|
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 ... |
116-694 |
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: 991.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 116 QPYEWISYKEVSDRAECVGSALLHRGFKPSHVQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADL 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 196 SLVFCDKpdkarvllasvekgetpilntivimdsfgvdlvergkkcGVEVFSMREIEELGRAHRQKPMPPKPEDLAVICF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 276 TSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPSSDDVLISFLPLAHMFERIVECVVLCHGARIGFFQGDIRLLMDDL 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 356 KTLQPTVFPVVPRLLNRMFDKIFG--QADSSLKRWLLDFASKRKEAELRSGIVRNNSFWDKVIFRKIQASLGGRVKLMVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 434 GAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEMNYLAA--KGEGEVCIK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 512 GVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHGE 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 592 SLQAFLVGVVVPDPDTLHNWAKKK-GFEGSYQELCRNKDVKKYILEDMVRIGKESGLKSFEQVKDIVLHTEMFSIENGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 2032642720 671 TPTLKAKRPELRKYFQSQIDELYA 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
80-694 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 718.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 80 ELLSYY--YDDVRTVYDIFQRGLQVSNNGPCLGFRKPNQ----PYEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIF 153
Cdd:PLN02736 32 KLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKG--ACVGLY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 154 SQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFCdKPDKARVLLASVekGETPILNTIVIMDSFGVD 233
Cdd:PLN02736 110 FINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRLIVVVGGADEP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 234 LVERGKKCGVEVFSMREIEELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEksFVPSsd 313
Cdd:PLN02736 187 LPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYPS-- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 314 DVLISFLPLAHMFERIVECVVLCHGARIGFFQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFG--QADSSLKRWLLD 391
Cdd:PLN02736 263 DVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 392 FASKRKEAELRSGivRNNS-FWDKVIFRKIQASLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLS 470
Cdd:PLN02736 343 AAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 471 LPGDWTAGHVGAPMPCNIIKLVDVQEMNYLAAKG---EGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPN 547
Cdd:PLN02736 421 DEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPG 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 548 GTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHGESLQAFLVGVVVPDPDTLHNWAKKKGFE-GSYQELCR 626
Cdd:PLN02736 501 GRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCN 580
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032642720 627 NKDVKKYILEDMVRIGKESGLKSFEQVKDIVLHTEMFSIENGLLTPTLKAKRPELRKYFQSQIDELYA 694
Cdd:PLN02736 581 DPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-696 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 550.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 86 YDDVRTVYDIFQRGLQVSNNGPCLGfRKPNQPYEWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQ 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDR--VAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 166 ACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFCDKPDKARVLLASveKGETPILNTIVIMDsfgvdlvERGKKCGVEV 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 246 FSMREIEELGRAHRQKPM------PPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKttekSFVPSSDDVLISF 319
Cdd:COG1022 155 LSLDELLALGREVADPAElearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLE----RLPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 320 LPLAHMFERIVECVVLCHGARIGFfQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQADSS--LKRWLLDFA---S 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 395 KRKEAELRSGivRNNSFW--------DKVIFRKIQASLGGRVKLMVTGAAPVSASVLTFLRtALGCQFYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFR-ALGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 467 CSLSLPGDWTAGHVGAPMPCNIIKLVDvqemnylaakgEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 547 NGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHGESlQAFLVGVVVPDPDTLHNWAKKKG-FEGSYQELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGlPYTSYAELA 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032642720 626 RNKDVKKYILEDMVRIGKesGLKSFEQVKDI-VLHTEmFSIENGLLTPTLKAKRPELRKYFQSQIDELYANA 696
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFrLLPKE-FTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-681 |
9.20e-178 |
|
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: 514.45 E-value: 9.20e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 116 QPYEWISYKEVSDRAECVGSALLHRGFKPshVQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADL 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 196 SLVFCDKPDkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpeDLAVICF 275
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 276 TSGTTGNPKGAMITHQNIVSNASAFMKTTEksfvPSSDDVLISFLPLAHMFERI-VECVVLCHGARIGFFQgDIRLLMDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 355 LKTLQPTVFPVVPRLLNRMFDKIFGQADSSLKRWLLDFASkrkeaelrsgivrnnsfwdkvifrkiqaslGGRVKLMVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 435 AAPVSASVLTFLRtALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvqemnylaakgEGEVCIKGVN 514
Cdd:cd05907 220 GAPLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 515 VFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHGESlQ 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 595 AFLVGVVVPDPDTLHNWAKKKG-FEGSYQELCRNKDVKKYILEDMVRIGKEsgLKSFEQVKDIVLHTEMFSIENGLLTPT 673
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 2032642720 674 LKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
88-697 |
1.85e-169 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 500.91 E-value: 1.85e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 88 DVRTVYDIFQRGLQVSNNGPCLGFRKPNQ----PYEWISYKEVSDRAECVGSALLHRGFKPSHvqYIGIFSQNRPEWVII 163
Cdd:PLN02861 41 DIDSPWQFFSDAVKKYPNNQMLGRRQVTDskvgPYVWLTYKEVYDAAIRIGSAIRSRGVNPGD--RCGIYGSNCPEWIIA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 164 EQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFCDKPDKARVLlaSVEKGETPILNTIVIMDSFGVDLVERGKKCGV 243
Cdd:PLN02861 119 MEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 244 EVFSMREIEELGRAHRQKPmPPKPEDLAVICFTSGTTGNPKGAMITHQNIVS---NASAFMKTTEKsfVPSSDDVLISFL 320
Cdd:PLN02861 197 SCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAevlSTDHLLKVTDR--VATEEDSYFSYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 321 PLAHMFERIVECVVLCHGARIGFFQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQADSS--LKRWLLDFASKRKE 398
Cdd:PLN02861 274 PLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGgmLRKKLFDFAYNYKL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 399 AELRSGIVRNNS--FWDKVIFRKIQASLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWT 476
Cdd:PLN02861 354 GNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFS 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 477 -AGHVGAPMPCNIIKLVDVQEMNY--LAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PLN02861 434 mVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKII 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 554 DRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHGESLQAFLVGVVVPDPDTLHNWAKKKGFEGSYQELCRNKDVKKY 633
Cdd:PLN02861 513 DRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKY 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032642720 634 ILEDMVRIGKESGLKSFEQVKDIVLHTEMFSIENGLLTPTLKAKRPELRKYFQSQIDELYANAK 697
Cdd:PLN02861 593 ILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-695 |
2.03e-168 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 498.19 E-value: 2.03e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 88 DVRTVYDIFQRGLQVSNNGPCLGFRKPNQ----PYEWISYKEVSDRAECVGSALLHRGFKPSHvqYIGIFSQNRPEWVII 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGS--RVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 164 EQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC-DKpdKARVLLASVEKGETPiLNTIVIMDSFGVDLVERGKKCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEPDCKSAKR-LKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 243 VEVFSMREIEELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQN---IVSNASAFMKTTEKSFvpSSDDVLISF 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 320 LPLAHMFERIVECVVLCHGARIGFFQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFG--QADSSLKRWLLDFASKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 398 EAELRSGIVRNNS--FWDKVIFRKIQASLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 476 TA-GHVGAPMPCNIIKLVDVQEMNY--LAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKI 552
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 553 IDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHGESLQAFLVGVVVPDPDTLHNWAKKKGFEGSYQELCRNKDVKK 632
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032642720 633 YILEDMVRIGKESGLKSFEQVKDIVLHTEMFSIENGLLTPTLKAKRPELRKYFQSQIDELYAN 695
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRK 654
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-697 |
7.33e-165 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 489.15 E-value: 7.33e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 87 DDVRTVYDIFQRGLQVSNNGPCLGFR-----KPNQpYEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWV 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKDE--AKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 162 IIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFCDkpDKARVLLASVEKGETPILNTIVIMDSFGVDLVERGKKC 241
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--EKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 242 GVEVFSMREIEELGRAhRQKPMP-PKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASA---FMKTTEKSFvpSSDDVLI 317
Cdd:PLN02614 197 GLVIYAWDEFLKLGEG-KQYDLPiKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGvirLLKSANAAL--TVKDVYL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 318 SFLPLAHMFERIVECVVLCHGARIGFFQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQADSS--LKRWLLDFASK 395
Cdd:PLN02614 274 SYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 396 RKEAELRSGI--VRNNSFWDKVIFRKIQASLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPG 473
Cdd:PLN02614 354 YKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 474 DW-TAGHVGAPMPCNIIKLVDVQEMNY--LAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTL 550
Cdd:PLN02614 434 ELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSM 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 551 KIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHGESLQAFLVGVVVPDPDTLHNWAKKKGFEGSYQELCRNKDV 630
Cdd:PLN02614 513 KIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKA 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032642720 631 KKYILEDMVRIGKESGLKSFEQVKDIVLHTEMFSIENGLLTPTLKAKRPELRKYFQSQIDELYANAK 697
Cdd:PLN02614 593 KEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
3.50e-160 |
|
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: 471.31 E-value: 3.50e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 117 PYEWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLS 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKPGDK--VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 197 LVFCDkpdkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmpPKPEDLAVICFT 276
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 277 SGTTGNPKGAMITHQNIVSNASAFMKTTEKsfVPSSDDVLISFLPLAHMFERIVECVVLCHGARIGFfqGDIRLLMD--- 353
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPE--LLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 354 -----DLKTLQPTVFPVVPRLLNRMFDKIFGQAD--SSLKRWLLDFASKRKEAELRSGIvrNNSFWDKVIFRKIQASLGG 426
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNpmGGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 427 RVKLMVTGAAPVSASVLTFLRTALgCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEMNYLAAKGE- 505
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFLNIVL-CPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 506 -GEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVA 584
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 585 QVFVHGESLQAFLVGVVVPDPDTLHNWAKKKGF-EGSYQELCRNKDVKKYILEDMVRIGKESGLKSFEQVKDIVLHTEMF 663
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 2032642720 664 SIENGLLTPTLKAKR 678
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
60-694 |
1.81e-138 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 422.22 E-value: 1.81e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 60 QSVEVE-GGE--HARRSSllNSDELLSYYYDDVRTVYDIFQRGLQVSNNGPCLGFRKPNQ------------------PY 118
Cdd:PLN02387 27 RGVPVDvGGEpgYAIRNA--RFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKLISrefetssdgrkfeklhlgEY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLV 198
Cdd:PLN02387 105 EWITYGQVFERVCNFASGLVALGHNKE--ERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDkpDKARVLLASVEKGETPILNTIVIMDSFGVDLVERGKKCGVEVFSMREIEELGRAHRQKPMPPKPEDLAVICFTSG 278
Cdd:PLN02387 183 ICD--SKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNIVSNASAFMKTteksfVP--SSDDVLISFLPLAHMFERIVECVVLCHGARIGFfqGDIRLLMD--- 353
Cdd:PLN02387 261 STGLPKGVMMTHGNIVATVAGVMTV-----VPklGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsn 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 354 --------DLKTLQPTVFPVVPRLLNRMFDKIFGQADSS--LKRWLLDFASKRKEAELR------SGIVRnnSFWDKVIF 417
Cdd:PLN02387 334 kikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 RKIQASLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEM 497
Cdd:PLN02387 412 KKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEG 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 498 NYLAAKG---EGEVCIKGVNVFRGYLKDPEKTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 570
Cdd:PLN02387 492 GYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSL 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 571 EKIENVYLRCEAVAQVFVHGESLQAFLVGVVVPDPDTLHNWAKKKGFE-GSYQELCRNKDVKKYILEDMVRIGKESGLKS 649
Cdd:PLN02387 572 GKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEK 651
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2032642720 650 FEQVKDIVLHTEMFSIENGLLTPTLKAKRPELRKYFQSQIDELYA 694
Cdd:PLN02387 652 FEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-563 |
3.41e-132 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 396.30 E-value: 3.41e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 117 PYEWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLS 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKGDR--VAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 197 LVFCDKPDKARVLLASVEKGETPILNTIVIMDSFGVDLVergkkcgvevfsMREIEELGRAHRQKPMPPKPEDLAVICFT 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 277 SGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPSSDDVLISFLPLAHMFERIVEC-VVLCHGARIGFFQGDIRL----L 351
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALdpaaL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 352 MDDLKTLQPTVFPVVPRLLNRMFDKifgqadSSLKRWLLdfaskrkeaelrsgivrnnsfwdkvifrkiqaslgGRVKLM 431
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNMLLEA------GAPKRALL-----------------------------------SSLRLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 432 VTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDW---TAGHVGAPMPCNIIKLVDVQEMNYLAAKGEGEV 508
Cdd:pfam00501 283 LSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGEL 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2032642720 509 CIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 363 CVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
121-695 |
3.98e-104 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 333.10 E-value: 3.98e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKP-SHVqyiGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVF 199
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKgSNV---AIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 200 CDKpDKARVLLASVEKGETPilNTIVI-MDSFGVDLvergKKCGVEVFSMREIEELGR---AHRQKPMPPKPEDLAVICF 275
Cdd:PTZ00216 199 CNG-KNVPNLLRLMKSGGMP--NTTIIyLDSLPASV----DTEGCRLVAWTDVVAKGHsagSHHPLNIPENNDDLALIMY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 276 TSGTTGNPKGAMITHQNIVSNASAF-MKTTEKSFVPSSDDVLISFLPLAHMFERIVECVVLCHGARIGFfqGDIRLLMD- 353
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDt 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 354 ------DLKTLQPTVFPVVPRLlnrmFDKIFGQADS------SLKRWLLDFASKRKEAELRSGivRNNSFWDKVIFRKIQ 421
Cdd:PTZ00216 350 farphgDLTEFRPVFLIGVPRI----FDTIKKAVEAklppvgSLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSAPR 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 422 ASLGGRVKLMVTGAAPVSASVLTFLRTALGCqFYEGYGQTEcTAGC-SLSLPGDWTAGHVGAPMPCNIIKLVDVQEMNYl 500
Cdd:PTZ00216 424 AVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTE-TVCCgGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKH- 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 501 AAKGE--GEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYL 578
Cdd:PTZ00216 501 TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYG 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 579 RCEAVAQ----VFVHgeSLQAFLVGVVVPDPDTLHNWAKKKGFEGSYQELCRNKDVKKYILEDMVRIGKESGLKSFEQVK 654
Cdd:PTZ00216 581 QNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVR 658
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2032642720 655 DIVLHTEMFSIENGLLTPTLKAKRPELRKYFQSQIDELYAN 695
Cdd:PTZ00216 659 HVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
2.74e-93 |
|
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: 297.35 E-value: 2.74e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 116 QPYEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADL 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAG--EKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 196 SLVFcdkpdkarvllasVEKGetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkPEDLAVICF 275
Cdd:cd17640 79 VALV-------------VEND--------------------------------------------------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 276 TSGTTGNPKGAMITHQNI---VSNASAFMKtteksfvPSSDDVLISFLPLAHMFERIVECVVLCHGARIGFfqGDIRLLM 352
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLlhqIRSLSDIVP-------PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLK 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 353 DDLKTLQPTVFPVVPRLlnrmfdkifgqadsslkrWlldfaskrkEAeLRSGI---VRNNSFWDKVIFRKiqASLGGRVK 429
Cdd:cd17640 167 DDLKRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLF--FLSGGIFK 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 430 LMVTGAAPVSASVLTFLRtALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEMNYLAAKGEGEVC 509
Cdd:cd17640 217 FGISGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVW 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 510 IKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVH 589
Cdd:cd17640 296 VRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 590 GESlQAFLVGVVVPDPDTLHNWAKKKG--FEGSYQELCRNKDV-KKYILEDMVRIGKESGLKSFEQVKDIVLHTEMFsIE 666
Cdd:cd17640 376 GQD-QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVlKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPF-IE 453
|
570
....*....|...
gi 2032642720 667 NGLLTPTLKAKRP 679
Cdd:cd17640 454 NGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-685 |
1.08e-80 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 265.49 E-value: 1.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 118 YEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSL 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPG--SKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 198 VFCDKPDKARVLLASVekGETPILNTIVIMDSFGVDlvergkkcgvevfsmREIEELGRAHR--QKPMPPKPEDLAVICF 275
Cdd:cd05932 82 LFVGKLDDWKAMAPGV--PEGLISISLPPPSAANCQ---------------YQWDDLIAQHPplEERPTRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 276 TSGTTGNPKGAMITHQNIVSNASAFMKTteksFVPSSDDVLISFLPLAHMFERI-VECVVLCHGARIgFFQGDIRLLMDD 354
Cdd:cd05932 145 TSGTTGQPKGVMLTFGSFAWAAQAGIEH----IGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 355 LKTLQPTVFPVVPRLL----NRMFDKIfgqADSSLKRWLldfaskrkeaelrsgivrNNSFWDKVIFRKIQASLG-GRVK 429
Cdd:cd05932 220 VQRARPTLFFSVPRLWtkfqQGVQDKI---PQQKLNLLL------------------KIPVVNSLVKRKVLKGLGlDQCR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 430 LMVTGAAPVSASVLTFLRTaLGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvqemnylaakgEGEVC 509
Cdd:cd05932 279 LAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEIL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 510 IKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVH 589
Cdd:cd05932 347 VRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 590 GESLQAfLVGVVVpdpdtLHNWAKKKGFEGSYQELCRNkdvKKYILEDMvrigkESGLKSFEQVKDIVLHTEMFSIENGL 669
Cdd:cd05932 427 GSGLPA-PLALVV-----LSEEARLRADAFARAELEAS---LRAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGI 492
|
570
....*....|....*.
gi 2032642720 670 LTPTLKAKRPELRKYF 685
Cdd:cd05932 493 LTPTLKIKRNVLEKAY 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
121-615 |
9.51e-79 |
|
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: 258.59 E-value: 9.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADlslvfc 200
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDR--VALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSG------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 dkpdkARVLLAsvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpedlAVICFTSGTT 280
Cdd:COG0318 97 -----ARALVT-----------------------------------------------------------ALILYTSGTT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVSNASAFMKTTEksfvPSSDDVLISFLPLAHMFERIVECV-VLCHGARI----GFfqgDIRLLMDDL 355
Cdd:COG0318 113 GRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFGLTVGLLaPLLAGATLvllpRF---DPERVLELI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 356 KTLQPTVFPVVPRLLNRMFDkifgqadsslkrwlldfASKRKEAELRSgivrnnsfwdkvifrkiqaslggrVKLMVTGA 435
Cdd:COG0318 186 ERERVTVLFGVPTMLARLLR-----------------HPEFARYDLSS------------------------LRLVVSGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 436 APVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTA--GHVGAPMPCNIIKLVDVqEMNYLAAKGEGEVCIKGV 513
Cdd:COG0318 225 APLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVDE-DGRELPPGEVGEIVVRGP 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 514 NVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAVAQVFV----- 588
Cdd:COG0318 304 NVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpd 381
|
490 500 510
....*....|....*....|....*....|.
gi 2032642720 589 --HGESLQAFLVGV--VVPDPDTLHNWAKKK 615
Cdd:COG0318 382 ekWGERVVAFVVLRpgAELDAEELRAFLRER 412
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-693 |
2.08e-74 |
|
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: 251.12 E-value: 2.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 113 KPNQPYEWISYKEVSDRAECVGSALLHRGFKPSHvqYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNK 192
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFH--GVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 193 ADLSLVFCDKPDKARVLLASveKGETPILNTIVImdsFGVDLVErgKKCGVevFSMREIEELGR-----AHRQKPMPPKP 267
Cdd:cd05933 79 SEANILVVENQKQLQKILQI--QDKLPHLKAIIQ---YKEPLKE--KEPNL--YSWDEFMELGRsipdeQLDAIISSQKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 268 EDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPSSDDVLISFLPLAHMFERIVEC-VVLCHGARIGFFQG 346
Cdd:cd05933 150 NQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFAQP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 347 DIR--LLMDDLKTLQPTVFPVVPRLLNRMFDKI-FGQADSS-LKRWLLDFAsKRK--EAELRSGIVRNNSFW-----DKV 415
Cdd:cd05933 230 DALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkAVGAKSGtLKRKIASWA-KGVglETNLKLMGGESPSPLfyrlaKKL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 416 IFRKIQASLG-GRVKLMVTGAAPVSASVLTFLrTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDV 494
Cdd:cd05933 309 VFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 495 QemnylaAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIE 574
Cdd:cd05933 388 D------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 575 N-VYLRCEAVAQVFVHGESLQaFLVGVVV----PDPDT----------LHNWAKKKGFEGSY-QELCRNKD--VKKYILE 636
Cdd:cd05933 462 DaVKKELPIISNAMLIGDKRK-FLSMLLTlkceVNPETgepldelteeAIEFCRKLGSQATRvSEIAGGKDpkVYEAIEE 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032642720 637 DMVRIGKESGLKSFEQVKDIVLHTEmFSIENGLLTPTLKAKRPELRKYFQSQIDELY 693
Cdd:cd05933 541 GIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
118-671 |
5.36e-70 |
|
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: 239.28 E-value: 5.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 118 YEWISYKEVSDRAECVGSAllhrgFKPSHV----QYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKA 193
Cdd:cd17632 65 FETITYAELWERVGAVAAA-----HDPEQPvrpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 194 DLSLVFCDkPDKARVLLASVEKGETPilNTIVIMDSFGVDLVER-----------GKKCGVEVFSM-REIEELGRAHRQK 261
Cdd:cd17632 140 EPRLLAVS-AEHLDLAVEAVLEGGTP--PRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLiAVRGRDLPPAPLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 262 PMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPSsddVLISFLPLAHMFERIVECVVLCHGArI 341
Cdd:cd17632 217 RPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPAS---ITLNFMPMSHIAGRISLYGTLARGG-T 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 342 GFFQG--DIRLLMDDLKTLQPTVFPVVPRLlnrmFDKIFGQADSSLKRWLLDFA-----SKRKEAELRsgivrnnsfwDK 414
Cdd:cd17632 293 AYFAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSVAGAdaetlAERVKAELR----------ER 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 415 VifrkiqasLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTEctAGCSLSLpgdwtaGHVGAPmPCNIIKLVDV 494
Cdd:cd17632 359 V--------LGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRP-PVLDYKLVDV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 495 QEMNYLAAKG---EGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 571
Cdd:cd17632 422 PELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVA 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 572 KIENVYLRCEAVAQVFVHGESLQAFLVGVVVPDPDTLhnwakkkgfEGSYQELCRNKdvkkyILEDMVRIGKESGLKSFE 651
Cdd:cd17632 502 RLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDAL---------AGEDTARLRAA-----LAESLQRIAREAGLQSYE 567
|
570 580
....*....|....*....|
gi 2032642720 652 QVKDIVLHTEMFSIENGLLT 671
Cdd:cd17632 568 IPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
121-678 |
2.47e-69 |
|
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: 236.94 E-value: 2.47e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDV--VAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 ---DKPDKARVLLAsvekgETPILNTIVIMDSFGVDLVERGKkcgveVFSMREIEELGRA-HRQKP-------MPPKPED 269
Cdd:cd17641 90 edeEQVDKLLEIAD-----RIPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPglyerevAAGKGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 270 LAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpsSDDVLISFLPLAHMFERIVECVVLCHGARIGFFQGDIR 349
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLG----PGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 350 LLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQ-ADSS-----LKRWLLDFASKRKEAELRS---GIVRNNSFW--DKVIFR 418
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIAADVRARmMDATpfkrfMFELGMKLGLRALDRGKRGrpvSLWLRLASWlaDALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 419 KIQASLG-GRVKLMVTGAAPVSASVLTFLRtALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVqem 497
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 498 nylaakgeGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN-- 575
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENkl 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 576 ---VYLRcEAVaqVFVHGeslQAFLVGVVVPDPDTLHNWAKKKGFE-GSYQELCRNKDVKKYILEDMVRIGKEsgLKSFE 651
Cdd:cd17641 464 kfsPYIA-EAV--VLGAG---RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQ 535
|
570 580
....*....|....*....|....*...
gi 2032642720 652 QV-KDIVLHTEMfSIENGLLTPTLKAKR 678
Cdd:cd17641 536 RIrRFLLLYKEL-DADDGELTRTRKVRR 562
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-678 |
1.53e-68 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 231.95 E-value: 1.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTG--DRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpeDLAVICFTSGTT 280
Cdd:cd05914 86 SDED----------------------------------------------------------------DVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVSNAsAFMKTTEKSfvpSSDDVLISFLPLAHMFERIVECVV-LCHGARIGFFQGDIRLLMDDLKTLQ 359
Cdd:cd05914 102 GNSKGVMLTYRNIVSNV-DGVKEVVLL---GKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 360 PTVFPVVPRLLnRMFDKIFG--QADSSLKRWLLDFASKRKEAELRsgivrnnsfwdKVIFRKIQASLGGRVKLMVTGAAP 437
Cdd:cd05914 178 VTPTLGVPVPL-VIEKIFKMdiIPKLTLKKFKFKLAKKINNRKIR-----------KLAFKKVHEAFGGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 438 VSASVLTFLRTaLGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPmpcniIKLVDVQEMNYLAAKGEGEVCIKGVNVFR 517
Cdd:cd05914 246 INPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 518 GYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVA--QVFVHGESLQA 595
Cdd:cd05914 320 GYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 596 flvgVVVPDPDTLHNWAKKkgfegsyqelcrNKDVKKYILEDmVRIGKESGLKSFEQVKDIVLHTEMFSienglLTPTLK 675
Cdd:cd05914 400 ----LAYIDPDFLDVKALK------------QRNIIDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFE-----KTPKGK 457
|
...
gi 2032642720 676 AKR 678
Cdd:cd05914 458 IKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-615 |
5.04e-67 |
|
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: 223.70 E-value: 5.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 269 DLAVICFTSGTTGNPKGAMITHQNIVSNASAFmkttEKSFVPSSDDVLISFLPLAHMFERIVECVVLCHGARIGFFQG-D 347
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAAL----AASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKfD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IRLLMDDLKTLQPTVFPVVPRLLNRMFDkifgqadsslkrwlldfASKRKEAELRSgivrnnsfwdkvifrkiqaslggr 427
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLK-----------------APESAGYDLSS------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 428 VKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWT--AGHVGAPMPCNIIKLVDVqEMNYLAAKGE 505
Cdd:cd04433 116 LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDP-DGGELPPGEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 506 GEVCIKGVNVFRGYLKDPEKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYLRCEAVAQ 585
Cdd:cd04433 195 GELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAE 272
|
330 340 350
....*....|....*....|....*....|....*....
