|
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 ... |
116-706 |
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: 898.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 196 STVIVDKpqkavlllehverketpglkliilmepfeealkdrgqecGVVIKSMQTIEDCGQRNHRVPVvsssasgsllsk 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPP------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGF 355
Cdd:cd05927 110 PPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 356 FQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIF--CQADTPVKRWFLEFAAKRKQAEVRSGIIRNDSIWDELFFNKIQ 433
Cdd:cd05927 190 YSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFnkVQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIEELNYW- 512
Cdd:cd05927 270 QALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDa 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 513 -TCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIR 591
Cdd:cd05927 350 kDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYAR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 592 SEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWA-QKRGIEGTYVELCTNRELKKAILEDMVSLGKEGGLHSFEQVKAIHI 670
Cdd:cd05927 430 SPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHL 509
|
570 580 590
....*....|....*....|....*....|....*.
gi 1333574464 671 HSDMFSVQNGLLTPTLKAKRPELREYFKKQIEDLYS 706
Cdd:cd05927 510 EPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
80-706 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 689.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 80 QLLTHY--YDDARTMYEVFRRGLSISGNGPCLGFRKPNQ----PYQWLSYQEVADRAEFLGSGLLQHNCK--ACtdqfIG 151
Cdd:PLN02736 32 KLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPkgAC----VG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 152 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVdKPQKAVLLLEHVerKETPGLKLIILMEPFE 231
Cdd:PLN02736 108 LYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRLIVVVGGAD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 232 EALKDRGQECGVVIKSMQTIEDCGQRNHRVPVvsssasgsllskPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG 311
Cdd:PLN02736 185 EPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFR------------PPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 312 FLKVTEkvIFPrqDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIF- 390
Cdd:PLN02736 253 SSLSTK--FYP--SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITn 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 391 -CQADTPVKRWFLEFAAKRKQAEVRSGiiRNDS-IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYE 468
Cdd:PLN02736 329 aVKESGGLKERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 469 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIEELNYwTCKGE----GEICVKGPNVFKGYLKDPDRTKEALDS 544
Cdd:PLN02736 407 GYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNY-TSEDQpyprGEICVRGPIIFKGYYKDEVQTREVIDE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 545 DGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWA 624
Cdd:PLN02736 486 DGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWA 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 625 QKRGIE-GTYVELCTNRELKKAILEDMVSLGKEGGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIED 703
Cdd:PLN02736 566 ASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISD 645
|
...
gi 1333574464 704 LYS 706
Cdd:PLN02736 646 MYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-706 |
4.48e-172 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 505.79 E-value: 4.48e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 86 YDDARTMYEVFRRGLSISGNGPCLGfRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 166 ACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHveRKETPGLKLIILMEPFEEALKDRgqecgvvI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDPRGLRDDPR-------L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 246 KSMQTIEDCGqRNHRVPvvsssASGSLLSKPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQD 325
Cdd:COG1022 155 LSLDELLALG-REVADP-----AELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 326 DVLISFLPLAHMFERVIQSVVYCHGGRVGFfQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFCQAD--TPVKR---- 399
Cdd:COG1022 225 DRTLSFLPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRklfr 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 400 WFLEFAAKRKQAEVRSGIIR-----NDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE 474
Cdd:COG1022 304 WALAVGRRYARARLAGKSPSlllrlKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 475 CTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDieelnywtckgEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIG 554
Cdd:COG1022 383 TSPVITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 555 KWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIE-GTY 633
Cdd:COG1022 452 ELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSY 530
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333574464 634 VELCTNRELKKAILEDMVSLGKegGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEDLYS 706
Cdd:COG1022 531 AELAQDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-693 |
3.75e-158 |
|
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: 464.76 E-value: 3.75e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 196 STVIVDKPqkavlllehverketpglkliilmepfeealkdrgqecgvviksmqtiedcgqrnhrvpvvsssasgsllsk 275
Cdd:cd05907 79 KALFVEDP------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 ppkpSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVG 354
Cdd:cd05907 87 ----DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIY 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 FFQgDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFCQADTPVKRWFLEFAAkrkqaevrsgiirndsiwdelffnkiqa 434
Cdd:cd05907 159 FAS-SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV---------------------------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 435 slGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDieelnywtc 514
Cdd:cd05907 210 --GGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD--------- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 515 kgEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEP 594
Cdd:cd05907 278 --DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPL 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 595 VAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIEG-TYVELCTNRELKKAILEDMVSLGKEggLHSFEQVKAIHIHSD 673
Cdd:cd05907 356 ISQAVVIGDGRP-FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LSRYEQIKKFLLLPE 432
|
570 580
....*....|....*....|
gi 1333574464 674 MFSVQNGLLTPTLKAKRPEL 693
Cdd:cd05907 433 PFTIENGELTPTLKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-690 |
1.62e-151 |
|
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: 449.74 E-value: 1.62e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 117 PYQWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINT 192
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLvelgLKPGDK------VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 193 ADISTVIVDkpqkavlllehverketpglkliilmepfeealkdrgqecgvviksmqtiedcgqrnhrvpvvsssasgsl 272
Cdd:cd17639 76 TECSAIFTD----------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 273 lskpPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqDDVLISFLPLAHMFERVIQSVVYCHGGR 352
Cdd:cd17639 85 ----GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP--DDRYLAYLPLAHIFELAAENVCLYRGGT 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 VGFfqGDIRLLSDDMKALC--------PTIFPVVPRLLNRMYDKIFCQADTP--VKRWFLEFAAKRKQAEVRSGIirnDS 422
Cdd:cd17639 159 IGY--GSPRTLTDKSKRGCkgdltefkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALKEGP---GT 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 423 -IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHI 501
Cdd:cd17639 234 pLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEI 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 502 KLVDIEELNYWTCKGE--GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEY 579
Cdd:cd17639 313 KLVDWEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEY 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 580 VAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYVELCTNRELKKAILEDMVSLGKEGG 658
Cdd:cd17639 393 IALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQKAVLKSLAETARAAG 472
|
570 580 590
....*....|....*....|....*....|..
