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPL 411
Cdd:COG1020 735 --------------------LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPI 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 412 PCNHIKLVDvEELN---YWACkgeGEICVRGPNVFKGYLKDPDRTKEA-----LDSDG--WLHTGDIGKWLPAGTLKVID 481
Cdd:COG1020 795 ANTRVYVLD-AHLQpvpVGVP---GELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLG 870
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795413665 482 RKKHifklaQ----------GEyvapekIENIyIRSQP-VAQIYV--HGDSL-KAFLVGIVVPDPEVMPSWAQKR 542
Cdd:COG1020 871 RADD-----QvkirgfrielGE------IEAA-LLQHPgVREAVVvaREDAPgDKRLVAYVVPEAGAAAAAALLR 933
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
192-532 |
2.19e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 101.28 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 192 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwaptcaDVHISYLPLAHMfermvqsvvychggrV 268
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANivpYAERLGLGAD-------DVILMASPMAHQ---------------T 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 GFFQGDIRLLSDDMKALCPTIFPVVprllnRMYDKI------FSQANTPlkrWLLEFAakRKQAEVRSGIirndsiwdel 342
Cdd:PRK13295 252 GFMYGLMMPVMLGATAVLQDIWDPA-----RAAELIrtegvtFTMASTP---FLTDLT--RAVKESGRPV---------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 343 ffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLV 419
Cdd:PRK13295 312 ------SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTkeALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEK 499
Cdd:PRK13295 381 D-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVE 456
|
330 340 350
....*....|....*....|....*....|....
gi 795413665 500 IENIYIRSQPVAQiyvhgdslkaflVGIV-VPDP 532
Cdd:PRK13295 457 IEALLYRHPAIAQ------------VAIVaYPDE 478
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
169-533 |
6.73e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 99.55 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 169 ALELSATSSIQ------DCGQENHHAP---VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfsgFLKVTESQWAP-- 237
Cdd:PRK06839 114 ALSMQKVSYVQrvisitSLKEIEDRKIdnfVEKNESASFIICYTSGTTGKPKGAVLTQENM------FWNALNNTFAIdl 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 238 TCADVHISYLPLAHMfermvqsvvychgGRVGFFQgdirllsddmkalCPTIFP----VVPRLLNRmyDKIFSQANTplK 313
Cdd:PRK06839 188 TMHDRSIVLLPLFHI-------------GGIGLFA-------------FPTLFAggviIVPRKFEP--TKALSMIEK--H 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 314 RWLLEFAAKRKQAEVRSGIIRNDSIWDElffnkiqaslggcVRMIVTGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTA 392
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCSKFETTNLQS-------------VRWFYNGGAPCPeELMREFIDR--GFLFGQGFGMTE-TS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 393 GCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIG 469
Cdd:PRK06839 302 PTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLA 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795413665 470 KWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 533
Cdd:PRK06839 380 RVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV---------INKLSDVYEVAVVG--RQHVK 431
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
182-517 |
7.53e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 99.27 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQP-DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTESQ-WapTCAdvhisyLPLAHM--FE 254
Cdd:PRK03640 127 GPKEEAEIQEEFDlDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSalnLGLTEDDcW--LAA------VPIFHIsgLS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 255 RMVQSVVYchGGRV----GFFQGDI-RLLSDDMKalcpTIFPVVPRLLNRMYDKIfSQANTPlkrwllefaakrkqaevr 329
Cdd:PRK03640 199 ILMRSVIY--GMRVvlveKFDAEKInKLLQTGGV----TIISVVSTMLQRLLERL-GEGTYP------------------ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 330 sgiirnDSiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GH 406
Cdd:PRK03640 254 ------SS-----------------FRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 407 VGAPL-PCNhIKLVDveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKH 485
Cdd:PRK03640 309 AGKPLfPCE-LKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSD 384
|
330 340 350
....*....|....*....|....*....|..
gi 795413665 486 IFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 517
Cdd:PRK03640 385 LI-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
187-540 |
1.01e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 98.90 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 187 HAPVPP--QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvTESQWAPtcadvHISYL---PLAHMFERMVQSVV 261
Cdd:PRK06188 158 PAPLVAaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQL--AEWEWPA-----DPRFLmctPLSHAGGAFFLPTL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 262 YchggRVGFFqgdIRLLSDDMKALCPTI--------FpVVPRLLNRmydkifsqantplkrwLLEFAAKRKqaevrsgii 333
Cdd:PRK06188 231 L----RGGTV---IVLAKFDPAEVLRAIeeqritatF-LVPTMIYA----------------LLDHPDLRT--------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 334 RNDSiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------ 407
Cdd:PRK06188 278 RDLS------------SL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltsc 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 408 GAPLPCNHIKLVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHI 486
Cdd:PRK06188 342 GRPTPGLRVALLD-EDGREVA-QGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDM 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795413665 487 FkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 540
Cdd:PRK06188 419 I-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
191-501 |
2.49e-21 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 99.23 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 191 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD---FSGFLKVTESqwaptcaDVHISYLPLAHMFERMVQ--------- 258
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNieqISDVFNLRND-------DVILSSLPFFHSFGLTVTlwlpllegi 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 259 SVVYcH-----GGRVGffqgdirLLSDDMKA--LC--PTIFpvvprllnRMYdkifsqantplkrwllefaakrkqaevr 329
Cdd:PRK08633 851 KVVY-HpdptdALGIA-------KLVAKHRAtiLLgtPTFL--------RLY---------------------------- 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 330 sgiIRNDSIWDELFfnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWT- 403
Cdd:PRK08633 887 ---LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRq 954
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 404 ----SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL---DSDGWLHTGDIGKWLPAGT 476
Cdd:PRK08633 955 tgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGF 1034
|
330 340
....*....|....*....|....*
gi 795413665 477 LKVIDRKKHIFKLAqGEYVAPEKIE 501
Cdd:PRK08633 1035 LTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-511 |
5.19e-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: 94.85 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTESQWAPTcaDVHISYLPLAHMFERMVQsvvychgGRVGFFQG 273
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDPD--DVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaAKRKQAEVRSGIirndsiwdelffnkiqaslgG 353
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 354 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DVEELNYWACK 430
Cdd:cd05944 122 SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 431 GE--GEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQ 508
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
...
gi 795413665 509 PVA 511
Cdd:cd05944 280 AVA 282
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
182-471 |
6.33e-21 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 96.72 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLK----VTESQ--WAPtcADV----HISYL---P 248
Cdd:COG0365 171 AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyvldLKPGDvfWCT--ADIgwatGHSYIvygP 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 249 LAH-----MFERmvqSVVYCHGGRvgFFQgdirlLSDDMKalcPTIFPVVPRLLnRMydkifsqantpLKRWLLEFAAKR 323
Cdd:COG0365 249 LLNgatvvLYEG---RPDFPDPGR--LWE-----LIEKYG---VTVFFTAPTAI-RA-----------LMKAGDEPLKKY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 324 KQAevrsgiirndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaGCTFTTPGDWT 403
Cdd:COG0365 304 DLS-----------------------SL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--GGIFISNLPGL 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795413665 404 S---GHVGAPLPCNHIKLVDvEELNywACKG--EGEICVRG--PNVFKGYLKDPDRTKEAL--DSDGWLHTGDIGKW 471
Cdd:COG0365 355 PvkpGSMGKPVPGYDVAVVD-EDGN--PVPPgeEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARR 428
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
171-620 |
6.57e-21 |
|
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: 96.73 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 171 ELSATSSIQDCgqENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtesQWAPTCAD---VHISYL 247
Cdd:cd05921 145 ELAATPPTAAV--DAAFAAV--GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLE-----QTYPFFGEeppVLVDWL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 248 PLAHMF--ERMVQSVVYcHGGRV---------GFFQGDIRLLSDDMkalcPTIFPVVPrllnrmydkifsqantplKRWl 316
Cdd:cd05921 216 PWNHTFggNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVP------------------AGW- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 317 lefaakrkqaEVRSGIIRNDSIWDELFFNKiqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTEC 390
Cdd:cd05921 272 ----------EMLVAALEKDEALRRRFFKR--------LKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATET 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 391 TAGCTFTTPGDWTSGHVGAPLPCNHIKLVdveelnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGK 470
Cdd:cd05921 334 APTATFTHWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 471 WL----PAGTLKVIDRKKHIFKLAQGEYVA--PekieniyIRSQPVAQI--YVHgDSL-----KAFLVGIVVPDPEVMPs 537
Cdd:cd05921 406 LAdpddPAKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDLLACR- 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 538 wAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIhIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIE 617
Cdd:cd05921 477 -RLVGLQEASDAEVLRHAKVRAAFRDRLAALNGEATGSSSRIARAL-LLDEPPSIDKGEITDKGYINQRAVLERRAALVE 554
|
...
gi 795413665 618 ELY 620
Cdd:cd05921 555 RLY 557
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
195-525 |
6.67e-21 |
|
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: 95.48 E-value: 6.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGnvvadfsgflkvtesqwaptcadvhisyLPLAHMfermvQSVVYCHGGRvgffQGD 274
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHS----------------------------YPLGHI-----PTAAYWLGLR----PDD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 275 IRLLSDD----MKALCPTIFPV---VPRLLN--------RMYDKI-------FSQANTPLKRWLLEFAAKRKQAEVRSgi 332
Cdd:cd05972 124 IHWNIADpgwaKGAWSSFFGPWllgATVFVYegprfdaeRILELLerygvtsFCGPPTAYRMLIKQDLSSYKFSHLRL-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 333 irndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLP 412
Cdd:cd05972 202 -------------------------VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 413 CNHIKLVDvEELNYWACKGEGEICVRGPNV--FKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlA 490
Cdd:cd05972 257 GYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-S 333
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 795413665 491 QGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 525
Cdd:cd05972 334 SGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
191-533 |
7.99e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 96.65 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 191 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPtcaDVHISYLPlahMFermvqsvvYCHGGRVGF 270
Cdd:PRK06178 205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGED---SVFLSFLP---EF--------WIAGENFGL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 271 fqgdirllsddmkalcptIFPvvprllnrmydkIFSQANTPL-KRW-LLEFAAKRKQAEVRSGIIRNDSIwDELF----- 343
Cdd:PRK06178 271 ------------------LFP------------LFSGATLVLlARWdAVAFMAAVERYRVTRTVMLVDNA-VELMdhprf 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 344 ----FNKIQASlgGCVRMIvtgaAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAP 410
Cdd:PRK06178 320 aeydLSSLRQV--RVVSFV----KKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLP 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 411 LPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLa 490
Cdd:PRK06178 393 VPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV- 470
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 795413665 491 QGEYVAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGivVPDPE 533
Cdd:PRK06178 471 NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
187-532 |
9.34e-21 |
|
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: 96.16 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 187 HAPVPPQPD----DLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvtesqwaptcadvhisylplahmfermVQSVVY 262
Cdd:cd12119 151 ESPEYDWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLV-----------------------------------LHAMAA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 263 CHGGRVGFFQGDirllsddmkalcpTIFPVVPrllnrMYdkifsQANTplkrWLLEFAA-----------KRKQAEVRSG 331
Cdd:cd12119 196 LLTDGLGLSESD-------------VVLPVVP-----MF-----HVNA----WGLPYAAamvgaklvlpgPYLDPASLAE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 332 IIRND---------SIWDELF--FNKIQASLGGCVRMIVTGAAPASPTVLGFlrAALGCQVYEGYGQTECTAGCTFTTPg 400
Cdd:cd12119 249 LIEREgvtfaagvpTVWQGLLdhLEANGRDLSSLRRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 401 dwTSGHV--------------GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLH 464
Cdd:cd12119 326 --PSEHSnlsedeqlalrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLR 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 465 TGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflvgIVVPDP 532
Cdd:cd12119 402 TGDVATIDEDGYLTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
196-537 |
9.48e-21 |
|
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: 93.55 E-value: 9.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADVHISYLPLAHM--FERMVQSVVycHGGRVGFFQG 273
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG----LHSRLGFGGGDSWLLSLPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 DiRLLSDDMKALCPTIFPVVPRLLNRMYDKifSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslgg 353
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 354 cVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDveelnywack 430
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 431 gEGEICVRGPNVFKGYLKDPdrTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyIRSQP- 509
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAA-LAAHPa 252
|
330 340 350
....*....|....*....|....*....|.