gi 2032642720 586 VFVHG---ESLQAFLVGVVVP------DPDTLHNWAKKK 615
Cdd:cd04433 273 AAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-615 |
3.43e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 227.09 E-value: 3.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPS-HVqyiGIFSQNRPEWVIieqACYAFSM---VVVPLYDTLGAEAITYIVNKADLS 196
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGdRV---AIWAPNSPHWVI---AALGALKagaVVVPLNTRYTADEAAYILARGDAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 197 LVFCDKPdkarvLLASVEKGET--PILNTIVIMDSFGVDLVERGKKCGVEVFSMREIEELGRAHRqkpmppkPEDLAVIC 274
Cdd:PRK07656 105 ALFVLGL-----FLGVDYSATTrlPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVD-------PDDVADIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 275 FTSGTTGNPKGAMITHQNIVSNASAFMKTTEksfVPSSDDVLISfLPLAHMFERIVeCVVLC--HGARI----GFfqgDI 348
Cdd:PRK07656 173 FTSGTTGRPKGAMLTHRQLLSNAADWAEYLG---LTEGDRYLAA-NPFFHVFGYKA-GVNAPlmRGATIlplpVF---DP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 349 RLLMDDLKTLQPTVFPVVPRLLNRMFDkifgqadsslkrwlldfASKRKEAELRSgivrnnsfwdkvifrkiqaslggrV 428
Cdd:PRK07656 245 DEVFRLIETERITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------L 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 429 KLMVTGAAPVSASVLTFLRTALGCQ-FYEGYGQTECTAGCSLSLPGD---WTAGHVGAPMPCNIIKLVDVQEmNYLAAKG 504
Cdd:PRK07656 284 RLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVNELG-EEVPVGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 505 EGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVA 584
Cdd:PRK07656 363 VGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2032642720 585 QVFV-------HGESLQAFlvgvVVP------DPDTLHNWAKKK 615
Cdd:PRK07656 442 EAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-606 |
3.45e-65 |
|
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: 223.63 E-value: 3.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDV--VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDKARVLLASVEKGETPilnTIVIMDSFGVDLVERGKkcGVEVFSMREIEELgrahrqkPMPPK--PEDLAVICFTSG 278
Cdd:cd05911 89 DPDGLEKVKEAAKELGPKD---KIIVLDDKPDGVLSIED--LLSPTLGEEDEDL-------PPPLKdgKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNIVSNASaFMKTTEKSFVPSsDDVLISFLPLAHMF--ERIVECvvLCHGA-RIGFFQGDIRLLMDDL 355
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLS-QVQTFLYGNDGS-NDVILGFLPLYHIYglFTTLAS--LLNGAtVIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 356 KTLQPTVFPVVPRLLNRMF-DKIFGQAD-SSLKRWLldfaskrkeaelrsgivrnnsfwdkvifrkiqaslggrvklmvT 433
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAkSPLLDKYDlSSLRVIL-------------------------------------------S 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 434 GAAPVSASVLTFLRTALG-CQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPcNI-IKLVDVQEMNYLAAKGEGEVCIK 511
Cdd:cd05911 270 GGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEPGEICVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 512 GVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFVHGe 591
Cdd:cd05911 349 GPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG- 426
|
490
....*....|....*
gi 2032642720 592 slqaflvgvvVPDPD 606
Cdd:cd05911 427 ----------IPDEV 431
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
92-615 |
3.18e-64 |
|
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: 220.51 E-value: 3.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 92 VYDIFQRGLQVSNNGPCLGFRKpnqpyEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFS 171
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPG--DRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 172 MVVVPLYDTLGAEAITYIVNKADlslvfcdkpdkARVllasvekgetpilntIVIMDSFgVDLVERGKKcgvevfsmrei 251
Cdd:cd05936 74 AVVVPLNPLYTPRELEHILNDSG-----------AKA---------------LIVAVSF-TDLLAAGAP----------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 252 eelgrahRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPssDDVLISFLPLAHMFERIVE 331
Cdd:cd05936 116 -------LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEG--DDVVLAALPLFHVFGLTVA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 332 CVV-LCHGARIGFFQG-DIRLLMDDLKTLQPTVFPVVPRllnrMFDKIFGQADsslkrwlldfaskrkeaelrsgivrnn 409
Cdd:cd05936 187 LLLpLALGATIVLIPRfRPIGVLKEIRKHRVTIFPGVPT----MYIALLNAPE--------------------------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 410 sfwdkviFRKIQASlggRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECT-AGCSLSLPGDWTAGHVGAPMPCNI 488
Cdd:cd05936 236 -------FKKRDFS---SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTE 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 489 IKLVDVQemNYLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 567
Cdd:cd05936 306 VKIVDDD--GEELPPGEvGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFN 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032642720 568 IAPEKIENVYLRCEAVAQVFV-------HGESLQAFLV---GVVVpDPDTLHNWAKKK 615
Cdd:cd05936 382 VYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVVlkeGASL-TEEEIIAFCREQ 438
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-615 |
4.71e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 205.04 E-value: 4.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 86 YDDVRTVYDIFQRGLQVSNNGPCLGFRKPNqpyewISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQ 165
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKKG--DRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 166 ACYAFSMVVVPLYDTLGAEAITYIVNKADlslvfcdkpdkARVLLASVE--------KGETPILNTIVIMDSfgvdlvER 237
Cdd:PRK06187 75 AVPKIGAVLHPINIRLKPEEIAYILNDAE-----------DRVVLVDSEfvpllaaiLPQLPTVRTVIVEGD------GP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 238 GKKCGVEVfsmREIEELGRAhrQKPMPPKPE----DLAVICFTSGTTGNPKGAMITHQNIVSN---ASAFMKTTeksfvp 310
Cdd:PRK06187 138 AAPLAPEV---GEYEELLAA--ASDTFDFPDidenDAAAMLYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLS------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 311 sSDDVLISFLPLAHMFERIVECVVLCHGARI---GFFqgDIRLLMDDLKTLQPTVFPVVPRLLNRMFdkifgQADSSLKR 387
Cdd:PRK06187 207 -RDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPENLLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 388 WLldfaskrkeaelrsgivrnnsfwdkvifrkiqaslgGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGC 467
Cdd:PRK06187 279 DF------------------------------------SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 468 SLSLP-----GDWT-AGHVGAPMPCNIIKLVDvQEMNYLAAKGE--GEVCIKGVNVFRGYLKDPEKTAEALDkDGWLHTG 539
Cdd:PRK06187 323 SVLPPedqlpGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTG 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 540 DIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAVAQVFV-------HGESLQAFLVG--VVVPDPDTLHN 610
Cdd:PRK06187 401 DVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAEVAVigvpdekWGERPVAVVVLkpGATLDAKELRA 479
|
....*
gi 2032642720 611 WAKKK 615
Cdd:PRK06187 480 FLRGR 484
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-607 |
1.05e-49 |
|
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: 179.73 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADlslvfc 200
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDR--VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSG------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 dkpdkARVLLasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpEDLAVICFTSGTT 280
Cdd:cd17631 93 -----AKVLF---------------------------------------------------------DDLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVSNASAfmktTEKSFVPSSDDVLISFLPLAHMFERIVECV-VLCHGARI----GFfqgDIRLLMDDL 355
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVN----ALAALDLGPDDVLLVVAPLFHIGGLGVFTLpTLLRGGTVvilrKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 356 KTLQPTVFPVVPRLLNRMFDKifGQADSslkrwlLDFASkrkeaeLRSGIVrnnsfwdkvifrkiqaslggrvklmvtGA 435
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQH--PRFAT------TDLSS------LRAVIY---------------------------GG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 436 APVSASVLTFLRtALGCQFYEGYGQTECTAGCSLSLPGDW--TAGHVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGV 513
Cdd:cd17631 223 APMPERLLRALQ-ARGVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 514 NVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYLRCEAVAQVFV----- 588
Cdd:cd17631 301 HVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVigvpd 378
|
490 500
....*....|....*....|.
gi 2032642720 589 --HGESLQAflvgVVVPDPDT 607
Cdd:cd17631 379 ekWGEAVVA----VVVPRPGA 395
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-695 |
5.87e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 169.13 E-value: 5.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 233 DLVERGKKCGVevfSMREIEEL--GRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNI------VSNASAFMKTT 304
Cdd:PTZ00342 270 DLKEKAKKLGI---SIILFDDMtkNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKKYN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 305 EKSFvpssddvlISFLPLAHMFERIVECVVLCHGARIGFFQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQAD-- 382
Cdd:PTZ00342 347 PKTH--------LSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnl 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 383 SSLKRWLLdfaskRKEAELRSGivRNNSFWDKV------IFRKIQASLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYE 456
Cdd:PTZ00342 419 PPLKRFLV-----KKILSLRKS--NNNGGFSKFlegithISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 457 GYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIikLVDVQEMNYLAAKG---EGEVCIKGVNVFRGYLKDPEKTAEALDKD 533
Cdd:PTZ00342 492 GYGLTETTGPIFVQHADDNNTESIGGPISPNT--KYKVRTWETYKATDtlpKGELLIKSDSIFSGYFLEKEQTKNAFTED 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 534 GWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHG-ESLQAFLvGVVVPDPDTLHNWA 612
Cdd:PTZ00342 570 GYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLFKCL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 613 KKKGF-------EGSYQELCRNKDVKK-----YILEDMVRIGKESGLKSFEQVKDIVLHTEMFSIENgLLTPTLKAKRPE 680
Cdd:PTZ00342 649 KDDNMlestginEKNYLEKLTDETINNniyvdYVKGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFY 727
|
490
....*....|....*...
gi 2032642720 681 LRK---YFQSQIDELYAN 695
Cdd:PTZ00342 728 VFKdyaFFIDQVKKIYKN 745
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
269-637 |
1.51e-43 |
|
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: 162.84 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 269 DLAVICFTSGTTGNPKGAMITHQNIVSNASAFmkTTEKSFvpSSDDVLISFLPLAHMFERIVecVVLC---HGARI---G 342
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRAL--VDAWRW--TEDDVLLHVLPLHHVHGLVN--ALLCplfAGASVeflP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 343 FF---QGDIRLLMDDLktlqpTVFPVVP----RLLnrmfdkifgqADSSLKRWLLDFASKRKEAELRsgivrnnsfwdkv 415
Cdd:cd05941 164 KFdpkEVAISRLMPSI-----TVFMGVPtiytRLL----------QYYEAHFTDPQFARAAAAERLR------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 416 ifrkiqaslggrvkLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTEctAGCSLSLP--GDWTAGHVGAPMPCNIIKLVD 493
Cdd:cd05941 216 --------------LMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 494 VQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEK 572
Cdd:cd05941 280 EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALE 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032642720 573 IENVYLRCEAVAQVFVHGESLQAF---LVGVVVP-------DPDTLHNWAKkkgfegsyQELCRNKDVKKYILED 637
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAK--------QRLAPYKRPRRLILVD 425
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
121-606 |
1.24e-41 |
|
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: 158.55 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFc 200
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDV--VLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAF- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 dkpdkarVLLASVEKGEtPILNTIVIMDS--FGVDLVERGKKCGVEvfsmreieelgrahrqkPMPPKPE----DLAVIC 274
Cdd:cd05904 110 -------TTAELAEKLA-SLALPVVLLDSaeFDSLSFSDLLFEADE-----------------AEPPVVVikqdDVAALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 275 FTSGTTGNPKGAMITHQNIVSNASAFMKTTEKsfVPSSDDVLISFLPLAHMFERiveCVVLCHGARIG--------Ffqg 346
Cdd:cd05904 165 YSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGS--NSDSEDVFLCVLPMFHIYGL---SSFALGLLRLGatvvvmprF--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 347 DIRLLMDDLKTLQPTVFPVVPRLLNRMFDK-IFGQAD-SSLKRwlldfaskrkeaelrsgivrnnsfwdkvifrkiqasl 424
Cdd:cd05904 237 DLEELLAAIERYKVTHLPVVPPIVLALVKSpIVDKYDlSSLRQ------------------------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 ggrvklMVTGAAPVSASVL-TFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVG-----APMPCniIKLVDVQEMN 498
Cdd:cd05904 280 ------IMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNVE--AKIVDPETGE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 499 YLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYL 578
Cdd:cd05904 352 SLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLL 430
|
490 500
....*....|....*....|....*...
gi 2032642720 579 rceavaqvfVHGESLQAflvgVVVPDPD 606
Cdd:cd05904 431 ---------SHPEILDA----AVIPYPD 445
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
119-615 |
3.28e-39 |
|
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: 151.70 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLV 198
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGDR--VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDKPDKARVLLASVEKGETpILNtiVIMDSFGVDLVERGKKCGVEVFSMREIEELGrahrqkpmPPKPEDLAVICFTSG 278
Cdd:cd05926 91 LTPKGELGPASRAASKLGLA-ILE--LALDVGVLIRAPSAESLSNLLADKKNAKSEG--------VPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNIVSNasafMKTTEKSFVPSSDDVLISFLPLAHMFERIVECV-VLCHGARI----GFfqgDIRLLMD 353
Cdd:cd05926 160 TTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLsTLAAGGSVvlppRF---SASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 354 DLKTLQPTVFPVVPRLLnrmfdKIfgqadsslkrwLLDFASKRKEAELRSgivrnnsfwdkviFRKIQASlggrvklmvt 433
Cdd:cd05926 233 DVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESPPPK-------------LRFIRSC---------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 434 gAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLS-LPGDW-TAGHVGAPmpcNIIKLVDVQEM-NYLAAKGEGEVCI 510
Cdd:cd05926 274 -SASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNpLPPGPrKPGSVGKP---VGVEVRILDEDgEILPPGVVGEICL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 511 KGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAVAQ--VF- 587
Cdd:cd05926 350 RGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEavAFg 428
|
490 500 510
....*....|....*....|....*....|....*...
gi 2032642720 588 ----VHGESLQAflvgVVVP------DPDTLHNWAKKK 615
Cdd:cd05926 429 vpdeKYGEEVAA----AVVLregasvTEEELRAFCRKH 462
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
264-616 |
3.96e-39 |
|
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: 151.33 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 264 PPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTteksFVPSSDDVLISFLPLAHMFerivecvvlchgariGF 343
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAI----FDPNPEDVVFGALPFFHSF---------------GL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 344 FQGDIRLLMDDLKTLQ---PTVFPVVPRLLNRMFDKIFGQADSSLKrwlldfaskrkeaelrsGIVRNnsfWDKVIFRki 420
Cdd:cd05909 204 TGCLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPTFLR-----------------GYARA---AHPEDFS-- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 421 qaslggRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPG-DWTAGHVGAPMPCNIIKLVDVQEMNY 499
Cdd:cd05909 262 ------SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 500 LAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN-VYL 578
Cdd:cd05909 336 VPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDiLSE 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2032642720 579 RCE---AVAQVFV----HGESLQAFLVGvVVPDPDTLHNWAKKKG 616
Cdd:cd05909 414 ILPednEVAVVSVpdgrKGEKIVLLTTT-TDTDPSSLNDILKNAG 457
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
249-605 |
5.08e-39 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 152.34 E-value: 5.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 249 REIEELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSN---ASAFMKTTEKsfVPSSDDVLISFLPLAHM 325
Cdd:PRK08751 189 REALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGK--LEEGCEVVITALPLYHI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 326 FE---------RIVECVVLCHGARigffqgDIRLLMDDLKTLQPTVFPVVPRLLNRMFdkifgqadsslkrwlldfaskr 396
Cdd:PRK08751 267 FAltanglvfmKIGGCNHLISNPR------DMPGFVKELKKTRFTAFTGVNTLFNGLL---------------------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 397 keaelrsgivrNNSFWDKVIFRKIQASLGGrvklmvtGAApVSASVLTFLRTALGCQFYEGYGQTECT-AGCSLSLPGDW 475
Cdd:PRK08751 319 -----------NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 476 TAGHVGAPMPCNIIKLVDvqEMNYLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIID 554
Cdd:PRK08751 380 YNGSIGLPIPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVD 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2032642720 555 RKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFVHG----ESLQAFLVGVVVPDP 605
Cdd:PRK08751 458 RKKDMI-LVSGFNVYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-615 |
1.64e-38 |
|
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: 146.27 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAF---MKTTEksfvpssDDVLISFLPLAHMFErIVECVVLC--HGARI 341
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIgerLGLTE-------QDRLCIPVPLFHCFG-SVLGVLACltHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 342 GF----FqgDIRLLMDDLKTLQPTVFPVVPRllnrMFDKIFGQADSSLkrwlLDFASkrkeaeLRSGIvrnnsfwdkvif 417
Cdd:cd05917 73 VFpspsF--DPLAVLEAIEKEKCTALHGVPT----MFIAELEHPDFDK----FDLSS------LRTGI------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 rkiqaslggrvklmvTGAAPVSASVLTFLRTALGC-QFYEGYGQTECTAGCSLSLPGD---WTAGHVGAPMPCNIIKLVD 493
Cdd:cd05917 125 ---------------MAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHTEAKIVD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 494 vQEMNYLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEK 572
Cdd:cd05917 190 -PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPRE 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2032642720 573 IENVYLRCEAVAQVFV-------HGESLQAFLVGVVVPDP--DTLHNWAKKK 615
Cdd:cd05917 268 IEEFLHTHPKVSDVQVvgvpderYGEEVCAWIRLKEGAELteEDIKAYCKGK 319
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
182-598 |
1.72e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 150.68 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 182 GAEAITYIVNKADLSLVFCDKPDKARVLLASVEKGETPILNTIVimdsfgvDLVERGKKCGVEVFSM----REIEELGRA 257
Cdd:PRK05677 122 GAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLKRLLI-------NAVVKHVKKMVPAYHLpqavKFNDALAKG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 258 HRQ--KPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAfMKTTEKSFVPSSDDVLISFLPLAHMFERIVECVVL 335
Cdd:PRK05677 195 AGQpvTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAM 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 336 chgarigffqgdirLLMDDLKTLQPTvfpvvPRLLNRMFdkifgqadSSLKRWLLdfaskrkeaelrSGIVRNNSFWDKV 415
Cdd:PRK05677 274 --------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNTLFVAL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 416 I----FRKIQASlggRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKL 491
Cdd:PRK05677 315 CnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 492 VDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 571
Cdd:PRK05677 392 ID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPN 469
|
410 420 430
....*....|....*....|....*....|....
gi 2032642720 572 KIENVYLRCEAVAQVFV-------HGESLQAFLV 598
Cdd:PRK05677 470 ELEDVLAALPGVLQCAAigvpdekSGEAIKVFVV 503
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
150-615 |
2.70e-38 |
|
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: 147.60 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 150 IGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFCDKPDKARVLLA-SVEKGETPILNTIVIMD 228
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLLEEKDFQAdSLDRIEAAGRYETSLSA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 229 SFgvdlvergkkcgvevfsmreieelgrahrqkPMppkpEDLAVICFTSGTTGNPKGAMITHQNIVSNAsafMKTTEKSF 308
Cdd:TIGR01923 107 SF-------------------------------NM----DQIATLMFTSGTTGKPKAVPHTFRNHYASA---VGSKENLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 309 VPSSDDVLISfLPLAHM--FERIVECVVlcHGARIGFFQGDIRLLmDDLKTLQPTVFPVVPRLLNRMFDKifGQADSSLK 386
Cdd:TIGR01923 149 FTEDDNWLLS-LPLYHIsgLSILFRWLI--EGATLRIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNENLR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 387 RWLLdfaskrkeaelrsgivrnnsfwdkvifrkiqaslggrvklmvtGAAPVSAsvlTFLRTAL--GCQFYEGYGQTE-C 463
Cdd:TIGR01923 223 KILL-------------------------------------------GGSAIPA---PLIEEAQqyGLPIYLSYGMTEtC 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 464 TAGCSLSLPGDWTAGHVGAPMPCNIIKL-VDVQEmnylaakGEGEVCIKGVNVFRGYLkDPEKTAEALDKDGWLHTGDIG 542
Cdd:TIGR01923 257 SQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 543 KWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFV-------HGESLQAFLVGVVVPDPDTLHNWAKKK 615
Cdd:TIGR01923 329 ELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQVPVAYIVSESDISQAKLIAYLTEK 407
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
121-606 |
3.87e-38 |
|
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: 149.21 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDR--IAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDKARVLlaSVEKgETPILNTIVIMDSfGVDLveRGKKCgVEVFSMREIEELGRAHRQKPMP-PKPEDLAVICFTSGT 279
Cdd:cd17642 123 SKKGLQKVL--NVQK-KLKIIKTIIILDS-KEDY--KGYQC-LYTFITQNLPPGFNEYDFKPPSfDRDEQVALIMNSSGS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 280 TGNPKGAMITHQNIVSNASAFMKTTEKSfVPSSDDVLISFLPLAHMFERIVECVVLCHGARIGF-FQGDIRLLMDDLKTL 358
Cdd:cd17642 196 TGLPKGVQLTHKNIVARFSHARDPIFGN-QIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmYKFEEELFLRSLQDY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 359 QPTVFPVVPRLLnrmfdkifgqadsslkrwlldfaskrkeaelrsgivrnnSFWDK-VIFRKIQASlggRVKLMVTGAAP 437
Cdd:cd17642 275 KVQSALLVPTLF---------------------------------------AFFAKsTLVDKYDLS---NLHEIASGGAP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 438 VSASVLTFLRTALGCQFY-EGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEMNYLAAKGEGEVCIKGVNVF 516
Cdd:cd17642 313 LSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 517 RGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFVHGeslqaf 596
Cdd:cd17642 393 KGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG------ 465
|
490
....*....|
gi 2032642720 597 lvgvvVPDPD 606
Cdd:cd17642 466 -----IPDED 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
172-598 |
4.18e-38 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 149.43 E-value: 4.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 172 MVVV---PLY----------DTlGAEAITYIVNkadlslvFcdkpdkARVLLASVEKgeTPILNtiVIMDSFGvDLVERG 238
Cdd:PRK08974 99 MIVVnvnPLYtprelehqlnDS-GAKAIVIVSN-------F------AHTLEKVVFK--TPVKH--VILTRMG-DQLSTA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 239 KKCGV-----------------EVFSMREIEELGRaHRQKPMPP-KPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAf 300
Cdd:PRK08974 160 KGTLVnfvvkyikrlvpkyhlpDAISFRSALHKGR-RMQYVKPElVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 301 MKTTEKSFVPSSDDVLISFLPLAHMFERIVECVVLCH-GARIGFFQG--DIRLLMDDLKTLQPTVFPVVPRLLNRMFdki 377
Cdd:PRK08974 238 AKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIElGGQNLLITNprDIPGFVKELKKYPFTAITGVNTLFNALL--- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 378 fgqadsslkrwlldfaskrkeaelrsgivrNNSFWDKVIFrkiqaslgGRVKLMVTGAAPVSASVLTFLRTALGCQFYEG 457
Cdd:PRK08974 315 ------------------------------NNEEFQELDF--------SSLKLSVGGGMAVQQAVAERWVKLTGQYLLEG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 458 YGQTECT---AGCSLSLPGdwTAGHVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDG 534
Cdd:PRK08974 357 YGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDG 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 535 WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVF-------VHGESLQAFLV 598
Cdd:PRK08974 433 WLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
121-608 |
1.16e-37 |
|
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: 145.51 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHvqYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGD--RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DkpdkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpedLAVICFTSGTT 280
Cdd:cd05934 82 D--------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVSNASAFMKttekSFVPSSDDVLISFLPLAHMferivecVVLCHGARIGFFQGdirllmddlktlqp 360
Cdd:cd05934 94 GPPKGVVITHANLTFAGYYSAR----RFGLGEDDVYLTVLPLFHI-------NAQAVSVLAALSVG-------------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 361 TVFPVVPRllnrmfdkifgqadsslkrwlldFASKRkeaelrsgivrnnsFWDKVifRKIQASLGGRVKLM--------- 431
Cdd:cd05934 149 ATLVLLPR-----------------------FSASR--------------FWSDV--RRYGATVTNYLGAMlsyllaqpp 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 432 ----------VTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvqEMNYLA 501
Cdd:cd05934 190 spddrahrlrAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD--DDGQEL 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 502 AKGE-GEVCIKGVN---VFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVY 577
Cdd:cd05934 268 PAGEpGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAI 345
|
490 500 510
....*....|....*....|....*....|....*
gi 2032642720 578 LRCEAVAQVFVHG----ESLQAFLVGVVVPDPDTL 608
Cdd:cd05934 346 LRHPAVREAAVVAvpdeVGEDEVKAVVVLRPGETL 380
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
265-643 |
4.66e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 146.68 E-value: 4.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 265 PKPEDLAVICFTSGTTGNPKGAMITHQNIVSNAS---AFMKTteksfVPSSDDVLISFLPLAHMFErivecVVLChgARI 341
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPG-----LGDGPERVLAALPMFHAYG-----LTLC--LTL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 342 GFFQG---------DIRLLMDDLKTLQPTVFPVVPRLLNRMFDkifgqadsslkrwlldfASKRKEAELRSgiVRNNsfw 412
Cdd:PRK05605 284 AVSIGgelvllpapDIDLILDAMKKHPPTWLPGVPPLYEKIAE-----------------AAEERGVDLSG--VRNA--- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 413 dkvifrkiqaslggrvklmVTGAAPVSASVLTFLRTALGCQFYEGYGQTECT---AGCSLSlpGDWTAGHVGAPMPCNII 489
Cdd:PRK05605 342 -------------------FSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMS--DDRRPGYVGVPFPDTEV 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 490 KLVDVQEMNYLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 568
Cdd:PRK05605 401 RIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNV 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 569 APEKIENVYLRCEAVAQVFVHG-------ESLQAFLV---GVVVpDPDTLHNWAKKKgfegsyqeLCRNKdVKK--YILE 636
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGlpredgsEEVVAAVVlepGAAL-DPEGLRAYCREH--------LTRYK-VPRrfYHVD 548
|
....*....
gi 2032642720 637 DMVR--IGK 643
Cdd:PRK05605 549 ELPRdqLGK 557
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-615 |
8.05e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 142.60 E-value: 8.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 91 TVYDIFQRGLQVSNNGPCLGFRKPNQPYEWISYKEVSDRaecVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAF 170
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDR---LARGLLALGVQPG--DRVGIWAPNCAEWLLTQFATARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 171 SMVVVPLYDTLGAEAITYIVNKADLSLVFC----DKPDKARVL------LASVEKGET-----PILNTIVIMD-----SF 230
Cdd:PRK12583 94 GAILVNINPAYRASELEYALGQSGVRWVICadafKTSDYHAMLqellpgLAEGQPGALacerlPELRGVVSLApapppGF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 231 GV--DLVERGkkcgvEVFSMREIEElgrahRQKPMppKPEDLAVICFTSGTTGNPKGAMITHQNIVSNAsafmKTTEKSF 308
Cdd:PRK12583 174 LAwhELQARG-----ETVSREALAE-----RQASL--DRDDPINIQYTSGTTGFPKGATLSHHNILNNG----YFVAESL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 309 VPSSDDVLISFLPLAHMFErIVECVVLC--HGARIgFFQGDirlLMDDLKTLQP------TVFPVVPRllnrMFdkiFGQ 380
Cdd:PRK12583 238 GLTEHDRLCVPVPLYHCFG-MVLANLGCmtVGACL-VYPNE---AFDPLATLQAveeercTALYGVPT----MF---IAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 381 ADSSlKRWLLDFASkrkeaeLRSGIVrnnsfwdkvifrkiqaslggrvklmvtGAAPVSASVLTFLRTALGC-QFYEGYG 459
Cdd:PRK12583 306 LDHP-QRGNFDLSS------LRTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 460 QTECTAGCSLSLPGD---WTAGHVGAPMPCNIIKLVDVqEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWL 536
Cdd:PRK12583 352 MTETSPVSLQTTAADdleRRVETVGRTQPHLEVKVVDP-DGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWM 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 537 HTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFV-------HGESLQAFLV---GVVVpDPD 606
Cdd:PRK12583 431 HTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVfgvpdekYGEEIVAWVRlhpGHAA-SEE 508
|
....*....
gi 2032642720 607 TLHNWAKKK 615
Cdd:PRK12583 509 ELREFCKAR 517
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-599 |
1.34e-35 |
|
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: 137.25 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 269 DLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEksfVPSSDDVLIsFLPLAHMFERIVECVV-LCHGARI---GFF 344
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCAD---LTEDDRYLI-INPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 qgDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKifgqadsslkrwlldfaSKRKEAELRSgivrnnsfwdkvifrkiqasl 424
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDLSS--------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 ggrVKLMVTGAAPVSASVLTFLRTALGCQ-FYEGYGQTECTAGcSLSLPGD---WTAGHVGAPMPCNIIKLVDvqemnyl 500
Cdd:cd17638 117 ---LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 501 aakgEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRC 580
Cdd:cd17638 186 ----DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEH 260
|
330 340
....*....|....*....|....*.
gi 2032642720 581 EAVAQVFV-------HGESLQAFLVG 599
Cdd:cd17638 261 PGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
267-607 |
2.15e-35 |
|
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: 139.59 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSnasaFMKTTEKSFVPSSDDVLISFLPLAH------MFerivecVVLCHGAR 340
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdvsvweIF------GALLAGAT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 341 I----GFFQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQADSSLKRWLLdfaskrkeaelrsgivrnnsfwdkvi 416
Cdd:cd05930 162 LvvlpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLV-------------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 417 frkiqaslggrvklmvtGAAPVSASVLTFLRTAL-GCQFYEGYGQTECTAGCSL--SLPGDWTAGHV--GAPMPCNIIKL 491
Cdd:cd05930 216 -----------------GGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYyrVPPDDEEDGRVpiGRPIPNTRVYV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 492 VDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqG 565
Cdd:cd05930 279 LD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-G 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2032642720 566 EYIAPEKIENVYLRCEAVAQVFV---HGESLQAFLVGVVVPDPDT 607
Cdd:cd05930 357 YRIELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGG 401
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
247-598 |
2.42e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 141.50 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 247 SMREIEELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSN---ASAFMKTTE---KSFVPSSDDVLISFL 320
Cdd:PRK12492 186 PFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqVRACLSQLGpdgQPLMKEGQEVMIAPL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 321 PLAHMFERIVECVVLchgarigFFQGDIRLLMDDlktlqptvfpvvPRLLNRmFDKifgqadsSLKRWLLdfaskrkeae 400
Cdd:PRK12492 266 PLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPG-FIK-------ELGKWRF---------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 401 lrSGIVRNNSFW----DKVIFRKIQASlggRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWT 476
Cdd:PRK12492 309 --SALLGLNTLFvalmDHPGFKDLDFS---ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 477 A-GHVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PRK12492 384 RlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDR 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2032642720 556 KKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFV-------HGESLQAFLV 598
Cdd:PRK12492 463 KKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
122-598 |
3.29e-35 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 140.72 E-value: 3.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 122 SYKEVSDRAECVGSALLHRGFKP-SHVqyiGIFSQNRPEWVIIEQACYAFSMVVV---PLYDTlgAEaITYIVNKADLSL 197
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKgDRV---GIWAPNVPEWVLTQFATAKIGAILVtinPAYRL--SE-LEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 198 VFC-------DKPDKARVL---LASVEKGET-----PILNTIVIMDSfgvdlverGKKCGVEVFSmrEIEELGR------ 256
Cdd:PRK08315 119 LIAadgfkdsDYVAMLYELapeLATCEPGQLqsarlPELRRVIFLGD--------EKHPGMLNFD--ELLALGRavddae 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 257 -AHRQKPMppKPEDLAVICFTSGTTGNPKGAMITHQNIVSNAS---AFMKTTEKsfvpssDDVLISfLPLAHMFEriveC 332
Cdd:PRK08315 189 lAARQATL--DPDDPINIQYTSGTTGFPKGATLTHRNILNNGYfigEAMKLTEE------DRLCIP-VPLYHCFG----M 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 333 V-----VLCHGARI-----GFfqgdirllmDDLKTLQ-------------PTVFpvVPRLLNRMFDKifgqadsslkrwl 389
Cdd:PRK08315 256 VlgnlaCVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 390 LDFASkrkeaeLRSGI-------VRnnsfwdkvIFRKIQASLGgrvklM--VTGAapvsasvltflrtalgcqfyegYGQ 460
Cdd:PRK08315 312 FDLSS------LRTGImagspcpIE--------VMKRVIDKMH-----MseVTIA----------------------YGM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 461 TECTAGCSLSLPGD------WTaghVGAPMPCNIIKLVDVqEMNYLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALDKD 533
Cdd:PRK08315 351 TETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDP-ETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032642720 534 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAV--AQVF-V----HGESLQAFLV 598
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGEEVCAWII 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
2.30e-34 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 138.23 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVV---PLY----------DTlGAEAIT 187
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKG--ARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYtprelehqlkDS-GAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 188 YIVNkadlslvFcdkpdkARVLLASVEKgeTPILNTIV--IMDSFG-----VDLVERGKKCGVEVFSM------REIEEL 254
Cdd:PRK07059 126 VLEN-------F------ATTVQQVLAK--TAVKHVVVasMGDLLGfkghiVNFVVRRVKKMVPAWSLpghvrfNDALAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 255 GRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSN---ASAFMKTTEKSfvPSSDDVLISF--LPLAHMFERI 329
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANvlqMEAWLQPAFEK--KPRPDQLNFVcaLPLYHIFALT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 330 VECVVlchGARIGffqG---------DIRLLMDDLKTLQPTVFPVVPRLLNRMFdkifgqadsslkrwlldfaskrkeae 400
Cdd:PRK07059 269 VCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL-------------------------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 401 lrsgivrNNSFWDKVIFRKIQASLGGrvklmvtGAApVSASVLTFLRTALGCQFYEGYGQTEcTAGCSLSLPGDWTA--G 478
Cdd:PRK07059 317 -------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSE-TSPVATCNPVDATEfsG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 479 HVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:PRK07059 381 TIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKD 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2032642720 559 IFkLAQGEYIAPEKIENV------YLRCEAVAQVFVH-GESLQAFlvgVVVPDPD 606
Cdd:PRK07059 460 MI-LVSGFNVYPNEIEEVvashpgVLEVAAVGVPDEHsGEAVKLF---VVKKDPA 510
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
262-588 |
6.78e-34 |
|
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: 134.32 E-value: 6.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 262 PMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKttekSFVPSSDDVLISFLPLAhmFERIVE--CVVLCHGA 339
Cdd:TIGR01733 114 DAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR----RYGLDPDDRVLQFASLS--FDASVEeiFGALLAGA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 340 R--------IGFFQGDIRLLMDDLKTlqpTVFPVVPRLLNRMFDkifgQADSSLKRwlldfaskrkeaelrsgivrnnsf 411
Cdd:TIGR01733 188 TlvvppedeERDDAALLAALIAEHPV---TVLNLTPSLLALLAA----ALPPALAS------------------------ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 412 wdkvifrkiqaslggrVKLMVTGAAPVSASVL-TFLRTALGCQFYEGYGQTECTAGCS-LSLPGDWTAGHV----GAPMP 485
Cdd:TIGR01733 237 ----------------LRLVILGGEALTPALVdRWRARGPGARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 486 CNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:TIGR01733 301 NTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRID 379
|
330 340 350
....*....|....*....|....*....|.