gi 1333574464 659 LHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKR 690
Cdd:cd17639 473 LEKFEIPQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
58-705 |
3.33e-147 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 444.46 E-value: 3.33e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 58 LMQSEEVKDSGGARRSVigdGPQLLTHYYDDA--------RTMYEVFRRGLSISGNGPCLGFR-----KPNQpYQWLSYQ 124
Cdd:PLN02614 8 IFQVEEGKEGSDGRPSV---GPVYRSIFAKDGfpnpiegmDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 125 EVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQ 204
Cdd:PLN02614 84 EVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 205 KAVLLLEHVERKETPGLKLIILMEPFEEALKDRGQECGVVIKSMQTIEDCGQ-RNHRVPVvsssasgsllskpPKPSDLS 283
Cdd:PLN02614 160 KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEgKQYDLPI-------------KKKSDIC 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 284 IVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDI 360
Cdd:PLN02614 227 TIMYTSGTTGDPKGVMISNESIVTLIAGvirLLKSANAAL--TVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 361 RLLSDDMKALCPTIFPVVPRLLNRMYDKIFCQADTP--VKRWFLEFAAKRKQAEVRSGI--IRNDSIWDELFFNKIQASL 436
Cdd:PLN02614 305 KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDKLVFNKVKQGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 437 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDIEELNY--WT 513
Cdd:PLN02614 385 GGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLESVPEMEYdaLA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 514 CKGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSE 593
Cdd:PLN02614 465 STPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 594 PVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYVELCTNRELKKAILEDMVSLGKEGGLHSFEQVKAIHIHSD 673
Cdd:PLN02614 544 AVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPV 623
|
650 660 670
....*....|....*....|....*....|..
gi 1333574464 674 MFSVQNGLLTPTLKAKRPELREYFKKQIEDLY 705
Cdd:PLN02614 624 PFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-705 |
8.07e-147 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 443.10 E-value: 8.07e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 88 DARTMYEVFRRGLSISGNGPCLGFRKPNQ----PYQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIA 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 164 ELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV-DKPQKAVLlleHVERKETPGLKLIILMEPFEEALKDRGQECG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 243 VVIKSMQTIEDCGQRNHRVPvvsssasgsllsKPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEKV 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSET------------NPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlFMEQFEDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 320 IfpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIF--CQADTPV 397
Cdd:PLN02430 263 M--THDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQkaLQELNPR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 398 KRWFLEFAAKRKQAEVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC 475
Cdd:PLN02430 341 RRLIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 476 TAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDIEELNYwTCKGE---GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTG 551
Cdd:PLN02430 421 LGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGY-DPLGEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTG 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 552 DIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEG 631
Cdd:PLN02430 499 DIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTG 578
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333574464 632 TYVELCTNRELKKAILEDMVSLGKEGGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEDLY 705
Cdd:PLN02430 579 SFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-706 |
9.61e-147 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 442.74 E-value: 9.61e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 117 PYQWLSYQEVADRAEFLGSGLLQ------HNCkactdqfiGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYII 190
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSrgvnpgDRC--------GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 191 NTADISTVIVDKPQKAVLLleHVERKETPGLKLIILMEPFEEALKDRGQECGVVIKSMQTIEDCGQRNHRVPvvsssasg 270
Cdd:PLN02861 146 NHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 271 sllskPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSVVY 347
Cdd:PLN02861 216 -----PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRVA--TEEDSYFSYLPLAHVYDQVIETYCI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 348 CHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIF--CQADTPVKRWFLEFAAKRKQAEVRSGIIRNDS--I 423
Cdd:PLN02861 289 SKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMqkISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 424 WDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--GHVGAPLPCNHI 501
Cdd:PLN02861 369 LDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvGTVGVPMTTIEA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 502 KLVDIEELNY--WTCKGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEY 579
Cdd:PLN02861 448 RLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEY 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 580 VAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYVELCTNRELKKAILEDMVSLGKEGGL 659
Cdd:PLN02861 527 VAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQL 606
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1333574464 660 HSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEDLYS 706