gi 795413665 510 VAQIYVHG---DSLKAFLVGIVVPDPEVMPS 537
Cdd:cd17630 253 VRDAFVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
153-537 |
9.89e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.11 E-value: 9.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 153 PATHIPWWWSRSMTPWALELSATSSIQ-DCGQENHHAPVPPQ---PDDLSIVcFTSGTTGNPKGAMLTHGNVVADFSGFl 228
Cdd:PRK05852 131 EPTTRWWPLTVNVGGDSGPSGGTLSVHlDAATEPTPATSTPEglrPDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAI- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 229 kVTESQWAPtcADVHISYLPLAH---MFERMVQSVVycHGGRV-----GFFQGdiRLLSDDMKALCPTIFPVVPrllnrm 300
Cdd:PRK05852 209 -ITGYRLSP--RDATVAVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--HTFWDDIKAVGATWYTAVP------ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 301 ydkifsqantPLKRWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQ 380
Cdd:PRK05852 276 ----------TIHQILLERAATEPSGRKPAAL-----------------------RFIRSCSAPLTAETAQALQTEFAAP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 381 VYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DVEELNYWACkgeGEICVRGPNVFKGYLKD 449
Cdd:PRK05852 323 VVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPLPAGAV---GEVWLRGTTVVRGYLGD 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 450 PDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAF---LVG 526
Cdd:PRK05852 398 PTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAA 475
|
410
....*....|.
gi 795413665 527 IVVPDPEVMPS 537
Cdd:PRK05852 476 VIVPRESAPPT 486
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
189-501 |
2.03e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.06 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkVTESQWAPTcADVHISYLPLAH-MfermvqsvvychgGR 267
Cdd:PRK07768 146 PVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAM--FVAAEFDVE-TDVMVSWLPLFHdM-------------GM 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGFfqgdirlLSDDMKALC------PTIFPVVPRLLNRMYDKiFSQANTPLKRWLLEFAAKR--KQAEvrsgiirnDSIW 339
Cdd:PRK07768 210 VGF-------LTVPMYFGAelvkvtPMDFLRDPLLWAELISK-YRGTMTAAPNFAYALLARRlrRQAK--------PGAF 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 DElffnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD-------- 401
Cdd:PRK07768 274 DL-----------SSLRFALNGAEPIDPADVedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevd 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 402 ------------WTSGHV------GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWL 463
Cdd:PRK07768 339 adllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWL 416
|
330 340 350
....*....|....*....|....*....|....*...
gi 795413665 464 HTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIE 501
Cdd:PRK07768 417 DTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
188-542 |
6.03e-20 |
|
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: 93.12 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF------------LKVTesqwaPTCADvhIS----YLPLah 251
Cdd:cd12116 119 PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMrerlglgpgdrlLAVT-----TYAFD--ISllelLLPL-- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 252 mfermvqsvvyCHGGRVGFFQGDI----RLLSDDMKALCPTIFpvvprllnrmydkifsQAnTP-LKRWLLefaakrkqa 326
Cdd:cd12116 190 -----------LAGARVVIAPRETqrdpEALARLIEAHSITVM----------------QA-TPaTWRMLL--------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 327 evrsgiirnDSIWDELffnkiqASLggcvRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTS 404
Cdd:cd12116 233 ---------DAGWQGR------AGL----TALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 405 GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTL 477
Cdd:cd12116 291 IPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRL 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795413665 478 KVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 542
Cdd:cd12116 370 EYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
117-517 |
6.19e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 93.71 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 117 LNF-WGLDFSSTIVKHAPISLLVFlhkigqSGSLRSWP----ATHIP-WWW-------SRSMTPWALELSATSSIQdcgq 183
Cdd:PLN02860 87 LNYrWSFEEAKSAMLLVRPVMLVT------DETCSSWYeelqNDRLPsLMWqvflespSSSVFIFLNSFLTTEMLK---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 184 enHHAPVPPQ------PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfSGFLKVTESQWAPTcaDVHISYLPLAH------ 251
Cdd:PLN02860 157 --QRALGTTEldyawaPDDAVLICFTSGTTGRPKGVTISHSALIV--QSLAKIAIVGYGED--DVYLHTAPLCHigglss 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 252 -MFERMVQSvvyCHggrVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrMYDkifsqantplkrwLLEFAAKRKqaevrs 330
Cdd:PLN02860 231 aLAMLMVGA---CH---VLLPKFDAKAALQAIKQHNVTSMITVPAM---MAD-------------LISLTRKSM------ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 331 giirndsIWDElffnkiqaslGGCVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-- 403
Cdd:PLN02860 283 -------TWKV----------FPSVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTle 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 404 ---------------SGH------VGAPLPcnHIKLvdveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW 462
Cdd:PLN02860 342 spkqtlqtvnqtkssSVHqpqgvcVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGW 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 795413665 463 LHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 517
Cdd:PLN02860 416 LDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
187-503 |
1.10e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 92.92 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 187 HAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEsqwAPTCADVHISYLPLAHMfeRMVQSVVychgg 266
Cdd:PRK07786 166 HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFHI--AGIGSML----- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 267 rVGFFQGdirllsddmkalCPT-IFPVVPRLLNRMYDkifsqantplkrwLLEfaakrkqAEVRSGIIRNDSIWDELFFN 345
Cdd:PRK07786 236 -PGLLLG------------APTvIYPLGAFDPGQLLD-------------VLE-------AEKVTGIFLVPAQWQAVCAE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 346 KIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDv 421
Cdd:PRK07786 283 QQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVAARVVD- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 422 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIE 501
Cdd:PRK07786 361 ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVE 438
|
..
gi 795413665 502 NI 503
Cdd:PRK07786 439 NV 440
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
194-545 |
2.76e-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: 90.95 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTH----GNVVADF--------SGFLKVTESQWAPTCA--DVHISYL----P-LAHMFE 254
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQfpfnlfprDGDLYWTPADWAWIGGllDVLLPSLyfgvPvLAHRMT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 255 RmvqsvvychggrvgfFQGD--IRLLSD---DMKALCPTIFpvvprllnrmydKIFSQANTPLKRWLLEfaakrkqaevr 329
Cdd:cd05971 167 K---------------FDPKaaLDLMSRygvTTAFLPPTAL------------KMMRQQGEQLKHAQVK----------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 330 sgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGH 406
Cdd:cd05971 209 -------------------------LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 407 VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPN--VFKGYLKDPDRTKEALDSDgWLHTGDIGKWLPAGTLKVIDRKK 484
Cdd:cd05971 262 MGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDD 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 485 HIFKLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPEVMPSWAQKRGIE 545
Cdd:cd05971 340 DVITSS-GYRIGPAEIEECLLKHPAVLMAAVvgipdpiRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
189-543 |
3.35e-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: 90.87 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV-------ADFSGFLKVTESQWAPTCADVhisylplahmferMVQSV- 260
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAnlvawqaRASSLGPGARTLQFAGLGFDV-------------SVQEIf 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 -VYCHGGRVGFFQGDIRLLSDDMKALCPTifpvvpRLLNRMYdkifsqANTPLKRWLLEfAAKRKQAEvrsgiirndsiw 339
Cdd:cd17651 197 sTLCAGATLVLPPEEVRTDPPALAAWLDE------QRISRVF------LPTVALRALAE-HGRPLGVR------------ 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 delffnkiqaslGGCVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPC 413
Cdd:cd17651 252 ------------LAALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 414 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIF 487
Cdd:cd17651 320 TRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQV 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795413665 488 KLaQGEYVAPEKIENIYIRSQPVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKRG 543
Cdd:cd17651 399 KI-RGFRIELGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELRA 456
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
189-621 |
5.05e-19 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 91.84 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSGFLKvteSQWAPTCADVH--ISYLPLAHMFERMVQS 259
Cdd:PTZ00297 588 PVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDISTLVM---TGVLPSSFKKHlmVHFTPFAMLFNRVFVL 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 260 VVYCHGGRVGffQGDIRLLSDDMKALCPTIFPVVPRLlnrmydkiFSQANTPLKR----------WLLEfaakrKQAEVR 329
Cdd:PTZ00297 665 GLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE-----RAFQLR 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 330 SGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYegygQTECTAGCTFTtpg 400
Cdd:PTZ00297 730 SRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF----FLPSEGVFCVD--- 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 401 dwtsghvGAPLPCNHIKLVDVEELNYWACKGEGEICVRGpnvfkgylkDPDRTKEAldsdgwlhtgdIGKWLPAGTLKVI 480
Cdd:PTZ00297 803 -------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-----------AAQWKRDRTLRLL 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 481 DRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKRGIE--GTYADLCTSKDL 557
Cdd:PTZ00297 856 GPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGegGGPARQLGWTEL 934
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 558 KK----AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 621
Cdd:PTZ00297 935 VAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
189-469 |
7.27e-19 |
|
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: 90.38 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvtesQWAPTCADVHISYLPLAH-MfermvqsvvychgGR 267
Cdd:cd05931 143 PPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdM-------------GL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VG------FFQGDIRLLSddmkalcPTIFpvvprlLNRmydkifsqantPLkRWL-----------------LEFAAKRK 324
Cdd:cd05931 206 IGglltplYSGGPSVLMS-------PAAF------LRR-----------PL-RWLrlisryratisaapnfaYDLCVRRV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 325 QAEVRSGIirndsiwdELffnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGC 394
Cdd:cd05931 261 RDEDLEGL--------DL----------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 395 TFTTPG----------DWTSGHV----------------GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLK 448
Cdd:cd05931 319 SGGPPGtgpvvlrvdrDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWG 398
|
330 340
....*....|....*....|....*..
gi 795413665 449 DPDRTKE------ALDSDGWLHTGDIG 469
Cdd:cd05931 399 RPEATAEtfgalaATDEGGWLRTGDLG 425
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
146-533 |
8.11e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 90.02 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 146 SGSLRSWPATHIPWWWSRSMTPWALELSATSSIQDCGQENHHA-PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF 224
Cdd:PRK08314 140 SDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAPpPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 225 SGFlkvteSQWAP-TCADVHISYLPLAHM--FERMVQSVVYChGGRVgffqgdirllsddmkalcpTIFP-----VVPRL 296
Cdd:PRK08314 220 VGS-----VLWSNsTPESVVLAVLPLFHVtgMVHSMNAPIYA-GATV-------------------VLMPrwdreAAARL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 297 LNRMydKIFSQANTPlkRWLLEFAAKRKQAEvrsgiiRNDSiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAA 376
Cdd:PRK08314 275 IERY--RVTHWTNIP--TMVVDFLASPGLAE------RDLS------------SL----RYIGGGGAAMPEAVAERLKEL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 377 LGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE 455
Cdd:PRK08314 329 TGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 456 A---LDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlv 525
Cdd:PRK08314 408 AfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV-- 484
|
....*...