gi 2032642720 558 HIFKLaQGEYIAPEKIENVYLRCEAVAQVFV 588
Cdd:TIGR01733 380 DQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-606 |
9.15e-34 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 135.77 E-value: 9.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSH---VQyigifSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSL 197
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDrvaVQ-----VEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 198 VFCDkPDKARVLLASVEKGETPILNTiviMDSFGV-DLVERGKKCGvEVFsmreieelgrahrqKPMPPKPEDLAVICFT 276
Cdd:PRK07514 104 VVCD-PANFAWLSKIAAAAGAPHVET---LDADGTgSLLEAAAAAP-DDF--------------ETVPRGADDLAAILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 277 SGTTGNPKGAMITHQNIVSNAsafmKTTEKSFVPSSDDVLISFLPLAHMFERIVEC-VVLCHGARIGFFQG-DIRLLMDD 354
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNA----LTLVDYWRFTPDDVLIHALPIFHTHGLFVATnVALLAGASMIFLPKfDPDAVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 355 LKtlQPTVFPVVPRLLNRMFdkifgqADSSLKRwlldfaskrkeaelrsgivrnnsfwdkvifrkiqaSLGGRVKLMVTG 434
Cdd:PRK07514 241 MP--RATVMMGVPTFYTRLL------QEPRLTR-----------------------------------EAAAHMRLFISG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 435 AAPVSASvlTFL----RTalGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEMNYLAAKGEGEVCI 510
Cdd:PRK07514 278 SAPLLAE--THRefqeRT--GHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 511 KGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIfkLAQGEY-IAPEKIENVYLRCEAVAQVFV- 588
Cdd:PRK07514 354 KGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEGEIDELPGVVESAVi 431
|
490 500
....*....|....*....|....
gi 2032642720 589 ---H---GESlqafLVGVVVPDPD 606
Cdd:PRK07514 432 gvpHpdfGEG----VTAVVVPKPG 451
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
122-598 |
2.07e-33 |
|
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: 133.66 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 122 SYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKAdlslvfcd 201
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDV--VAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 202 kpdKARVLlasvekgetpilntiVIMDSFgvdlvergkkcgvevfsmreieelgRAHRQKPMPpkpEDLAVICFTSGTTG 281
Cdd:cd05903 73 ---KAKVF---------------VVPERF-------------------------RQFDPAAMP---DAVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 282 NPKGAMITHQNIVSNASAFMkttEKSFVPSSDDVLISfLPLAHMFERIvecvvlcHGARIGFFQGDIRLLMDDLktlQPT 361
Cdd:cd05903 107 EPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAHQTGFV-------YGFTLPLLLGAPVVLQDIW---DPD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 362 VfpvVPRLLNRMFDKIFGQADSslkrwlldFASKRKEAELRSGIVRNnsfwdkvifrkiqaslggRVKLMVTGAAPVSAS 441
Cdd:cd05903 173 K---ALALMREHGVTFMMGATP--------FLTDLLNAVEEAGEPLS------------------RLRTFVCGGATVPRS 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 442 VLTFLRTALGCQFYEGYGQTECTAGCSLSLPGD-WTAGHV-GAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGY 519
Cdd:cd05903 224 LARRAAELLGAKVCSAYGSTECPGAVTSITPAPeDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGY 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 520 LKDPEKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFV-------HGES 592
Cdd:cd05903 303 LDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVvalpderLGER 380
|
....*.
gi 2032642720 593 LQAFLV 598
Cdd:cd05903 381 ACAVVV 386
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-610 |
1.30e-32 |
|
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: 131.90 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 266 KPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpSSDDVL----ISF-LPLAHMFerivecVVLCHGA- 339
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT---SESRVLqfasYTFdVSILEIF------TTLAAGGc 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 340 --------RIGFFQGDIRLLMDDLKTLQPTVFpvvpRLLNRmfdkifgQADSSLKRwlldfaskrkeaelrsgivrnnsf 411
Cdd:cd05918 175 lcipseedRLNDLAGFINRLRVTWAFLTPSVA----RLLDP-------EDVPSLRT------------------------ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 412 wdkvifrkiqaslggrvklMVTGAAPVSASVLTflRTALGCQFYEGYGQTECTAGCSLSLPG-DWTAGHVGAPMPCNIIk 490
Cdd:cd05918 220 -------------------LVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 491 LVDVQEMNYLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRK 556
Cdd:cd05918 278 VVDPDNHDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRK 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 557 KHIFKLaQGEYIAPEKIENVYLRC-----EAVAQVFVH-GESLQAFLVGVVVPDPDTLHN 610
Cdd:cd05918 358 DTQVKI-RGQRVELGEIEHHLRQSlpgakEVVVEVVKPkDGSSSPQLVAFVVLDGSSSGS 416
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-580 |
1.37e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 132.95 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 113 KPNQPYEWiSYKEVSDRAECVGSALLHRGFKPSHVQYIGIfsqnrPEW---VIIEQACYAFSMVVVPLYDTLGAEAITYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPGDRVAFQL-----PGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 190 VNKADLSLVFCDKPDKAR--VLLASVEKGETPILNTIVIMDSFGVDLVErgkkcgvevFSMREIEELGRAhRQKPMPPKP 267
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSS---------LSLSQIIADYEP-LTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 268 EDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpsSDDVLISFLPLAHmferiveCVVLCHGARIGFFQGD 347
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH-------ATGFLHGVTAPFLIGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IRLLMDDLKTLQPTvfpvvpRLLNR------------MFDkifgqadsslkrwLLDfASKRKEAELRSgivrnnsfwdkv 415
Cdd:PRK06087 256 RSVLLDIFTPDACL------ALLEQqrctcmlgatpfIYD-------------LLN-LLEKQPADLSA------------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 416 ifrkiqaslggrVKLMVTGAAPVSASVLtflRTAL--GCQFYEGYGQTECT--AGCSLSLPGDWTAGHVGAPMPCNIIKL 491
Cdd:PRK06087 304 ------------LRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 492 VDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 571
Cdd:PRK06087 369 VD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSR 446
|
....*....
gi 2032642720 572 KIENVYLRC 580
Cdd:PRK06087 447 EVEDILLQH 455
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
121-604 |
2.07e-32 |
|
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: 130.51 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWV-----IIEQ-ACYafsmvvVPLYDTLGAEAITYIVNKAD 194
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPG--DVVPLLSDRSLEMLvailaILKAgAAY------VPLDAKLPSARIQAILRTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 195 LSLVFCdkpdkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmPPKPEDLAVIC 274
Cdd:cd17653 95 ATLLLT---------------------------------------------------------------TDSPDDLAYII 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 275 FTSGTTGNPKGAMITHQNI---VSNASAFMKTTeksfvPSSDDVL---ISFLP-LAHMFerivecVVLCHGARIgFFQGD 347
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRGVlnyVSQPPARLDVG-----PGSRVAQvlsIAFDAcIGEIF------STLCNGGTL-VLADP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IRLLMDDLKTLqpTVFPVVPRLLnrmfdkifgqadsslkrwlldfaskrkeaelrsGIVRNNSFwdkvifrkiqaslgGR 427
Cdd:cd17653 180 SDPFAHVARTV--DALMSTPSIL---------------------------------STLSPQDF--------------PN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 428 VKLMVTGAAPVSASVLTflRTALGCQFYEGYGQTECTAGCSLS--LPGDWTagHVGAPMPCNIIKLVDVQEMNYLAAKgE 505
Cdd:cd17653 211 LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQPVPEGV-V 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 506 GEVCIKGVNVFRGYLKDPEKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYLR 579
Cdd:cd17653 286 GEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQ 364
|
490 500
....*....|....*....|....*...
gi 2032642720 580 -CEAVAQV--FVHGESLQAFlvgvVVPD 604
Cdd:cd17653 365 sQPEVTQAaaIVVNGRLVAF----VTPE 388
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
91-609 |
2.31e-32 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 132.54 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 91 TVYDIFQRGLQVSNNGPCLGFRKPNQPYEWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAF 170
Cdd:COG0365 10 IAYNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDR--VAIYLPNIPEAVIAMLACARI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 171 SMVVVPLYDTLGAEAITYIVNKADLSLVFCD----KPDKARVLLASVEK--GETPILNTIVIMDSFGVDLVERGkkcgvE 244
Cdd:COG0365 88 GAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEG-----D 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 245 VFSMREIEELGRAHRQKPMPPkpEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTeksFVPSSDDVLISFLPLA- 323
Cdd:COG0365 163 LDWDELLAAASAEFEPEPTDA--DDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV---LDLKPGDVFWCTADIGw 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 324 ---HMFeriveCVV--LCHGARIGFFQG-----DIRLLMDDLKTLQPTVFPVVPRLLnRMfdkifgqadssLKRWLLDFA 393
Cdd:COG0365 238 atgHSY-----IVYgpLLNGATVVLYEGrpdfpDPGRLWELIEKYGVTVFFTAPTAI-RA-----------LMKAGDEPL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 394 SKRKEAELRsgivrnnsfwdkvifrkiqaslggrvkLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPG 473
Cdd:COG0365 301 KKYDLSSLR---------------------------LLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 474 DWT-AGHVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKG--VNVFRGYLKDPEKTAEAL--DKDGWLHTGDIGKWLPNG 548
Cdd:COG0365 354 LPVkPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDG 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 549 TLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAVAQVFVhgeslqaflVGvvVPDPDTLH 609
Cdd:COG0365 433 YFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAV---------VG--VPDEIRGQ 481
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
122-605 |
6.05e-32 |
|
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: 130.44 E-value: 6.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 122 SYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWViieQACYAFSM---VVVPLYDTLGAEAITYIVNKADLSLV 198
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPG--DRVATLAWNTHRHL---ELYYAVPGmgaVLHTINPRLFPEQIAYIINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDkpdkaRVLLASVE--KGETPILNTIVIMDSFGVDLVERGKkcGVEVFSmreiEELGRAHRQKPMPPKPE-DLAVICF 275
Cdd:cd12119 102 FVD-----RDFLPLLEaiAPRLPTVEHVVVMTDDAAMPEPAGV--GVLAYE----ELLAAESPEYDWPDFDEnTAAAICY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 276 TSGTTGNPKGAMITHQNIVSNAsafMKTTEKSFVP-SSDDVlisFLPLAHMFerivecvvlcH-------------GARI 341
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSLVLHA---MAALLTDGLGlSESDV---VLPVVPMF----------HvnawglpyaaamvGAKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 342 ----GFFQGDirLLMDDLKTLQPTVFPVVPRLLNRMFDkifgqadsSLKRWLLDFASKRKeaelrsgivrnnsfwdkvif 417
Cdd:cd12119 235 vlpgPYLDPA--SLAELIEREGVTFAAGVPTVWQGLLD--------HLEANGRDLSSLRR-------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 rkiqaslggrvklMVTGAAPVSASVLTFLRtALGCQFYEGYGQTE-CTAGCSLSLPGDWTAGHV----------GAPMPC 486
Cdd:cd12119 285 -------------VVIGGSAVPRSLIEAFE-ERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPVPG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 487 NIIKLVDVqEMNYLAAKGE--GEVCIKGVNVFRGYLKDPEkTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 564
Cdd:cd12119 351 VELRIVDD-DGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG- 427
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2032642720 565 GEYIAPEKIENVYLRCEAVAQVFVhgeslqaflvgVVVPDP 605
Cdd:cd12119 428 GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
119-605 |
3.84e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 127.62 E-value: 3.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWiSYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLV 198
Cdd:PRK09088 22 RW-TYAELDALVGRLAAVLRRRGCVDG--ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDkpdkarvllASVEKGETPILNtiviMDSFgvdlvergkkcgvevfsMREIEELGRAHRqKPMPPkpEDLAVICFTSG 278
Cdd:PRK09088 99 LGD---------DAVAAGRTDVED----LAAF-----------------IASADALEPADT-PSIPP--ERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNIVSNASAFMKTTEKsfvpssdDVLISFLPLAHMFERI--VECV--VLCHGARI----GFFQGDIRL 350
Cdd:PRK09088 146 TSGQPKGVMLSERNLQQTAHNFGVLGRV-------DAHSSFLCDAPMFHIIglITSVrpVLAVGGSIlvsnGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 351 LMDDLkTLQPTVFPVVPRLLnRMFdkifgqadsslkrwlldfaskrkeaelrsgivRNNSFWDKVIFRKIQAslggrvkl 430
Cdd:PRK09088 219 RLGDP-ALGITHYFCVPQMA-QAF--------------------------------RAQPGFDAAALRHLTA-------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 431 MVTGAAP-VSASVLTFLrtALGCQFYEGYGQTEctAGCSLSLPGDWT-----AGHVGAPMPCNIIKLVDVQEmNYLAAKG 504
Cdd:PRK09088 257 LFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQG-NDCPAGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 505 EGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRceava 584
Cdd:PRK09088 332 PGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLAD----- 405
|
490 500
....*....|....*....|.
gi 2032642720 585 qvfvHGESLQAFLVGvvVPDP 605
Cdd:PRK09088 406 ----HPGIRECAVVG--MADA 420
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
95-574 |
1.38e-30 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 126.63 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 95 IFQRGLQVSNNgPCLGFRKPNQPYewiSYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIieqacyAFsmvv 174
Cdd:PLN02246 29 CFERLSEFSDR-PCLIDGATGRVY---TYADVELLSRRVAAGLHKLGIRQGDV--VMLLLPNCPEFVL------AF---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 175 vplydtLGAEAITYIVNKADlslVFCDKPDKARVLLASVEKgetpilntIVIMDSFGVDLVER-GKKCGVEVFSMREIEE 253
Cdd:PLN02246 93 ------LGASRRGAVTTTAN---PFYTPAEIAKQAKASGAK--------LIITQSCYVDKLKGlAEDDGVTVVTIDDPPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 254 lGRAH-------RQKPMPP---KPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPSSDDVLISFLPLA 323
Cdd:PLN02246 156 -GCLHfseltqaDENELPEveiSPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 324 HMFEriVECVVLChGARIG--------FfqgDIRLLMDDLKTLQPTVFPVVPRLL-----NRMFDKifgqadsslkrwlL 390
Cdd:PLN02246 235 HIYS--LNSVLLC-GLRVGaailimpkF---EIGALLELIQRHKVTIAPFVPPIVlaiakSPVVEK-------------Y 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 391 DFASkrkeaelrsgivrnnsfwdkvifrkiqaslggrVKLMVTGAAPVSASVLTFLRTAL-GCQFYEGYGQTEctAGCSL 469
Cdd:PLN02246 296 DLSS---------------------------------IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 470 SL-------PGDWTAGHVGAPMPCNIIKLVDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIG 542
Cdd:PLN02246 341 AMclafakePFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIG 420
|
490 500 510
....*....|....*....|....*....|..
gi 2032642720 543 KWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 574
Cdd:PLN02246 421 YIDDDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
264-604 |
1.56e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 128.89 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 264 PPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTteksFVPSSDDVLISFLPLAHMFERIVE--------CVVL 335
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDV----FNLRNDDVILSSLPFFHSFGLTVTlwlpllegIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 336 CH-----GARIG--FFQGDIRLLmddLKTlqPTVFpvvpRLLNRmfdkifgqadsSLKRWLLDFASKRkeaelrsgivrn 408
Cdd:PRK08633 854 YHpdptdALGIAklVAKHRATIL---LGT--PTFL----RLYLR-----------NKKLHPLMFASLR------------ 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 409 nsfwdkvifrkiqaslggrvkLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLP-----GDWT-----AG 478
Cdd:PRK08633 902 ---------------------LVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEG 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 479 HVGAPMPCNIIKLVDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEAL---DKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PRK08633 961 SVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2032642720 556 KKHIFKLAqGEYIAPEKIEnvylrcEAVAQVFvhGESLQAFLVgVVVPD 604
Cdd:PRK08633 1041 YSRFAKIG-GEMVPLGAVE------EELAKAL--GGEEVVFAV-TAVPD 1079
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-606 |
1.70e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 125.25 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 173 VVVPLYDTLGAEAITYIVNKADLSLVFCDKPDKARVLLASVEkgeTPILNTIVIMDSfgvdlvergkkcgvevfsMREIE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPA---SPDPGTVLDADG------------------IRAAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 253 ELGRAHrqkpmPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASA---FMKTTEksfvpssDDVLISFLPLAHMFERI 329
Cdd:cd05922 107 ASAPAH-----EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITA-------DDRALTVLPLSYDYGLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 330 VECVVLCHGARIgFFQGDIRL---LMDDLKTLQPTVFPVVPRLlnrmfdkiFGQADSslkrwlLDFAsKRKEAELRsgiv 406
Cdd:cd05922 175 VLNTHLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPST--------YAMLTR------LGFD-PAKLPSLR---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 407 rnnsfwdkvifrkIQASLGGRvklmvtgaapVSASVLTFLRTAL-GCQFYEGYGQTECTAGCSLsLPGDWTA---GHVGA 482
Cdd:cd05922 235 -------------YLTQAGGR----------LPQETIARLRELLpGAQVYVMYGQTEATRRMTY-LPPERILekpGSIGL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 483 PMPCNiiKLVDVQEMNYLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 561
Cdd:cd05922 291 AIPGG--EFEILDDDGTPTPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIK 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 562 LAqGEYIAPEKIEN------VYLRCEAVAQVFVHGESLQAFLVGVVVPDPD 606
Cdd:cd05922 369 LF-GNRISPTEIEAaarsigLIIEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
122-605 |
2.42e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 125.82 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 122 SYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFCD 201
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKG--DRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 202 kPDKARVLLASVEKGEtpilntiviMDSFGVDLVERGkkcGVEVFSMREIEELgrAHRQKPMPPKP----EDLAVICFTS 277
Cdd:PRK08316 116 -PALAPTAEAALALLP---------VDTLILSLVLGG---REAPGGWLDFADW--AEAGSVAEPDVeladDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 278 GTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpsSDDVLISFLPLAHMFERIV---ECVVLchGARIGFFQG-DIRLLMD 353
Cdd:PRK08316 181 GTESLPKGAMLTHRALIAEYVSCIVAGDMS----ADDIPLHALPLYHCAQLDVflgPYLYV--GATNVILDApDPELILR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 354 DLKTLQPTVF---PVV-PRLLNRmfdKIFGQAD-SSLkrwlldfaskrkeaelrsgivrnnsfwdkvifRKIQaslggrv 428
Cdd:PRK08316 255 TIEAERITSFfapPTVwISLLRH---PDFDTRDlSSL--------------------------------RKGY------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 429 klmvTGAAPVSASVLTFLRTAL-GCQFYEGYGQTECTAGCSLSLPGDwTAGHVG-APMPC-NI-IKLVDvQEMNYLAAKG 504
Cdd:PRK08316 293 ----YGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAGRPVlNVeTRVVD-DDGNDVAPGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 505 EGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAVA 584
Cdd:PRK08316 367 VGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVA 444
|
490 500
....*....|....*....|.
gi 2032642720 585 QVFVHGeslqaflvgvvVPDP 605
Cdd:PRK08316 445 EVAVIG-----------LPDP 454
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-671 |
3.83e-30 |
|
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: 125.62 E-value: 3.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 107 PCLGFRKPNQPYEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACY---AFSMVVVPLYDTLGA 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAE--RPLLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 184 E--AITYIVNKADLSLVFCDKPDKARVLLASVEKGETPILntIVIMDSFGVDLVERGkkcgvEVFSMREIEELGRAHRQK 261
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLV--VSRNAVAGRGAISFA-----ELAATPPTAAVDAAFAAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 262 pmppKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTteKSFVPSSDDVLISFLPLAHMF-ERIVECVVLCHGAR 340
Cdd:cd05921 163 ----GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT--YPFFGEEPPVLVDWLPWNHTFgGNHNFNLVLYNGGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 341 I---------GFFQGDIRllmdDLKTLQPTVFPVVPrllnrmfdkifgqadsslKRWLLDFASKRKEAELRSgivrnnSF 411
Cdd:cd05921 237 LyiddgkpmpGGFEETLR----NLREISPTVYFNVP------------------AGWEMLVAALEKDEALRR------RF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 412 WDkvifrkiqaslggRVKLMVTGAAPVSASVLTFLrTALGCQ-------FYEGYGQTEcTAGCSLSLPGDWT-AGHVGAP 483
Cdd:cd05921 289 FK-------------RLKLMFYAGAGLSQDVWDRL-QALAVAtvgeripMMAGLGATE-TAPTATFTHWPTErSGLIGLP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 484 MPCNIIKLVdvqemnylAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWL----PNGTLKIIDRKKHI 559
Cdd:cd05921 354 APGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAED 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 560 FKLAQGEYIA--PekienvyLRCEAVAQ-------VFVHGESlQAFLVGVVVPDPDTLHnwAKKKGFEGSYQELCRNKDV 630
Cdd:cd05921 426 FKLASGTWVSvgP-------LRARAVAAcaplvhdAVVAGED-RAEVGALVFPDLLACR--RLVGLQEASDAEVLRHAKV 495
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2032642720 631 KKYILEDMVRIGKESGlKSFEQVKDIVLHTEMFSIENGLLT 671
Cdd:cd05921 496 RAAFRDRLAALNGEAT-GSSSRIARALLLDEPPSIDKGEIT 535
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-696 |
7.62e-30 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 126.89 E-value: 7.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 89 VRTVYDIFQRGLQVSNNGPCLGFRKPNQPYEWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACY 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPGDV--IGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 169 AFSMVVVPLYDTlgAEAITYIVNKADLSLVFCDKPDKARVLLASVEKgetpiLNTIVIMDSFgVDLVER--GKKCGVEVF 246
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILTCRSRK-----LETVVYTHSF-YDEDDHavARDLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 247 SMREIEELGRAhrqKPMPPKPE-------DLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTtekSFVPSS--DDVLI 317
Cdd:PTZ00297 576 PYEFVEQKGRL---CPVPLKEHvttdtvfTYVVDNTTSASGDGLAVVRVTHADVLRDISTLVMT---GVLPSSfkKHLMV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 318 SFLPLAHMFERIVECVVLCHGARIGffQGDIRLLMDDLKTLQPTVFPVVPRLlnrmfdkiFGQADSSLKR---------- 387
Cdd:PTZ00297 650 HFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavys 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 388 WLLDfaskrKEAELRSGIV----RNNSFWDKVIFRKIQASLGGRVKLMVTGAAPVSASvltflrtalgcqfyegYGQTEC 463
Cdd:PTZ00297 720 WLFE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTS----------------FSLLEH 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 464 TAGCSlslpgdwtaghvgapMPCniiklvdVQEMNYLAAkgEGEVCIKG-----VNVFRGYLKDPEKTAE----ALDKDG 534
Cdd:PTZ00297 779 ISVCY---------------VPC-------LREVFFLPS--EGVFCVDGtpapsLQVDLEPFDEPSDGAGigqlVLAKKG 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 535 WL-HTGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENVYLRCEAVAQVFVHGESLQAfLVGVVVPDPDTLH-NW 611
Cdd:PTZ00297 835 EPrRTLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEW 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 612 AKKKGFE--GSYQELCRNKDVKKY----ILEDMVRIGKESGLKSfEQVKDIV-LHTEMFSIENGLLTPTLKAKRPELRKY 684
Cdd:PTZ00297 914 RQSHCMGegGGPARQLGWTELVAYasslLTADFACIAKENGLHP-SNVPEYVhLHPHAFKDHSTFLTPYGKIRRDAVHSY 992
|
650
....*....|..
gi 2032642720 685 FQSQIDELYANA 696
Cdd:PTZ00297 993 FSSVIERFYSDV 1004
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-590 |
1.69e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 123.05 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHR-GFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSL 197
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKG--ERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 198 VFCDKPDKARVLLASvekgetpilntivimdsfgvdlvergKKCGVE-VFSMREIEELGRAHRQKPMPPKPEDLAVICFT 276
Cdd:PRK06839 104 LFVEKTFQNMALSMQ--------------------------KVSYVQrVISITSLKEIEDRKIDNFVEKNESASFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 277 SGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpsSDDVLISFLPLAHMFE-RIVECVVLCHGARI---GFFQGDIRLLM 352
Cdd:PRK06839 158 SGTTGKPKGAVLTQENMFWNALNNTFAIDLT----MHDRSIVLLPLFHIGGiGLFAFPTLFAGGVIivpRKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 353 ddLKTLQPTVFPVVPRLLNRMFDkifgqadsslkrwlldfASKRKEAELRSgivrnnsfwdkvifrkiqaslggrVKLMV 432
Cdd:PRK06839 234 --IEKHKVTVVMGVPTIHQALIN-----------------CSKFETTNLQS------------------------VRWFY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 433 TGAAPVSASVLTFLRTAlGCQFYEGYGQTECTAGCSLSLPGDW--TAGHVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCI 510
Cdd:PRK06839 271 NGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 511 KGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFVHG 590
Cdd:PRK06839 349 RGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-608 |
2.97e-29 |
|
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: 124.97 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVI----IEQA--CYafsmvvVPLYDTLGAEAITYIVNK 192
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGPGDL--VGVCLERSLEMVVallaVLKAgaAY------VPLDPAYPAERLAYMLED 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 193 ADLSLVFCDKpdkarvllasvekgetpilntivimdsfgvDLVERGKKCGVEVFSMREIEELGRAHRQKPMPPKPEDLAV 272
Cdd:COG1020 572 AGARLVLTQS------------------------------ALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 273 ICFTSGTTGNPKGAMITHQNIVSNASAFMKTteksFVPSSDDVLISFLPLAH------MFerivecVVLCHGARIGFFQG 346
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRR----YGLGPGDRVLQFASLSFdasvweIF------GALLSGATLVLAPP 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 347 DIRLLMDDLKTL----QPTVFPVVPRLLnRMFDKIFGQADSSLKRWLLdfaskrkeaelrsgivrnnsfwdkvifrkiqa 422
Cdd:COG1020 692 EARRDPAALAELlarhRVTVLNLTPSLL-RALLDAAPEALPSLRLVLV-------------------------------- 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 423 slGGRvklmvtgAAPVSAsVLTFLRTALGCQFYEGYGQTECTAGCSLSL--PGDWTAGHV--GAPMPCNIIKLVDvQEMN 498
Cdd:COG1020 739 --GGE-------ALPPEL-VRRWRARLPGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD-AHLQ 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 499 yLAAKG-EGEVCIKGVNVFRGYLKDPEKTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 570
Cdd:COG1020 808 -PVPVGvPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIEL 885
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2032642720 571 EKIENVYLRCEAVAQ--VFVHGESLQA-FLVGVVVPDPDTL 608
Cdd:COG1020 886 GEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAA 926
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-607 |
5.43e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 121.63 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYdTLGAEA-ITYIVNKADLS-LV 198
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDA--VALLSLNRPEVLMAIGAAQLAGLRRTALH-PLGSLDdHAYVLEDAGIStLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDKP--DKARVLLASVekgetPILNTIVIMDSF--GVDLvergkkcgvevfsmreieeLGRAHRQKPMPPKPE----DL 270
Cdd:PRK06188 115 VDPAPfvERALALLARV-----PSLKHVLTLGPVpdGVDL-------------------LAAAAKFGPAPLVAAalppDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 271 AVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEksfVPSSddvlISFL---PLAH----MFeriveCVVLCHGARIGF 343
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE---WPAD----PRFLmctPLSHaggaFF-----LPTLLRGGTVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 344 FQG-DIRLLMDDLKTLQPTVFPVVPRLLNRmfdkifgqadsslkrwLLDFASKRKeAELRSgivrnnsfwdkvifrkiqa 422
Cdd:PRK06188 239 LAKfDPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDLSS------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 423 slggrVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHV------GAPMPCNIIKLVDvQE 496
Cdd:PRK06188 283 -----LETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-ED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 497 MNYLAAkGE-GEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK06188 357 GREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVED 433
|
490 500 510
....*....|....*....|....*....|....*....