Cdd:PLN02861 607 RGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
79-706 |
3.94e-129 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 398.34 E-value: 3.94e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 79 PQLLTHYYDDARTMYEVFRRGLSISGNGPCLGFRKPNQ------------------PYQWLSYQEVADRAEFLGSGLLQ- 139
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKLISrefetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 140 -HNckacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ--KAVLLLEHVERk 216
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlkKLIDISSQLET- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 217 etpgLKLIILMEpfEEALKD---RGQECGVVIKSMQTIEDCGQRNHRVPVVsssasgsllskpPKPSDLSIVCFTSGTTG 293
Cdd:PLN02387 202 ----VKRVIYMD--DEGVDSdssLSGSSNWTVSSFSEVEKLGKENPVDPDL------------PSPNDIAVIMYTSGSTG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 294 NPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFfqGDIRLLSD-------- 365
Cdd:PLN02387 264 LPKGVMMTHGNIVATVAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 366 ---DMKALCPTIFPVVPRLLNRMYDKIFCQADTP---VKRWFlEFAAKRKQAEVR------SGIIRndSIWDELFFNKIQ 433
Cdd:PLN02387 339 tkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKgglAKKLF-DIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIEELNYWT 513
Cdd:PLN02387 416 AVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLI 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 514 CKG---EGEICVKGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIE 586
Cdd:PLN02387 496 SDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVE 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 587 NIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GTYVELCTNRELKKAILEDMVSLGKEGGLHSFEQV 665
Cdd:PLN02387 576 AALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIP 655
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1333574464 666 KAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEDLYS 706
Cdd:PLN02387 656 AKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-575 |
1.29e-121 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 369.33 E-value: 1.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 117 PYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 197 TVIVDKPQKAVLLLEHVERKETPGLKLIILMEPFEEAlkdrgqecgvviksmQTIEDCGQRNHRVPVVSssasgsllsKP 276
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKE---------------EPLPEEAKPADVPPPPP---------PP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 PKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGF 355
Cdd:pfam00501 152 PDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 356 FQGDIRL----LSDDMKALCPTIFPVVPRLLNRMydkifcqadtpvkrwfleFAAKRKQAEVRSGiirndsiwdelffnk 431
Cdd:pfam00501 232 PPGFPALdpaaLLELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS--------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 432 iqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLPCNHIKLVDIEE 508
Cdd:pfam00501 279 --------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDET 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333574464 509 LNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLA 575
Cdd:pfam00501 351 GEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
119-705 |
1.40e-92 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 302.67 E-value: 1.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 119 QWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTAD 194
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLaelgLTKGSN------VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 195 iSTVIVDKPQKAVLLLEHVERKETPGLKLIILmepfeEALKDrgqecGVVIKSMQTI--EDcgqrnhrvpVVSSSASGSL 272
Cdd:PTZ00216 194 -CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPA-----SVDTEGCRLVawTD---------VVAKGHSAGS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 273 LSKPPKPS---DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYC 348
Cdd:PTZ00216 254 HHPLNIPEnndDLALIMYTSGTTGDPKGVMHTHGSLTAGILALeDRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 349 HGGRVGFfqGDIRLLSD-------DMKALCPTIFPVVPRLLNRMydKIFCQADTP----VKRWFLEFAAKRKQAEVRSGi 417
Cdd:PTZ00216 334 RGALIGF--GSPRTLTDtfarphgDLTEFRPVFLIGVPRIFDTI--KKAVEAKLPpvgsLKRRVFDHAYQSRLRALKEG- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 418 iRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtpGDWTSGHVGAP 495
Cdd:PTZ00216 409 -KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT--GDLEPNAVGQL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 496 LPCNHIKLVDIEELNYwTCKGE--GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFK 573
Cdd:PTZ00216 485 LKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAK 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 574 LAQGEYVAPEKIENIYIRSEPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKRGIEGTYVELCTNRELKKAILED 649
Cdd:PTZ00216 564 NCLGEYIALEALEALYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATES 641
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 650 MVSLGKEGGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEDLY 705
Cdd:PTZ00216 642 LQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-690 |
3.78e-78 |
|
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: 258.94 E-value: 3.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 118 YQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 198 VIVDKpqkavllLEHVERKE--TPGLKLIILMEPFEEALKDRGqecgvviksMQTIEDCGQRNHRVPvvsssasgsllsk 275
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQ---------WDDLIAQHPPLEERP------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGF 355