gi 795413665 526 giVVPDPE 533
Cdd:PRK08314 485 --VVLRPE 490
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
193-535 |
1.28e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 89.48 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTESQwAPTCAD-----VhisylPLAHMFErMVQSVVYC--HG 265
Cdd:PRK08315 197 DPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAM-KLTEEDrlcipV-----PLYHCFG-MVLGNLACvtHG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 266 GRV-----GFfqgdirllsDDMKAL-------C------PTIFPVV---PRLlnRMYDkiFSQantplkrwllefaakrk 324
Cdd:PRK08315 267 ATMvypgeGF---------DPLATLaaveeerCtalygvPTMFIAEldhPDF--ARFD--LSS----------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 325 qaeVRSGIirndsiwdelffnkiqasLGGcvrmivtgaapaSPtvlgflraalgC------QVYE---------GYGQTE 389
Cdd:PRK08315 317 ---LRTGI------------------MAG------------SP-----------CpievmkRVIDkmhmsevtiAYGMTE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 390 CTAGCTFTTPGD------WTsghVGAPLPCNHIKLVDVEelnywacKGE-------GEICVRGPNVFKGYLKDPDRTKEA 456
Cdd:PRK08315 353 TSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqGELCTRGYSVMKGYWNDPEKTAEA 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 457 LDSDGWLHTGDIGkwlpagtlkVIDrkkhifklAQGeYVapeKI------------ENIYIRsqpvaQI----YVHGDSL 520
Cdd:PRK08315 423 IDADGWMHTGDLA---------VMD--------EEG-YV---NIvgrikdmiirggENIYPR-----EIeeflYTHPKIQ 476
|
410
....*....|....*....
gi 795413665 521 KAFLVGivVPDP----EVM 535
Cdd:PRK08315 477 DVQVVG--VPDEkygeEVC 493
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
193-542 |
1.71e-18 |
|
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: 88.29 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvtesqwaptcaDVHISYLPLAHMfermvqsvvychggRVGFFQ 272
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR-----------EYELDSFPVRLL--------------QMASFS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 273 GDIrLLSDDMKALCP--TIFPVVPRLL---NRMYDKIFSQ-----ANTP-LKRWLLEFAAKRKQ--AEVRSGIIRNDSIW 339
Cdd:cd17650 146 FDV-FAGDFARSLLNggTLVICPDEVKldpAALYDLILKSritlmESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 DElFFNKIQASLGGCVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLV 419
Cdd:cd17650 225 AQ-DFKTLAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKVIDRKKHIFKLaQGE 493
Cdd:cd17650 285 D-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGF 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 494 YVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEvmPSWAQKR 542
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
189-542 |
3.33e-18 |
|
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: 87.77 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsgflkvtesqwaptcadvhisylplaHMFERMVQSVVYCHGGRV 268
Cdd:cd17655 131 EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVV-----------------------------NLVEWANKVIYQGEHLRV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 GFFQGdirlLSDDMkalcpTIFPVVPRLL--NRMYdkIFSQANTPLKRWLLEFAAKRkqaevRSGIIR-NDSIWDELffN 345
Cdd:cd17655 182 ALFAS----ISFDA-----SVTEIFASLLsgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDlTPAHLKLL--D 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 346 KIQASLGGCVRMIVTGAAPASPTVLGFL--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLV 419
Cdd:cd17655 244 AADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYIL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGE 493
Cdd:cd17655 324 D-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGY 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 494 YVAPEKIENIYIRSQPVAQ---IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 542
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEavvIARKDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
160-532 |
4.15e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 87.68 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 160 WWSRSMTPWALELSATSSIQDCGQENHHAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflKVTESQWAPT 238
Cdd:PRK08316 135 ILSLVLGGREAPGGWLDFADWAEAGSVAEPdVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVS--CIVAGDMSAD 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 239 caDVHISYLPLAHMFERMVqsvvychggrvgFFQGDIRLLSDDMKALCPTIfpvvprllNRMYDKIFSQANTPLkrwlle 318
Cdd:PRK08316 213 --DIPLHALPLYHCAQLDV------------FLGPYLYVGATNVILDAPDP--------ELILRTIEAERITSF------ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 319 FAAKrkqaevrsgiirndSIWDELF----FNKIQASlggCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAG 393
Cdd:PRK08316 265 FAPP--------------TVWISLLrhpdFDTRDLS---SLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 394 CTFTTPGDwtsgHVGAP----LPCNHI--KLVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTG 466
Cdd:PRK08316 328 ATVLGPEE----HLRRPgsagRPVLNVetRVVD-DDGNDVA-PGEvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSG 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795413665 467 DIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 532
Cdd:PRK08316 401 DLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA---------LYTHPAVAEVAVIG--LPDP 454
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
178-550 |
5.08e-18 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 86.75 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 178 IQDCgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSG--FLKVTESqwaptcaDVHISylpLAHMF 253
Cdd:cd05919 78 ARDC----EARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAreALGLTPG-------DRVFS---SAKMF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 254 ermvqsVVYCHGGRVGF--FQGDIRLLSDD----------MKALCPTIFPVVPRllnrMYDKIFSQANTPlkrwllefaa 321
Cdd:cd05919 144 ------FGYGLGNSLWFplAVGASAVLNPGwptaervlatLARFRPTVLYGVPT----FYANLLDSCAGS---------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 322 krkQAEVRSgiIRndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT-- 398
Cdd:cd05919 204 ---PDALRS--LR-----------------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnr 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 399 PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTL 477
Cdd:cd05919 254 PGAWRLGSTGRPVPGYEIRLVD--EEGHTIPPGEeGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 478 KVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV----HGDSL---KAFlvgiVVPDPEVMPSWAQKRGIEGTYAD 550
Cdd:cd05919 331 THAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAF----VVLKSPAAPQESLARDIHRHLLE 405
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
187-532 |
1.52e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 85.71 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 187 HAPVPPQ----PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTESqwaptcaDVHISYLPLAHMFERMVQS 259
Cdd:PRK06145 137 GLEIPPQaavaPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLTAS-------ERLLVVGPLYHVGAFDLPG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 260 V-VYCHGGRVGF---FQGDIRLLSDDMKALCPTIFpvVPRLLNRMYdkifsQANTPLK------RWLLefAAKRKQAEVR 329
Cdd:PRK06145 210 IaVLWVGGTLRIhreFDPEAVLAAIERHRLTCAWM--APVMLSRVL-----TVPDRDRfdldslAWCI--GGGEKTPESR 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 330 sgiIRNdsiwdelffnkiqaslggcvrmivtgaapasptvlgFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHV 407
Cdd:PRK06145 281 ---IRD------------------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGST 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 408 GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIF 487
Cdd:PRK06145 322 GRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 795413665 488 kLAQGEYVAPEKIEN-IYIRSQ--PVAQIYVHGDSLKAFLVGIVVPDP 532
Cdd:PRK06145 400 -ISGGENIASSEVERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
186-521 |
3.21e-17 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 85.53 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 186 HHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFsgflkvtesqwapTCADVHISYLPLAHMFerm 256
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADF-------------TPNDRFMSALPLFHSF--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 257 vqsvvychGGRVGFFQgdiRLLSDDMKALCPTI--FPVVPRLLnrmYDK----IFSQANtplkrWLLEFAakrkqaevrs 330
Cdd:PRK08043 420 --------GLTVGLFT---PLLTGAEVFLYPSPlhYRIVPELV---YDRnctvLFGTST-----FLGNYA---------- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 331 giiRNDSIWDelFFNkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 410
Cdd:PRK08043 471 ---RFANPYD--FAR---------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 411 LPCNHIKLVDVEELNywacKGeGEICVRGPNVFKGYLK--DPDRTK-------EALDSDGWLHTGDIGKWLPAGTLKVID 481
Cdd:PRK08043 537 LPGMDARLLSVPGIE----QG-GRLQLKGPNIMNGYLRveKPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQG 611
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 795413665 482 RKKHIFKLAqGEYVAPEKIENIYIRSQPVAQiyvHGDSLK 521
Cdd:PRK08043 612 RAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
189-532 |
5.03e-17 |
|
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: 84.27 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVC-FTSGTTGNPKGAMLTH--------GNVVAdfsgflkvtesqWAptcADVHISYLPLAHMFermvqs 259
Cdd:cd12118 126 WIPPADEWDPIALnYTSGTTGRPKGVVYHHrgaylnalANILE------------WE---MKQHPVYLWTLPMF------ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 260 vvYCHGGrvGFFQGdirllsddMKALCPTIfpVVPRLLNrmYDKIFsqantplkRWLLE-----FAAkrkqAEVRSGIIR 334
Cdd:cd12118 185 --HCNGW--CFPWT--------VAAVGGTN--VCLRKVD--AKAIY--------DLIEKhkvthFCG----APTVLNMLA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 335 NDSIWDelffnkiQASLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAP 410
Cdd:cd12118 237 NAPPSD-------ARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERAR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 411 LPC----NHIKL--VDVEELNY-----WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKV 479
Cdd:cd12118 307 LKArqgvRYVGLeeVDVLDPETmkpvpRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEI 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 795413665 480 IDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 532
Cdd:cd12118 386 KDRSKDII-ISGGENISSVEVEGV---------LYKHPAVLEAAVVA--RPDE 426
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
187-532 |
6.27e-17 |
|
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: 84.08 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 187 HAPVPPQPDDLSIVCFTSGTTGNPKgaMLTHGNV--------------VADFSGFLKVTESQWAPTC-ADVHISYLPLAH 251
Cdd:cd05970 177 TANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTyplghivtakywqnVREGGLHLTVADTGWGKAVwGKIYGQWIAGAA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 252 MFermvqsvVYCHGGrvgFFQGDI--RLLSDDMKALC--PTIFpvvprllnrmydkifsqantplkRWLlefaakrkqae 327
Cdd:cd05970 255 VF-------VYDYDK---FDPKALleKLSKYGVTTFCapPTIY-----------------------RFL----------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 328 VRSGIIRNDsiwdelfFNKIqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGH 406
Cdd:cd05970 291 IREDLSRYD-------LSSL--------RYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 407 VGAPLPCNHIKLVDVEELnywACKG--EGEICVRGPN-----VFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKV 479
Cdd:cd05970 355 MGKPAPGYEIDLIDREGR---SCEAgeEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWF 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 795413665 480 IDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDP 532
Cdd:cd05970 431 VGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG-----------VPDP 471
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
193-533 |
8.76e-17 |
|
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: 83.13 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTESQWAPTCADVHISYLPLAHMFermvqSV-----VYCHGGR 267
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGFFQGDIRLLSDDMkalcptifpvvPRLLNRMYDKIFSQanTPLkrwllefAAKRKQAEVRSGIIRNDSIwdelffnki 347
Cdd:cd17643 162 LVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQ--TPS-------AFYQLVEAADRDGRDPLAL--------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 348 qaslggcvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLV 419
Cdd:cd17643 213 --------RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQG 492
Cdd:cd17643 285 D-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RG 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 795413665 493 EYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPE 533
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
162-534 |
8.81e-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: 83.40 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 162 SRSMTPWALELsATSSIQDCGQENHHAPVPP---QPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgflKVTESQWAPT 238
Cdd:cd12117 101 DRSLAGRAGGL-EVAVVIDEALDAGPAGNPAvpvSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR------LVKNTNYVTL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 239 CA-DVHISYLPL---AHMFErmvqsvVY---CHGGRVgffqgdirllsddmkALCPTIFPVVPRLLnrmydkifsqantp 311
Cdd:cd12117 174 GPdDRVLQTSPLafdASTFE------IWgalLNGARL---------------VLAPKGTLLDPDAL-------------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 312 lkrwllefaakrkQAEVRSGIIrnDSIWdeL---FFNKI----QASLGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYE 383
Cdd:cd12117 219 -------------GALIAEEGV--TVLW--LtaaLFNQLadedPECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 384 GYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKE 455
Cdd:cd12117 281 GYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLD--EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 456 ALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLV 525
Cdd:cd12117 356 RFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAA-LRAHPgVREAVVvvrEDAGGDKRLV 433
|
....*....