gi 2032642720 576 VYLRCEAVAQVFV-------HGESLQAflvgVVVPDPDT 607
Cdd:PRK06188 434 VLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGA 468
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-628 |
1.87e-28 |
|
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: 119.71 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 120 WISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVF 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDT--VAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 200 CDKPDKARVLLASVEKGETPIlntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmPPKPE-DLAVICFTSG 278
Cdd:cd12118 107 VDREFEYEDLLAEGDPDFEWI-------------------------------------------PPADEwDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQ----NIVSNASAF-MKTteksfvpssDDVLISFLPLAHmferiveCVVLCHGARIGFFQG------- 346
Cdd:cd12118 144 TTGRPKGVVYHHRgaylNALANILEWeMKQ---------HPVYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrk 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 347 -DIRLLMDDLKTLQPTVFPVVPRLLNRMFDkifgqADSSLKRwlldfaskrkeaelrsgivrnnsfwdkvifrkiqaSLG 425
Cdd:cd12118 208 vDAKAIYDLIEKHKVTHFCGAPTVLNMLAN-----APPSDAR-----------------------------------PLP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 426 GRVKLMVTGAAPvSASVLtFLRTALGCQFYEGYGQTEcTAG----CSL-----SLPGDWTA--------GHVGApmpcNI 488
Cdd:cd12118 248 HRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWkpewdELPTEERArlkarqgvRYVGL----EE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 489 IKLVDVQEMNYLAAKGE--GEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 566
Cdd:cd12118 321 VDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGE 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032642720 567 YIAPEKIENVylrceavaqVFVHGESLQAFLVGvvVPDP---DTLHNWAK-KKGFEGSYQEL---CRNK 628
Cdd:cd12118 399 NISSVEVEGV---------LYKHPAVLEAAVVA--RPDEkwgEVPCAFVElKEGAKVTEEEIiafCREH 456
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
242-557 |
1.91e-28 |
|
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: 120.08 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 242 GVEVFSMREIEELGRAHRQKPMPPK-PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAfmKTTEKSFVPssDDVLISFL 320
Cdd:cd05906 140 GLPGIRVLSIEELLDTAADHDLPQSrPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 321 PLAHmferiVECVVLCHGArigffqgDIRLLMDDLKTLQPTVFPVVPRLLnRMFDKIfgQADSSlkrWLLDFA-SKRKEA 399
Cdd:cd05906 216 PLDH-----VGGLVELHLR-------AVYLGCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPNFAfALLNDL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 400 ELRsgivRNNSFWDKvifrkiqaslgGRVKLMVTGAAPVSASVLTFLRTAL---GCQ---FYEGYGQTECTAGC--SLSL 471
Cdd:cd05906 278 LEE----IEDGTWDL-----------SSLRYLVNAGEAVVAKTIRRLLRLLepyGLPpdaIRPAFGMTETCSGViySRSF 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 472 P-GDWTAGH----VGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGkWLP 546
Cdd:cd05906 343 PtYDHSQALefvsLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLD 420
|
330
....*....|.
gi 2032642720 547 NGTLKIIDRKK 557
Cdd:cd05906 421 NGNLTITGRTK 431
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
265-608 |
2.87e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 118.94 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 265 PKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFmkttEKSFVPSSDDVLISFLPLAHMferivecvvlcHGARIGFF 344
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHV-----------HGLVLGVL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 qGDIRLLMDDLKTLQPTVFPVVPRLLNR--MFdkiFGQAdsslkrwlldfaskrkeaelrsgivrnnSFWDKVIFRKIQA 422
Cdd:PRK07787 190 -GPLRIGNRFVHTGRPTPEAYAQALSEGgtLY---FGVP----------------------------TVWSRIAADPEAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 423 SLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvQEMNYLAA 502
Cdd:PRK07787 238 RALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPH 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 503 KGE--GEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLAQGEyiapekIE 574
Cdd:PRK07787 317 DGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE------IE 390
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2032642720 575 NVYLRCEAVAQVFVHGES-------LQAFLVGVVVPDPDTL 608
Cdd:PRK07787 391 TALLGHPGVREAAVVGVPdddlgqrIVAYVVGADDVAADEL 431
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
263-634 |
4.04e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 119.37 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 263 MPPKPE-DLAVICFTSGTTGNPKGAMITHQNIVSNAsaFMKTTEKSFVPSSDDVLISFLPLAHMFERI-VECVVLCHGAR 340
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNT--LMGVQWLYNCKEGEEVVLGVLPFFHVYGMTaVMNLSIMQGYK 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 341 IGFF-QGDIRLLMDDLKTLQPTVFPVVPRLLNRMfdkifgqadssLKRWLLdfaskrKEAELRSgivrnnsfwdkvifrk 419
Cdd:PRK06710 278 MVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIAL-----------LNSPLL------KEYDISS---------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 420 iqaslggrVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECT-AGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEMN 498
Cdd:PRK06710 325 --------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 499 YLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYL 578
Cdd:PRK06710 397 ALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLY 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032642720 579 RCEAVAQVFV-------HGESLQAFLVgvvvpdpdtlhnwaKKKGFEGSYQELcrNKDVKKYI 634
Cdd:PRK06710 475 EHEKVQEVVTigvpdpyRGETVKAFVV--------------LKEGTECSEEEL--NQFARKYL 521
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-606 |
6.74e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 118.54 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 269 DLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVpsSDDVLISFLPLAHMFERIVECVVLCH--GARIGFFQG 346
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMI--GQVVTLGLIPFFHIYGITGICCATLRnkGKVVVMSRF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 347 DIRLLMDDLKTLQPTVFPVVPRL-LNRMFDKIFGQAD-SSLKrwlldfaskrkeaelrsgivrnnsfwdkvifrkiqasl 424
Cdd:PLN02330 263 ELRTFLNALITQEVSFAPIVPPIiLNLVKNPIVEEFDlSKLK-------------------------------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 ggrVKLMVTGAAPVSASVLT-FLRTALGCQFYEGYGQTECTagCSLSLPGDWTAGH-------VGAPMPCNIIKLVDVQE 496
Cdd:PLN02330 305 ---LQAIMTAAAPLAPELLTaFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 497 MNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENV 576
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330 340 350
....*....|....*....|....*....|
gi 2032642720 577 YLRCEAVAQVfvhgeslqaflvgVVVPDPD 606
Cdd:PLN02330 459 LLTHPSVEDA-------------AVVPLPD 475
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
121-591 |
7.21e-28 |
|
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: 116.68 E-value: 7.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITyivnkadlslvfc 200
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKG--DRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELA------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 dkpdkarvllasvekgetpilntivimdsfgvdlvergkkcgvevFSMREIEelgrahrqkpmpPKPEDLAVICFTSGTT 280
Cdd:cd05912 67 ---------------------------------------------FQLKDSD------------VKLDDIATIMYTSGTT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVSNASAFMKT---TEksfvpssDDVLISFLPLAH------MFERIVE-CVVLCHGArigfFqgDIRL 350
Cdd:cd05912 90 GKPKGVQQTFGNHWWSAIGSALNlglTE-------DDNWLCALPLFHisglsiLMRSVIYgMTVYLVDK----F--DAEQ 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 351 LMDDLKTLQPTVFPVVPRLLNRMFDKIFGQADSSLKRWLLdfaskrkeaelrsgivrnnsfwdkvifrkiqaslggrvkl 430
Cdd:cd05912 157 VLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL---------------------------------------- 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 431 mvtGAAPVSASVLTFLRTaLGCQFYEGYGQTEcTAGCSLSLPGDWTA---GHVGAPMPCNIIKLVDvqemNYLAAKGEGE 507
Cdd:cd05912 197 ---GGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIED----DGQPPYEVGE 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 508 VCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVF 587
Cdd:cd05912 268 ILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAG 345
|
....
gi 2032642720 588 VHGE 591
Cdd:cd05912 346 VVGI 349
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
262-576 |
1.13e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 118.02 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 262 PMPP-KPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSF-VPSSDDVLISFLPLAHMFERIVECV-VLCHG 338
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYeYPGSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 339 ARI----GFFQGDIRLLMDDLKTlqpTVFPVVPRLLNRMFDKIFGQADSSLKrwlldfaskrkeaelrsgivrnnsfwdk 414
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 415 vifrkiqaSLggrvKLMVTGAAPVSA-SVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGH--VGAPMPCNIIKL 491
Cdd:PLN02574 320 --------SL----KQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNMQAKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 492 VDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 571
Cdd:PLN02574 388 VDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPA 466
|
....*
gi 2032642720 572 KIENV 576
Cdd:PLN02574 467 DLEAV 471
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-604 |
1.21e-27 |
|
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: 117.01 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLV 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDR--VAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDKPDKARVLLasvekgetpilntivimdsfGVDLVERGkkcgvevfsmreIEELGRAHRQKPMPPKPEDLAVICFTSG 278
Cdd:cd12116 89 LTDDALPDRLPA--------------------GLPVLLLA------------LAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNIVSNASAFMKTteksFVPSSDDVL---------IS----FLPLahmferivecvvlCHGARIGFFQ 345
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSMRER----LGLGPGDRLlavttyafdISllelLLPL-------------LAGARVVIAP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 346 GDI----RLLMDDLKTLQPTVFpvvprllnrmfdkifgQADSSLKRWLLDfASKRKEAELRsgivrnnsfwdkvifrkiq 421
Cdd:cd12116 200 RETqrdpEALARLIEAHSITVM----------------QATPATWRMLLD-AGWQGRAGLT------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 422 aslggrvklMVTGAAPVSASVLTFLrTALGCQFYEGYGQTECT--AGCSLSLPGDwTAGHVGAPMPCNIIKLVDVQeMNY 499
Cdd:cd12116 244 ---------ALCGGEALPPDLAARL-LSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDAA-LRP 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 500 LAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:cd12116 312 VPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGE 390
|
490 500 510
....*....|....*....|....*....|....
gi 2032642720 573 IENVYLRCEAVAQ--VFVHGESLQAFLVGVVVPD 604
Cdd:cd12116 391 IEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
173-584 |
1.49e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 173 VVVPLYDTLGAEAITYIVNKADLSLVFCDKP-------DKARVLLASVekgetPILNTIVIMD---------SFGVDLVE 236
Cdd:PRK07529 108 IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEVDlarylpgpkRLAVPLIR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 237 RGKKCGVEVFSmREIEELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNA---SAFMKTTEksfvpssD 313
Cdd:PRK07529 183 RKAHARILDFD-AELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLGP-------G 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 314 DVLISFLPLAHMFERIVEC---------VVLC--HGAR-IGFFQGDIRLLmddlKTLQPTVFPVVPRLLNRMFDKIFGQA 381
Cdd:PRK07529 255 DTVFCGLPLFHVNALLVTGlaplargahVVLAtpQGYRgPGVIANFWKIV----ERYRINFLSGVPTVYAALLQVPVDGH 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 382 D-SSLKrwlldFASkrkeaelrsgivrnnsfwdkvifrkiqaslggrvklmvTGAAPVSASVLTFLRTALGCQFYEGYGQ 460
Cdd:PRK07529 331 DiSSLR-----YAL--------------------------------------CGAAPLPVEVFRRFEAATGVRIVEGYGL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 461 TECTAGCSLSLP-GDWTAGHVGAPMPCNIIKLVDVQEM-NYL--AAKGE-GEVCIKGVNVFRGYLkDPEKTAEALDKDGW 535
Cdd:PRK07529 368 TEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGW 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2032642720 536 LHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVA 584
Cdd:PRK07529 447 LNTGDLGRIDADGYFWLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-613 |
3.75e-27 |
|
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: 114.88 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNkadlslvfc 200
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILN--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDKARVLLASVEkgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpeDLAVICFTSGTT 280
Cdd:cd05935 71 DSGAKVAVVGSELD------------------------------------------------------DLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVSNASAfmktTEKSFVPSSDDVLISFLPLAHM--FERIVECVVLCHGARIGFFQGDIRLLMDDLKTL 358
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ----SAVWTGLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 359 QPTVFPVVPRLLNRMFdkifgqadSSLKRWLLDFASkrkeaelrsgivrnnsfwdkvifrkiqaslggrVKLMVTGAAPV 438
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--------ATPEFKTRDLSS---------------------------------LKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 439 SASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEMNYLAAKGEGEVCIKGVNVFRG 518
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 519 YLKDPEKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAVAQVFV------- 588
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490 500 510
....*....|....*....|....*....|.
gi 2032642720 589 HGESLQAFLV------GVVvpDPDTLHNWAK 613
Cdd:cd05935 371 VGEEVKAFIVlrpeyrGKV--TEEDIIEWAR 399
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
122-605 |
3.78e-27 |
|
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: 114.74 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 122 SYKEVSDRAECVGSALLHRGFKPSHVQYIgiFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFCD 201
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAV--LLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 202 KpdkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpEDLAVICFTSGTTG 281
Cdd:cd05972 80 A-----------------------------------------------------------------EDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 282 NPKGAMITHqnivSNASAFMKTTEKSFVPSSDDV-------------LISFL-PLAHMFeriveCVVLCHGARIgffqgD 347
Cdd:cd05972 95 LPKGVLHTH----SYPLGHIPTAAYWLGLRPDDIhwniadpgwakgaWSSFFgPWLLGA-----TVFVYEGPRF-----D 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IRLLMDDLKTLQPTVFPVVPRLLNRMFdkifgQADSSlKRWLldfaskrkeaelrsgivrnnsfwdkvifrkiqaslgGR 427
Cdd:cd05972 161 AERILELLERYGVTSFCGPPTAYRMLI-----KQDLS-SYKF------------------------------------SH 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 428 VKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvQEMNYLAAKGEGE 507
Cdd:cd05972 199 LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGD 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 508 VCIK--GVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYLRCEAVAQ 585
Cdd:cd05972 278 IAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAE 355
|
490 500
....*....|....*....|
gi 2032642720 586 VFVhgeslqaflvgVVVPDP 605
Cdd:cd05972 356 AAV-----------VGSPDP 364
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-606 |
5.49e-27 |
|
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: 115.12 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 111 FRKPNQPY-----EWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVI----IEQACYAFsmvvVPLYDTL 181
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGPD--TIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 182 GAEAITYIVNKADLSLVFCDKPDKARVLLASvekgetpilnTIVIMDSfgvdlvergkkcgvEVFSMREIEELgrahrqk 261
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENL------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 262 PMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFmkttEKSFVPSSDDVLISFLPLAhmFERIVECV--VLCHGA 339
Cdd:cd17655 131 EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA----NKVIYQGEHLRVALFASIS--FDASVTEIfaSLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 340 RIGFFQ----GDIRLLMDDLKTLQPTVFPVVPRLLNrmfdkifgqadsslkrwLLDfaskrkeaelrsgivrnnsfwdkv 415
Cdd:cd17655 205 TLYIVRketvLDGQALTQYIRQNRITIIDLTPAHLK-----------------LLD------------------------ 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 416 ifrKIQASLGGRVKLMVTGAAPVSASVLTFL--RTALGCQFYEGYGQTECTAGCSLSL--PGDWTAGHV--GAPMPCNII 489
Cdd:cd17655 244 ---AADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIYQyePETDQQVSVpiGKPLGNTRI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 490 KLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLa 563
Cdd:cd17655 321 YILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI- 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2032642720 564 QGEYIAPEKIENVYLRCEAVAQ--VFVH-GESLQAFLVGVVVPDPD 606
Cdd:cd17655 399 RGYRIELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSEKE 444
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
121-605 |
1.18e-26 |
|
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: 113.50 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGfkPSHVQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd05945 17 LTYRELKERADALAAALASLG--LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DkpdkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkPEDLAVICFTSGTT 280
Cdd:cd05945 95 D-----------------------------------------------------------------GDDNAYIIFTSGST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVS----NASAFMKTTEKSFVPSSDdvlISF-LPLAHMFerivecVVLCHGArigffqgdirllmddl 355
Cdd:cd05945 110 GRPKGVQISHDNLVSftnwMLSDFPLGPGDVFLNQAP---FSFdLSVMDLY------PALASGA---------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 356 ktlqpTVFPVvPRLLNRMFDKIF-GQADSSLKRWlldfaskrkeaelrsgiVRNNSFWDKVIFRK-IQASLGGRVKLMVT 433
Cdd:cd05945 165 -----TLVPV-PRDATADPKQLFrFLAEHGITVW-----------------VSTPSFAAMCLLSPtFTPESLPSLRHFLF 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 434 GAAPVSASVLTFLRTAL-GCQFYEGYGQTECTAGCSL------------SLPgdwtaghVGAPMPCNIIKLVDvQEMNYL 500
Cdd:cd05945 222 CGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYievtpevldgydRLP-------IGYAKPGAKLVILD-EDGRPV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 501 AAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVY 577
Cdd:cd05945 294 PPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAAL 372
|
490 500 510
....*....|....*....|....*....|..
gi 2032642720 578 LRCEAVAQVFV----HGESLQAfLVGVVVPDP 605
Cdd:cd05945 373 RQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKP 403
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-544 |
3.10e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 114.21 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 112 RKPNQPY--------EW--ISYKEVSDRAECVGSALLHRGFkpshvqyigifSQNRPeWVI-----IEQACYAF-SM--- 172
Cdd:PRK08180 51 EAPDRVFlaergadgGWrrLTYAEALERVRAIAQALLDRGL-----------SAERP-LMIlsgnsIEHALLALaAMyag 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 173 ----VVVPLYDTLGA--EAITYIVNKADLSLVFCDKPDKARVLLASVEKGETPILntivimdsfgvdlVERGKKCGVEVF 246
Cdd:PRK08180 119 vpyaPVSPAYSLVSQdfGKLRHVLELLTPGLVFADDGAAFARALAAVVPADVEVV-------------AVRGAVPGRAAT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 247 SMREIEELGR------AHRQKpmppKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTekSFVPSSDDVLISFL 320
Cdd:PRK08180 186 PFAALLATPPtaavdaAHAAV----GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF--PFLAEEPPVLVDWL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 321 PLAHMF--ERIVEcVVLCHGARI---------GFFQGDIRllmdDLKTLQPTVFPVVPR----LLNRMfdkifgqadssl 385
Cdd:PRK08180 260 PWNHTFggNHNLG-IVLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemLVPAL------------ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 386 krwlldfaskRKEAELRsgivrnnsfwdkvifrkiqASLGGRVKLMVTGAAPVSASVLTFL----RTALGCQ--FYEGYG 459
Cdd:PRK08180 323 ----------ERDAALR-------------------RRFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERirMMTGLG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 460 QTEcTAGCSLSL--PGDwTAGHVGAPMPCNIIKLVDVQemnylaakGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLH 537
Cdd:PRK08180 374 MTE-TAPSATFTtgPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYR 443
|
....*..
gi 2032642720 538 TGDIGKW 544
Cdd:PRK08180 444 SGDAVRF 450
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
121-607 |
7.31e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 112.18 E-value: 7.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGfkpshVQY---IGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSL 197
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRG-----VGFgdrVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 198 VFCDKpdkARVLLASVEKGETPILNTIVIMDSFGVDLVergkkCGVEvfsmREIEELGRAHrqkPMPPKPEDL-AVICFT 276
Cdd:PRK07786 118 VVTEA---ALAPVATAVRDIVPLLSTVVVAGGSSDDSV-----LGYE----DLLAEAGPAH---APVDIPNDSpALIMYT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 277 SGTTGNPKGAMITHQNIVSNASAFMKTTEksfVPSSDDVLISFLPLAHmferivecvVLCHGARIGFFQGDIRLLMDDLK 356
Cdd:PRK07786 183 SGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFH---------IAGIGSMLPGLLLGAPTVIYPLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 357 TLQPTVfpvvprllnrmfdkifgqadsslkrwLLDFAskrkEAELRSGIVRNNSFWDKVIfrKIQASLGGRVKLMVT--G 434
Cdd:PRK07786 251 AFDPGQ--------------------------LLDVL----EAEKVTGIFLVPAQWQAVC--AEQQARPRDLALRVLswG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 435 AAPVSASVLTFLRTAL-GCQFYEGYGQTECTAGCSLSLPGDWTA--GHVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIK 511
Cdd:PRK07786 299 AAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 512 GVNVFRGYLKDPEKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFVHGE 591
Cdd:PRK07786 378 APTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGR 455
|
490
....*....|....*....
gi 2032642720 592 SLQAF---LVGVVVPDPDT 607
Cdd:PRK07786 456 ADEKWgevPVAVAAVRNDD 474
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-615 |
3.22e-25 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 107.03 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 269 DLAVICFTSGTTGNPKGAMITHQNIVSNASAFmktteKSFVP--SSDDVLISfLPLAHM--FERIVECVVLchGARIGFF 344
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGL-----HSRLGfgGGDSWLLS-LPLYHVggLAILVRSLLA--GAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 QGDiRLLMDDLKTLQPTVFPVVPRLLNRMFDKifGQADSSLKRwlldfaskrkeaelrsgivrnnsfwdkviFRKIqaSL 424
Cdd:cd17630 73 ERN-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS-----------------------------LRAV--LL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 GGrvklmvtgaAPVSAsVLTFLRTALGCQFYEGYGQTE---CTAGCSLSLPGDwtaGHVGAPMPCNIIKLVDvqemnyla 501
Cdd:cd17630 119 GG---------APIPP-ELLERAADRGIPLYTTYGMTEtasQVATKRPDGFGR---GGVGVLLPGRELRIVE-------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 502 akgEGEVCIKGVNVFRGYLKDPEKtaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCE 581
Cdd:cd17630 178 ---DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHP 251
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2032642720 582 AVAQVFV-------HGESLQAFLVGVVVPDPDTLHNWAKKK 615
Cdd:cd17630 252 AVRDAFVvgvpdeeLGQRPVAVIVGRGPADPAELRAWLKDK 292
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-606 |
4.16e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 110.05 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 112 RKPNQPYEW-----ISYKEVSDRAECVgSALLHR--GFKPShvQYIGIFSQNRPEWVIieqACYAFSM---VVVPLYDTL 181
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQecGVRKG--DRVLLYMQNSPQFVI---AYYAILRanaVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 182 GAEAITYIVNKADLSLVFCdkpdkARVLLASVEK--GETPILNTIVIM--DSFGVD---------LVERGKKCGVEVFSM 248
Cdd:PRK08314 96 REEELAHYVTDSGARVAIV-----GSELAPKVAPavGNLRLRHVIVAQysDYLPAEpeiavpawlRAEPPLQALAPGGVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 249 REIEELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNA--SAFMKTTeksfvpSSDDVLISFLPLAHmf 326
Cdd:PRK08314 171 AWKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAvgSVLWSNS------TPESVVLAVLPLFH-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 327 eriVECVVLCHGARIgfFQGDIRLLM---------DDLKTLQPTVFPVVPRLLnrmfdkifgqadsslkrwlLDF-ASKR 396
Cdd:PRK08314 243 ---VTGMVHSMNAPI--YAGATVVLMprwdreaaaRLIERYRVTHWTNIPTMV-------------------VDFlASPG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 397 -KEAELRSgivrnnsfwdkvifrkiQASLGGrvklmvtGAAPVSASVLTFLRTALGCQFYEGYGQTEcTAGCSLSLPGDW 475
Cdd:PRK08314 299 lAERDLSS-----------------LRYIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 476 TA-GHVGAPMPCNIIKLVDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEA---LDKDGWLHTGDIGKWLPNGTLK 551
Cdd:PRK08314 354 PKlQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFF 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032642720 552 IIDRKKHIFKlAQGEYIAPEKIENVYLRCEAVAQVFV-------HGESLQAflvgVVVPDPD 606
Cdd:PRK08314 434 ITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKA----VVVLRPE 490
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-608 |
6.06e-25 |
|
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: 109.14 E-value: 6.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFc 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPG--QRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAV- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 dkpdkarvllASVEKGETPilntiVIMDSFGVDLVErgkkcGVEVfSMREIEELGRAhrQKPMPPKPEDLAVICFTSGTT 280
Cdd:cd05923 106 ----------IAVDAQVMD-----AIFQSGVRVLAL-----SDLV-GLGEPESAGPL--IEDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVSNAsAFMkTTEKSFVPSSDDVLISFLPLAHMferivecvvlchgarIGFFQgdirLLMDDLkTLQP 360
Cdd:cd05923 163 GLPKGAVIPQRAAESRV-LFM-STQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-ALDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 361 TVFPVvprllnRMFDKIfgqadsslkrwlldFASKRKEAELRSGIVRNNSFWDKVIFRKIQAS--LGGRVKLMVTGAApV 438
Cdd:cd05923 221 TYVVV------EEFDPA--------------DALKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTFAGAT-M 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 439 SASVLTFLRTALGCQFYEGYGQTEctAGCSLSLPgDWTAGHVGAPMPCNIIKLVDVQE--MNYLAAKGEGEVCIK--GVN 514
Cdd:cd05923 280 PDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIGGspDEALANGEEGELIVAaaADA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 515 VFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFVHG---E 591
Cdd:cd05923 357 AFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvadE 434
|
490
....*....|....*..
gi 2032642720 592 SLQAFLVGVVVPDPDTL 608
Cdd:cd05923 435 RWGQSVTACVVPREGTL 451
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
121-598 |
1.51e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 107.74 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKG--DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPdkarvlLASVEKGETPILntivimdsfgvdlvergkkcgvevfsmreIEELGRAHRQKPMPPKPEDL---AVICFTS 277
Cdd:PRK03640 106 DDD------FEAKLIPGISVK-----------------------------FAELMNGPKEEAEIQEEFDLdevATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 278 GTTGNPKGAMITHQNIVSNA--SAF-MKTTEKsfvpssDDVLISfLPLAH------MFERIVecvvlcHGARIGFFQG-D 347
Cdd:PRK03640 151 GTTGKPKGVIQTYGNHWWSAvgSALnLGLTED------DCWLAA-VPIFHisglsiLMRSVI------YGMRVVLVEKfD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IRLLMDDLKTLQPTVFPVVPRLLNRMFDKIfgqadsslkrwlldfaskrKEAELrsgivrNNSFwdkvifrkiqaslggr 427
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQRLLERL-------------------GEGTY------PSSF---------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 428 vKLMVTGAAPVSASVLTflrtalGCQ-----FYEGYGQTEcTAGCSLSLPGDWTA---GHVGAPM-PCNIiKLVDvqEMN 498
Cdd:PRK03640 257 -RCMLLGGGPAPKPLLE------QCKekgipVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCEL-KIEK--DGV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 499 YLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYL 578
Cdd:PRK03640 326 VVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 403
|
490 500
....*....|....*....|....*..