Cdd:cd05932 133 TRFPEQLATLIYTSGTTGQPKGVMLTFGS----FAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 356 FQGDIRLLSDDMKALCPTIFPVVPRLL----NRMYDKIfcqadtPVKRwfLEFAAKrkqAEVRSGIIRndsiwdelffNK 431
Cdd:cd05932 209 FAESLDTFVEDVQRARPTLFFSVPRLWtkfqQGVQDKI------PQQK--LNLLLK---IPVVNSLVK----------RK 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 432 IQASLG-GCVRMIVTGAAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDieeln 510
Cdd:cd05932 268 VLKGLGlDQCRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE----- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 511 ywtckgEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYI 590
Cdd:cd05932 342 ------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLA 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 591 RSEPVAQIYVHGDSLKAfLVGIVVPDPEvmpswAQKRGIEGTYVELctnRELKKAILEDMvslgkEGGLHSFEQVKAIHI 670
Cdd:cd05932 416 EHDRVEMVCVIGSGLPA-PLALVVLSEE-----ARLRADAFARAEL---EASLRAHLARV-----NSTLDSHEQLAGIVV 481
|
570 580
....*....|....*....|
gi 1333574464 671 HSDMFSVQNGLLTPTLKAKR 690
Cdd:cd05932 482 VKDPWSIDNGILTPTLKIKR 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-691 |
8.24e-77 |
|
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: 254.21 E-value: 8.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 116 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 196 STVIVDkpqkavlllehverketpglkliilmepfeealkdrgqecgvviksmqtiedcgqrNHrvpvvsssasgsllsk 275
Cdd:cd17640 79 VALVVE--------------------------------------------------------ND---------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 ppkPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGF 355
Cdd:cd17640 87 ---SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 356 fqGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFCQ--ADTPVKRWFLEFAAkrkqaevrsgiirndsiwdelffnkiq 433
Cdd:cd17640 160 --TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL--------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 asLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIEELNYWT 513
Cdd:cd17640 211 --SGGIFKFGISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLP 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 514 CKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSE 593
Cdd:cd17640 288 PGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSP 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 594 PVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGI---EGTYVELCTNRELKKAILEDMVSLGKEGGLHSFEQVKAIHI 670
Cdd:cd17640 368 FIEQIMVVGQDQK-RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFAL 446
|
570 580
....*....|....*....|.
gi 1333574464 671 HSDMFsVQNGLLTPTLKAKRP 691
Cdd:cd17640 447 LEEPF-IENGEMTQTMKIKRN 466
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-705 |
2.39e-66 |
|
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: 229.94 E-value: 2.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 113 KPNQPYQWLSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIR 187
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRqaakaFLKLGLERFHG-------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 188 YIINTADISTVIVDKPQKAVLLLEhvERKETPGLKLII-LMEPFEEALKDrgqecgvvIKSMQTIEDCG------QRNHR 260
Cdd:cd05933 74 YVAETSEANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKEKEPN--------LYSWDEFMELGrsipdeQLDAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 261 VPVVsssasgsllskppKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFER 340
Cdd:cd05933 144 ISSQ-------------KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 341 VIQS-VVYCHGGRVGFFQGDIR--LLSDDMKALCPTIFPVVPRLLNRMYDKI---FCQAdTPVKRWFLEFAaKRKQAEV- 413
Cdd:cd05933 211 ILDIwLPIKVGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETn 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 414 ------RSGIIRNDSIWDELFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPG 485
Cdd:cd05933 289 lklmggESPSPLFYRLAKKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 486 DWTSGHVGAPLPCNHIKLVDIEelnywtCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKII 565
Cdd:cd05933 367 AYRLLSCGKALPGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYIT 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 566 DRKKHIFKLAQGEYVAPEKIENIYIRSEP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKRGI 629
Cdd:cd05933 441 GRIKELIITAGGENVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGS 518
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333574464 630 EGTYVELCTNRE---LKKAILEDMVSLGKEGGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELREYFKKQIEDLY 705
Cdd:cd05933 519 QATRVSEIAGGKdpkVYEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
92-617 |
3.41e-65 |
|
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: 222.76 E-value: 3.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 92 MYEVFRRGLSISGNGPCLGFRkpnqpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYS 171
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 172 MVVVPLYDTLGPGAIRYIINTADISTVIVdkpqkAVLLlehverketpglkliilmepfeealkdrgqecgvviksmqti 251
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT-----ALIL------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 252 edcgqrnhrvpvvsssasgsllskppkpsdlsivcFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISF 331
Cdd:COG0318 107 -----------------------------------YTSGTTGRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVA 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 332 LPLAHMF---ERVIQSVVycHGGRV----GFfqgDIRLLSDDMKALCPTIFPVVPRLLNRMYDKI-FCQADTPvkrwfle 403