gi 795413665 526 GIVVPDPEV 534
Cdd:cd12117 434 AYVVAEGAL 442
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
192-503 |
1.12e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 84.25 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 192 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA---------DFSGflkvtesqwaptcADVHISYLPLAHMFermvqsvvy 262
Cdd:PRK06814 790 RDPDDPAVILFTSGSEGTPKGVVLSHRNLLAnraqvaariDFSP-------------EDKVFNALPVFHSF--------- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 263 chggrvGFFQGDIRLLSDDMKAL---CPTIFPVVPRLLnrmYDK----IFSqANTPLkrwllefaakrkqaevrSGIIRN 335
Cdd:PRK06814 848 ------GLTGGLVLPLLSGVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFL-----------------NGYARY 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 336 DSIWDelFFNkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNH 415
Cdd:PRK06814 901 AHPYD--FRS---------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIE 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 416 IKLVDVEELNywacKGeGEICVRGPNVFKGYLK-DPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEY 494
Cdd:PRK06814 970 YRLEPVPGID----EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEM 1042
|
....*....
gi 795413665 495 VAPEKIENI 503
Cdd:PRK06814 1043 ISLAAVEEL 1051
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
193-536 |
1.27e-16 |
|
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: 82.75 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVA------------DFSGFLKVTesqwaPTCADVHI--SYLPLahmfermvq 258
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAflqwaaaafsaeELAGVLAST-----SICFDLSVfeLFGPL--------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 259 svvyCHGGRVGFFQGDIRLLsdDMKALCP-TIFPVVPRLLnrmydkifsqantplkRWLLEFaakrkqaevrsgiirnds 337
Cdd:cd12115 169 ----ATGGKVVLADNVLALP--DLPAAAEvTLINTVPSAA----------------AELLRH------------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 338 iwdelffNKIQASlggcVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCN 414
Cdd:cd12115 209 -------DALPAS----VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 415 HIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFK 488
Cdd:cd12115 278 QAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVK 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 489 LaQGEYVAPEKIENIyIRSQP-VAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 536
Cdd:cd12115 357 V-RGFRIELGEIEAA-LRSIPgVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
194-598 |
1.51e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.17 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVT-ESQWAPTcaDVHISYLPLAHMFermvqsvvychGGRVGFfQ 272
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRpREPDPPP--PVSLDWMPWNHTM-----------GGNANF-N 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 273 GDIR----LLSDDMKALcPTIFPVVPRLLNRMYDKIFsqANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelFFNKIq 348
Cdd:PRK12582 285 GLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVY--GNVPAGYAMLAEAMEKDDALRRS------------FFKNL- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 349 aslggcvRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTEcTAGCTFTTpgDWTS---GHVGAPLPCNHIKLV 419
Cdd:PRK12582 349 -------RLMAYGGATLSDDLYERMQAlavrTTGHRIpfYTGYGATE-TAPTTTGT--HWDTervGLIGLPLPGVELKLA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DVEElNYwackgegEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKVIDRKKHIFKLAQGEYV 495
Cdd:PRK12582 419 PVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 496 --APEKIENIYIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGieGTYADLCTSKDLKKAILEDMVRLGKESG 573
Cdd:PRK12582 491 svGTLRPDAVAACSPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVVKHPAVLAILREGLSAHNAEAG 567
|
410 420
....*....|....*....|....*
gi 795413665 574 LHSfEQVKAIHIHSDMFSVQNGLLT 598
Cdd:PRK12582 568 GSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
196-503 |
5.93e-16 |
|
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: 79.61 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteSQWAPTCADVHISYLPLAHMFE--RMVQSVVYcHGGRVGFfqG 273
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQK---EGLNWVVGDVTYLPLPATHIGGlwWILTCLIH-GGLCVTG--G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 DIRLLSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRkqaevrsgIIRNDSIWDELFFNkiqas 350
Cdd:cd17635 76 ENTTYKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR--------AIAADVRFIEATGL----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 351 lggcvrmivtgaapasptvlgflraalgCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNYWAc 429
Cdd:cd17635 143 ----------------------------TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795413665 430 KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 503
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
194-510 |
7.49e-16 |
|
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: 80.61 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESqwapTCADVHISYLPLAHmfermvqsvvychggRVGFFQG 273
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 DIRLLSDDMKA-LCPT-IFPVVPRLLNRMYDK----IFSQANTPLKrWLLEFAAKRKQAEvrsgiirndsiWDElffnki 347
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL------ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 348 qaslgGCVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF--------------------- 396
Cdd:cd05908 228 -----SSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthge 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 397 -------TTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 468
Cdd:cd05908 299 pepevdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDL 376
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 795413665 469 GkWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 510
Cdd:cd05908 377 G-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
384-540 |
1.40e-15 |
|
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: 78.11 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 384 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSD 460
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 461 GWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqgeyvapekIENIY-------IRSQP-VAQIYVhgdslkaflvgIVVPDp 532
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 795413665 533 evmPSWAQ 540
Cdd:cd17636 276 ---PRWAQ 280
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
348-532 |
1.70e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 79.68 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 348 QASLGGCVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------ 414
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 415 HIKLVDVEELNYWAC-------KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIF 487
Cdd:PLN03102 368 ILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 795413665 488 kLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGIvvPDP 532
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
192-533 |
3.69e-15 |
|
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: 78.65 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 192 PQPDDlsiVCF---TSGTTGNPKGAMLTHgnvvADFsgFLKVTESqwAPTCA----DVHISYLPLAHMFErM----VQSV 260
Cdd:COG1021 181 PDPDD---VAFfqlSGGTTGLPKLIPRTH----DDY--LYSVRAS--AEICGldadTVYLAALPAAHNFP-LsspgVLGV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 VYcHGGRVgffqgdirLLSDDMKALcpTIFP-----------VVPRLLNRMydkifsqantplkrwlLEFAAKRKQAevr 329
Cdd:COG1021 249 LY-AGGTV--------VLAPDPSPD--TAFPlierervtvtaLVPPLALLW----------------LDAAERSRYD--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 330 sgiirndsiwdeLffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH 406
Cdd:COG1021 299 ------------L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 407 -VGAPL-PCNHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLK 478
Cdd:COG1021 354 tQGRPIsPDDEVRIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLV 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 795413665 479 VIDRKK-HIFKlaQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDPE 533
Cdd:COG1021 427 VEGRAKdQINR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
203-533 |
4.73e-15 |
|
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: 78.14 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 203 TSGTTGNPKGAMLTHgnvvADFSGFLKVTesqwAPTCA----DVHISYLPLAHMFERM---VQSVVYChGGRVgffqgdi 275
Cdd:cd05920 147 SGGTTGTPKLIPRTH----NDYAYNVRAS----AEVCGldqdTVYLAVLPAAHNFPLAcpgVLGTLLA-GGRV------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 276 rLLSDDmkALCPTIFPVVPRllnrmyDKIFSQANTP--LKRWLlEFAAKRKQAEvrsgiirndsiwdelffnkiqASLgg 353
Cdd:cd05920 211 -VLAPD--PSPDAAFPLIER------EGVTVTALVPalVSLWL-DAAASRRADL---------------------SSL-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 354 cvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDvEELNYWACKG 431
Cdd:cd05920 258 --RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 432 EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENiyirsqpva 511
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN--------- 404
|
330 340
....*....|....*....|..
gi 795413665 512 QIYVHGDSLKAFLVGivVPDPE 533
Cdd:cd05920 405 LLLRHPAVHDAAVVA--MPDEL 424
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
194-505 |
2.00e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtesqWAPTCADVHISYLPLAHMFermvqsvvychggrvGFFqg 273
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFN-- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 274 dirllsddmkalCPTIFPVVPRLlnrmyDKIFSQanTPLK-RWLLEFAAKRKQAEVRSGIIRNDSIwdeLFFNKIQASLG 352
Cdd:PRK06334 241 ------------SCTLFPLLSGV-----PVVFAY--NPLYpKKIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESCL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 353 GCVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVDvEELNYWA 428
Cdd:PRK06334 299 PSLRFVVIGGDAFKDSLYqEALKTFPHIQLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIVS-EETKVPV 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795413665 429 CKGE-GEICVRGPNVFKGYL-KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYI 505
Cdd:PRK06334 376 SSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
188-544 |
3.15e-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: 75.48 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESqwaptcaDVHISYLPLAH--------MFER 255
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADiyWTAELYArnVLGIRED-------DVCFSAAKLFFayglgnslTFPL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 256 MVQSVVYCHGGRVgffqgDIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGIirn 335
Cdd:cd05959 229 SVGATTVLMPERP-----TPAAVFKRIRRYRPTVFFGVPTLYAAM------------------LAAPNLPSRDLSSL--- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 336 dsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPC 413
Cdd:cd05959 283 --------------------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 414 NHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGE 493
Cdd:cd05959 341 YEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGI 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 494 YVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPSWAQKRGI 544
Cdd:cd05959 418 WVSPFEVESALVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDSEALEEEL 471
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
181-531 |
3.69e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 76.35 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 181 CGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTESQWAPTCADVHISYLPLAHMFERMVQSV 260
Cdd:PRK12467 642 CGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFG 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 VYCHGGRVgffqgdirLLSDDMKALCPTIFpvvprllnrmYDKIFSQANTPLKrwllefaakrkqaevrsgiiRNDSIWD 340
Cdd:PRK12467 718 ALASGATL--------HLLPPDCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQ 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 341 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHVGAPLPCNHI 416
Cdd:PRK12467 760 ALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGL 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 417 KLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFKL 489
Cdd:PRK12467 840 YILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI 918
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 795413665 490 aQGEYVAPEKIENIyIRSQP-------VAQIYVHGDSLKAFLVGIVVPD 531
Cdd:PRK12467 919 -RGFRIELGEIEAR-LLAQPgvreavvLAQPGDAGLQLVAYLVPAAVAD 965
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
190-533 |
6.18e-14 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 74.62 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 190 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTES----QWAPTCADVHIS--YLPLAHMfERMVqsv 260
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMqdeYPLGPGdrvlQKTPLSFDVSVWelFWPLVAG-ARLV--- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 VYCHGGRvgffqGDIRLLSDDMKALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkqaevrsgiirndsiwd 340
Cdd:cd17646 209 VARPGGH-----RDPAYLAALIREHGVTTCHFVPSML------------------------------------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 341 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIK 417
Cdd:cd17646 241 RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLY 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 418 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKVIDRKKHIFKLaQ 491
Cdd:cd17646 321 VLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-R 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 795413665 492 GEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPE 533
Cdd:cd17646 399 GFRVEPGEIEAA-LAAHPaVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
347-515 |
1.32e-13 |
|
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: 73.37 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 347 IQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDVE 422
Cdd:cd05974 191 IQQDLASFdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 423 ElnywACKGEGEICV-----RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAP 497
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 795413665 498 EKIENIYIRSQPVAQIYV 515
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
189-534 |
2.26e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 72.79 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGflkvtesqwaptcadvhisyLPLAHMFERMVQSVVYC----- 263
Cdd:PRK07867 146 FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAG--------------------VMLAQRFGLGPDDVCYVsmplf 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 264 HGGRVgffqgdirllsddMKALCPTIFpvvprllnrmydkifSQANTPLKRwllEFAAKRKQAEVRS-GIIrndsiwdel 342
Cdd:PRK07867 204 HSNAV-------------MAGWAVALA---------------AGASIALRR---KFSASGFLPDVRRyGAT--------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 343 FFNKIqaslGGCVRMIVtgAAP-----------------ASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTPGDWTSG 405
Cdd:PRK07867 244 YANYV----GKPLSYVL--ATPerpddadnplrivygneGAPGDIARFARRFGCVVVDGFGSTE--GGVAITRTPDTPPG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 406 HVGaPLPCNhIKLVDVE--------------ELNYWACKGEgEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKW 471
Cdd:PRK07867 316 ALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYR 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795413665 472 LPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 534
Cdd:PRK07867 392 DADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPDPVV 442
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
191-525 |
3.21e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 72.57 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 191 PPQPDDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFLKvtesqWAPTCADVHISYLPLAHmfermvqsvvyCHGGrv 268
Cdd:PLN02479 190 PPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNALI-----WGMNEGAVYLWTLPMFH-----------CNGW-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 gffqgdirLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTplkrwllEFAAkrkqAEVRSGIIRNDSIWDELFfnkiq 348
Cdd:PLN02479 252 --------CFTWTLAALCGTNICLRQVTAKAIYSAIANYGVT-------HFCA----APVVLNTIVNAPKSETIL----- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 349 aSLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH--------- 415
Cdd:PLN02479 308 -PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryigleg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 416 IKLVDVEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGE 493
Cdd:PLN02479 384 LDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGE 461
|
330 340 350
....*....|....*....|....*....|..