gi 2032642720 579 RCEAVAQVFVHGESLQ-------AFLV 598
Cdd:PRK03640 404 SHPGVAEAGVVGVPDDkwgqvpvAFVV 430
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
90-605 |
3.78e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.06 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 90 RTVYDIFQRGLQVSNNGPCL-GFRKPNQPYEWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACY 168
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVtAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDV--VSCQLPNWWEFTVLYLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 169 AFSMVVVPLYDTLGAEAITYIVNKADlSLVFC--------DKPDKARVLlasveKGETPILNTIVIMDSFGVDLVERgkk 240
Cdd:PRK13295 102 RIGAVLNPLMPIFRERELSFMLKHAE-SKVLVvpktfrgfDHAAMARRL-----RPELPALRHVVVVGGDGADSFEA--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 241 cgveVFSMREIEELGRA------HRqkpmpPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpsSDD 314
Cdd:PRK13295 173 ----LLITPAWEQEPDApailarLR-----PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLG----ADD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 315 VLISFLPLAHMferivecvvlchgarIGFFQGDIRLLMDDLKT-LQPTVFPVvprllnRMFDKI------FGQADSSlkr 387
Cdd:PRK13295 240 VILMASPMAHQ---------------TGFMYGLMMPVMLGATAvLQDIWDPA------RAAELIrtegvtFTMASTP--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 388 WLLDFASKRKEAelrsgivrnnsfwdkvifRKIQASLggrvKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAgC 467
Cdd:PRK13295 296 FLTDLTRAVKES------------------GRPVSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-V 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 468 SLSLPGD---WTAGHVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEalDKDGWLHTGDIGKW 544
Cdd:PRK13295 353 TLTKLDDpdeRASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARI 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032642720 545 LPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFVHG---ESLQAFLVGVVVPDP 605
Cdd:PRK13295 430 DADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAypdERLGERACAFVVPRP 492
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-615 |
6.64e-24 |
|
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: 105.75 E-value: 6.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVI----IEQA--CYafsmvvVPLYDTLGAEAITYIVNKAD 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGPGDV--VGVLAERSPELVVallaVLKAgaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 195 LSLVFCDKPDKARVllasvekGETPILNTIVIMDSFGVDLVERGkkcgvevfsmreieelgrahrqkpmPPKPEDLAVIC 274
Cdd:cd12117 95 AKVLLTDRSLAGRA-------GGLEVAVVIDEALDAGPAGNPAV-------------------------PVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 275 FTSGTTGNPKGAMITHQNIVSNAsafmktTEKSFVP-SSDDVLISFLPL---AHMFErIVecVVLCHGARIgffqgdirL 350
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVRLV------KNTNYVTlGPDDRVLQTSPLafdASTFE-IW--GALLNGARL--------V 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 351 LMDDLKTLQPTVFPvvpRLLNR-----MFdkifgqADSSLKRWLLDFASkrkeaelrsgivrnnsfwdkvifrkiqASLG 425
Cdd:cd12117 206 LAPKGTLLDPDALG---ALIAEegvtvLW------LTAALFNQLADEDP---------------------------ECFA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 426 GRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECT--AGCSLSLPGDWTAGHV--GAPMPCNIIKLVDVQEMnyLA 501
Cdd:cd12117 250 GLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLDEDGR--PV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 502 AKGE-GEVCIKGVNVFRGYLKDPEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 574
Cdd:cd12117 328 PPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2032642720 575 NVYLRCEAVAQVFV------HGE-SLQAFLVGVVVPDPDTLHNWAKKK 615
Cdd:cd12117 407 AALRAHPGVREAVVvvredaGGDkRLVAYVVAEGALDAAELRAFLRER 454
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-607 |
1.15e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 105.60 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLV-- 198
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRG--DRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLvv 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 ---FcDKPDKARVLlASVEKGETPILNTIVIMDSFGVDLVERGKKCGVEVFSMreieELGRAHRQKPMPPKPEDLAVICF 275
Cdd:PRK06164 114 wpgF-KGIDFAAIL-AAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFAL----PDPAPPAAAGERAADPDAGALLF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 276 T-SGTTGNPK------GAMITHQNIVSNASAFmktteksfvpSSDDVLISFLPLahmferiveCVVLCHGARIGFFQGDI 348
Cdd:PRK06164 188 TtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF---------CGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 349 RLLMDDLKTLQPTVfpvvpRLL-----------NRMFDKIFGQADSSLkrwllDFASKRkeaelRSGIVrnnSFwdkvif 417
Cdd:PRK06164 249 PLVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGFA---SF------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 rkiqaslggrvklmvtgaAPVSASVLTFLRTAlGCQFYEGYGQTECTAGCSL-SLPGDWTAGHV--GAPM-PCNIIKLVD 493
Cdd:PRK06164 305 ------------------APALGELAALARAR-GVPLTGLYGSSEVQALVALqPATDPVSVRIEggGRPAsPEARVRARD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 494 VQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 573
Cdd:PRK06164 366 PQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEI 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 2032642720 574 ENVYLRCEAVAQVFVHGESLQAFLVGV--VVPDPDT 607
Cdd:PRK06164 445 EHALEALPGVAAAQVVGATRDGKTVPVafVIPTDGA 480
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-609 |
3.16e-23 |
|
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: 103.89 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGPEDR--VAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKpdkarvllasvekgetpilntivimdsfgvDLVERGKKCGVEVFSMREIEELGRAHRQKPmPPKPEDLAVICFTSGTT 280
Cdd:cd17646 102 TA------------------------------DLAARLPAGGDVALLGDEALAAPPATPPLV-PPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVsNASAFMKTtEKSFVPSsDDVL--------IS----FLPLAHMferivECVVLC-HGARigffqGD 347
Cdd:cd17646 151 GRPKGVMVTHAGIV-NRLLWMQD-EYPLGPG-DRVLqktplsfdVSvwelFWPLVAG-----ARLVVArPGGH-----RD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IRLLMDDLKTLQPTVFPVVPRLLnrmfdkifgqadsslkRWLLDFASKRKEAELRsgivrnnsfwdkvifrkiqaslggR 427
Cdd:cd17646 218 PAYLAALIREHGVTTCHFVPSML----------------RVFLAEPAAGSCASLR------------------------R 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 428 VklmVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSL-SLPGDWTAGHV--GAPMPCNIIKLVDvQEMNYLAAKG 504
Cdd:cd17646 258 V---FCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 505 EGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYL 578
Cdd:cd17646 334 PGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALA 412
|
490 500 510
....*....|....*....|....*....|....
gi 2032642720 579 RCEAVAQVFV---HGESLQAFLVGVVVPDPDTLH 609
Cdd:cd17646 413 AHPAVTHAVVvarAAPAGAARLVGYVVPAAGAAG 446
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-605 |
3.52e-23 |
|
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: 101.19 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 269 DLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpsSDDVLISFLPLAHMFERIVECVVLCHGARigffqgdi 348
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLT----EADVYLNMLPLFHIAGLNLALATFHAGGA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 349 RLLMDD------LKTLQP---TVFPVVPRLLNRMFDKIfgqadsslkrwlldfasKRKEAELRSgiVRNnsfwdkvifrk 419
Cdd:cd17637 69 NVVMEKfdpaeaLELIEEekvTLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH----------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 420 iqaslggrvklmVTGA-APvsASVLTFLRTAlGCQFYEGYGQTEcTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvQEMN 498
Cdd:cd17637 119 ------------VLGLdAP--ETIQRFEETT-GATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 499 YLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENV 576
Cdd:cd17637 182 PVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV 259
|
330 340
....*....|....*....|....*....
gi 2032642720 577 YLRCEAVAQVFVHGeslqaflvgvvVPDP 605
Cdd:cd17637 260 ILEHPAIAEVCVIG-----------VPDP 277
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
121-605 |
4.70e-23 |
|
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: 103.73 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHvqYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd05970 48 FTFAELADYSDKTANFFKAMGIGKGD--TVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDkarVLLASVEKG--ETPILNTIVimdSFGVDLVErgkkcGVEVFSmREIEELGR--AHRQKPMPPKPEDLAVICFT 276
Cdd:cd05970 126 IAED---NIPEEIEKAapECPSKPKLV---WVGDPVPE-----GWIDFR-KLIKNASPdfERPTANSYPCGEDILLVYFS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 277 SGTTGNPKgaMITHQNIvsnasafmktteksfvpssddvlisfLPLAHMFerivecvvlchgarIGFFQGDIRllMDDLK 356
Cdd:cd05970 194 SGTTGMPK--MVEHDFT--------------------------YPLGHIV--------------TAKYWQNVR--EGGLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 357 -TLQPTVFPvvprllNRMFDKIFGQADSSLKRWLLDFASKRKEAEL-RSGIVRNNSFW-DKVIFR-KIQASLG----GRV 428
Cdd:cd05970 230 lTVADTGWG------KAVWGKIYGQWIAGAAVFVYDYDKFDPKALLeKLSKYGVTTFCaPPTIYRfLIREDLSrydlSSL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 429 KLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAgCSLSLPG-DWTAGHVGAPMPCNIIKLVDvQEMNYLAAKGEGE 507
Cdd:cd05970 304 RYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 508 VCI-----KGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYLRCEA 582
Cdd:cd05970 382 IVIrtskgKPVGLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPA 459
|
490 500
....*....|....*....|...
gi 2032642720 583 VAQVFVHGeslqaflvgvvVPDP 605
Cdd:cd05970 460 VLECAVTG-----------VPDP 471
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
173-632 |
8.63e-23 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 102.45 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 173 VVVPLYDTLGAEAITYIVNKADLSLVFCDK---PDKARVLlasvEKGETPiLNTIVIMDsfgvdlVERGKKCGVEVFSMR 249
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTSAqfyPMYRQIQ----QEDATP-LRHICLTR------VALPADDGVSSFTQL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 250 EIEELGRAHRQKPMppKPEDLAVICFTSGTTGNPKGAMITHQNIVsnASAFMKTTEKSFvpSSDDVLISFLPLAHmferi 329
Cdd:PRK08008 157 KAQQPATLCYAPPL--STDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL--RDDDVYLTVMPAFH----- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 330 VECvvLCHGArigffqgdirllMddlktlqpTVFPVVPRLLnrmfdkifgqadsslkrwLLDFASKRKeaelrsgivrnn 409
Cdd:PRK08008 226 IDC--QCTAA------------M--------AAFSAGATFV------------------LLEKYSARA------------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 410 sFWDKVifRKIQASLGGRVKLMVTG--AAPVSA--------SVLTFLR----------TALGCQFYEGYGQTECTAGCSL 469
Cdd:PRK08008 254 -FWGQV--CKYRATITECIPMMIRTlmVQPPSAndrqhclrEVMFYLNlsdqekdafeERFGVRLLTSYGMTETIVGIIG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 470 SLPGD---WTAghVGAPMPCNIIKLVDVQEmNYLAAKGEGEVCIKGV---NVFRGYLKDPEKTAEALDKDGWLHTGDIGK 543
Cdd:PRK08008 331 DRPGDkrrWPS--IGRPGFCYEAEIRDDHN-RPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 544 WLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAVAQVFVHG-------ESLQAFLV---GVVVPDPDTL----H 609
Cdd:PRK08008 408 VDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGikdsirdEAIKAFVVlneGETLSEEEFFafceQ 486
|
490 500
....*....|....*....|....*...
gi 2032642720 610 NWAKKK-----GFEGSYQELCRNKDVKK 632
Cdd:PRK08008 487 NMAKFKvpsylEIRKDLPRNCSGKIIKK 514
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-612 |
1.80e-22 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 101.00 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTE-KSFVPSSDDVL-ISFLPLAHMFERivecvVLCHGARIGFF 344
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYElDSFPVRLLQMAsFSFDVFAGDFAR-----SLLNGGTLVIC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 QGDIRL----LMDDLKTLQPTVFPVVPRLLNRMFDKIF--GQADSSLKrwLLDFASKRKEAElrsgivrnnsfWDKVIFR 418
Cdd:cd17650 167 PDEVKLdpaaLYDLILKSRITLMESTPALIRPVMAYVYrnGLDLSAMR--LLIVGSDGCKAQ-----------DFKTLAA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 419 KIQASlggrvklMVTgaapVSASVLTflRTALGCQFYEGYGQTECTAGcslSLPgdwtaghVGAPMPCNIIKLVDvQEMN 498
Cdd:cd17650 234 RFGQG-------MRI----INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 499 YLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:cd17650 290 PQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGE 368
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2032642720 573 IENVYLRCEAVAQVFV---HGESLQAFLVGVVVPDpDTLhNWA 612
Cdd:cd17650 369 IESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA-ATL-NTA 409
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
119-574 |
2.01e-22 |
|
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: 101.55 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHRGfKPShvQYIGIFSQNRPEWVIIEQAC-YAfSMVVVPLYDTLGAEAItyivnkADLSL 197
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPG--DRVLLLAPPGLDFVAAFLGClYA-GAIAVPLPPPTPGRHA------ERLAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 198 VFCDkpDKARVLLASVEkgetpilntivIMDSFGVDLVERGKKCGVEVFSMREIEELGRAHRQKPMPPkPEDLAVICFTS 277
Cdd:cd05931 93 ILAD--AGPRVVLTTAA-----------ALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD-PDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 278 GTTGNPKGAMITHQNIVSNASAFMktteKSFVPSSDDVLISFLPLAH-MferivecvvlchgariGFFQGdirllmddlk 356
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIR----RAYGLDPGDVVVSWLPLYHdM----------------GLIGG---------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 357 TLQPtvfpvvprllnrmfdkIFGQADSSL----------KRWL-----------------LDFASKRKEAELRSGIvrnn 409
Cdd:cd05931 209 LLTP----------------LYSGGPSVLmspaaflrrpLRWLrlisryratisaapnfaYDLCVRRVRDEDLEGL---- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 410 sfwDkvifrkiqasLgGRVKLMVTGAAPVSASVLT-FLRTALGCQF-----YEGYGQTECTAGCSLSLPG---------- 473
Cdd:cd05931 269 ---D----------L-SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATLFVSGGPPGtgpvvlrvdr 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 474 DWTAGHV----------------GAPMPCNIIKLVDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAE------ALD 531
Cdd:cd05931 335 DALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATD 414
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2032642720 532 KDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 574
Cdd:cd05931 415 EGGWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIE 455
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-591 |
3.12e-22 |
|
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: 99.09 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAfMKTTEKSfvpSSDDVLISFLPLAHMFERIVECVVLchgarigFFQG 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWM-LALNSLF---DPDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 347 DIRLLMDDLKTLQPTVFPVVPRLLnrmfdkifgqadsslKRWLLDFASKRKEAelrsgivrnnsfWDKVIFRKIQASLGG 426
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLV---------------ERYRITSLSTVPTV------------YAALLQVPVNADISS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 427 rVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLP-GDWTAGHVGAPMPCNIIKLVDVQ-EMNYL--AA 502
Cdd:cd05944 123 -LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 503 KGE-GEVCIKGVNVFRGYLKDpEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCE 581
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330
....*....|
gi 2032642720 582 AVAQVFVHGE 591
Cdd:cd05944 280 AVAFAGAVGQ 289
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-615 |
3.80e-22 |
|
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: 100.07 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHqnivSNASAFMKTTEKSFVPSSDDVLISFLPLAHMFErivecV-----VLCHGARI 341
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSH----ANVLALFAATQRWFGFNEDDVWTLFHSYAFDFS-----VweiwgALLHGGRL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 342 gffqgdirLLMDDLKTLQPTVFPvvpRLLNRMFDKIFGQADSSLKRwLLDFASKRKEA--ELRSgivrnnsfwdkVIFrk 419
Cdd:cd17643 163 --------VVVPYEVARSPEDFA---RLLRDEGVTVLNQTPSAFYQ-LVEAADRDGRDplALRY-----------VIF-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 420 iqaslggrvklmvtGAAPVSASVLT--FLRTALGC-QFYEGYGQTECTAGCSL------SLPGDwTAGHVGAPMPCNIIK 490
Cdd:cd17643 218 --------------GGEALEAAMLRpwAGRFGLDRpQLVNMYGITETTVHVTFrpldaaDLPAA-AASPIGRPLPGLRVY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 491 LVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLa 563
Cdd:cd17643 283 VLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI- 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 564 QGEYIAPEKIENVYLRCEAVAQVFV---HGESLQAFLVGVVVPDPDT------LHNWAKKK 615
Cdd:cd17643 361 RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGAaadiaeLRALLKEL 421
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-671 |
3.86e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 101.28 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 107 PCLGFRKPNQ-PYEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPL---YDTLG 182
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGLDPG--RPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 183 AE--AITYIVNKADLSLVFCDKpdkarvlLASVEKGetpilntIVIMDSFGVDLVERGKKC-GVEVFSMREI------EE 253
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQS-------GAPFARA-------LAALDLLDVTVVHVTGPGeGIASIAFADLaatpptAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 254 LGRAHRQKpmppKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTekSFVPSSD-DVLISFLPLAHMFE-RIVE 331
Cdd:PRK12582 210 VAAAIAAI----TPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLR--PREPDPPpPVSLDWMPWNHTMGgNANF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 332 CVVLCHGARI---------GFFQGDIRllmdDLKTLQPTVFPVVPRLLNRMFDKIfgQADSSLKRwlldfaskrkeaelr 402
Cdd:PRK12582 284 NGLLWGGGTLyiddgkplpGMFEETIR----NLREISPTVYGNVPAGYAMLAEAM--EKDDALRR--------------- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 403 sgivrnnSFwdkviFRKIQaslggrvkLMVTGAAPVSASVLTFLR----TALGCQ--FYEGYGQTEcTAGCSLSLpgDWT 476
Cdd:PRK12582 343 -------SF-----FKNLR--------LMAYGGATLSDDLYERMQalavRTTGHRipFYTGYGATE-TAPTTTGT--HWD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 477 A---GHVGAPMPCNIIKLVDVQEmNYlaakgegEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWL----PNGT 549
Cdd:PRK12582 400 TervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 550 LKIIDRKKHIFKLAQGEYIAPEKienvyLRCEAVA-------QVFVHGESlQAFLVGVVVPDPDTLHNWAKKKGfeGSYQ 622
Cdd:PRK12582 472 LIFDGRVAEDFKLSTGTWVSVGT-----LRPDAVAacspvihDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPE 543
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2032642720 623 ELCRNKDVKKYILEDMVRIGKESGLKSfEQVKDIVLHTEMFSIENGLLT 671
Cdd:PRK12582 544 DVVKHPAVLAILREGLSAHNAEAGGSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
119-598 |
1.00e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 98.66 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLV 198
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDR--VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDKPDkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpeDLAVICFTSG 278
Cdd:cd05971 83 VTDGSD----------------------------------------------------------------DPALIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNIVSNASAFMKTTEksFVPSSDDVLIS-------------FLPLAHMferivECVVLCHGARiGFFQ 345
Cdd:cd05971 99 TTGPPKGALHAHRVLLGHLPGVQFPFN--LFPRDGDLYWTpadwawigglldvLLPSLYF-----GVPVLAHRMT-KFDP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 346 GDIRLLMDDLKT----LQPTVFpvvprllnrmfdKIFGQADSSLKRWLLdfaskrkeaELRSgivrnnsfwdkvifrkiq 421
Cdd:cd05971 171 KAALDLMSRYGVttafLPPTAL------------KMMRQQGEQLKHAQV---------KLRA------------------ 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 422 aslggrvklMVTGAAPVSASVLTFLRTALGCQFYEGYGQTEC---TAGCSLSLPGDwtAGHVGAPMPCNIIKLVDvQEMN 498
Cdd:cd05971 212 ---------IATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGT 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 499 YLAAKGEGEVCIK--GVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENV 576
Cdd:cd05971 280 PLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEEC 357
|
490 500
....*....|....*....|....*....
gi 2032642720 577 YLRCEAVAQVFV-------HGESLQAFLV 598
Cdd:cd05971 358 LLKHPAVLMAAVvgipdpiRGEIVKAFVV 386
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-608 |
1.55e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.81 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLydtlgaeaityivnkaDLSLVFC 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDR--VALRMGSNAEFVVALLAASRADLVVVPL----------------DPALPIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDKARVLLASVekgetpilntiVIMDSFGV-DLVERGKKC---GVEVFSMREIEE------LGRAHRQKPMPPKPEDL 270
Cdd:PRK05852 106 EQRVRSQAAGARV-----------VLIDADGPhDRAEPTTRWwplTVNVGGDSGPSGgtlsvhLDAATEPTPATSTPEGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 271 ----AVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpsSDDVLISFLPLAHMFERIVECV-VLCHGARI---- 341
Cdd:PRK05852 175 rpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLS----PRDATVAVMPLYHGHGLIAALLaTLASGGAVllpa 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 342 -GFFQGdiRLLMDDLKTLQPTVFPVVPrllnrmfdkifgqadsSLKRWLLDFA----SKRKEAELRsgIVRNNSfwdkvi 416
Cdd:PRK05852 251 rGRFSA--HTFWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKPAALR--FIRSCS------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 417 frkiqaslggrvklmvtgaAPVSASVLTFLRTALGCQFYEGYGQTECT----------AGCSLSlPGDWT--AGHVGAPM 484
Cdd:PRK05852 305 -------------------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQTEN-PVVSTglVGRSTGAQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 485 pcniIKLV--DVQEmnyLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:PRK05852 365 ----IRIVgsDGLP---LPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINR 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2032642720 563 AqGEYIAPEKIENVYLRCEAV--AQVF-----VHGESLQAFLV--GVVVPDPDTL 608
Cdd:PRK05852 437 G-GEKISPERVEGVLASHPNVmeAAVFgvpdqLYGEAVAAVIVprESAPPTAEEL 490
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
121-606 |
2.48e-21 |
|
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: 97.80 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVfc 200
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARGVGPGDL--VALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 dkpdkarvLLASVEKGETPilntivimdsfgvdlVERGkkcGVEVFSMREIEELGRAHRqkPMPPKPEDLAVICFTSGTT 280
Cdd:cd17651 97 --------LTHPALAGELA---------------VELV---AVTLLDQPGAAAGADAEP--DPALDADDLAYVIYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITH---------QNIVSNASAFMKTTekSFVPSSDDVlisflplahMFERIVEcvVLCHGARIGFFQGDIRll 351
Cdd:cd17651 149 GRPKGVVMPHrslanlvawQARASSLGPGARTL--QFAGLGFDV---------SVQEIFS--TLCAGATLVLPPEEVR-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 352 MDDlktlqptvfpvvprllnrmfdkifgqadSSLKRWLLdfaskrkeaelRSGIVRnnSFWDKVIFRKI------QASLG 425
Cdd:cd17651 214 TDP----------------------------PALAAWLD-----------EQRISR--VFLPTVALRALaehgrpLGVRL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 426 GRVKLMVTGAAPVSASVLT--FLRTALGCQFYEGYGQTECTAGCSLSLPGD---WTA-GHVGAPMPCNIIKLVDvqEMNY 499
Cdd:cd17651 253 AALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD--AALR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 500 LAAKG-EGEVCIKGVNVFRGYLKDPEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:cd17651 331 PVPPGvPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGE 409
|
490 500 510
....*....|....*....|....*....|....*..
gi 2032642720 573 IENVYLRCEAVAQ--VFVHGE-SLQAFLVGVVVPDPD 606
Cdd:cd17651 410 IEAALARHPGVREavVLAREDrPGEKRLVAYVVGDPE 446
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
242-583 |
4.41e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 97.37 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 242 GVEVfsmREIEELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVpssDDVLISFLP 321
Cdd:PRK07768 129 GIRV---LTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVE---TDVMVSWLP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 322 LAH-MferivecvvlchgARIGFFQGDIRLLMDDLKtLQPTVFPVVPRLLNRMFDKIFGQ-------ADSSLKRwLLDFA 393
Cdd:PRK07768 203 LFHdM-------------GMVGFLTVPMYFGAELVK-VTPMDFLRDPLLWAELISKYRGTmtaapnfAYALLAR-RLRRQ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 394 SKRKEAELRSgivrnnsfwdkvifrkiqaslggrVKLMVTGAAPVS-ASVLTFL---------RTALGCqfyeGYGQTEC 463
Cdd:PRK07768 268 AKPGAFDLSS------------------------LRFALNGAEPIDpADVEDLLdagarfglrPEAILP----AYGMAEA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 464 TAGCSLSLPGD--------------------WTAGHV------GAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFR 517
Cdd:PRK07768 320 TLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTP 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032642720 518 GYLkDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAV 583
Cdd:PRK07768 399 GYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIERAAARVEGV 462
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-606 |
4.61e-21 |
|
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: 96.96 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPG--DLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDkarvllasVEKGETPILNTIVIMDSfgvdlvergkkcgvevfsmreieeLGRAHRQKPMPPKPEDLAVICFTSGTT 280
Cdd:cd12114 91 DGPD--------AQLDVAVFDVLILDLDA------------------------LAAPAPPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNiVSNASAfmkTTEKSFVPSSDDVLISFLPLAH------MFErivecvVLCHGARIGFFQGDIR----L 350
Cdd:cd12114 139 GTPKGVMISHRA-ALNTIL---DINRRFAVGPDDRVLALSSLSFdlsvydIFG------ALSAGATLVLPDEARRrdpaH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 351 LMDDLKTLQPTVFPVVPRLLNRMFDKI--FGQADSSLKRWLLdfaskrkeaelrSGivrnnsfwdkvifRKIQASLGGRV 428
Cdd:cd12114 209 WAELIERHGVTLWNSVPALLEMLLDVLeaAQALLPSLRLVLL------------SG-------------DWIPLDLPARL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 429 KLMVTGAAPVSasvltflrtaLGcqfyegyGQTEcTAGCSLSLP-----GDWTAGHVGAPMPcNiiklvdvQEMNYLAAK 503
Cdd:cd12114 264 RALAPDARLIS----------LG-------GATE-ASIWSIYHPidevpPDWRSIPYGRPLA-N-------QRYRVLDPR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 504 GE-------GEVCIKGVNVFRGYLKDPEKTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:cd12114 318 GRdcpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGE 396
|
490 500 510
....*....|....*....|....*....|....*.
gi 2032642720 573 IENVYLRCEAVAQ--VFVHGESLQAFLVGVVVPDPD 606
Cdd:cd12114 397 IEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDND 432
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
90-588 |
1.65e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 95.60 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 90 RTVYDIFQRGLQVSNNGPCLGFRKpnqpyEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYA 169
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKRG--DRVALMCGNRIEFLDVFLGCAW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 170 FSMVVVPLYDTLGAEAITYIVNKADLSLVFCDKPDKARvlLASVEKGETPiLNTIVIMDSFGVDLVERGkkcgvevFSMR 249
Cdd:PRK06155 94 LGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAA--LEAADPGDLP-LPAVWLLDAPASVSVPAG-------WSTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 250 EIEELGRAhrQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIV---SNASAFMKTTEksfvpssDDVLISFLPLAH-- 324
Cdd:PRK06155 164 PLPPLDAP--APAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYwwgRNSAEDLEIGA-------DDVLYTTLPLFHtn 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 325 ---MFERivecvVLCHGARI---------GFFqgdirllmDDLKTLQPTVF----PVVPRLLnrmfdkifgqadsslkrw 388
Cdd:PRK06155 235 alnAFFQ-----ALLAGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL------------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 389 lldfaSKRKEAELRSGIVRnnsfwdkvifrkiqASLGGrvklmvtgaaPVSASVLTFLRTALGCQFYEGYGQTECTAGCS 468
Cdd:PRK06155 284 -----SQPARESDRAHRVR--------------VALGP----------GVPAALHAAFRERFGVDLLDGYGSTETNFVIA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 469 LSLPGDwTAGHVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVF---RGYLKDPEKTAEALdKDGWLHTGDIGKWL 545
Cdd:PRK06155 335 VTHGSQ-RPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRD 411
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2032642720 546 PNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYLRCEAVAQVFV 588
Cdd:PRK06155 412 ADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAV 453
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
112-590 |
1.73e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 95.34 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 112 RKPNQPY-----EWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAI 186
Cdd:PRK06145 14 RTPDRAAlvyrdQEISYAEFHQRILQAAGMLHARGIGQGDV--VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 187 TYIVNKADLSLVFCDKPDKARVLLasvekgETPIlntiVIMDSFGVDLVERGKKCGVEVFSMReieelgrahrqkpmPPK 266
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVAL------ETPK----IVIDAAAQADSRRLAQGGLEIPPQA--------------AVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIvsnasaFMKTTEKSFV--PSSDDVLISFLPLAHM--FErIVECVVLCHGARIG 342
Cdd:PRK06145 148 PTDLVRLMYTSGTTDRPKGVMHSYGNL------HWKSIDHVIAlgLTASERLLVVGPLYHVgaFD-LPGIAVLWVGGTLR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 343 FFQG-DIRLLMDDLKTLQPTVFPVVPRLLNRMF-----DKIfgqaDSSLKRWLLDFASKRKEAELRSgivrnnsfwdkvi 416
Cdd:PRK06145 221 IHREfDPEAVLAAIERHRLTCAWMAPVMLSRVLtvpdrDRF----DLDSLAWCIGGGEKTPESRIRD------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 417 frkiqaslggrvklmvtgaapvsasvltFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTA--GHVGAPMPCNIIKLVDv 494
Cdd:PRK06145 284 ----------------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 495 QEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK06145 335 GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVE 412
|
490
....*....|....*.