Cdd:COG0318 148 LPLFHVFgltVGLLAPLL--AGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLRHPeFARYDLS------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 404 faakrkqaevrsgiirndsiwdelffnkiqaslggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT 483
Cdd:COG0318 216 -----------------------------------SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNP 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 484 PGDWTS--GHVGAPLPCNHIKLVDIE--ELNywtcKGE-GEICVKGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLP 558
Cdd:COG0318 261 EDPGERrpGSVGRPLPGVEVRIVDEDgrELP----PGEvGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDE 335
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 559 AGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDP 617
Cdd:COG0318 336 DGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
118-649 |
1.42e-63 |
|
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: 221.53 E-value: 1.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 118 YQWLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 197
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 198 VIVDKPQKAVLLLEHveRKETPGLKLIILMEPFEEALKDRGQecgvvIKSMQTIEDCGQRNHRV-PVVSSSASGSLlskp 276
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRALDRRdPGLYEREVAAG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 pKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFER---VIQSVVycHGGRV 353
Cdd:cd17641 156 -KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQmysVGQALV--CGFIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 GFFQgDIRLLSDDMKALCPTIFPVVPRLLN--------RMYDKifcqadTPVKRWF--------LEFAAKRKQAEVRSGI 417
Cdd:cd17641 229 NFPE-EPETMMEDLREIGPTFVLLPPRVWEgiaadvraRMMDA------TPFKRFMfelgmklgLRALDRGKRGRPVSLW 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 418 IRNDS-IWDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGA 494
Cdd:cd17641 302 LRLASwLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 495 PLPCNHIKlvdIEElnywtckgEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKL 574
Cdd:cd17641 380 PFPGTEVR---IDE--------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTT 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 575 AQGEYVAPEKIENIYIRSEPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYVELCTNRELKKAILED 649
Cdd:cd17641 449 SDGTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKE 523
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
121-683 |
2.37e-60 |
|
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: 213.09 E-value: 2.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSgllQHNCKACTD--QFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 198
Cdd:cd17632 68 ITYAELWERVGAVAA---AHDPEQPVRpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 199 IVDKPQKAvLLLEHVERKETPGLKLIILMEPFEEALKD-----RGQECGVviksmqtieDCGQRNHRVPVVSSSASGSLL 273
Cdd:cd17632 145 AVSAEHLD-LAVEAVLEGGTPPRLVVFDHRPEVDAHRAalesaRERLAAV---------GIPVTTLTLIAVRGRDLPPAP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 274 SKPPKPSD--LSIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGG 351
Cdd:cd17632 215 LFRPEPDDdpLALLIYTSGSTGTPKGAMYTE-RLVATF--WLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 352 rVGFFQG--DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFCQADTPVKRWF-----LEFAAKRKQAEVRsgiirndsiw 424
Cdd:cd17632 292 -TAYFAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadAETLAERVKAELR---------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 425 delffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtSGHVGAPlPCNHIKLV 504
Cdd:cd17632 357 --------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 505 DIEELNYWTCKG---EGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVA 581
Cdd:cd17632 420 DVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVT 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 582 PEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEvmpswAQKRGiegtyvelcTNRELKKAILEDMVSLGKEGGLHS 661
Cdd:cd17632 500 VARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQD-----ALAGE---------DTARLRAALAESLQRIAREAGLQS 565
|
570 580
....*....|....*....|..
gi 1333574464 662 FEQVKAIHIHSDMFSVQNGLLT 683
Cdd:cd17632 566 YEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-690 |
1.01e-59 |
|
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: 208.45 E-value: 1.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLgSGLLQHNCKACTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPQkavlllehverketpglkliilmepfeealkdrgqecgvviksmqtiedcgqrnhrvpvvsssasgsllskppkps 280
Cdd:cd05914 86 SDED---------------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTEKVifpRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDI 360
Cdd:cd05914 90 DVALINYTSGTTGNSKGVMLTYRNIVSNVDG-VKEVVLL---GKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 361 ---RLLSDDMKALCPTIfpVVPRLLNRMYDKIFCQADTPVKRWFLEFAAKrkqaevrsgIIRNDSIWdELFFNKIQASLG 437
Cdd:cd05914 166 psaKIIALAFAQVTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-KLAFKKVHEAFG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 438 GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIEELNywtckGE 517
Cdd:cd05914 234 GNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPAT-----GE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 518 GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVA- 596
Cdd:cd05914 308 GEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLe 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 597 -QIYVHGDSLKAflvgIVVPDPEVMPSWAQKrgiegtyvelctNRELKKAILEDMV-SLGKEggLHSFEQVKAIHIHSDM 674
Cdd:cd05914 388 sLVVVQEKKLVA----LAYIDPDFLDVKALK------------QRNIIDAIKWEVRdKVNQK--VPNYKKISKVKIVKEE 449
|
570
....*....|....*.