gi 795413665 494 YVAPEKIENIyirsqpvaqIYVHGDSLKAFLV 525
Cdd:PLN02479 462 NISSLEVENV---------VYTHPAVLEASVV 484
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
188-536 |
7.04e-13 |
|
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: 71.15 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHG---NVVADfsgflkvTESQWAPTCADVHISYLPLAHMFermvqSV---- 260
Cdd:cd12114 119 PPVDVAPDDLAYVIFTSGSTGTPKGVMISHRaalNTILD-------INRRFAVGPDDRVLALSSLSFDL-----SVydif 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 -VYCHGGRVgffqgdirllsddmkalcptifpVVPRLlnrmydkifSQANTPlKRWllefaakrKQAEVRSGIirndSIW 339
Cdd:cd12114 187 gALSAGATL-----------------------VLPDE---------ARRRDP-AHW--------AELIERHGV----TLW 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 delffNKIQASLGgcvrMIVTgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF---- 396
Cdd:cd12114 222 -----NSVPALLE----MLLD-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpid 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 397 TTPGDWTSGHVGAPLPCNHIKLVDV--EELNYWackGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG--WLHTGDIGK 470
Cdd:cd12114 292 EVPPDWRSIPYGRPLANQRYRVLDPrgRDCPDW---VPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGR 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 471 WLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 536
Cdd:cd12114 369 YRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
174-532 |
9.39e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 70.84 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 174 ATSSIQDCGQENHHAPVPPQP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVADFsgFLKVTEsqwaptcADVH 243
Cdd:PRK07470 139 AGLDYEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLADL--MPGTTE-------QDAS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 244 ISYLPLAHM--FERMVQSVvycHGGRVgffqgdIRLLSDDMKAlcptifPVVPRLLNRMYDKIFSQANTPLKrWLLEFAA 321
Cdd:PRK07470 210 LVVAPLSHGagIHQLCQVA---RGAAT------VLLPSERFDP------AEVWALVERHRVTNLFTVPTILK-MLVEHPA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 322 krkqaevrsgIIRNDsiwdelffnkiQASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-- 399
Cdd:PRK07470 274 ----------VDRYD-----------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPPal 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 400 ---GDWTSGHVGaplPCNH--------IKLVDVEELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGD 467
Cdd:PRK07470 329 hdaEDGPDARIG---TCGFertgmevqIQDDEGRELP----PGEtGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGD 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795413665 468 IGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDP 532
Cdd:PRK07470 401 LGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAVSEVAVLG--VPDP 453
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
359-525 |
9.41e-13 |
|
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: 70.96 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 359 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVR 438
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 439 -GPN----VFKGYLKDPDRTKEALDSDGWLhTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQI 513
Cdd:cd05928 376 vKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170
....*....|....*....
gi 795413665 514 YV-------HGDSLKAFLV 525
Cdd:cd05928 454 AVvsspdpiRGEVVKAFVV 472
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
195-537 |
1.25e-12 |
|
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: 70.20 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTESqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGR--V 268
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYavnvLRLRED-------DRFVGSPPLAFTFGLGGVLLFPFGVGAsgV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 GFFQGDIRLLSDDMKALCPTIFPVVPRllnrMYdkifsqantplkRWLLEFAAKRKQaevrsgiirndsiwdelffnkiq 348
Cdd:cd05958 170 LLEEATPDLLLSAIARYKPTVLFTAPT----AY------------RAMLAHPDAAGP----------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 349 asLGGCVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYW 427
Cdd:cd05958 211 --DLSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 428 ACKGE-GEICVRGPNVFKgYLKDPDRTKEAldSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIR 506
Cdd:cd05958 286 VPDGTiGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQ 361
|
330 340 350
....*....|....*....|....*....|....
gi 795413665 507 SQPVAQIYVHGDSLKAFLV---GIVVPDPEVMPS 537
Cdd:cd05958 362 HPAVAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-530 |
1.41e-12 |
|
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: 70.18 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 192 PQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTESQWAPTCADVHISYLPLAHMFERM--VQSVVychggrvg 269
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 270 ffqgdirllsDDMKALCPTifPVVPRllnrmydKIFSqantPLKRWllefaakrkqaEVrSGIIRNDSIWDEL--FFNKI 347
Cdd:cd05910 150 ----------PDMDPTRPA--RADPQ-------KLVG----AIRQY-----------GV-SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 348 QASLGGcVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 415
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 416 IKLV--DVEELNYWACKGE------GEICVRGPNVFKGYLKDPDRTKEALDSDG----WLHTGDIGKWLPAGTLKVIDRK 483
Cdd:cd05910 274 VRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 795413665 484 KHIFKLAQGEYVapekieniyirSQPVAQIY-VHGDSLKAFLVGIVVP 530
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
431-486 |
2.74e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.59 E-value: 2.74e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 431 GE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHI 486
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
188-494 |
3.32e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 69.16 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKvteSQWAPTCADVHISYLPLAHMFERM--VQSVVychg 265
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA-LR---EDYGIEPGEIDLPTFPLFALFGPAlgMTSVI---- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 266 grvgffqgdirllsDDMKALCP-TIFPvvprllnrmyDKIFSQ----------ANTPLKRWLLEFAAKRKQaevrsgiir 334
Cdd:PRK09274 239 --------------PDMDPTRPaTVDP----------AKLFAAierygvtnlfGSPALLERLGRYGEANGI--------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 335 ndsiwdelffnkiqaSLGGCVRMIVTGAaPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSG 405
Cdd:PRK09274 286 ---------------KLPSLRRVISAGA-PVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNG 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 406 H---VGAPLPCNHIKLVDV--EELNYWA-----CKGE-GEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGk 470
Cdd:PRK09274 350 AgicVGRPVDGVEVRIIAIsdAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG- 428
|
330 340
....*....|....*....|....*
gi 795413665 471 WL-PAGTLKVIDRKKHIFKLAQGEY 494
Cdd:PRK09274 429 YLdAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
113-536 |
4.80e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 68.62 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 113 WPtglNFWGLDFSStIVKHAPISLLVFLHKIGQSGslRSWPATHIPWWWSRSMTPwALELSATSSIqdcgqenhhAPVPP 192
Cdd:PRK06164 114 WP---GFKGIDFAA-ILAAVPPDALPPLRAIAVVD--DAADATPAPAPGARVQLF-ALPDPAPPAA---------AGERA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFT-SGTTGNPK------GAMLTHGNVVADFSGFlkvtesqwAPtcADVHISYLPLahmfermvqSVVYCHG 265
Cdd:PRK06164 178 ADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIARAYGY--------DP--GAVLLAALPF---------CGVFGFS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 266 GRVGFFQGDIRLLSDDMKALCPTIfpvvpRLL-----------NRMYDKIFSQANTPLkrwllEFAAKRkqaevRSGIir 334
Cdd:PRK06164 239 TLLGALAGGAPLVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGF-- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 335 ndsiwdelffnkiqASLggcvrmivtgaAPASPTVLGFLRAAlGCQVYEGYGQTECTA---GCTFTTPgdWTSGHVGAPL 411
Cdd:PRK06164 302 --------------ASF-----------APALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRIEGGGR 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 412 PCN---HIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFK 488
Cdd:PRK06164 354 PASpeaRVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLR 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 795413665 489 LAqGEYVAPEKIENIYIRSQPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 536
Cdd:PRK06164 434 LG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
193-542 |
6.91e-12 |
|
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: 67.85 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV---TES----QWAPTCADVHISYLplahmfermvqSVVYCHG 265
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEygiTSSdrvlQFASIAFDVAAEEI-----------YVTLLSG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 266 GRVGFFQGDIRLLSDDMKALCP----TIFPVVPrllnrmydkifsqantplkrwllefaakrkqaevrsgiirndSIWDE 341
Cdd:cd17644 173 ATLVLRPEEMRSSLEDFVQYIQqwqlTVLSLPP------------------------------------------AYWHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 342 LFFNKIQASLGG--CVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLP 412
Cdd:cd17644 211 LVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 413 CNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH--------TGDIGKWLPAGTLKVIDRKK 484
Cdd:cd17644 291 NTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRID 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795413665 485 HIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 542
Cdd:cd17644 370 NQVKI-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPSTVELR 429
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
188-517 |
9.71e-12 |
|
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: 67.53 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHgNVVADFSGFLkVTESQWAPTCADVHISYLPLAHMfermvqsvvychggr 267
Cdd:cd05923 143 EDPPREPEQPAFVFYTSGTTGLPKGAVIPQ-RAAESRVLFM-STQAGLRHGRHNVVLGLMPLYHV--------------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGFFQgdirLLSDDMkALCPTIFPVvprllnrmydKIFSQANtplkrwllefAAKRKQAEVRSGIIRNDSIWDELFFNKI 347
Cdd:cd05923 206 IGFFA----VLVAAL-ALDGTYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHLDALAAAAE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 348 QASLG-GCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVDV-EELN 425
Cdd:cd05923 261 FAGLKlSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIgGSPD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 426 YWACKG-EGEICVR--GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 502
Cdd:cd05923 338 EALANGeEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIER 415
|
330
....*....|....*
gi 795413665 503 IYIRSQPVAQIYVHG 517
Cdd:cd05923 416 VLSRHPGVTEVVVIG 430
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
362-533 |
2.51e-11 |
|
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: 66.25 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 362 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPcNHIKLVDvEELNYWACKGEGEICVRG 439
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 440 PNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRsqpvaqiyvHGD 518
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 795413665 519 SLKAFLVGivVPDPE 533
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
188-515 |
2.58e-11 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 66.32 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPP---QPDDLSIVCFTSGTTGNPKGAMLTHG-------NVVADfsgfLKVTESqwaptcaDVHISYLPLAH------ 251
Cdd:PRK06155 170 APAPAaavQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAED----LEIGAD-------DVLYTTLPLFHtnalna 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 252 MFERMVQSVVYCHGGRV---GFFqgdirllsDDMKALCPTIFpvvpRLLNRMYDKIFSQANTPLKRwllefaakrkqaev 328
Cdd:PRK06155 239 FFQALLAGATYVLEPRFsasGFW--------PAVRRHGATVT----YLLGAMVSILLSQPARESDR-------------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 329 rsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPASptVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTSGHVG 408
Cdd:PRK06155 293 -----------------------AHRVRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTETNFVI-AVTHGSQRPGSMG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 409 APLPCNHIKLVDVEELNYWAckGE-GEICVRG--PNVF-KGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKK 484
Cdd:PRK06155 347 RLAPGFEARVVDEHDQELPD--GEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIK 423
|
330 340 350
....*....|....*....|....*....|..