gi 2032642720 575 NVYLRCEAVAQVFVHG 590
Cdd:PRK06145 413 RVIYELPEVAEAAVIG 428
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-605 |
2.28e-20 |
|
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: 95.13 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEW-VIIEQACYAFsmvVVPLydtlgaeAITYIVNKADLSLVF 199
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKRE--ERVLLIMLDTVDFpTAFLGAIRAG---IVPV-------PVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 200 CDKpdKARVLLASVEKgeTPILNTIV-IMDSFGVDLVERGKKCGVEVFSMREIEELGRAHRQKPMPPKPEDLAVICFTSG 278
Cdd:cd05959 98 EDS--RARVVVVSGEL--APVLAAALtKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNIVSNASAFMKTTEKSfvpSSDDVLISFLPLAHMFErivecvvLCHGARIGFFQGDIRLLM------ 352
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNVLGI---REDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 353 ----DDLKTLQPTVFPVVPRLLNRMFDKifgqadsslkrwllDFASKRKEAELRsgivrnnsfwdkvifrkiqaslggrv 428
Cdd:cd05959 244 aavfKRIRRYRPTVFFGVPTLYAAMLAA--------------PNLPSRDLSSLR-------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 429 kLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvQEMNYLAAKGEGEV 508
Cdd:cd05959 284 -LCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 509 CIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENVYLRCEAVAQVFV 588
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500
....*....|....*....|
gi 2032642720 589 HGESLQAFL---VGVVVPDP 605
Cdd:cd05959 440 VGVEDEDGLtkpKAFVVLRP 459
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
264-613 |
2.68e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 95.11 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 264 PPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFmktTEKSFVPSSDDVLISFLPlahMFerivecvvlchgarigF 343
Cdd:PRK06178 205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAA---YAVAVVGGEDSVFLSFLP---EF----------------W 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 344 FQGDirllmdDLKTLQPTVF--PVVprLLNRM-------------FDKIFGQADSSLKrwLLDFaSKRKEAELRS-GIVR 407
Cdd:PRK06178 263 IAGE------NFGLLFPLFSgaTLV--LLARWdavafmaaveryrVTRTVMLVDNAVE--LMDH-PRFAEYDLSSlRQVR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 408 NNSFwdkviFRKIQASLGGRvklmvtgaapvsasvltfLRTALGCQFYEG-YGQTEcTAGCSlslpgDWTAG-------- 478
Cdd:PRK06178 332 VVSF-----VKKLNPDYRQR------------------WRALTGSVLAEAaWGMTE-THTCD-----TFTAGfqdddfdl 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 479 -----HVGAPMPCNIIKLVDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PRK06178 383 lsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYL 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 554 DRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFV-------HGESLQAFLvgVVVP----DPDTLHNWAK 613
Cdd:PRK06178 462 GRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVvgrpdpdKGQVPVAFV--QLKPgadlTAAALQAWCR 529
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
267-695 |
4.96e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.48 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAfmkttEKSFVP-SSDDVLISFLPLAHMfERIVECVVL-----CHGAR 340
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLA-----KIAIVGyGEDDVYLHTAPLCHI-GGLSSALAMlmvgaCHVLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 341 IGFfqgDIRLLMDDLKTLQPTVFPVVPRLLnrmfdkifgqADsslkrwLLDFASKRKEAELRSGIvrnnsfwdkvifRKI 420
Cdd:PLN02860 245 PKF---DAKAALQAIKQHNVTSMITVPAMM----------AD------LISLTRKSMTWKVFPSV------------RKI 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 421 QASLGG-------RVKLMVTGAAPVSA-------SVLTFLRtaLGCQFYEGYGQTECTAGCSLSLPGDWTAGH-VGAPMP 485
Cdd:PLN02860 294 LNGGGSlssrllpDAKKLFPNAKLFSAygmteacSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 486 CNIIKL-VDVqemnylaAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 564
Cdd:PLN02860 372 HVELKIgLDE-------SSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 565 GEYIAPEKIENVYLRCEAVAQVFVHG---ESLQAFLVGVVvpdpdTLH-NWAkkkgFEGSYQELCR-NKDVKKYILEDMV 639
Cdd:PLN02860 444 GENVYPEEVEAVLSQHPGVASVVVVGvpdSRLTEMVVACV-----RLRdGWI----WSDNEKENAKkNLTLSSETLRHHC 514
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032642720 640 RigkESGLKSFEQVKDIVLHTEMFSienglLTPTLKAKRPELRKYFQSQIDELYAN 695
Cdd:PLN02860 515 R---EKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSN 562
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-606 |
5.24e-20 |
|
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: 94.06 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSH---VQyigifSQNRPEWVIieqACYA-FSMVVVPLYdTL----GAEaITYIVNK 192
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDrvvVQ-----LPNVAEFVI---VFFAlFRAGAIPVF-ALpahrRAE-ISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 193 ADLSLVFCdkPDKA-----RVLLASVeKGETPILNTIVIMDSFGvdlvergkkcgvevfSMREIEELGRAHRQKPMP-PK 266
Cdd:COG1021 121 SEAVAYII--PDRHrgfdyRALAREL-QAEVPSLRHVLVVGDAG---------------EFTSLDALLAAPADLSEPrPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKgaMI--THQNIVSN--ASA----FmktteksfvpSSDDVLISFLPLAHMFERIVECV--VLC 336
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPK--LIprTHDDYLYSvrASAeicgL----------DADTVYLAALPAAHNFPLSSPGVlgVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 337 HGARIgffqgdirLLMDDLKTL---------QPTVFPVVPRLLNRMfdkifgqadsslkrwlLDFASKRKeAELRSgivr 407
Cdd:COG1021 251 AGGTV--------VLAPDPSPDtafpliereRVTVTALVPPLALLW----------------LDAAERSR-YDLSS---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 408 nnsfwdkvifrkiqaslggrVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTE----CTagcSLSLPGDWTAGHVGAP 483
Cdd:COG1021 302 --------------------LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEglvnYT---RLDDPEEVILTTQGRP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 484 M-PCNIIKLVDVQEmNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFK 561
Cdd:COG1021 359 IsPDDEVRIVDEDG-NPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2032642720 562 laQGEYIAPEKIENVYLRCEAVAQVFVhgeslqaflvgVVVPDPD 606
Cdd:COG1021 438 --GGEKIAAEEVENLLLAHPAVHDAAV-----------VAMPDEY 469
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-606 |
1.34e-19 |
|
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: 92.00 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGPESR--VGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DkpdkarvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkPEDLAVICFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHqnivSNASAFMKTTEKSFvpSSDD---VL----ISF-LPLAHMFerivecVVLCHGARIGFFQGDIRLLm 352
Cdd:cd12115 118 GRPKGVAIEH----RNAAAFLQWAAAAF--SAEElagVLastsICFdLSVFELF------GPLATGGKVVLADNVLALP- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 353 dDLK-----TLQPTVfPVVPRLLNRMfDKIfgqaDSSLKrwLLDFASKRKEAELrsgivrnnsfwdkviFRKIQASLGGR 427
Cdd:cd12115 185 -DLPaaaevTLINTV-PSAAAELLRH-DAL----PASVR--VVNLAGEPLPRDL---------------VQRLYARLQVE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 428 vklmvtgaapvsasvltflrtalgcQFYEGYGQTECTA---GCSLSlPGDWTAGHVGAPMPCNIIKLVDvQEMNYLAAKG 504
Cdd:cd12115 241 -------------------------RVVNLYGPSEDTTystVAPVP-PGASGEVSIGRPLANTQAYVLD-RALQPVPLGV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 505 EGEVCIKGVNVFRGYLKDPEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYL 578
Cdd:cd12115 294 PGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALR 372
|
490 500 510
....*....|....*....|....*....|.
gi 2032642720 579 RCEAVAQ--VFVHGESL-QAFLVGVVVPDPD 606
Cdd:cd12115 373 SIPGVREavVVAIGDAAgERRLVAYIVAEPG 403
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
121-607 |
1.86e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 92.44 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSAL---LHRGfKPSHVqyiGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSL 197
Cdd:PRK07867 29 TSWREHIRGSAARAAALrarLDPT-RPPHV---GVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 198 VFCDkpDKARVLLASVEKGeTPILNTivimDSfgvdlvergkkcgvevfsmREIEELGRAHRQKPMPPK---PEDLAVIC 274
Cdd:PRK07867 105 VLTE--SAHAELLDGLDPG-VRVINV----DS-------------------PAWADELAAHRDAEPPFRvadPDDLFMLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 275 FTSGTTGNPKGAMITHQNIVSNASAFmktTEKsFVPSSDDVLISFLPLAHMFERIVE-CVVLCHGARI---------GFf 344
Cdd:PRK07867 159 FTSGTSGDPKAVRCTHRKVASAGVML---AQR-FGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 qgdirllMDDLKTLQPTVFPVVPRLLNRMF--DKIFGQADSSLKrwlldfaskrkeaelrsgivrnnsfwdkvifrkiqa 422
Cdd:PRK07867 234 -------LPDVRRYGATYANYVGKPLSYVLatPERPDDADNPLR------------------------------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 423 slggrvklMVTGAAPVSASVLTFLRTaLGCQFYEGYGQTEctAGCSLSLPGDWTAGHVGAPMPCniIKLVDVQ------- 495
Cdd:PRK07867 271 --------IVYGNEGAPGDIARFARR-FGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecpp 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 -------EMNYLAAKGEgEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:PRK07867 338 aedadgrLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENL 414
|
490 500 510
....*....|....*....|....*....|....*....
gi 2032642720 569 APEKIENVYLRCEAVAQVFVHGeslqaflvgvvVPDPDT 607
Cdd:PRK07867 415 GTAPIERILLRYPDATEVAVYA-----------VPDPVV 442
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
266-615 |
2.48e-19 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 91.34 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 266 KPEDLAVICFTSGTTGNPKGAMITHQNIVSnasaFMKTTEKSF-VPSSDDVLIsFLPLAhmFERIVE--CVVLCHGARIg 342
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVN----LSHGLIKEYgITSSDRVLQ-FASIA--FDVAAEeiYVTLLSGATL- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 343 ffqgdirllmddlkTLQPtvfpvvprllNRMFdkifgqadSSLKrwllDFASKRKEAELRsgiVRN--NSFWDKVIFRKI 420
Cdd:cd17644 176 --------------VLRP----------EEMR--------SSLE----DFVQYIQQWQLT---VLSlpPAYWHLLVLELL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 421 QASLGG--RVKLMVTGAAPVSASVLTFLRTALG--CQFYEGYGQTECTAGCSLSLPGDWTAGH-----VGAPMPcNIIKL 491
Cdd:cd17644 217 LSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIA-NTQVY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 492 VDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLa 563
Cdd:cd17644 296 ILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI- 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 564 QGEYIAPEKIENVYLRCEAVAQVFV---HGESLQAFLVGVVVP------DPDTLHNWAKKK 615
Cdd:cd17644 375 RGFRIELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPhyeespSTVELRQFLKAK 435
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
268-598 |
5.59e-19 |
|
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: 90.21 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 268 EDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKtteKSFVPSSDDVLISflpLAHMFEriveCVVLCHGARIGFFQGD 347
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IRLLMDDLKT----------LQPTVFPVVPRLLNRMFDKIFGQADSslkrwlldfaskrkeaeLRSgivrnnsfwdkvif 417
Cdd:cd05919 161 SAVLNPGWPTaervlatlarFRPTVLYGVPTFYANLLDSCAGSPDA-----------------LRS-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 rkiqaslggrVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvQEM 497
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 498 NYLAAKGEGEVCIKGVNVFRGYLKDPEKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVY 577
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*...
gi 2032642720 578 LRCEAVAQVFV------HGES-LQAFLV 598
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVV 384
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
120-605 |
6.93e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 90.78 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 120 WISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWViieQACYAFSM---VVVPLYDTLGAEAITYIVNKADls 196
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIGRGDT--VAVLLPNIPAMV---EAHFGVPMagaVLNTLNTRLDAASIAFMLRHGE-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 197 lvfcdkpdkARVLLASVEKGET--------PILNTIVImdsfGVDLVERGkkcGVEVFSMREIEEL---GRAHRQKPMPP 265
Cdd:PRK08162 116 ---------AKVLIVDTEFAEVarealallPGPKPLVI----DVDDPEYP---GGRFIGALDYEAFlasGDPDFAWTLPA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 266 KPEDLAVICFTSGTTGNPKGAMITHQ----NIVSNASAF-MKtteksfvPSSddVLISFLPLAHmferiveCVVLCH--- 337
Cdd:PRK08162 180 DEWDAIALNYTSGTTGNPKGVVYHHRgaylNALSNILAWgMP-------KHP--VYLWTLPMFH-------CNGWCFpwt 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 338 -GARIG----FFQGDIRLLMDDLKTLQPTVF---PVVPRLLNRMfdkifgqadsslkrwlldfaskrkEAELRSGIvrnn 409
Cdd:PRK08162 244 vAARAGtnvcLRKVDPKLIFDLIREHGVTHYcgaPIVLSALINA------------------------PAEWRAGI---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 410 sfwdkvifrkiqaslGGRVKLMVTGAAPvSASVLTFLRtALGCQFYEGYGQTEcTAG----CSL-----SLPGDWTA--- 477
Cdd:PRK08162 296 ---------------DHPVHAMVAGAAP-PAAVIAKME-EIGFDLTHVYGLTE-TYGpatvCAWqpewdALPLDERAqlk 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 478 GHVGAPMPC-NIIKLVDVQEMNYLAAKGE--GEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIID 554
Cdd:PRK08162 358 ARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKD 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 555 RKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFVhgeslqaflvgVVVPDP 605
Cdd:PRK08162 437 RSKDII-ISGGENISSIEVEDVLYRHPAVLVAAV-----------VAKPDP 475
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
90-604 |
1.05e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 91.38 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 90 RTVYDIFQRGLQVSNNGPCLGFRKpnqpyEWISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYA 169
Cdd:PRK12467 512 DCVHQLIEAQARQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAGVGPD--VLVGIAVERSIEMVVGLLAVLK 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 170 FSMVVVPLYDTLGAEAITYIVNKADLSLVFCDKPDKARVLLasvekgetPILNTIVIMDSFGvDLVErgkkcgvevfsmr 249
Cdd:PRK12467 585 AGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPV--------PAGLRSLCLDEPA-DLLC------------- 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 250 eieelGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSnasaFMKTTEKSFVPSSDDVLISFLPLAHMFERI 329
Cdd:PRK12467 643 -----GYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVT 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 330 VECVVLCHGARIGFFQGDIRL----LMDDLKTLQPTVFPVVPrllnrmfdkifgqadsslkrwlldfaskrkeaelrsgi 405
Cdd:PRK12467 714 ELFGALASGATLHLLPPDCARdaeaFAALMADQGVTVLKIVP-------------------------------------- 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 406 vrnnSFWDKVIFRKIQASLGGRVKLMVTGAA-PVSASVLTFlRTALGCQFYEGYGQTECTAGCSL----SLPGDWTAGHV 480
Cdd:PRK12467 756 ----SHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-ALGPGARLINHYGPTETTVGVSTyelsDEERDFGNVPI 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 481 GAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKD------GWLH-TGDIGKWLPNGTLKII 553
Cdd:PRK12467 831 GQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYL 909
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032642720 554 DRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFV------HGESLQAFLVGVVVPD 604
Cdd:PRK12467 910 GRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaqpgdAGLQLVAYLVPAAVAD 965
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
268-598 |
1.07e-18 |
|
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: 88.09 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 268 EDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpSSDDVLISFLPLAHMFERIVECVVLCHGARIGFFQGD 347
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNW---VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IRL--LMDDLKTLQPTVFPVVPRLLNRMfdkifgqadsslkrwLLDFASKRKEAE-LRSgivrnnsfwdkvifrkiqasl 424
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVPsLRL--------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 ggrvkLMVTGAAPVSASVLTFLRTALgCQFYEGYGQTECTAGCSLSLPGDWT-AGHVGAPMPCNIIKLVDVQEMNYLAAk 503
Cdd:cd17635 122 -----IGYGGSRAIAADVRFIEATGL-TNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSA- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 504 GEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYL----- 578
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAEgvsgv 272
|
330 340
....*....|....*....|...
gi 2032642720 579 ---RCEAVAQVfVHGESLQAFLV 598
Cdd:cd17635 273 qecACYEISDE-EFGELVGLAVV 294
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-585 |
5.27e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 88.23 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 259 RQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFmkTTEKSFVPssDDVLISFLPLAHMFERIVECVV-LCH 337
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQI--KTIADFTP--NDRFMSALPLFHSFGLTVGLFTpLLT 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 338 GARIGFFQgdirllmddlktlQPTVFPVVPRLL-NRMFDKIFGQADsslkrWLLDFASkrkeaelrsgivrnnsFWDKVI 416
Cdd:PRK08043 432 GAEVFLYP-------------SPLHYRIVPELVyDRNCTVLFGTST-----FLGNYAR----------------FANPYD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 417 FrkiqaslgGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVQE 496
Cdd:PRK08043 478 F--------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPG 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 497 MnylaAKGeGEVCIKGVNVFRGYLK--DP-------EKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 567
Cdd:PRK08043 550 I----EQG-GRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEM 623
|
330
....*....|....*...
gi 2032642720 568 IAPEKIENVYLRCEAVAQ 585
Cdd:PRK08043 624 VSLEMVEQLALGVSPDKQ 641
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
267-607 |
6.29e-18 |
|
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: 86.92 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIvsnaSAFMKTTEKSFVPSSDDVLISFLPLAhmFERIVE--CVVLCHGARigff 344
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGL----ANLAAAQIAAFDVGPGSRVLQFASPS--FDASVWelLMALLAGAT---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 qgdirLLMDDLKTLQPtvfpvvprllnrmfdkifGQAdsslkrwLLDFASKRK--EAELRSGIVRNNSfwdkvifrkiQA 422
Cdd:cd17652 162 -----LVLAPAEELLP------------------GEP-------LADLLREHRitHVTLPPAALAALP----------PD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 423 SLGGRVKLMVTGAAPVSASVLtflRTALGCQFYEGYGQTECTAGCSLSLP-GDWTAGHVGAPMPCNIIKLVDvQEMNYLA 501
Cdd:cd17652 202 DLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 502 AKGEGEVCIKGVNVFRGYLKDPEKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 574
Cdd:cd17652 278 PGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVE 356
|
330 340 350
....*....|....*....|....*....|....*.
gi 2032642720 575 NVYLRCEAVAQ--VFVHGESL-QAFLVGVVVPDPDT 607
Cdd:cd17652 357 AALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGA 392
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
255-575 |
7.05e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 88.48 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 255 GRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNAsaFMKTTEKSFvpSSDDVLISFLPLAHMFerivecvv 334
Cdd:PRK06814 780 GRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANR--AQVAARIDF--SPEDKVFNALPVFHSF-------- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 335 lchgariGFFQGDIRLLMDDLKTL---QPTVFPVVPRLLnrmFDK----IFGqADSSLkrwlldfaskrkeaelrSGIVR 407
Cdd:PRK06814 848 -------GLTGGLVLPLLSGVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFL-----------------NGYAR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 408 NNSFWDkviFRkiqaslggRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCN 487
Cdd:PRK06814 900 YAHPYD---FR--------SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGI 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 488 IIKLVDVQEMNylaaKGeGEVCIKGVNVFRGYLKdPEK--TAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 565
Cdd:PRK06814 969 EYRLEPVPGID----EG-GRLFVRGPNVMLGYLR-AENpgVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-G 1040
|
330
....*....|
gi 2032642720 566 EYIAPEKIEN 575
Cdd:PRK06814 1041 EMISLAAVEE 1050
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-604 |
8.86e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPE--VRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDKARVLLASvekgetpilntivimdsfgvdlvergkkcGVEVFSMREIEELGRAHRQKPMPP-KPEDLAVICFTSGT 279
Cdd:PRK12316 2107 QRHLLERLPLPA-----------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 280 TGNPKGAMITHQNIVsnasAFMKTTEKSFVPSSDDVLISFLPLAhmFERIVE--CVVLCHGARIgffqgdirLLMDDlkT 357
Cdd:PRK12316 2158 TGLPKGVAVSHGALV----AHCQAAGERYELSPADCELQFMSFS--FDGAHEqwFHPLLNGARV--------LIRDD--E 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 358 LqptvfpvvpRLLNRMFDKIFGQADSslkrwLLDFASkrkeaelrsgivrnnSFWDKVIFRKIQASLGGRVKLMVTGAAP 437
Cdd:PRK12316 2222 L---------WDPEQLYDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 438 VSASVLTFLRTALGCQF-YEGYGQTECTAGCSLslpgdWTAGHV----GAPMPcnIIKLVDVQ-------EMNYLAAKGE 505
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYlFNGYGPTEAVVTPLL-----WKCRPQdpcgAAYVP--IGRALGNRrayildaDLNLLAPGMA 2345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 506 GEVCIKGVNVFRGYLKDPEKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYL 578
Cdd:PRK12316 2346 GELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQ 2424
|
490 500
....*....|....*....|....*....
gi 2032642720 579 RCEAVAQVFV---HGESLQAfLVGVVVPD 604
Cdd:PRK12316 2425 AHPAVREAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-583 |
8.91e-18 |
|
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: 86.77 E-value: 8.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKsfvpSSDDVLISFLPLAHMFERIVecvvlCHGARIgfFQG 346
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTHDMGLIA-----FHLAPL--IAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 347 DIRLLMddlktlqPT-VFPVVPRLlnrmfdkifgqadsslkrWLldfaskRKEAELRSGIVRNNSFWDKVIFRKIQASLG 425
Cdd:cd05908 174 MNQYLM-------PTrLFIRRPIL------------------WL------KKASEHKATIVSSPNFGYKYFLKTLKPEKA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 426 GRVKL-----MVTGAAPVSASVLTFLRTALGC------QFYEGYGQTECTAGCSLSLPGD-------------------- 474
Cdd:cd05908 223 NDWDLssirmILNGAEPIDYELCHEFLDHMSKyglkrnAILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepe 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 475 --------WTAGHVGAPMPCNIIKLVDvqEMNYLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGkWL 545
Cdd:cd05908 303 vdkkdsecLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FI 379
|
330 340 350
....*....|....*....|....*....|....*...
gi 2032642720 546 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAV 583
Cdd:cd05908 380 RNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
267-612 |
3.08e-17 |
|
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: 84.73 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTteksFVPSSDDVLISFLPLAhmFERIVECVV--LCHGARIgff 344
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER----YGLTPGDRELQFASFN--FDGAHEQLLppLICGACV--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 qgdirlLMDDLKTLQPtvfpvvPRLLNRMFDK----IFGQADSSLKRWLLDFASKrkeaelrsgivrnnsfwdkvifrki 420
Cdd:cd17649 164 ------VLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADRT------------------------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 421 QASLGGRVKLMVTGAAPVSASVLTFLRTAlGCQFYEGYGQTECTAG-----CSLSLPGDWTAGHVGAPMPCNIIKLVDVQ 495
Cdd:cd17649 207 GDGRPPSLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEATVTplvwkCEAGAARAGASMPIGRPLGGRSAYILDAD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 eMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17649 286 -LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRI 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2032642720 569 APEKIENVYLRCEAVAQVFVHGES--LQAFLVGVVVP-DPDTLHNWA 612
Cdd:cd17649 364 ELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLrAAAAQPELR 410
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-576 |
1.01e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 83.71 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTteksFVPSSDDVLISFLPLAHMFerivecvvlchgariGFFQG 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 347 DIRLLMDDLktlqPTVF---PVVPRLLNRMFDK----IFGQA----DSSLKrwlldfASKRKEAELRSgivrnnsfwdkv 415
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTpvffDYILK------TAKKQESCLPS------------ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 416 ifrkiqaslggrVKLMVTGAAPVSASVLT-FLRTALGCQFYEGYGQTECTAGCSLSL---PGDWTAghVGapMPCNIIKL 491
Cdd:PRK06334 301 ------------LRFVVIGGDAFKDSLYQeALKTFPHIQLRQGYGTTECSPVITINTvnsPKHESC--VG--MPIRGMDV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 492 VDVQEMNYL-AAKGE-GEVCIKGVNVFRGYL-KDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 568
Cdd:PRK06334 365 LIVSEETKVpVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMV 443
|
....*...
gi 2032642720 569 APEKIENV 576
Cdd:PRK06334 444 SLEALESI 451
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-608 |
2.26e-16 |
|
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: 82.06 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFmktTEKSFVPSSDDVLISFLPlAHMFERIVE--CVVLCHGARIGFF 344
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL---SERYFGRDNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 QGDIRL----LMDDLKTLQPTVFPVVPRLLnRMFDkiFGQADSsLKRWLL---DFASKRkeaelrsgivrnnsfwdkviF 417
Cdd:cd17648 169 PDEMRFdpdrFYAYINREKVTYLSGTPSVL-QQYD--LARLPH-LKRVDAageEFTAPV--------------------F 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 RKIQASLGGRVklmvtgaapvsasvltflrtalgcqfYEGYGQTEC--TAGCSLSLPGDWTAGHVGAPMPcNIIKLVDVQ 495
Cdd:cd17648 225 EKLRSRFAGLI--------------------------INAYGPTETtvTNHKRFFPGDQRFDKSLGRPVR-NTKCYVLND 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 EMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFK 561
Cdd:cd17648 278 AMKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2032642720 562 LaQGEYIAPEKIENVYLRCEAVAQVFV--------HGESLQAFLVGVVVPDPDTL 608
Cdd:cd17648 358 I-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
421-638 |
3.82e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.99 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 421 QASLGGRVKLMVTGAAPVSASVLTFLRtaLGCQFYEGYGQTECTAG---CSLS-----LPGDWTAgHVGAPMPCNIIKLV 492
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPvlfCEWQdewnrLPENQQM-ELKARQGVSILGLA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 493 DV-------QEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 565
Cdd:PLN03102 373 DVdvknketQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGG 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 566 EYIAPEKIENVylrceavaqVFVHGESLQAFLVGvvVPDPdtlhNWAK--------KKGFEGSYQE----LCRNKDVKKY 633
Cdd:PLN03102 451 ENISSVEVENV---------LYKYPKVLETAVVA--MPHP----TWGEtpcafvvlEKGETTKEDRvdklVTRERDLIEY 515
|
....*
gi 2032642720 634 ILEDM 638
Cdd:PLN03102 516 CRENL 520
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
267-588 |
6.35e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 80.69 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNA---SAFMKTTeksfvpSSDDVLISfLPLAHmferivecvV--------- 334
Cdd:PRK09029 134 PQRLATMTLTSGSTGLPKAAVHTAQAHLASAegvLSLMPFT------AQDSWLLS-LPLFH---------Vsgqgivwrw 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 335 LCHGARIGFfqGDIRLLMDDLK-----TLQPTvfpvvprllnrmfdkifgQadssLKRWLldfASKRKEAELRsgivrnn 409
Cdd:PRK09029 198 LYAGATLVV--RDKQPLEQALAgcthaSLVPT------------------Q----LWRLL---DNRSEPLSLK------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 410 sfwdKVIfrkiqasLGGrvklmvtGAAPVSasvLTFLRTALGCQFYEGYGQTE----CTAGCSLSLPGdwtaghVGAPMP 485
Cdd:PRK09029 244 ----AVL-------LGG-------AAIPVE---LTEQAEQQGIRCWCGYGLTEmastVCAKRADGLAG------VGSPLP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 486 CNIIKLVDvqemnylaakgeGEVCIKGVNVFRGYLKDPEKTAeALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQG 565
Cdd:PRK09029 297 GREVKLVD------------GEIWLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGG 361
|
330 340
....*....|....*....|...
gi 2032642720 566 EYIAPEKIENVYLRCEAVAQVFV 588
Cdd:PRK09029 362 EGIQPEEIERVINQHPLVQQVFV 384
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-614 |
9.40e-16 |
|
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: 80.29 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVS----NASAF-MKTTEKSFVPSSddvlISFLPLA-HMFERIVEcvvlchGAR 340
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNlcewHRPYFgVTPADKSLVYAS----FSFDASAwEIFPHLTA------GAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 341 IGFFQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKiFGQADSSLKRWLLDFASKRKEAELRsgivrnnsfwdkvifrki 420
Cdd:cd17645 173 LHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQ-FMQLDNQSLRVLLTGGDKLKKIERK------------------ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 421 qaslggrvklmvtgaapvsasvltflrtalGCQFYEGYGQTECTAgCSLSLPGDWTAGHVGAPMPCNIIKLVDVQEMNYL 500
Cdd:cd17645 234 ------------------------------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 501 AAKG-EGEVCIKGVNVFRGYLKDPEKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:cd17645 283 QPIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEI 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2032642720 574 ENVYLRCEAV---AQVFVHGESLQAFLVGVVVP----DPDTLHNWAKK 614
Cdd:cd17645 362 EPFLMNHPLIelaAVLAKEDADGRKYLVAYVTApeeiPHEELREWLKN 409
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
121-605 |
1.13e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 80.47 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:PRK07470 33 WTWREIDARVDALAAALAARGVRKG--DRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 --DKPDKARvllaSVEKGETPILNTIVIMDSFGVDlvergkkcgvevfsmrEIEELGRAHRQKPMPPKPEDLAVIC---F 275
Cdd:PRK07470 111 haDFPEHAA----AVRAASPDLTHVVAIGGARAGL----------------DYEALVARHLGARVANAAVDHDDPCwffF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 276 TSGTTGNPKGAMITHQN---IVSN--ASAFMKTTEksfvpssDDVLISFLPLAHMfERIVECVVLCHGARIGFFQGDiRL 350
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQmafVITNhlADLMPGTTE-------QDASLVVAPLSHG-AGIHQLCQVARGAATVLLPSE-RF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 351 LMDDLKTL----QPTVFPVVPRLLNRMFDkifgqaDSSLKRWllDFASKRKeaelrsgivrnnsfwdkVIFrkiqaslgg 426
Cdd:PRK07470 242 DPAEVWALverhRVTNLFTVPTILKMLVE------HPAVDRY--DHSSLRY-----------------VIY--------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 427 rvklmvtGAAPVSASVLTFLRTALGCQFYEGYGQTECTaGCSLSLP------GDWTAGHVGapmPCNIIKL---VDVQ-- 495
Cdd:PRK07470 288 -------AGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNITVLPpalhdaEDGPDARIG---TCGFERTgmeVQIQdd 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 EMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK07470 357 EGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE 434
|
490 500 510
....*....|....*....|....*....|
gi 2032642720 576 VYLRCEAVAQVFVHGeslqaflvgvvVPDP 605
Cdd:PRK07470 435 KLLTHPAVSEVAVLG-----------VPDP 453
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
420-608 |
2.59e-15 |
|
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: 78.76 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 420 IQASLGG-RVKLM-VTGAA-PVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSlPGD-WTAGHVGAPMPCNIIKLVDVQ 495
Cdd:cd05974 191 IQQDLASfDVKLReVVGAGePLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 EmnylAAKGEGEVCI-----KGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 570
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170 180 190
....*....|....*....|....*....|....*...
gi 2032642720 571 EKIENVYLRCEAVAQvfvhgeslqaflvGVVVPDPDTL 608
Cdd:cd05974 344 FELESVLIEHPAVAE-------------AAVVPSPDPV 368
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
269-598 |
2.75e-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: 78.91 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 269 DLAVICFTSGTTGNPKGAMITHQNIVSNASAfmkTTEKSFVpSSDDVLISFLPLAHMFerIVECV----VLCHGARIGFF 344
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRA---SAEVCGL-DQDTVYLAVLPAAHNF--PLACPgvlgTLLAGGRVVLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 Q-GDIRLLMDDLKTLQPTVFPVVPRLLnrmfdkifgqadsslKRWLlDFASKRKeAELRSgivrnnsfwdkvifrkiqas 423
Cdd:cd05920 214 PdPSPDAAFPLIEREGVTVTALVPALV---------------SLWL-DAAASRR-ADLSS-------------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 424 lggrVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTE----CTAgcsLSLPGDWTAGHVGAPM-PCNIIKLVDvQEMN 498
Cdd:cd05920 257 ----LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD-EEGN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 499 YLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYL 578
Cdd:cd05920 329 PVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLL 407
|
330 340
....*....|....*....|....*..