gi 1333574464 675 FSVqngllTPTLKAKR 690
Cdd:cd05914 450 FEK-----TPKGKIKR 460
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
121-627 |
3.44e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 205.52 E-value: 3.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGK-GDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 -------DKPQKAVL-LLEHVERKETP-GLKLIILMEPFEEALKdrgqecgvviksmqtiedCGQRNHRVPVVsssasgs 271
Cdd:PRK07656 109 lglflgvDYSATTRLpALEHVVICETEeDDPHTEKMKTFTDFLA------------------AGDPAERAPEV------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 272 llskppKPSDLSIVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTEKvifprqDDVLISfLPLAHMFerviqsvvyc 348
Cdd:PRK07656 164 ------DPDDVADILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG------DRYLAA-NPFFHVF---------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 349 hGGRVGF---------------FQGD--IRLLSDDMkalcPTIFPVVPRLLNRMYDkifcqadtpvkrwflefAAKRKQA 411
Cdd:PRK07656 221 -GYKAGVnaplmrgatilplpvFDPDevFRLIETER----ITVLPGPPTMYNSLLQ-----------------HPDRSAE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 412 EVRSgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---W 487
Cdd:PRK07656 279 DLSS------------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 488 TSGHVGAPLPCNHIKLVDieELNYWTCKGE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIID 566
Cdd:PRK07656 335 VAGTIGTAIAGVENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVD 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333574464 567 RKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 627
Cdd:PRK07656 413 RKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAYVVlkpGAELTEEELI-AYCREH 481
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
281-618 |
1.10e-57 |
|
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: 199.05 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFerVIQSVVYC--HGGRVGFFQG 358
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG--GLFGLLGAllAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 -DIRLLSDDMKALCPTIFPVVPRLLNRMydkifcqadtpvkrwflefaakRKQAEVRSgiiRNDSiwdelffnkiqaslg 437
Cdd:cd04433 75 fDPEAALELIEREKVTILLGVPTLLARL----------------------LKAPESAG---YDLS--------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 438 gCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDiEELNYWTCK 515
Cdd:cd04433 115 -SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVD-PDGGELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 516 GEGEICVKGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPV 595
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|...
gi 1333574464 596 AQIYVHGdslkaflvgivVPDPE 618
Cdd:cd04433 271 AEAAVVG-----------VPDPE 282
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
93-610 |
2.59e-55 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 196.24 E-value: 2.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 93 YEVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKaCTDQfIGVFAQNRPEWIIAELACYTYSM 172
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQ-PGDR-VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 173 VVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmEPFEEALKDrgqecgvviksmqtie 252
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA--------------------------VSFTDLLAA---------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 253 dcgqrnhrvpvvsssASGSLLSKPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfpRQDDVLISFL 332
Cdd:cd05936 113 ---------------GAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAAL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 333 PLAHMFErviQSVVYCHGGRVGFFQ------GDIRLLsDDMKALCPTIFPVVPRLLNRMydkifCQADTPVKRWFlefaa 406
Cdd:cd05936 176 PLFHVFG---LTVALLLPLALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPTMYIAL-----LNAPEFKKRDF----- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 407 krkqaevrSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD 486
Cdd:cd05936 242 --------SSL-----------------------RLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDG 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 487 WT-SGHVGAPLPCNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKII 565
Cdd:cd05936 291 PRkPGSIGIPLPGTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIV 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1333574464 566 DRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 610
Cdd:cd05936 369 DRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-610 |
3.44e-52 |
|
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: 188.19 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPQKAVLLLehVERKETPGLKlIILMEPFEEALKDRGQecgvviksMQTIEDCGQRNHRVPVVSSsasgsllskppKPS 280
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVLSIED--------LLSPTLGEEDEDLPPPLKD-----------GKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSgFLKVTEKVIFPRqDDVLISFLPLAHMFErvIQSVVYC--HGGRV----G 354
Cdd:cd05911 147 DTAAILYSSGTTGLPKGVCLSHRNLIANLS-QVQTFLYGNDGS-NDVILGFLPLYHIYG--LFTTLASllNGATViimpK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 FFqgdirllSDDMKALCP----TIFPVVPRLLNRMydkifcqADTPvkrwflefaakrkqaevrsgiirndsiwdelFFN 430
Cdd:cd05911 223 FD-------SELFLDLIEkykiTFLYLVPPIAAAL-------AKSP-------------------------------LLD 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 431 KIQASlggCVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIEEL 509
Cdd:cd05911 258 KYDLS---SLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGK 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 510 NYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIy 589
Cdd:cd05911 335 DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV- 412
|
490 500
....*....|....*....|....*....