gi 795413665 485 HIFKlAQGEYVAPEKIENIyIRSQP-VAQIYV 515
Cdd:PRK06155 424 DAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
193-542 |
2.80e-11 |
|
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: 65.74 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTH---GNVVADFSGFLKVTE----SQWAPTCADVHISYLPLAhmfermvqsvvYCHG 265
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHrglANLAAAQIAAFDVGPgsrvLQFASPSFDASVWELLMA-----------LLAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 266 GRvgffqgdirllsddmkaLCptifpVVPRLLnrmydkifSQANTPLKRWLlefaakrkQAEVRSGIIRNDSIWDELffn 345
Cdd:cd17652 160 AT-----------------LV-----LAPAEE--------LLPGEPLADLL--------REHRITHVTLPPAALAAL--- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 346 kIQASLGGCVRMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDvEEL 424
Cdd:cd17652 199 -PPDDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 425 NYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAP 497
Cdd:cd17652 274 RPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIEL 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 795413665 498 EKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 542
Cdd:cd17652 353 GEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
193-541 |
7.48e-11 |
|
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: 64.50 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQWAPTCADVHISYLPLAhmFERMVQSVV--YCHGGRVGF 270
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCEWHRPYFGVTPADKSLVYASFS--FDASAWEIFphLTAGAALHV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 271 FQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLkRWLLEFAAKRKQAEVRsgiirndsiwdelffnkiqas 350
Cdd:cd17645 176 VPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSL-RVLLTGGDKLKKIERK--------------------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 351 lggcvrmivtgaapasptvlgflraalGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWAC 429
Cdd:cd17645 234 ---------------------------GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 430 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENI 503
Cdd:cd17645 286 GVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPF 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 795413665 504 ---YIRSQPVAQIYVHGDSLKAFLVGIVVP----DPEVMPSWAQK 541
Cdd:cd17645 365 lmnHPLIELAAVLAKEDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
190-566 |
9.02e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.57 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 190 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTESQWAPTCADVHISYLPLAhmFERMVQSVVY--CHGGR 267
Cdd:PRK12467 1713 VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTSFA--FDVSVWELFWplINGAR 1786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VgffqgdirLLSDDMKALCPtifpvvprllNRMYDKIFSQANTplkrwLLEFAAKRKQAevrsgiirndsiwdelfFNKI 347
Cdd:PRK12467 1787 L--------VIAPPGAHRDP----------EQLIQLIERQQVT-----TLHFVPSMLQQ-----------------LLQM 1826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 348 QASLGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-----CTFTTPGDWTSGHVGAPLPCNHIKLV 419
Cdd:PRK12467 1827 DEQVEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYIL 1906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 420 DvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQG 492
Cdd:PRK12467 1907 D-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RG 1984
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795413665 493 EYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWAQKRgieGTYADlcTSKDLKKAILED-MV 566
Cdd:PRK12467 1985 FRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDDEAQ---VALRA--ILKNHLKASLPEyMV 2056
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
356-537 |
1.31e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.95 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 356 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEG 433
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 434 EICVRGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 510
Cdd:PRK12406 352 EIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGV 427
|
170 180 190
....*....|....*....|....*....|
gi 795413665 511 AQIYVHGDSLKAF---LVGIVVPDPEVMPS 537
Cdd:PRK12406 428 HDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
367-515 |
1.40e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 63.74 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 367 PTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLVDveelnywackgeGEICVRGPNVFKGY 446
Cdd:PRK09029 253 PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGY 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795413665 447 LKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV 515
Cdd:PRK09029 319 WRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
187-546 |
1.91e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.59 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 187 HAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPLAhmFERMVQSV--VYC 263
Cdd:PRK12316 4685 HDPaVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLI 4758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 264 HGGRVgffqgdirLLSDDMKALcPTifpvvpRLLNRMYDKIFSQANTPLKRW--LLEFAAKRKQ-AEVRsgiirndsiwd 340
Cdd:PRK12316 4759 NGASV--------VIRDDSLWD-PE------RLYAEIHEHRVTVLVFPPVYLqqLAEHAERDGEpPSLR----------- 4812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 341 elffnkiQASLGGcvrmivTGAAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNH 415
Cdd:PRK12316 4813 -------VYCFGG------EAVAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRS 4877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 416 IKLVDVEeLNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKVIDRKKHIFK 488
Cdd:PRK12316 4878 GYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVK 4956
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795413665 489 LaQGEYVAPEKIEnIYIRSQP-------VAQIYVHGdslkAFLVGIVVP-DPEVMPSWAQKRGIEG 546
Cdd:PRK12316 4957 I-RGFRIELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPqDPALADADEAQAELRD 5016
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
170-526 |
2.41e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 170 LELSATSSIQDCGQenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPL 249
Cdd:PRK12316 2123 LPLDRDAEWADYPD--TAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSF 2196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 250 AhmFERMVQSVVY--CHGGRVgffqgdirLLSDDMKalcptifpvvpRLLNRMYDKIFSQANTplkrwLLEFAAKRKQAE 327
Cdd:PRK12316 2197 S--FDGAHEQWFHplLNGARV--------LIRDDEL-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQL 2250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 328 VRsgiirndsiwdelffnkiQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWT 403
Cdd:PRK12316 2251 AE------------------HAERDGRppaVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWK 2307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 404 SGH----------VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TG 466
Cdd:PRK12316 2308 CRPqdpcgaayvpIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTG 2386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795413665 467 DIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENiYIRSQP-------VAQIYVHGDSLKAFLVG 526
Cdd:PRK12316 2387 DLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEA-RLQAHPavreavvVAQDGASGKQLVAYVVP 2451
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
194-540 |
6.95e-10 |
|
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: 61.62 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTESQWAPTCADVHISYLPL----AHmfERMVQSVVycHGGRV- 268
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACVv 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 ---GFFQGDIRLLSDDMKALCPTIFPVVPRLLNRmydkifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffn 345
Cdd:cd17649 165 lrpDELWASADELAEMVRELGVTVLDLPPAYLQQ------------LAEEADRTGDGRPPS------------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 346 kiqaslggcVRMIVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKL 418
Cdd:cd17649 214 ---------LRLYIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 419 VDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG-----WLHTGDIGKWLPAGTLKVIDRKKHIFKLaQ 491
Cdd:cd17649 282 LD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-R 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 795413665 492 GEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVP-DPEVMPSWAQ 540
Cdd:cd17649 360 GFRIELGEIEA-ALLEHPgvreAAVVALDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
173-503 |
7.56e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 61.71 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 173 SATSSIQDC-----GQENHHAPVPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAptcADVHISY 246
Cdd:PRK05851 124 AVDSSVTVHdlataAHTNRSASLTPPDSgGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAA---TDVGCSW 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 247 LPLAH-MfermvqsvvychggrvgffqGDIRLLSDDMKA----LCPTifpvvprllnrmydKIFSQAntPLK--RWLLEF 319
Cdd:PRK05851 201 LPLYHdM--------------------GLAFLLTAALAGaplwLAPT--------------TAFSAS--PFRwlSWLSDS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 320 AAKRKQA-EVRSGIIRNdsiwdelFFNKIQASLGGCVRMIVTGAAP----------ASPTVLGFLRAALGcqvyEGYGQT 388
Cdd:PRK05851 245 RATLTAApNFAYNLIGK-------YARRVSDVDLGALRVALNGGEPvdcdgferfaTAMAPFGFDAGAAA----PSYGLA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 389 ECTAGCTFTTPG-----------DWTSGH----VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPdrt 453
Cdd:PRK05851 314 ESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA--- 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 795413665 454 keALDSDGWLHTGDIGkWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 503
Cdd:PRK05851 391 --PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
202-533 |
1.15e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 61.07 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 202 FTSGTTGNPKGAM--LTHGNVVADFSGFLKVTeSQWAPTCAD-VHISYLPLAH----MFERMVQSvvycHGGRVGFFQgd 274
Cdd:PRK08276 147 YSSGTTGRPKGIKrpLPGLDPDEAPGMMLALL-GFGMYGGPDsVYLSPAPLYHtaplRFGMSALA----LGGTVVVME-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 275 iRLLSDDMKALCP----TIFPVVPRLLNRMydkifsqantpLKrwLLEfaakrkqaEVRSgiiRNDSiwdelffnkiqAS 350
Cdd:PRK08276 220 -KFDAEEALALIEryrvTHSQLVPTMFVRM-----------LK--LPE--------EVRA---RYDV-----------SS 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 351 LggcvRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVDvEELN 425
Cdd:PRK08276 264 L----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 426 YWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIY 504
Cdd:PRK08276 334 ELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLL 411
|
330 340
....*....|....*....|....*....
gi 795413665 505 IRSQPVAQIYVHGdslkaflvgivVPDPE 533
Cdd:PRK08276 412 VTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
198-511 |
1.24e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 60.88 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 198 SIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTESQWAPTCADVhisYLPLAHMFERMVQSVVYChGGRVGffqgdirl 277
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDA---VLPVVPMFHVNAWGLPYS-APLTG-------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 278 lsddmkalCPTIFPVvPRLLNR-MYDKIFSQANTplkrwlleFAAkrkqaevrsGIirnDSIWDELFFNKIQASLG-GCV 355
Cdd:PRK07008 245 --------AKLVLPG-PDLDGKsLYELIEAERVT--------FSA---------GV---PTVWLGLLNHMREAGLRfSTL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 356 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKLVDV 421
Cdd:PRK07008 296 RRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKIVGD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 422 E--ELNyWACKGEGEICVRGPNVFKGYLKdpdRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEK 499
Cdd:PRK07008 373 DgrELP-WDGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSID 446
|
330
....*....|..
gi 795413665 500 IENIYIRSQPVA 511
Cdd:PRK07008 447 IENVAVAHPAVA 458
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
195-542 |
1.25e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.44 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSGflkvTESQWAPTCADVHISYLPLahmferMVQSVV------- 261
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTAsadathDRLG----GPGQWLLALPAHHIAGLQV------LVRSVIagsepve 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 262 --YCHGGRVGFFQGDIRLLSDDMK--ALCPTifpvvpRLLNRMYDKIFSQAntplkrwLLEFAAkrkqaevrsgiirnds 337
Cdd:PRK07824 105 ldVSAGFDPTALPRAVAELGGGRRytSLVPM------QLAKALDDPAATAA-------LAELDA---------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 338 iwdelffnkiqaslggcvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNH 415
Cdd:PRK07824 156 --------------------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 416 IKLVDveelnywackgeGEICVRGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLPAGTLKVIDRKKHIFKLAqGE 493
Cdd:PRK07824 203 VRVED------------GRIALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GL 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 494 YVAPEKIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 542
Cdd:PRK07824 265 TVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
191-484 |
1.66e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.79 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 191 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTEsqwaptcADVHISYLPLAH-Mfermvqsvvychg 265
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIshdgLKVRP-------GDRCVSWLPFYHdM------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 266 GRVGFF------QgdirlLSDDmkaLCPT-IFPVVP----RLLNRMYDKI-FSQAntplkrWLLEFAAKRkqAEVRSGII 333
Cdd:PRK09192 232 GLVGFLltpvatQ-----LSVD---YLPTrDFARRPlqwlDLISRNRGTIsYSPP------FGYELCARR--VNSKDLAE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 334 RNDSIWdelffnkiqaslggcvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG-- 400
Cdd:PRK09192 296 LDLSCW----------------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsg 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 401 --------DWTSGH------------------VGAPLPCNHIKLVDV--EELNYwacKGEGEICVRGPNVFKGYLKDPDR 452
Cdd:PRK09192 355 ivveevdrDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEES 431
|
330 340 350
....*....|....*....|....*....|..