gi 2032642720 579 RCEAVAQVFV-------HGESLQAFLV 598
Cdd:cd05920 408 RHPAVHDAAVvampdelLGERSCAFVV 434
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
266-598 |
3.70e-15 |
|
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: 78.66 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 266 KPEDLAVICFTSGTTGNPKGAMITH----QNIVSNASAFMKTTEKSFVPSSDDVLISFLPLAHMFERIVE--CVVLCHGA 339
Cdd:cd05928 172 GSQEPMAIYFTSGTTGSPKMAEHSHsslgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQgaCVFVHHLP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 340 RIgffqgDIRLLMDDLKTLQPTVFPVVPrllnrmfdkifgqadsSLKRWLL--DFASKRkeaelrsgivrnnsfwdkviF 417
Cdd:cd05928 252 RF-----DPLVILKTLSSYPITTFCGAP----------------TVYRMLVqqDLSSYK--------------------F 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 RKIQASLggrvklmvTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDVqEM 497
Cdd:cd05928 291 PSLQHCV--------TGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD-NG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 498 NYLAAKGEGEVCI-----KGVNVFRGYLKDPEKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEK 572
Cdd:cd05928 362 NVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFE 439
|
330 340 350
....*....|....*....|....*....|...
gi 2032642720 573 IENVYLRCEAVAQVFV-------HGESLQAFLV 598
Cdd:cd05928 440 VESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
428-628 |
1.03e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.58 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 428 VKLMVTGAAPvSASVLtFLRTALGCQFYEGYGQTEcTAGCSL---------SLPGDwTAGHVGAPMPCNIIKL-----VD 493
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGPSTvcawkpewdSLPPE-EQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 494 VQEMNYLAAKGE--GEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 571
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032642720 572 KIENVYLRCEAVAQVFV-------HGESLQAFlvgvVVPDPDTlhNWAKKKGFEGSYQELCRNK 628
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAF----VTLKPGV--DKSDEAALAEDIMKFCRER 524
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
435-605 |
1.53e-14 |
|
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: 75.42 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 435 AAPVSASVLTFLRTALGCQFYeGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDV--QEMnylaAKGE-GEVCIK 511
Cdd:cd17636 121 AAPEWNDMATVDTSPWGRKPG-GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEdgREV----PDGEvGEIVAR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 512 GVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAVAQVFVHGe 591
Cdd:cd17636 196 GPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAVIG- 272
|
170
....*....|....
gi 2032642720 592 slqaflvgvvVPDP 605
Cdd:cd17636 273 ----------VPDP 276
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
119-590 |
1.89e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 76.75 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALlHRGFKPSHVQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLV 198
Cdd:PRK05620 37 EQTTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDKPDKARvlLASVEKgETPILNTIVIMDSFGVDLVERGKKCGVEVFSMrEIEELGRAhRQKPMPPKPEDLAV-ICFTS 277
Cdd:PRK05620 116 VADPRLAEQ--LGEILK-ECPCVRAVVFIGPSDADSAAAHMPEGIKVYSY-EALLDGRS-TVYDWPELDETTAAaICYST 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 278 GTTGNPKGAMITHQNIVSNaSAFMKTTEkSFVPSSDDVLISFLPLAHmferivecvVLCHGARIGFFQGDIRLLMDDLKT 357
Cdd:PRK05620 191 GTTGAPKGVVYSHRSLYLQ-SLSLRTTD-SLAVTHGESFLCCVPIYH---------VLSWGVPLAAFMSGTPLVFPGPDL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 358 LQPTVFPVVPRLLNRmfdkifgQADSSLKRWLldfaskrkeaELRSGIVRNNSfwDKVIFRKIQAslggrvklmvtGAAP 437
Cdd:PRK05620 260 SAPTLAKIIATAMPR-------VAHGVPTLWI----------QLMVHYLKNPP--ERMSLQEIYV-----------GGSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 438 VSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAP-------MPCNI-IKLVDVQEMNYLAAKGEGEVC 509
Cdd:PRK05620 310 VPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWAyrvsqgrFPASLeYRIVNDGQVMESTDRNEGEIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 510 IKGVNVFRGYLKDP----------------EKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 573
Cdd:PRK05620 390 VRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQL 468
|
490
....*....|....*..
gi 2032642720 574 ENVYLRCEAVAQVFVHG 590
Cdd:PRK05620 469 ENYIMAAPEVVECAVIG 485
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
265-604 |
3.96e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 76.74 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 265 PKPEDLAVICFTSGTTGNPKGAMITHQNIVsnasAFMKTTEKSFVPSSDDVLISFLPLAhmFERIVECVV--LCHGARIG 342
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 343 FFQGDIRL----LMDDLKTLQPTVFPVVPRLLNRmfdkiFGQADSSLKRWLldfaskrkeaELRsgivrnnsfwdKVIFr 418
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ-----LLQMDEQVEHPL----------SLR-----------RVVC- 1841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 419 kiqaslGGRvklmvtgAAPVSASVLTFLRtaLG-CQFYEGYGQTECTAG-----CSLSLPGDWTAGHVGAPMPcNIIKLV 492
Cdd:PRK12467 1842 ------GGE-------ALEVEALRPWLER--LPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIA-NLSTYI 1905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 493 DVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQG 565
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RG 1984
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2032642720 566 EYIAPEKIENVYLRCEAVAQ--VFVHGESLQAFLVGVVVPD 604
Cdd:PRK12467 1985 FRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPT 2025
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
101-608 |
7.92e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 74.68 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 101 QVSNNGPCLGFRkpNQPYEWisyKEVSDRAECVGSAL--LHRGFKPSHVqyiGIFSQNRPEWVIIEQACYAFSMVVVPLY 178
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTW---REVLAEAAARAAALiaLADPDRPLHV---GVLLGNTPEMLFWLAAAALGGYVLVGLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 179 DTLGAEAITYIVNKADLSLVFCDkpDKARVLLASVEKGETPILntivimdsfgvdlvergkkcgvEVFSMREIEELGRAH 258
Cdd:PRK13388 84 TTRRGAALAADIRRADCQLLVTD--AEHRPLLDGLDLPGVRVL----------------------DVDTPAYAELVAAAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 259 RQKPM-PPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAfmkTTEKsFVPSSDDVLISFLPLAHMfERIVE--CVVL 335
Cdd:PRK13388 140 ALTPHrEVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRA---LTER-FGLTRDDVCYVSMPLFHS-NAVMAgwAPAV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 336 CHGARI---------GFfqgdirllMDDLKTLQPTVFPVVPRLL-------NRMFDkifgqADSSLKRWLLDFASKRKEA 399
Cdd:PRK13388 215 ASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPRDIA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 400 ElrsgivrnnsfwdkvifrkiqaslggrvklmvtgaapvsasvltFLRTaLGCQFYEGYGQTEctAGCSLSLPGDWTAGH 479
Cdd:PRK13388 282 E--------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPPGS 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 480 VGAPMPCNIIKLVD-VQE------------MNYLAAKGEgEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLP 546
Cdd:PRK13388 315 IGRGAPGVAIYNPEtLTEcavarfdahgalLNADEAIGE-LVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDA 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032642720 547 NGTLKIIDRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFVHG----ESLQAFLVGVVVPDPDTL 608
Cdd:PRK13388 393 DGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATF 457
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-614 |
8.41e-14 |
|
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: 74.43 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 268 EDLAVICFTSGTTGNPKGAMITHQNIVsNASAFmkTTEKSFVPSSDDVL----ISFlplAHMFERIVEcvVLCHGARIGF 343
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV-NLLHF--EREKTNINFSDKVLqfatCSF---DVCYQEIFS--TLLSGGTLYI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 344 FQGDIRLLMDDLKTL------QPTVFPVVprllnrmfdkiFGQADSSLKRWLLDFASKRKEAeLRSG--IVRNNSFWDkv 415
Cdd:cd17656 200 IREETKRDVEQLFDLvkrhniEVVFLPVA-----------FLKFIFSEREFINRFPTCVKHI-ITAGeqLVITNEFKE-- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 416 IFRKIQASLGGRVklmvtgaAPVSASVLTFLRTALGCQFYEgygqtectagcslsLPGdwtaghVGAPMPCNIIKLVDVQ 495
Cdd:cd17656 266 MLHEHNVHLHNHY-------GPSETHVVTTYTINPEAEIPE--------------LPP------IGKPISNTWIYILDQE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 EMnyLAAKGE-GEVCIKGVNVFRGYLKDPEKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17656 319 QQ--LQPQGIvGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRI 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2032642720 569 APEKIENVYLRCEAVAQ--VFVHGES-----LQAFLVGVV-VPDPDTLHNWAKK 614
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEavVLDKADDkgekyLCAYFVMEQeLNISQLREYLAKQ 449
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-605 |
1.28e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 73.77 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKP-SHVqyiGIFSQNRPEWVIIEQACYAFSMVVVPL-YDTLGAEaITYIVNKADLSLV 198
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPgDHV---GIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 FCDKPDKARVllASVeKGETPILNTIVIMDSFGVDLVERGkkcGVEVFSMREIEELGRAhrqkPMPPKPEDLAVICfTSG 278
Cdd:PRK07798 105 VYEREFAPRV--AEV-LPRLPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-TGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNI--VSNASAFMKTTEksfvPSSDDVLISFLPLAHMFERIVECVVLCHGAR-----IGFFQGdirll 351
Cdd:PRK07798 174 TTGMPKGVMWRQEDIfrVLLGGRDFATGE----PIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSG----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 352 mddlktlQPTVFPVVPRL-------------LNRMFdkIFGQAdssLKRWLLDFASKRKEAELRSgivrnnsfwdkvifr 418
Cdd:PRK07798 245 -------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDLSS--------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 419 kiqaslggrVKLMVTGAAPVSASVLTFLRTAL-GCQFYEGYGQTECTAGCSLSLPGDwtAGHVGAP--MPCNIIKLVDvq 495
Cdd:PRK07798 298 ---------LFAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPrfTIGPRTVVLD-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 EMNYLAAKGEGEVCI--KGVNVFRGYLKDPEKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAP 570
Cdd:PRK07798 365 EDGNPVEPGSGEIGWiaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFP 443
|
490 500 510
....*....|....*....|....*....|....*
gi 2032642720 571 EKIENVYLRCEAVAQVFVhgeslqaflVGvvVPDP 605
Cdd:PRK07798 444 EEVEEALKAHPDVADALV---------VG--VPDE 467
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
119-606 |
2.63e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVnkadlslv 198
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDV--VALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIV-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 fCDKpdKARVLLASVEkgetpiLNTIVImdSFGVDLVER----GKKCGVEVFsmreieELGRAHRQKPMPPKPEDlAVIC 274
Cdd:PRK13390 93 -GDS--GARVLVASAA------LDGLAA--KVGADLPLRlsfgGEIDGFGSF------EAALAGAGPRLTEQPCG-AVML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 275 FTSGTTGNPKGAM--ITHQNIVSNASAFMKTTEKSFVPSSDDVLISFLPLAH--------MFERIVECVVLCHgarigff 344
Cdd:PRK13390 155 YSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHaaplrwcsMVHALGGTVVLAK------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 QGDIRLLMDDLKTLQPTVFPVVPRLLNRMFdkifgqadsslkrwlldfaskRKEAELRSgivrnnsfwdkvifRKIQASL 424
Cdd:PRK13390 228 RFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT--------------RYDVSSL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 GGrvklMVTGAAPVSASVLTFLRTALGCQFYEGYGQTEcTAGCSLSLPGDWTA--GHVGAPMpCNIIKLVDvQEMNYLAA 502
Cdd:PRK13390 273 RA----VIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSV-LGDLHICD-DDGNELPA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 503 KGEGEVCIKGVNVFRGYLKDPEKTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRC 580
Cdd:PRK13390 346 GRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMH 424
|
490 500
....*....|....*....|....*.
gi 2032642720 581 EAVAQVFVHGeslqaflvgvvVPDPD 606
Cdd:PRK13390 425 PAVHDVAVIG-----------VPDPE 439
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
248-576 |
9.17e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 71.47 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 248 MREIEELGRAHRQKPMPP---KPEDLAVICFTSGTTGNPKGAMITHQnivsnasafmktteksfvpssddvlisflplah 324
Cdd:PRK09274 151 GTTLATLLRDGAAAPFPMadlAPDDMAAILFTSGSTGTPKGVVYTHG--------------------------------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 325 MFERIVECVvlchGARIGFFQGDIrllmdDLKTlqptvFPVV----PRLLNRMF--------------DKIFGQADsslk 386
Cdd:PRK09274 198 MFEAQIEAL----REDYGIEPGEI-----DLPT-----FPLFalfgPALGMTSVipdmdptrpatvdpAKLFAAIE---- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 387 rwlldfaskrkeaelRSGIvrNNSFWDKVIFRKI-QASLGGRVKL----MVTGA-APVSASVLTFLRTAL--GCQFYEGY 458
Cdd:PRK09274 260 ---------------RYGV--TNLFGSPALLERLgRYGEANGIKLpslrRVISAgAPVPIAVIERFRAMLppDAEILTPY 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 459 GQTECTAGCSLS----LPGDWT-----AGH-VGAPMPCNIIKLVDV--------QEMNYLAAKGEGEVCIKGVNVFRGYL 520
Cdd:PRK09274 323 GATEALPISSIEsreiLFATRAatdngAGIcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRSYY 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032642720 521 KDPEKTAEA--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEY--IAPEKIENV 576
Cdd:PRK09274 403 NRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCERIFNT 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
267-626 |
1.07e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.91 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVsnasAFMKTTEKSFVPSSDDVLISFLPLAhmFERIVECV--VLCHGARIgff 344
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV--- 4763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 qgdirLLMDDLKTLQPTVFpvvpRLLNRMFDKIFGQADSSLKRWLLDFASKRKEAELRsgivrnnsfwdkvifrkiqasl 424
Cdd:PRK12316 4764 -----VIRDDSLWDPERLY----AEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR---------------------- 4812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 ggrvKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSL--SLPGDW---TAGHVGAPMPCNIIKLVDVQeMNY 499
Cdd:PRK12316 4813 ----VYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLwkARDGDAcgaAYMPIGTPLGNRSGYVLDGQ-LNP 4887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 500 LAAKGEGEVCIKGVNVFRGYLKDPEKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:PRK12316 4888 LPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGE 4966
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032642720 573 IENVYLRCEAVAQVFVHGE--SLQAFLVGVVVP-DPDTLHNWAKKKGFEGSYQELCR 626
Cdd:PRK12316 4967 IEARLREHPAVREAVVIAQegAVGKQLVGYVVPqDPALADADEAQAELRDELKAALR 5023
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
121-606 |
1.61e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 70.32 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADlslvfc 200
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDV--VAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 dkpdkARVLLASVEKGETpiLNTIVIMDSFGVD--LVERGKKCGVevfsmREIEELGRAHRQKPMPPKPEDlAVICFTSG 278
Cdd:PRK08276 84 -----AKVLIVSAALADT--AAELAAELPAGVPllLVVAGPVPGF-----RSYEEALAAQPDTPIADETAG-ADMLYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAM--ITHQNIVSNASAFMKTTEKSFVPSSDDVLISFLPLAHmferivecvvlchGARIGFFQGDIRL-----L 351
Cdd:PRK08276 151 TTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYH-------------TAPLRFGMSALALggtvvV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 352 M---DDLKTLQP------TVFPVVPRLLNRMF---DKIFGQAD-SSLKRwlldfaskrkeaelrsgivrnnsfwdkvifr 418
Cdd:PRK08276 218 MekfDAEEALALieryrvTHSQLVPTMFVRMLklpEEVRARYDvSSLRV------------------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 419 kiqaslggrvklMVTGAAP----VSASVLTFLrtalGCQFYEGYGQTEcTAGCSLSLPGDWTA--GHVGAPMPCnIIKLV 492
Cdd:PRK08276 267 ------------AIHAAAPcpveVKRAMIDWW----GPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLG-EVRIL 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 493 DvQEMNYLAAKGEGEVCIK-GVNVFRgYLKDPEKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAP 570
Cdd:PRK08276 329 D-EDGNELPPGEIGTVYFEmDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYP 404
|
490 500 510
....*....|....*....|....*....|....*.
gi 2032642720 571 EKIENVYLRCEAVAQVFVHGeslqaflvgvvVPDPD 606
Cdd:PRK08276 405 QEIENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
107-605 |
1.62e-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: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 107 PCLgfRKPNQpyEWiSYKEVSDRAECVGSALLHR-GFKPSHvqYIGIFSQNRPEWViieqACYAFSM----VVVPLYDTL 181
Cdd:cd05958 2 TCL--RSPER--EW-TYRDLLALANRIANVLVGElGIVPGN--RVLLRGSNSPELV----ACWFGIQkagaIAVATMPLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 182 GAEAITYIVNKADLSLVFCDKPDKARvllasvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqk 261
Cdd:cd05958 71 RPKELAYILDKARITVALCAHALTAS------------------------------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 262 pmppkpEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKsfvPSSDDVLISFLPLAHMFERIVECVVLCH-GAR 340
Cdd:cd05958 97 ------DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLR---LREDDRFVGSPPLAFTFGLGGVLLFPFGvGAS 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 341 IGFFQGDI-RLLMDDLKTLQPTVFPVVPRllnrMFDKIFGQADSSlkrwlldfaskrkeaelrsgivrnnsfwdkvifrk 419
Cdd:cd05958 168 GVLLEEATpDLLLSAIARYKPTVLFTAPT----AYRAMLAHPDAA----------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 420 iqASLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVDvQEMNY 499
Cdd:cd05958 209 --GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 500 LAAKGEGEVCIKGVNVFRGylkDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLR 579
Cdd:cd05958 286 VPDGTIGRLAVRGPTGCRY---LADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQ 361
|
490 500
....*....|....*....|....*....
gi 2032642720 580 CEAVAQVFVHGESLQAFLVGV---VVPDP 605
Cdd:cd05958 362 HPAVAECAVVGHPDESRGVVVkafVVLRP 390
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-599 |
2.41e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.97 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 268 EDLAVICFTSGTTGNPKGAMITHQNIVSNAsAFMKTTeksFVPSSDDVLISFLPLAhmFERIV-ECVV-LCHGARIGFF- 344
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERL-QWMQAT---YALDDSDVLMQKAPIS--FDVSVwECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 ---QGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQADSSLKRwlLDFASKRKEAELRsgivrnnsfwDKVIFRKIQ 421
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELR----------NRVLQRLPQ 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 422 ASLGGRvklmvtgaapvsasvltflrtalgcqfyegYGQTEcTA------GCSLSlpgDWTAGHVGAPMPCNIIKLVDvQ 495
Cdd:PRK05691 1415 VQLHNR------------------------------YGPTE-TAinvthwQCQAE---DGERSPIGRPLGNVLCRVLD-A 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 EMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:PRK05691 1460 ELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRV 1538
|
330 340 350
....*....|....*....|....*....|...
gi 2032642720 569 APEKIENVYLRCEAVAQ--VFVHGESLQAFLVG 599
Cdd:PRK05691 1539 EPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-598 |
2.65e-12 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 69.63 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 429 KLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTE----------------CTAGCSLSlPGD--WTAGHVGAPMPCNIIk 490
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnytrlddsderifTTQGRPMS-PDDevWVADADGNPLPQGEV- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 491 lvdvqemnylaakgeGEVCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GE 566
Cdd:PRK10946 381 ---------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGE 440
|
170 180 190
....*....|....*....|....*....|....*....
gi 2032642720 567 YIAPEKIENVYLRCEAVAQVF-------VHGESLQAFLV 598
Cdd:PRK10946 441 KIAAEEIENLLLRHPAVIHAAlvsmedeLMGEKSCAFLV 479
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
455-606 |
4.13e-12 |
|
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: 68.94 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 455 YEGYGQTECTAGCSLSlPGDWTA--GHVGAPMPcNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRgYLKDPEKTAEALDK 532
Cdd:cd05929 273 WEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNE 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032642720 533 DGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFVHGeslqaflvgvvVPDPD 606
Cdd:cd05929 349 GGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVG-----------VPDEE 410
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-585 |
8.69e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.04 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 260 QKPMPPkPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPssDDVLISFLPLAHmferivecvvlchga 339
Cdd:PRK05691 159 QEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNP--DDVIVSWLPLYH--------------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 340 RIGFFQGdirllmddlkTLQPtVFPVVPRLLnrMFDKIFGQADsslKRWLldfaskrkEA--ELRSGIVRNNSFWDKVIF 417
Cdd:PRK05691 221 DMGLIGG----------LLQP-IFSGVPCVL--MSPAYFLERP---LRWL--------EAisEYGGTISGGPDFAYRLCS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 RKI-QASLGG----RVKLMVTGAAPVSASVL-TFLRTALGC-----QFYEGYGQTECT---AGC-------SLSLPGDWT 476
Cdd:PRK05691 277 ERVsESALERldlsRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgipALELDAEAL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 477 AGHVGAP------MPCNI------IKLVDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEA-LDKDG--WLHTGDI 541
Cdd:PRK05691 357 ARNRAEPgtgsvlMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDL 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2032642720 542 GkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQ 585
Cdd:PRK05691 437 G-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-603 |
1.04e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 67.49 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 265 PKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFmkttEKSFVPSSDDVLISFLPLAHMFerivecvvlchGARIGff 344
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL----RQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 qgdirllmddLKTLQPTVFPVVPrllnrmfdkifGQADSslkRWLLDFASKRKEaelrSGIVRNNSFWDKVifrkiqASL 424
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARADP---QKLVGAIRQYGV----SIVFGSPALLERV------ARY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 GGR-------VKLMVTGAAPVSASVLTFLRTAL--GCQFYEGYGQTECTAGCS------LSLPGDWTAGH----VGAPMP 485
Cdd:cd05910 191 CAQhgitlpsLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 486 CNIIKLVDV--------QEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDG----WLHTGDIGKWLPNGTLKII 553
Cdd:cd05910 271 GVRVRIIEIddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFC 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2032642720 554 DRKKHIFKLAQGEYIApekienvyLRCEAVAQvfVHGESLQAFLVGVVVP 603
Cdd:cd05910 351 GRKAHRVITTGGTLYT--------EPVERVFN--THPGVRRSALVGVGKP 390
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
70-604 |
1.05e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.83 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 70 ARRSSLLNSDELLSYYYDDVRTVYDIFQRGLQVSNNGPCLGFRKpnqpyEWISYKEVSDRAECVGSALLHRGFKPSHVqy 149
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERGVGPDVL-- 3109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 150 IGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNkadlslvfcdkpDKARVLLASVEKGETPILNtivimds 229
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLE------------DSGAQLLLSQSHLRLPLAQ------- 3170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 230 fgvdlvergkkcGVEVFsMREIEELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIvsnaSAFMKTTEKSFV 309
Cdd:PRK12316 3171 ------------GVQVL-DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL----SNHLCWMQQAYG 3233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 310 PSSDDVLISFLPLAHMFERIVECVVLCHGARIGF----FQGDIRLLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQADSSL 385
Cdd:PRK12316 3234 LGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLagpeDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSL 3313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 386 KRWLLdfaskrkeaelrsgivrnnsfwdkvifrkiqaslGGRvklmvtgAAPVSASVLTFLRTALgcqfYEGYGQTECTA 465
Cdd:PRK12316 3314 KRIVC----------------------------------GGE-------ALPADLQQQVFAGLPL----YNLYGPTEATI 3348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 466 GCSLSLPGDWTAGH--VGAPMPCNIIKLVDVQeMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGW------LH 537
Cdd:PRK12316 3349 TVTHWQCVEEGKDAvpIGRPIANRACYILDGS-LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYR 3427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032642720 538 TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFVHGESLQAfLVGVVVPD 604
Cdd:PRK12316 3428 TGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPE 3492
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
119-606 |
2.17e-11 |
|
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: 66.61 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 119 EWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADlslv 198
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDV--VALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSS---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 199 fcdkpdkARVLLAsvekgetpilntivimdsfgvdlvergkkcgvevfsmreieelgrahrqkpmppkpeDLAVICFTSG 278
Cdd:cd05940 76 -------AKHLVV---------------------------------------------------------DAALYIYTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 279 TTGNPKGAMITHQNIVSNASAFMktteKSFVPSSDDVLISFLPLAHMFERIVE-CVVLCHGARIGF---FQGdiRLLMDD 354
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFA----GSGGALPSDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkFSA--SNFWDD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 355 LKTLQPTVFPVVPRLLnrmfdkifgqadsslkRWLLdfASKRKEAE------------LRSGIvrnnsfWDKVIFR-KIq 421
Cdd:cd05940 166 IRKYQATIFQYIGELC----------------RYLL--NQPPKPTErkhkvrmifgngLRPDI------WEEFKERfGV- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 422 aslgGRVklmvtgaapvsasvltflrtalgcqfYEGYGQTECTAGcSLSLPG-DWTAGHVGA----PMPCNIIKlVDVQE 496
Cdd:cd05940 221 ----PRI--------------------------AEFYAATEGNSG-FINFFGkPGAIGRNPSllrkVAPLALVK-YDLES 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 497 MNYL---------AAKGE-GE-VC-IKGVNVFRGYLkDPEKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:cd05940 269 GEPIrdaegrcikVPRGEpGLlISrINPLEPFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2032642720 559 IFKLaQGEYIAPEKIENVYLRCEAVAQVFVHgeslqaflvGVVVPDPD 606
Cdd:cd05940 348 TFRW-KGENVSTTEVAAVLGAFPGVEEANVY---------GVQVPGTD 385
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
239-605 |
2.45e-11 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 66.34 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 239 KKCGV-----EVFSMREIEELGRAHRQKPMPpKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTteksFVPSSD 313
Cdd:cd17654 85 KKCHVsyllqNKELDNAPLSFTPEHRHFNIR-TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSL----FNITSE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 314 DVLIsFLPLAHMFERIVECVV-LCHGArigffqgdirllmddlkTL--QPTVFPVVPRLLNRMFDKIFG----QADSSLK 386
Cdd:cd17654 160 DILF-LTSPLTFDPSVVEIFLsLSSGA-----------------TLliVPTSVKVLPSKLADILFKRHRitvlQATPTLF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 387 RwllDFASKRKEAELRSGIvrnnsfwdkvifrkiqASLggRVkLMVTGAAPVSASVLTFLR-TALGCQFYEGYGQTECTA 465
Cdd:cd17654 222 R---RFGSQSIKSTVLSAT----------------SSL--RV-LALGGEPFPSLVILSSWRgKGNRTRIFNIYGITEVSC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 466 GCSLSLPGDWTAG-HVGAPMPCNIIKLVDVQemnylAAKGEGEVCIKGVNVfRGYLKDPEKTAEALdkdgWLHTGDIGKw 544
Cdd:cd17654 280 WALAYKVPEEDSPvQLGSPLLGTVIEVRDQN-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT- 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032642720 545 LPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRC---EAVAQVFVHGESLQAFLVGVVVPDP 605
Cdd:cd17654 349 VKDGELFFLGRKDSQIKRR-GKRINLDLIQQVIESClgvESCAVTLSDQQRLIAFIVGESSSSR 411
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
123-574 |
2.61e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 66.57 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 123 YKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQAC-YAfSMVVVPLY--DTLGAEAItYIvnkadlslvf 199
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPG--DRVALIAETDGDFVEAFFACqYA-GLVPVPLPlpMGFGGRES-YI---------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 200 cdkpDKARVLLASVEKgetpilnTIVIMDSFGVDLVER--GKKCGVEVFSMREIEELGRAHRQKPmPPKPEDLAVICFTS 277
Cdd:PRK09192 118 ----AQLRGMLASAQP-------AAIITPDELLPWVNEatHGNPLLHVLSHAWFKALPEADVALP-RPTPDDIAYLQYSS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 278 GTTGNPKGAMITHQNIVSNASAFMKTTEKsFVPSsdDVLISFLPLAH-MferivecvvlchgARIGFFQGDI--RLLMDD 354
Cdd:PRK09192 186 GSTRFPRGVIITHRALMANLRAISHDGLK-VRPG--DRCVSWLPFYHdM-------------GLVGFLLTPVatQLSVDY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 355 LKTLQPTVFPVVprllnrmfdkifgqadsslkrWLlDFASKRkeaelRSGIVRNNSFWDKVIFRKIQ-ASLGG----RVK 429
Cdd:PRK09192 250 LPTRDFARRPLQ---------------------WL-DLISRN-----RGTISYSPPFGYELCARRVNsKDLAEldlsCWR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 430 LMVTGAAPVSASVLT----------FLRTAlgcqFYEGYGQTECTAGCSLSLPG--------DWTA----GHV------- 480
Cdd:PRK09192 303 VAGIGADMIRPDVLHqfaeafapagFDDKA----FMPSYGLAEATLAVSFSPLGsgivveevDRDRleyqGKAvapgaet 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 481 ---------GAPMPCNIIKLVDVQEmNYLAAKGEGEVCIKGVNVFRGYLKDPEkTAEALDKDGWLHTGDIGkWLPNGTLK 551
Cdd:PRK09192 379 rrvrtfvncGKALPGHEIEIRNEAG-MPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLY 455
|
490 500
....*....|....*....|...