gi 1333574464 590 IRSEP------VAQIY--VHGDSLKAFLV 610
Cdd:cd05911 413 LLEHPgvadaaVIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-617 |
2.10e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 166.90 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 86 YDDARTMYEVFRRGLSISGNGPCLGFRKPNqpyqwLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 165
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 166 ACytySM---VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMEPFEEAlkdrgqe 240
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDGPAA------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 241 cgvviksmqtieDCGQRNHRVPVVSSSASGSLLSKPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVI 320
Cdd:PRK06187 140 ------------PLAPEVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWLK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 321 FpRQDDVLISFLPLAHmferviqsvvyCHG---GRVGFFQG---------DIRLLSDDMKALCPTIFPVVPRLLNRMYdk 388
Cdd:PRK06187 205 L-SRDDVYLVIVPMFH-----------VHAwglPYLALMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQMLL-- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 389 ifcQADTPVKRWFlefaakrkqaevrSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYE 468
Cdd:PRK06187 271 ---KAPRAYFVDF-------------SSL-----------------------RLVIYGGAALPPALLREFKEKFGIDLVQ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 469 GYGQTECTAGCTFTTPGDWTSGH------VGAPLPCNHIKLVDiEELNY--WTCKGEGEICVKGPNVFKGYLKDPDRTKE 540
Cdd:PRK06187 312 GYGMTETSPVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDElpPDGGEVGEIIVRGPWLMQGYWNRPEATAE 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333574464 541 ALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 617
Cdd:PRK06187 391 TID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVAEVAVIG--VPDE 454
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-634 |
3.91e-40 |
|
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: 154.41 E-value: 3.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSgLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPQKAVLLLEHVERKETPglKLIILMEPFEEALKdRGQECGVVIKSMQTIEDCGQRNHRVPVvsssasgsllskppKPS 280
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD--ARIVYLEDLRAKIS-KADKCKAFLAGKFPPKWLLRIFGVAPV--------------QPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFFQGDI 360
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSF---------------GLTGCLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 361 RLLSDDMKALC---PTIFPVVPRLLnrmYDK---IFCQADTpvkrwFLEFAAKRKQAEVRSGIirndsiwdelffnkiqa 434
Cdd:cd05909 209 LPLLSGIKVVFhpnPLDYKKIPELI---YDKkatILLGTPT-----FLRGYARAAHPEDFSSL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 435 slggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDIEELNYWT 513
Cdd:cd05909 264 ------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 514 CKGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSE 593
Cdd:cd05909 338 IGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEIL 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1333574464 594 P----VAQIYV----HGDSLKAFLVGIvVPDPEVMPSWAQKRGIEGTYV 634
Cdd:cd05909 416 PedneVAVVSVpdgrKGEKIVLLTTTT-DTDPSSLNDILKNAGISNLAK 463
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
278-588 |
4.17e-38 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 148.54 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifPRQDDVLISFLPLAHMFerviqsvvychgGRVGFFQ 357
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFHIY------------GLSSFAL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 GDIRL-----------LSDDMKALCP---TIFPVVPrllnrmydkifcqadtPVkrwfleFAAKRKQAEVRSGIIRndsi 423
Cdd:cd05904 222 GLLRLgatvvvmprfdLEELLAAIERykvTHLPVVP----------------PI------VLALVKSPIVDKYDLS---- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 424 wdelffnkiqaSLggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHVGAPLPCN 499
Cdd:cd05904 276 -----------SL----RQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 500 HIKLVDIEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEY 579
Cdd:cd05904 341 EAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQ 419
|
....*....
gi 1333574464 580 VAPEKIENI 588
Cdd:cd05904 420 VAPAELEAL 428
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
278-690 |
1.06e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 150.25 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNV------VADFSGFLKVTEKVIFprqddvliSFLPLAHMFERVIQSVVYCHGG 351
Cdd:PTZ00342 302 DPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKKYNPKTHL--------SYLPISHIYERVIAYLSFMLGG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 352 RVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFCQAD--TPVKRWFlefaAKRKQAEVRSGIIRNDSIWDELFF 429
Cdd:PTZ00342 374 TINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFSKFLEGIT 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 430 N---KIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-PCNHIKLV 504
Cdd:PTZ00342 450 HissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsPNTKYKVR 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 505 DIEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEK 584
Cdd:PTZ00342 529 TWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDM 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 585 IENIYIRSEPVAQIYVHG-DSLKAFLvGIVVPDPEVM------PSWAQKRGI-EGTYVELCTNRELKKAIL-----EDMV 651
Cdd:PTZ00342 609 LNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYvdyvkGKML 687
|
410 420 430
....*....|....*....|....*....|....*....