gi 795413665 453 TKeALDSDGWLHTGDIGkWLPAGTLKVIDRKK 484
Cdd:PRK09192 432 QD-VLAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
356-532 |
1.71e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 60.39 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 356 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 418
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 419 vdveelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHifklaQ----GEY 494
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 795413665 495 VAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDP 532
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
194-536 |
1.78e-09 |
|
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: 60.11 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTESQwaptcADVHISYLPLAHMFERMVQSVVYCHggrv 268
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNGDE-----AVLFFSNYVFDFFVEQMTLALLNGQ---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 269 gffqgDIRLLSDDMKALCPTIfpvvPRLLNRmyDKIFSQANTPLKRWLLEFAakrkqaevrsgiirndsiwdelffnkiq 348
Cdd:cd17648 164 -----KLVVPPDEMRFDPDRF----YAYINR--EKVTYLSGTPSVLQQYDLA---------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 349 aSLGGCVRMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNY 426
Cdd:cd17648 205 -RLPHLKRVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMKR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 427 WACKGEGEICVRGPNVFKGYLKDPDRTKE-------------ALDSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQG 492
Cdd:cd17648 282 VPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RG 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 493 EYVAPEKIENIY-----IRSQPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 536
Cdd:cd17648 361 QRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
189-534 |
1.98e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 60.41 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDlSIVCFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTESqwaptcaDVHISYLPLAHMFERMVQS 259
Cdd:PRK13390 143 RLTEQPCG-AVMLYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 260 VVYCHGGRVGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqantplkrwllefaakRKQAEVRSgiiRNDSi 338
Cdd:PRK13390 215 MVHALGGTVVLAKRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT---RYDV- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 339 wdelffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNH 415
Cdd:PRK13390 270 ----------SSL----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLH 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 416 IKLVDVEELNywackgEGEIcvrGPNVFK------GYLKDPDRTKEALDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIF 487
Cdd:PRK13390 335 ICDDDGNELP------AGRI---GTVYFErdrlpfRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 795413665 488 kLAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 534
Cdd:PRK13390 406 -ISGGVNIYPQETENALTMHPAVHDVAVIG-----------VPDPEM 440
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
195-501 |
2.25e-09 |
|
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: 60.18 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTESQwapTCADVHISYLPLAHM-FERMVQSVV--YCHGGRvgff 271
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFEREK---TNINFSDKVLQFATCsFDVCYQEIFstLLSGGT---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 272 qgdIRLLSDDMKALCPTIFPVVPRllNRMYDKIFSQAntplkrwLLEFAAKRKQaevrsgiirndsiwdelFFNkiqaSL 351
Cdd:cd17656 197 ---LYIIREETKRDVEQLFDLVKR--HNIEVVFLPVA-------FLKFIFSERE-----------------FIN----RF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 352 GGCVRMIVTGAAP--ASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNY 426
Cdd:cd17656 244 PTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 427 WACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKI 500
Cdd:cd17656 322 QPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEI 400
|
.
gi 795413665 501 E 501
Cdd:cd17656 401 E 401
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
188-525 |
2.41e-09 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 59.85 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSG--FLKVTESQWAPTCADVHISY-LPLAHMFERMVQSVVY 262
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYArnTLGIREDDVCFSAAKLFFAYgLGNALTFPMSVGATTV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 263 CHGGR---VGFFqgdirllsDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPlkrwllefaaKRKQAEVRsgiirndsiw 339
Cdd:TIGR02262 234 LMGERptpDAVF--------DRLRRHQPTIFYGVPTL----YAAMLADPNLP----------SEDQVRLR---------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 delffnkiqaslggcvrmIVTGAAPASPTVLGF-LRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHI 416
Cdd:TIGR02262 282 ------------------LCTSAGEALPAEVGQrWQARFGVDIVDGIGSTE--MLHIFLSnlPGDVRYGTSGKPVPGYRL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 417 KLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDigKWL--PAGTLKVIDRKKHIFKLAqGE 493
Cdd:TIGR02262 342 RLVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGD--KYVrnDDGSYTYAGRTDDMLKVS-GI 415
|
330 340 350
....*....|....*....|....*....|....*....
gi 795413665 494 YVAPEKIENIYIRSQPVAQIYVHG----DSL---KAFLV 525
Cdd:TIGR02262 416 YVSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
188-533 |
4.37e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 59.17 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 188 APVPPQPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtesqwaptcadvhiSYLPLaHMFERMVQSVVYCHGgr 267
Cdd:PRK07788 202 LPKPPKPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL----------------SRVPF-RAGETTLLPAPMFHA-- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGFFQGDI-----------------RLLSDDMKALCPTIFpVVPRLLNRMYDkifsqantplkrwLLEfaakrkqaEVRS 330
Cdd:PRK07788 261 TGWAHLTLamalgstvvlrrrfdpeATLEDIAKHKATALV-VVPVMLSRILD-------------LGP--------EVLA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 331 giirndsiwdelffnKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVG 408
Cdd:PRK07788 319 ---------------KYDTS---SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 409 APLPCNHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGTLKVIDR 482
Cdd:PRK07788 380 RPPKGVTVKILDengneVPR-------GVvGRIFVGNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGLLFVDGR 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 795413665 483 KKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 533
Cdd:PRK07788 449 DDDMI-VSGGENVFPAEVEDL---------LAGHPDVVEAAVIG--VDDEE 487
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
201-517 |
9.06e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 58.22 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 201 CFTSGTTGNPKGAMLTH-GNVVadfsgflkvtesqwaptcadvhisylplahmfermvQSVVYCHGGRVGFFQGDirlls 279
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSHrSNVL------------------------------------HALMANNGDALGTSAAD----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 280 ddmkalcpTIFPVVPrllnrMYdkifsQANTplkrWLLEFAAKRKQAEVRSGIIRND--SIWDELFFNKIQASLG----- 352
Cdd:PRK06018 222 --------TMLPVVP-----LF-----HANS----WGIAFSAPSMGTKLVMPGAKLDgaSVYELLDTEKVTFTAGvptvw 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 353 --------------GCVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV- 407
Cdd:PRK06018 280 lmllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLq 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 408 --GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKVIDRK 483
Cdd:PRK06018 357 kqGYPPFGVEMKITDDAgkELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRS 432
|
330 340 350
....*....|....*....|....*....|....
gi 795413665 484 KHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 517
Cdd:PRK06018 433 KDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
178-534 |
2.00e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 57.34 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 178 IQDCGQENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVteSQWAPTCADVHISYLPLAHMFERMV 257
Cdd:PRK13388 135 VAAAGALTPHREV--DAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALT--ERFGLTRDDVCYVSMPLFHSNAVMA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 258 Q-SVVYCHGGRVGF--------FQGDIRLLSddmkalcPTIFPVVPRLLNrmYdkIFSQ------ANTPLKRWLLEFAAK 322
Cdd:PRK13388 209 GwAPAVASGAAVALpakfsasgFLDDVRRYG-------ATYFNYVGKPLA--Y--ILATperpddADNPLRVAFGNEASP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 323 RKQAEvrsgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgFLRAaLGCQVYEGYGQTEctAGCTFTTPGDW 402
Cdd:PRK13388 278 RDIAE--------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 403 TSGHVGAPLPcnHIKLVDVEE---------------LNywACKGEGEICVR-GPNVFKGYLKDPDRTKEALdSDGWLHTG 466
Cdd:PRK13388 311 PPGSIGRGAP--GVAIYNPETltecavarfdahgalLN--ADEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSG 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 467 DIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 534
Cdd:PRK13388 386 DLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA-----------VPDERV 441
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
195-548 |
3.33e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 56.56 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGNVVAdFSGFLKVTESQWApTCADVHISYLPLAHMFERMVQSVVYC--HGGRV---G 269
Cdd:PRK05857 169 EDPLAMIFTSGTTGEPKAVLLANRTFFA-VPDILQKEGLNWV-TWVVGETTYSPLPATHIGGLWWILTClmHGGLCvtgG 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 270 FFQGDIR--LLSDDMKALCptifpVVPRLLNRM-YDKIFSQANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelffnk 346
Cdd:PRK05857 247 ENTTSLLeiLTTNAVATTC-----LVPTLLSKLvSELKSANATVPSLRLVGYGGSRAIAADVRF---------------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 347 IQAslggcvrmivTGAAPAsptvlgflraalgcQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDVEE 423
Cdd:PRK05857 306 IEA----------TGVRTA--------------QVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 424 LNYWACKGE-----GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPE 498
Cdd:PRK05857 361 IGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPD 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 795413665 499 KIENIYIRSQPV--AQIYVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 548
Cdd:PRK05857 439 EVDRIAEGVSGVreAACYEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
355-541 |
1.12e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 54.79 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 355 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNHiKLVDVEELN 425
Cdd:PRK05620 300 LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQVM 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 426 YWACKGEGEICVRGPNVFKGYLKDP----------------DRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKl 489
Cdd:PRK05620 379 ESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR- 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 490 AQGEYVAPEKIENIYIRSQPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK 541
Cdd:PRK05620 458 SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
343-525 |
1.75e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 343 FFNKIqasLGGC-------VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLP 412
Cdd:PRK06060 246 FFARV---IDSCspdsfrsLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 413 CNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkvidrKKHIF 487
Cdd:PRK06060 321 PYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADDT 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 795413665 488 KLAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFLV 525
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
349-533 |
1.95e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 53.68 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 349 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNY 426
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 427 WACKGEGEICV---RGPNV-FKGYLKDPDRTKealdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIEN 502
Cdd:cd05973 280 LGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|.