gi 2032642720 552 IIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09192 456 ITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-606 |
9.91e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 64.71 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 112 RKPNQPY-------EWISYKEVSDRAECVGSALLHRGFKP-SHVqyiGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGA 183
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLKRgDHV---AIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 184 EAITYIVNKADlslvfcdkpdkARVLLASVEKGE--------TPILNTIVIMDsfGVDLVERgkkcgvevfsmreIEELG 255
Cdd:PRK13391 86 AEAAYIVDDSG-----------ARALITSAAKLDvarallkqCPGVRHRLVLD--GDGELEG-------------FVGYA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 256 RAHRQKPMPPKPEDL--AVICFTSGTTGNPKG--AMITHQNIVSNASAFMkTTEKSFVPSSDDVLISFLPLAHMFERIVE 331
Cdd:PRK13391 140 EAVAGLPATPIADESlgTDMLYSSGTTGRPKGikRPLPEQPPDTPLPLTA-FLQRLWGFRSDMVYLSPAPLYHSAPQRAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 332 CVVLCHGARIgffqgdirLLMDD------LKTLQP---TVFPVVPRLLNRMfdkifgqadssLKrwLLDfaSKRKEAELR 402
Cdd:PRK13391 219 MLVIRLGGTV--------IVMEHfdaeqyLALIEEygvTHTQLVPTMFSRM-----------LK--LPE--EVRDKYDLS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 403 SgivrnnsfwdkvifrkiqaslggrVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTEcTAGCSLSLPGDWTA--GHV 480
Cdd:PRK13391 276 S------------------------LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 481 GAPMpCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRgYLKDPEKTAEALDKDG-WLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK13391 331 GRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFM 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2032642720 560 FkLAQGEYIAPEKIENVYLRCEAVAQVFVHGeslqaflvgvvVPDPD 606
Cdd:PRK13391 408 I-ISGGVNIYPQEAENLLITHPKVADAAVFG-----------VPNED 442
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
273-660 |
1.34e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 64.34 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 273 ICFTSGTTGNPKGAMITHQNIVSNASAfmkttekSFVP-----SSDDVLISFLPLAHMFERIVECVVLCHGARIGFFQGD 347
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHRSTVLHAYG-------AALPdamglSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 348 IrllmdDLKTLQ--------------PTVFPVvprLLNRMfdKIFGQADSSLKRwlldfaskrkeaelrsgivrnnsfwd 413
Cdd:PRK07008 254 L-----DGKSLYelieaervtfsagvPTVWLG---LLNHM--REAGLRFSTLRR-------------------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 414 kvifrkiqaslggrvklMVTGAAPVSASVLTFLRTALGCQFYEGYGQTE-------CT-AGCSLSLPGD------WTAGH 479
Cdd:PRK07008 298 -----------------TVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEmsplgtlCKlKWKHSQLPLDeqrkllEKQGR 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 480 V--GAPMpcniiKLVDV--QEMNYlAAKGEGEVCIKGVNVFRGYLKdpeKTAEALDkDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PRK07008 361 ViyGVDM-----KIVGDdgRELPW-DGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 556 KKHIFKlAQGEYIAPEKIENVylrceAVAQVFVHgeslQAFLVGVVVP--DPDTLHNWAKKKGFEGSYQELCR---NKDV 630
Cdd:PRK07008 431 SKDVIK-SGGEWISSIDIENV-----AVAHPAVA----EAACIACAHPkwDERPLLVVVKRPGAEVTREELLAfyeGKVA 500
|
410 420 430
....*....|....*....|....*....|....*...
gi 2032642720 631 KKYILEDMVRI--------GKESGLKSFEQVKDIVLHT 660
Cdd:PRK07008 501 KWWIPDDVVFVdaiphtatGKLQKLKLREQFRDYVLPT 538
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
242-639 |
1.49e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 64.15 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 242 GVEVFSMREIEELGRAHR--QKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNA----SAFMKTTEKSFV---PSS 312
Cdd:PRK04813 115 GIPVITLDELKDIFATGNpyDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTnwmlEDFALPEGPQFLnqaPYS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 313 DDvlisflpLAHMFerIVECvvLCHGARIGFFQGDI----RLLMDDLKTLQPTVFPVVPR-----LLNRMFDkifGQADS 383
Cdd:PRK04813 195 FD-------LSVMD--LYPT--LASGGTLVALPKDMtanfKQLFETLPQLPINVWVSTPSfadmcLLDPSFN---EEHLP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 384 SLKRWLLDF-ASKRKEAE-LRSgivrnnSFWDKVIfrkiqaslggrvklmvtgaapvsasvltflrtalgcqfYEGYGQT 461
Cdd:PRK04813 261 NLTHFLFCGeELPHKTAKkLLE------RFPSATI--------------------------------------YNTYGPT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 462 ECT-AGCSL-----------SLPgdwtaghVGAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEA 529
Cdd:PRK04813 297 EATvAVTSIeitdemldqykRLP-------IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 530 L-DKDGW--LHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENvYLR-----CEAVAQVFVHGESLQAfLVGVV 601
Cdd:PRK04813 369 FfTFDGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GYRIELEEIEQ-NLRqssyvESAVVVPYNKDHKVQY-LIAYV 444
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2032642720 602 VPdpdtlhnwaKKKGFEGSYQeLCRN--KDVKKYILEDMV 639
Cdd:PRK04813 445 VP---------KEEDFEREFE-LTKAikKELKERLMEYMI 474
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
267-604 |
1.51e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.18 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSfvpsSDDVLISFLPLAhmFERIVECV--VLCHGARIGFF 344
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELD----ANDRVLLFMSFS--FDGAQERFlwTLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 345 QGDIRllmDDLKTLQptvfpvvprLLNRMFDKIfgqadsslkrwlLDFASKRKEAELRSGIVRNnsfwdkvifrkiqasl 424
Cdd:PRK12467 3310 DNDLW---DPEELWQ---------AIHAHRISI------------ACFPPAYLQQFAEDAGGAD---------------- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 GGRVKLMVTGAAPVSASVLTFLRTALG-CQFYEGYGQTECTAGCSL-SLPGDWTAGHVGAPMPCNIIKL---VDVQEMNY 499
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLDGQLNP 3429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 500 LAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:PRK12467 3430 VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGE 3508
|
330 340 350
....*....|....*....|....*....|....
gi 2032642720 573 IENVYLRCEAVAQVFVHGESLQA--FLVGVVVPD 604
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARDGAGgkQLVAYVVPA 3542
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
432-605 |
2.37e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.56 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 432 VTGAAPVSASVLTFLRTALGCQFYEGYGQTE------CTAGCSLSLPGDwtaghVGAPMPCNIIKLVDvQEMNYLAAKGE 505
Cdd:PRK12406 277 IHAAAPCPADVKRAMIEWWGPVIYEYYGSTEsgavtfATSEDALSHPGT-----VGKAAPGAELRFVD-EDGRPLPQGEI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 506 GEVC--IKGVNVFRgYLKDPEKTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAV 583
Cdd:PRK12406 351 GEIYsrIAGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGV 427
|
170 180
....*....|....*....|....*
gi 2032642720 584 AQVFVHG---ESLQAFLVGVVVPDP 605
Cdd:PRK12406 428 HDCAVFGipdAEFGEALMAVVEPQP 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-604 |
2.50e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 86 YDDVRTVYDIFQRGLQVSNNGPCLGFRKpnqpyEWISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQ 165
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIERGVGPDVL--VGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 166 ACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFCDKPDKARVLLASvekgetpilntivimdsfgvdlvergkkcGVEV 245
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAA-----------------------------GVQV 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 246 FSMREIEELGRAHRQKPmpPK----PEDLAVICFTSGTTGNPKGAMITHQNIVS-------------NASAFMKTteksf 308
Cdd:PRK12316 631 LDLDRPAAWLEGYSEEN--PGtelnPENLAYVIYTSGSTGKPKGAGNRHRALSNrlcwmqqayglgvGDTVLQKT----- 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 309 vPSSDDVLIS--FLPLAhmferivecvvlcHGARIGFF-QGDIR---LLMDDLKTLQPTVFPVVPRLLNRMFDKIFGQAD 382
Cdd:PRK12316 704 -PFSFDVSVWefFWPLM-------------SGARLVVAaPGDHRdpaKLVELINREGVDTLHFVPSMLQAFLQDEDVASC 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 383 SSLKRWLLdfaskrkeaelrSGivrnnsfwdkvifrkiqASLGGRVKLMVTGAAPVsasvltflrtalgCQFYEGYGQTE 462
Cdd:PRK12316 770 TSLRRIVC------------SG-----------------EALPADAQEQVFAKLPQ-------------AGLYNLYGPTE 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 463 CTAGCSLSLPGDWTAGHV--GAPMPCNIIKLVDVQeMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEAL------DKDG 534
Cdd:PRK12316 808 AAIDVTHWTCVEEGGDSVpiGRPIANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGER 886
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 535 WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFVHGESLQAfLVGVVVPD 604
Cdd:PRK12316 887 MYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLE 954
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
250-583 |
2.65e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.25 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 250 EIEELGRAHRQKPMPPKP-EDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEksfVPSSDDVLISFLPLAH-Mfe 327
Cdd:PRK05851 133 DLATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG---LDAATDVGCSWLPLYHdM-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 328 rivecvvlchgarigffqGDIRLLMDDLKT----LQPTvfpvvprllnrmfdkifGQADSSLKRWLlDFASkrkeaELRS 403
Cdd:PRK05851 208 ------------------GLAFLLTAALAGaplwLAPT-----------------TAFSASPFRWL-SWLS-----DSRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 404 GIVRNNSFWDKVI---FRKIQASLGGRVKLMVTGAAPVSASVLTFLRTALG-CQFYEG-----YGQTECTAGCSLSLPG- 473
Cdd:PRK05851 247 TLTAAPNFAYNLIgkyARRVSDVDLGALRVALNGGEPVDCDGFERFATAMApFGFDAGaaapsYGLAESTCAVTVPVPGi 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 474 ----------DWTAGH----VGAPMPCNIIKLVDVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPektaeALDKDGWLHTG 539
Cdd:PRK05851 327 glrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTG 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2032642720 540 DIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYLRCEAV 583
Cdd:PRK05851 402 DLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERVAAQVRGV 443
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
273-592 |
2.96e-10 |
|
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: 62.04 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 273 ICFTSGTTGNPKGAMITHQNIVsnasAFMKTTEKSFVPSSDDVLISFLPLAHMFERIVECVVLCHG-ARIGFFQGDIRLL 351
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGgTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 352 MDDLKTLQPTVFPVVPRLLNrmfdkifgqadsSLKRWLldfaskRKEAELRSgIVRNNSFWDKVIFRKIQAslggrvklm 431
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQ------------ALARTL------EPESKIKS-IFSSGQKLFESTKKKLKN--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 432 vtgAAPVSasvltflrtalgcQFYEGYGQTEcTAGCSLSLPGD-WTAGHVGAPMPCNIIKLVDvqemnylAAKGE-GEVC 509
Cdd:cd17633 133 ---IFPKA-------------NLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRN-------ADGGEiGKIF 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 510 IKGVNVFRGYLKdpektAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAVAQVFVH 589
Cdd:cd17633 189 VKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVV 262
|
...
gi 2032642720 590 GES 592
Cdd:cd17633 263 GIP 265
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
264-606 |
3.04e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 63.91 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 264 PPKPEDLAVICFTSGTTGNPKGAMITHQNIVsNASAFMKT----TEKSFV----PSSDDVLI--SFLPLahmferIVecv 333
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV-NRLLWMQNhyplTADDVVlqktPCSFDVSVweFFWPF------IA--- 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 334 vlchGARIGFFQGD-------IRLLMDDLKTlqpTVFPVVPRllnrMFDKIFGQADSSLKRwlldfaskRKEAELRsgiv 406
Cdd:PRK10252 664 ----GAKLVMAEPEahrdplaMQQFFAEYGV---TTTHFVPS----MLAAFVASLTPEGAR--------QSCASLR---- 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 407 rnnsfwdkvifrkiqaslggRVklMVTGAApvsasvltfLRTALgCQFYEG---------YGQTEctAGCSLS-LP--GD 474
Cdd:PRK10252 721 --------------------QV--FCSGEA---------LPADL-CREWQQltgaplhnlYGPTE--AAVDVSwYPafGE 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 475 WTAGHVGAPMPCNI------IKLVDVQeMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGWL------HTGDIG 542
Cdd:PRK10252 767 ELAAVRGSSVPIGYpvwntgLRILDAR-MRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVA 845
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032642720 543 KWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFVH-----------GESLQafLVGVVVPDPD 606
Cdd:PRK10252 846 RWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTHacvinqaaatgGDARQ--LVGYLVSQSG 917
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
422-598 |
8.78e-10 |
|
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: 61.38 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 422 ASLGGRVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTEctagCSLSLPGDWTAGHV------GAPMPCNIIKLVDvQ 495
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE----LGMVLANHHALEHPvhagsaGRAMPGWRVAVLD-D 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 496 EMNYLAAKGEGEVCIKGVNV----FRGYLKDPEKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPE 571
Cdd:cd05973 276 DGDELGPGEPGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPF 350
|
170 180 190
....*....|....*....|....*....|....
gi 2032642720 572 KIENVYLRCEAVAQVFV-------HGESLQAFLV 598
Cdd:cd05973 351 DVESALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-603 |
7.78e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.41 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 267 PEDLAVICFTSGTTGNPKGAMITHQNIVSN------------ASAFMKTTEKSFvpssDDVLISFLPlAHMFerivecvv 334
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNqlskvpylalseADVIAQTASQSF----DISVWQFLA-APLF-------- 3934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 335 lchGARIGFFQGDI----RLLMDDLKTLQPTVFPVVPRLLNRMF--DKifgQADSSLkRWLL--------DFASKRKEAE 400
Cdd:PRK05691 3935 ---GARVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLptgeamppELARQWLQRY 4007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 401 LRSGIVrnNSFwdkvifrkiqaslggrvklmvtGAAPVSASVlTFLRTALgcqfyegygqtECTAGCSLSlpgdwtaghV 480
Cdd:PRK05691 4008 PQIGLV--NAY----------------------GPAECSDDV-AFFRVDL-----------ASTRGSYLP---------I 4042
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 481 GAPMPCNIIKLVDvQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTAEALDKDGW-------LHTGDIGKWLPNGTLKII 553
Cdd:PRK05691 4043 GSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYV 4121
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2032642720 554 DRKKHIFKLaQGEYIAPEKIENVYLRCEAV--AQVFVHGESLQAFLVGVVVP 603
Cdd:PRK05691 4122 GRIDHQVKI-RGYRIELGEIEARLHEQAEVreAAVAVQEGVNGKHLVGYLVP 4172
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
275-605 |
1.07e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 54.79 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 275 FTSGTTGNPKGAMITHQNIVSNasafMKTTEKSFVPSSDD-VLISFLPLAHMFerivecvvlCHGARIGFFQGDIRLLM- 352
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHS----FDCNVHDFHMKREDsVLIAGTLVHSLF---------LYGAISTLYVGQTVHLMr 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 353 --------DDLKTLQPTVFPVVPRLLnrmfdkifgqadsslkrwlldfaskrkEAELRSGIVRNNSfwdkvifrkiqasl 424
Cdd:PRK07638 217 kfipnqvlDKLETENISVMYTVPTML---------------------------ESLYKENRVIENK-------------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 425 ggrVKLMVTGAAPVSASVLTFLRTALGCQFYEGYGQTECTAGCSLSlPGDWTAGHVGAPMPCNIIKLVDVQEMNYLAAKG 504
Cdd:PRK07638 256 ---MKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVQKG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 505 E-GEVCIKGVNVFRGYLKDPEKTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVYLRCEAV 583
Cdd:PRK07638 332 EiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAV 409
|
330 340
....*....|....*....|..
gi 2032642720 584 AQVFVHGeslqaflvgvvVPDP 605
Cdd:PRK07638 410 DEIVVIG-----------VPDS 420
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
271-590 |
1.12e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 55.14 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 271 AVICFTSGTTGNPKGAMITHQnivSNA-SAFMKTTEKSFVPSSDDVLISFLPLAH------------MFERIVecvvlCH 337
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHR---SNVlHALMANNGDALGTSAADTMLPVVPLFHanswgiafsapsMGTKLV-----MP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 338 GARIgffqgDIRLLMDDLKTLQPTVFPVVPRLlnrmfdkifgqadsslkrWLLDFASKRKEaelrsgivrnnsfwdkvif 417
Cdd:PRK06018 252 GAKL-----DGASVYELLDTEKVTFTAGVPTV------------------WLMLLQYMEKE------------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 418 rkiQASLGGRVKLMVTGAAPVSASVLTFLRtaLGCQFYEGYGQTECTAGCSLS--------LPGDWTAGHV---GAPmPC 486
Cdd:PRK06018 290 ---GLKLPHLKMVVCGGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAalkppfskLPGDARLDVLqkqGYP-PF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 487 NI-IKLVDvQEMNYLAAKGE--GEVCIKGVNVFRGYLKdpeKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlA 563
Cdd:PRK06018 364 GVeMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-S 438
|
330 340
....*....|....*....|....*..
gi 2032642720 564 QGEYIAPEKIENVYLRCEAVAQVFVHG 590
Cdd:PRK06018 439 GGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
121-325 |
1.38e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 54.60 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALL-HRGFKPShvQYIGIFSQNRPEWViieqaCYAFSMVvvplydTLGAEAITYIVNKADLSLVF 199
Cdd:cd05938 6 YTYRDVDRRSNQAARALLaHAGLRPG--DTVALLLGNEPAFL-----WIWLGLA------KLGCPVAFLNTNIRSKSLLH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 200 CDKPDKARVLLASVEKGET--PILNTIvimdsfgvdlvergKKCGVEVFSMRE------IEELGRAHRQKPMPPKPEDL- 270
Cdd:cd05938 73 CFRCCGAKVLVVAPELQEAveEVLPAL--------------RADGVSVWYLSHtsntegVISLLDKVDAASDEPVPASLr 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032642720 271 --------AVICFTSGTTGNPKGAMITHQNIVSnASAFMktteKSFVPSSDDVLISFLPLAHM 325
Cdd:cd05938 139 ahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGFL----SLCGVTADDVIYITLPLYHS 196
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
121-290 |
1.49e-07 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 54.80 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPShvQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYIVNKADLSLVFC 200
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKG--DRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 -------DKP-------DKARVLLASVEKgetpilntIVIMDSFGVDLverGKKCGVEVFSMREIEELG-RAHRQKPMPP 265
Cdd:cd05968 170 adgftrrGREvnlkeeaDKACAQCPTVEK--------VVVVRHLGNDF---TPAKGRDLSYDEEKETAGdGAERTESEDP 238
|
170 180
....*....|....*....|....*
gi 2032642720 266 kpedlAVICFTSGTTGNPKGAMITH 290
Cdd:cd05968 239 -----LMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
121-586 |
2.27e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 53.86 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALlhRGFKPSHVQYIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAITYivnkadlslvFC 200
Cdd:PRK05857 42 LRYRELVAEVGGLAADL--RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIER----------FC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 201 DKPDKARVLLAsvEKGETPILNTIVIMDSFGVDLVERGKKCGVEVFSMrEIEELgrahRQKPMPPKPEDLAVIcFTSGTT 280
Cdd:PRK05857 110 QITDPAAALVA--PGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSL-DAASL----AGNADQGSEDPLAMI-FTSGTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 281 GNPKGAMITHQNIVSNASAFMKTTEKSFVPSSDDVLISFLPLAHM--FERIVECvvLCHGARIGFFQGDIRLLMDDLKTL 358
Cdd:PRK05857 182 GEPKAVLLANRTFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIggLWWILTC--LMHGGLCVTGGENTTSLLEILTTN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 359 QPTVFPVVPRLLNRMFdkifgqadsslkrwlldfaskrkeAELRSGIVRNNSfwdkvifrkiqaslggrVKLMVTGAAPV 438
Cdd:PRK05857 260 AVATTCLVPTLLSKLV------------------------SELKSANATVPS-----------------LRLVGYGGSRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 439 SASVLTFL-----RTAlgcQFYeGYGQTECTAGCslsLPGD------WTAGHVGAPMPCNIIKLVDVQEMNYLAAKGE-- 505
Cdd:PRK05857 299 IAADVRFIeatgvRTA---QVY-GLSETGCTALC---LPTDdgsivkIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGps 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 506 ---GEVCIKGVNVFRGYLKDPEKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENVylrCEA 582
Cdd:PRK05857 372 asfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI---AEG 446
|
....
gi 2032642720 583 VAQV 586
Cdd:PRK05857 447 VSGV 450
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
253-324 |
1.27e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.48 E-value: 1.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032642720 253 ELGRAHRQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSN----ASAFMKTTEKsfVPSSDDVLISFLPLAH 324
Cdd:PRK05850 145 DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANfeqlMSDYFGDTGG--VPPPDTTVVSWLPFYH 218
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
261-597 |
1.33e-06 |
|
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: 51.66 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 261 KPMPPKPE-DLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPSSddVLISFLPLAHmferiveCVVLCHGA 339
Cdd:cd05915 145 ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH-------VNAWCLPY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 340 RIGFFQGDI---------RLLMDDLKTLQPTVFPVVPRLLNrmfdkIFGQADSSLKR---W---LLDFASKRKEAELRsg 404
Cdd:cd05915 216 AATLVGAKQvlpgprldpASLVELFDGEGVTFTAGVPTVWL-----ALADYLESTGHrlkTlrrLVVGGSAAPRSLIA-- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 405 ivrnnsfwdkviFRKIqaslgGRVKLMVtgaapvsasvltflrtALGCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPM 484
Cdd:cd05915 289 ------------RFER-----MGVEVRQ----------------GYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 485 PCNIIKLVDVQEMNYLAAKGEGE----VCIKGVNVFRGYLKDPEKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:cd05915 336 LPIPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLI 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2032642720 561 KLAqGEYIAPEKIENVYLRCEAVAQVFV-------HGESLQAFL 597
Cdd:cd05915 416 KSG-GEWISSVDLENALMGHPKVKEAAVvaiphpkWQERPLAVV 458
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
1.60e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.41 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIieqACYAFSM--VVVPLYDT----------LG-AEAIT 187
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDV--VALLMENRPEYLA---AWLGLAKlgAVVALLNTqqrgavlahsLNlVDAKH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 188 YIVNKADLSLVFCDKPDKARVLLASVEKGETPIlntivimDSFGVDLVERgkkcgvevfSMREIEELGRAHRQKPMPpkp 267
Cdd:PRK08279 138 LIVGEELVEAFEEARADLARPPRLWVAGGDTLD-------DPEGYEDLAA---------AAAGAPTTNPASRSGVTA--- 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032642720 268 EDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEksfvPSSDDVLISFLPLAH 324
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
173-290 |
2.22e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 51.05 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 173 VVVPLYDTLGAEAITYIVNKADlslvfcdkpdkARV------LLASVEKGETPILNTIVIMDsfgvDLVERGKKCgvevf 246
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSE-----------AKVlittpaLLERKPADDLPSLKHVLLVG----EDVEEGPGT----- 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 247 sMREIEELGRAHRQKPMPP-KPEDLAVICFTSGTTGNPKG------AMITH 290
Cdd:PRK04319 184 -LDFNALMEQASDEFDIEWtDREDGAILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
121-615 |
2.32e-06 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 50.65 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 121 ISYKEVSDRAECVGSALLHRGFKPSHVqyIGIFSQNRPEWVIIEQACYAFSMVVVPLYDTLGAEAI-TYIVNKADLSLVF 199
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDR--VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVaGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 200 CD---KPDKARVLLASVEKG---ETPILNTIVIMDSFGVDLverGKKCGVEVFSMREIEELGRAHRQKPMppKPEDLAVI 273
Cdd:cd17634 163 ADggvRAGRSVPLKKNVDDAlnpNVTSVEHVIVLKRTGSDI---DWQEGRDLWWRDLIAKASPEHQPEAM--NAEDPLFI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 274 CFTSGTTGNPKGAMITHQNIVSNASAFMKTTeksFVPSSDDVLISFLPLAHMFER--IVECVVLChGARIGFFQGdirll 351
Cdd:cd17634 238 LYTSGTTGKPKGVLHTTGGYLVYAATTMKYV---FDYGPGDIYWCTADVGWVTGHsyLLYGPLAC-GATTLLYEG----- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 352 mddlKTLQPTvfpvvPRLLNRMFDK----IFGQADSSLKrwlldfaSKRKEAelrsgivrnnsfwDKVIFRKIQASLggr 427
Cdd:cd17634 309 ----VPNWPT-----PARMWQVVDKhgvnILYTAPTAIR-------ALMAAG-------------DDAIEGTDRSSL--- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 428 vKLMVTGAAPVSASVLTFLRTALG---CQFYEGYGQTECTAGCSLSLPG--DWTAGHVGAPMPCNIIKLVDvQEMNYLAA 502
Cdd:cd17634 357 -RILGSVGEPINPEAYEWYWKKIGkekCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVD-NEGHPQPG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 503 KGEGEVCIKGV--NVFRGYLKDPEKTAEALDK--DGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENVYL 578
Cdd:cd17634 435 GTEGNLVITDPwpGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVLV 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2032642720 579 RCEAVAQVFV-------HGESLQAFLV---GVVVPDP--DTLHNWAKKK 615
Cdd:cd17634 514 AHPKVAEAAVvgiphaiKGQAPYAYVVlnhGVEPSPElyAELRNWVRKE 562
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-605 |
2.64e-06 |
|
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: 50.07 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 265 PKPEDLAVICfTSGTTGNPKGAMITHQNIVSNASAFMKTTEKSFVPSSDDVL-------ISFLPLAHmferivecvvLCH 337
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKaaaaaagTVMFPAPP----------LMH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 338 GAR-----IGFFQGDiRLLMDDLKTLQPTVFPVVPR-LLNRMFdkIFGQAdssLKRWLLDfaskrkeaELRSGIVRNNSf 411
Cdd:cd05924 70 GTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDAGPYDLS- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 412 wdkvifrkiqaSLggrvKLMVTGAAPVSASVLT-FLRTALGCQFYEGYGQTECTA-GCSLSLPGDWTAGHVGAPMPCNII 489
Cdd:cd05924 135 -----------SL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANPDTVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 490 KLVDVQEMNyLAAKGEGEVCIKGvNVFRGYLKDPEKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGE 566
Cdd:cd05924 200 LDDDGRVVP-PGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG-GE 276
|
330 340 350
....*....|....*....|....*....|....*....
gi 2032642720 567 YIAPEKIENVYLRCEAVAQVFVHGeslqaflvgvvVPDP 605
Cdd:cd05924 277 KVFPEEVEEALKSHPAVYDVLVVG-----------RPDE 304
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
249-299 |
4.40e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 49.27 E-value: 4.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2032642720 249 REIEELGRAhrQKPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASA 299
Cdd:PRK07824 18 RRAALLRDA--LRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADA 66
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
451-598 |
9.91e-05 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 45.79 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 451 GCQFYEGYGQTECTAGCSLSLPGDWTAGHVGAPMPCNIIKLVdVQEMNYLAAKGEGEVCIKGVNVFRGYLKDPEKTaeaL 530
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---V 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032642720 531 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENVYLRCEAVAQVFVHG-------ESLQAFLV 598
Cdd:PRK06060 362 ANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
264-590 |
1.05e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 42.03 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 264 PPKPEDL---AVICF--TSGTTGNPKGAMITHQNIVSNASAfmktTEKSFVPSSDDVLISFLPLAHMFERIVeCV--VLC 336
Cdd:cd05939 95 PPSQDDVnfrDKLFYiyTSGTTGLPKAAVIVHSRYYRIAAG----AYYAFGMRPEDVVYDCLPLYHSAGGIM-GVgqALL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 337 HGA----RIGFfqgDIRLLMDDLKTLQPTVfpvvprllnrmfdkifGQADSSLKRWLLdfASKRKEAELRSgivrnnsfw 412
Cdd:cd05939 170 HGStvviRKKF---SASNFWDDCVKYNCTI----------------VQYIGEICRYLL--AQPPSEEEQKH--------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 413 dkvifrkiqaslggRVKLMVTGAapvsasvltfLRTALGCQFY---------EGYGQTECTagCSLslpGDWTaGHVGA- 482
Cdd:cd05939 220 --------------NVRLAVGNG----------LRPQIWEQFVrrfgipqigEFYGATEGN--SSL---VNID-NHVGAc 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032642720 483 ----PMPCNI--IKLVDVQEMNYLAAKGEGEVCIK------GVNV-----------FRGYLkDPEKTAEALDKDGWLH-- 537
Cdd:cd05939 270 gfnsRILPSVypIRLIKVDEDTGELIRDSDGLCIPcqpgepGLLVgkiiqndplrrFDGYV-NEGATNKKIARDVFKKgd 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032642720 538 ----TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENVYLRCEAVAQVFVHG 590
Cdd:cd05939 349 saflSGDVLVMDELGYLYFKDRTGDTFRW-KGENVSTTEVEGILSNVLGLEDVVVYG 404
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
261-324 |
4.42e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 40.10 E-value: 4.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032642720 261 KPMPPKPEDLAVICFTSGTTGNPKGAMITHQNIVSNASAFMKTTEKsfvpSSDDVLISFLPLAH 324
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEG----QEGDRGVSWLPFFH 232
|
|
| |