gi 795413665 503 IYIRSQPVAQIYVhgdslkaflvgIVVPDPE 533
Cdd:cd05973 355 ALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
193-512 |
2.40e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 193 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkvtesQWAPTCA--------DVHISYLPLAH---MFERMVQSV- 260
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVAN----------EQLIRHGfgidlnpdDVIVSWLPLYHdmgLIGGLLQPIf 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 --VYCHGGRVGFF--------------QGDIRLLSDDMKALCPtifpvvprllNRMYDKIFSQANtpLKRWLLEFAAkrk 324
Cdd:PRK05691 234 sgVPCVLMSPAYFlerplrwleaiseyGGTISGGPDFAYRLCS----------ERVSESALERLD--LSRWRVAYSG--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 325 qaevrSGIIRNDSIwdELFFNKIQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTA 392
Cdd:PRK05691 299 -----SEPIRQDSL--ERFAEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLM 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 393 GCTFTTPGdwtsghvgaplpcNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIG 469
Cdd:PRK05691 371 SCGRSQPG-------------HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG 437
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 795413665 470 kWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 512
Cdd:PRK05691 438 -FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
178-525 |
3.43e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 178 IQDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTE----SQWAPTCADVHISYLPLA 250
Cdd:PRK05691 3852 VQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEadviAQTASQSFDISVWQFLAA 3931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 251 HMFermvqsvvychGGRVGFFQGDIrllSDDMKALCP-------TIFPVVPRLLNRMydkifsqantplkrwllefaakr 323
Cdd:PRK05691 3932 PLF-----------GARVEIVPNAI---AHDPQGLLAhvqaqgiTVLESVPSLIQGM----------------------- 3974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 324 kqaevrsgiIRNDsiwdelffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------T 397
Cdd:PRK05691 3975 ---------LAED-----------RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaS 4034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 398 TPGDWTSghVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-------DSDGWLHTGDIGK 470
Cdd:PRK05691 4035 TRGSYLP--IGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLAR 4111
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 795413665 471 WLPAGTLKVIDRKKHI-----FKLAQGEYVApEKIENIYIRSQPVA-QIYVHGDSLKAFLV 525
Cdd:PRK05691 4112 RRSDGVLEYVGRIDHQvkirgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
410-470 |
2.06e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795413665 410 PLPCNHIK-----LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 470
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-541 |
1.05e-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: 48.15 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 192 PQPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTESQ-----------------WAPTCADVHISYLpLAHMF 253
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfRMLMGGADFGTGEFtpsedahkaaaaaagtvMFPAPPLMHGTGS-WTAFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 254 ERMVQSVVYCHGGRvgfFQGD--IRLLSddmKALCPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsg 331
Cdd:cd05924 79 GLLGGQTVVLPDDR---FDPEevWRTIE---KHKVTSMTIVGDAMARPLIDALRDAGPYDL------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 332 iirndsiwdelffnkiqASLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAP 410
Cdd:cd05924 134 -----------------SSL----FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 411 L-PCNHIKLVDVEELNYWACK--GEGEICVRGpNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKVIDRKK 484
Cdd:cd05924 190 FtRANPDTVVLDDDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGS 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 485 HIFKLAqGEYVAPEKIENIyIRSQP-VAQIYVHGdslkaflvgivVPDPEvmpsWAQK 541
Cdd:cd05924 269 VCINTG-GEKVFPEEVEEA-LKSHPaVYDVLVVG-----------RPDER----WGQE 309
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
196-533 |
1.14e-05 |
|
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: 48.12 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 196 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKVTesqwaptcaDVHISYLPLAHMFERMVQ-SVVYCHGGRVG 269
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGALPS---------DVLYTCLPLYHSTALIVGwSACLASGATLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 270 F--------FQGDIRllsddmKALCpTIFPVVPRLLnrmydkifsqantplkRWLLefAAKRKQAEVRsgiirndsiwde 341
Cdd:cd05940 153 IrkkfsasnFWDDIR------KYQA-TIFQYIGELC----------------RYLL--NQPPKPTERK------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 342 lffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-IK 417
Cdd:cd05940 196 ---HKVRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 418 LV--DVEELNYW---------ACKGE-----GEICVRGPnvFKGYLKDPDRTKEAL-----DSDGWLHTGDIGKWLPAGT 476
Cdd:cd05940 261 LVkyDLESGEPIrdaegrcikVPRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGF 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795413665 477 LKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSL-----KAFLVGIVVPDPE 533
Cdd:cd05940 339 WYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
355-502 |
1.29e-05 |
|
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: 47.40 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 355 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywacKGE 432
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEI 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 433 GEICVRGPNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 502
Cdd:cd17633 185 GKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
352-534 |
3.81e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 46.68 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 352 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDVE--ELNy 426
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 427 wacKGE-GEICVRGPNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyI 505
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKT-L 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 795413665 506 RSQP-VAQIYV-------HGDSLKAFlvgiVVPDPEV 534
Cdd:PRK13382 459 ATHPdVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
155-537 |
6.59e-05 |
|
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: 46.03 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 155 THIPWWWSRSMTPWALELSATSSIQdcgqenhHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGnvvadfsGF-LKVTES 233
Cdd:cd17634 199 TGSDIDWQEGRDLWWRDLIAKASPE-------HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTG-------GYlVYAATT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 234 qwaptcadvhisylpLAHMFERMVQSVVYChGGRVGFFQGDIRLLSDDMkALCPTIF-----PVVPRlLNRMYDKIFSQA 308
Cdd:cd17634 265 ---------------MKYVFDYGPGDIYWC-TADVGWVTGHSYLLYGPL-ACGATTLlyegvPNWPT-PARMWQVVDKHG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 309 NTPLkrWLLEFAAKRKQAEVRSGIIRNDsiwdelffnkiQASLggcvRMIVTGAAPASPTVLGFLRAALG---CQVYEGY 385
Cdd:cd17634 327 VNIL--YTAPTAIRALMAAGDDAIEGTD-----------RSSL----RILGSVGEPINPEAYEWYWKKIGkekCPVVDTW 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 386 GQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRG--PNVFKGYLKDPDRTKEALDS-- 459
Cdd:cd17634 390 WQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStf 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 460 DGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG--DSLKA-FLVGIVVPDPEVMP 536
Cdd:cd17634 469 KGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVLVAHPKVAEAAVVGipHAIKGqAPYAYVVLNHGVEP 547
|
.
gi 795413665 537 S 537
Cdd:cd17634 548 S 548
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
344-622 |
8.41e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 344 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDVEE 423
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 424 LNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 502
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 503 IYIRSQPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyadlCTSKDLKKAILEDmvrlgkesgLHSFEQV 580
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQLKSFCLQR---------LSSFKIP 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 795413665 581 KAIHIhsdmfsVQNGLLTPTLKAKRPELreyfKKQIEELYSI 622
Cdd:PRK07638 454 KEWHF------VDEIPYTNSGKIARMEA----KSWIENQEKI 485
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
189-222 |
1.68e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 44.50 E-value: 1.68e-04
10 20 30
....*....|....*....|....*....|....
gi 795413665 189 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 222
Cdd:PRK04319 199 IEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
148-251 |
1.74e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 44.48 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 148 SLRSWPATHIPWWWSRSMTPWALEL--SATSSIQDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV---A 222
Cdd:PRK08279 150 EARADLARPPRLWVAGGDTLDDPEGyeDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLkamG 229
|
90 100
....*....|....*....|....*....
gi 795413665 223 DFSGFLKVTESqwaptcaDVHISYLPLAH 251
Cdd:PRK08279 230 GFGGLLRLTPD-------DVLYCCLPLYH 251
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
345-509 |
1.89e-04 |
|
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: 44.34 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 345 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 417
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 418 LVDVEELNYWACKGEGE----ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGE 493
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|....*.
gi 795413665 494 YVAPEKIENIyIRSQP 509
Cdd:cd05915 421 WISSVDLENA-LMGHP 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
194-542 |
2.16e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.56 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-------TESQWAPTCADVHIS--YLPLAhmfermvqsvvycH 264
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAyglgvgdTVLQKTPFSFDVSVWefFWPLM-------------S 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 265 GGRVgffqgdirllsddmkalcptifPVVPRLLNRMYDKIFSQANTPLKRwLLEFAAKRKQAEVRSGIIrndsiwdelff 344
Cdd:PRK12316 721 GARL----------------------VVAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDEDV----------- 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 345 nkiqASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV--GAPLPCNHIKLVDVe 422
Cdd:PRK12316 767 ----ASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILDA- 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 423 ELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVA 496
Cdd:PRK12316 842 NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIE 920
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 795413665 497 PEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPD------PEVMPSWAQKR 542
Cdd:PRK12316 921 LGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
195-526 |
3.34e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 195 DDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTESQWAPTCADVHISYLPLAhmFErmvQSVVYCH-----GGRVG 269
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FD---VSVWECFwplitGCRLV 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 270 FF----QGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWlleFAAkrkqAEVRSGIIRNdsiwdelffn 345
Cdd:PRK05691 1344 LAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRL---FSG----GEALPAELRN---------- 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 346 kiqaslggcvrmivtgaapaspTVLGFLRAAlgcQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEE 423
Cdd:PRK05691 1407 ----------------------RVLQRLPQV---QLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCRVLD-AE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 424 LNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVA 496
Cdd:PRK05691 1461 LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVE 1539
|
330 340 350
....*....|....*....|....*....|..
gi 795413665 497 PEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 526
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
354-525 |
4.65e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 43.06 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 354 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGcTFTTPG---DWTSGhVGAPLPCNHIKLVDVEELNYwACK 430
Cdd:PRK13383 293 QLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPV-GPR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 431 GEGEICVRGPNVFKGYlkdPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 510
Cdd:PRK13383 370 VTGRIFVGGELAGTRY---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAV 444
|
170 180
....*....|....*....|..
gi 795413665 511 AQIYV-------HGDSLKAFLV 525
Cdd:PRK13383 445 ADNAVigvpderFGHRLAAFVV 466
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
190-221 |
5.24e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.11 E-value: 5.24e-04
10 20 30
....*....|....*....|....*....|..
gi 795413665 190 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV 221
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
194-517 |
5.83e-04 |
|
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: 42.80 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 194 PDDLSIVCFTSGTTGNPKGAMLTHG-NVVAD--FSGFLKVTESQWAPTCadvhisyLPLAH---MFERMVQSVVycHGGR 267
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRrTLVTSnlLSHDLNLKNGDRTYTC-------MPLYHgtaAFLGACNCLM--SGGT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 268 VGF--------FQGDIRllsdDMKAlcpTIFPVVPRLLnrmydkifsqantplkRWLLEFAAkrkqaevrsgiirndSIW 339
Cdd:cd05937 157 LALsrkfsasqFWKDVR----DSGA---TIIQYVGELC----------------RYLLSTPP---------------SPY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 340 DELffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL 418
Cdd:cd05937 199 DRD--HKVRVAWGNGLR----------PDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 419 --------VDVEELNYW----------ACKGE-GEICVRGPNV----FKGYLKDPDRTKEAL------DSDGWLHTGDIG 469
Cdd:cd05937 267 enqvvlvkMDPETDDPIrdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLL 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 795413665 470 KWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHG 517
Cdd:cd05937 347 RQDADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
188-251 |
9.07e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 42.24 E-value: 9.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795413665 188 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF----SGFLKVTESqwAPTCADVHISYLPLAH 251
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGG--VPPPDTTVVSWLPFYH 218
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
173-252 |
1.23e-03 |
|
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: 41.89 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 173 SATSSIQDCGQENHHAPVPPQPDDLS---------IVCFTSGTTGNPKGAMLTHGNVVAdFSGFLKVTesqwAPTCADVH 243
Cdd:cd05938 113 SNTEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLC----GVTADDVI 187
|
....*....
gi 795413665 244 ISYLPLAHM 252
Cdd:cd05938 188 YITLPLYHS 196
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
189-532 |
1.32e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 41.79 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 189 PVPPQPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVT-------ESQWAPTCADVHISYLPLAHMFERMVQSV 260
Cdd:PRK07798 158 FGERSPDDLYLLY-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATgepiedeEELAKRAAAGPGMRRFPAPPLMHGAGQWA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 261 VYchggrVGFFQGDIRLLSDDMKalcptifpvvprllnrmydkiFSQANtplkrwLLEFAAKRKqaeVRSGIIRNDS--- 337
Cdd:PRK07798 237 AF-----AALFSGQTVVLLPDVR---------------------FDADE------VWRTIEREK---VNVITIVGDAmar 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 338 -IWDELffnkiqASLGG----CVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwtSGHVGAPL 411
Cdd:PRK07798 282 pLLDAL------EARGPydlsSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 412 --PCNHIKLVDvEELNYWAcKGEGEICV--RGPNVFKGYLKDPDRTKEALDS-DG--WLHTGDIGKWLPAGTLKVIDRKK 484
Cdd:PRK07798 354 ftIGPRTVVLD-EDGNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGS 431
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 795413665 485 HIFKLAqGEYVAPEKIENIyIRSQPvaqiyvhgDSLKAFLVGivVPDP 532
Cdd:PRK07798 432 VCINTG-GEKVFPEEVEEA-LKAHP--------DVADALVVG--VPDE 467
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
444-532 |
2.16e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.18 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 444 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYVH 516
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 795413665 517 -----------GDSLKafLVGIVVPDP 532
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
182-254 |
7.50e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 39.35 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795413665 182 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKG-----------AMLTHGNVvadfsgF-LKVTESQWaptC-ADV-----H 243
Cdd:PRK00174 232 GASDECEPEPMDAEDPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYV------FdYKDGDVYW---CtADVgwvtgH 302
|
90
....*....|....*...
gi 795413665 244 --ISYLPLAH-----MFE 254
Cdd:PRK00174 303 syIVYGPLANgattlMFE 320
|
|
| |