gi 1333574464 652 SLGKEGGLHSFEQVKAIHIHSDMFSVQNgLLTPTLKAKR 690
Cdd:PTZ00342 688 EVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKR 725
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
281-621 |
1.29e-37 |
|
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: 145.90 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFERV--IQSVVYChGGRV---GF 355
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRW----TEDDVLLHVLPLHHVHGLVnaLLCPLFA-GASVeflPK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 356 FQGDIRLLSDDMKALcpTIFPVVPRllnrMYDKIfcqADTPvkrwflefaakrkqaevrsgiirndsiwdELFFNKIQAS 435
Cdd:cd05941 165 FDPKEVAISRLMPSI--TVFMGVPT----IYTRL---LQYY-----------------------------EAHFTDPQFA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 436 LGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDIEELN 510
Cdd:cd05941 207 RAAAaerLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 511 YWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK-HIFKlAQGEYVAPEKIENIY 589
Cdd:cd05941 285 PLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVL 363
|
330 340 350
....*....|....*....|....*....|....*
gi 1333574464 590 IRSEPVAQIYVHGDSLKAF---LVGIVVPDPEVMP 621
Cdd:cd05941 364 LAHPGVSECAVIGVPDPDWgerVVAVVVLRAGAAA 398
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
96-617 |
1.48e-36 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 142.75 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 96 FRRGLSISGNGPCLGFrkPNQPyqwLSYQEVADRAEFLGSGLlQHNCKACTDQfIGVFAQNRPEWIIAELACYTYSMVVV 175
Cdd:cd17631 1 LRRRARRHPDRTALVF--GGRS---LTYAELDERVNRLAHAL-RALGVAKGDR-VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 176 PLYDTLGPGAIRYIINTADiSTVIVDkpqkavlllehverketpglkliilmepfeealkdrgqecgvviksmqtiedcg 255
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 256 qrnhrvpvvsssasgsllskppkpsDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLA 335
Cdd:cd17631 99 -------------------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAA----LDLGPDDVLLVVAPLF 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 336 HMFE-RVIQSVVYCHGGRV----GFFQGDIRLLSDDMKAlcpTIFPVVPRLLNRMydkifcqADTPVkrwflefaakrkq 410
Cdd:cd17631 150 HIGGlGVFTLPTLLRGGTVvilrKFDPETVLDLIERHRV---TSFFLVPTMIQAL-------LQHPR------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 411 aevrsgiirndsiWDELFFnkiqASLggcvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS- 489
Cdd:cd17631 207 -------------FATTDL----SSL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRk 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 490 -GHVGAPLPCNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRK 568
Cdd:cd17631 265 lGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRK 342
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1333574464 569 KHIFKlAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 617
Cdd:cd17631 343 KDMII-SGGENVYPAEVEDV---------LYEHPAVAEVAVIG--VPDE 379
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
277-616 |
3.59e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.21 E-value: 3.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 PKPSDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEkviFPRQDDVLISFLPLAHMF--ERVIQSVVYCHGGRV 353
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANaAQGKAWVPG---LGDGPERVLAALPMFHAYglTLCLTLAVSIGGELV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 GFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmYDKIfcqadtpvkrwfLEFAAKRkqaevrsGIirndsiwdelffnkiq 433
Cdd:PRK05605 293 LLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV---------------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 aSLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPLPCNHIKLVDIEELN 510
Cdd:PRK05605 334 -DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDTEVRIVDPEDPD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 511 YWTCKGE-GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEniy 589
Cdd:PRK05605 410 ETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVE--- 484
|
330 340
....*....|....*....|....*..
gi 1333574464 590 irsEPVAQiyvHGDSLKAFLVGIVVPD 616
Cdd:PRK05605 485 ---EVLRE---HPGVEDAAVVGLPRED 505
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-617 |
5.81e-34 |
|
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: 136.29 E-value: 5.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 120 WLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 199
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK--GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 200 VDKpqkaVLLLEHVERKETPGLkliilmepfeeALKDRGQECGVVIKSMQtiedcgqrNHRVPVVSSSASGSLLSKPPKP 279
Cdd:cd05926 92 TPK----GELGPASRAASKLGL-----------AILELALDVGVLIRAPS--------AESLSNLLADKKNAKSEGVPLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 280 SDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvIFPrqDDVLISFLPLAHmferVIQSVVYC-----HGGRV- 353
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYK--LTP--DDRTLVVMPLFH----VHGLVASLlstlaAGGSVv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 ---GFfqgDIRLLSDDMKALCPTIFPVVPR----LLNRmydkifcqadtpvkrwflefaAKRKQAEVRSGIirndsiwde 426
Cdd:cd05926 221 lppRF---SASTFWPDVRDYNATWYTAVPTihqiLLNR---------------------PEPNPESPPPKL--------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 427 lffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPLPcNHIKL 503
Cdd:cd05926 268 --------------RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKPVG-VEVRI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 504 VDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPE 583
Cdd:cd05926 332 LD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPL 409
|
490 500 510
....*....|....*....|....*....|....
gi 1333574464 584 KIENIYIRSEPVAQIYVHGdslkaflvgivVPDP 617
Cdd:cd05926 410 EVDGVLLSHPAVLEAVAFG-----------VPDE 432
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
257-617 |
2.77e-31 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 129.23 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 257 RNHRVPVVSSsasgsllskppKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVifPRQDDVLISFLP 333
Cdd:PRK08751 196 RKHSMPTLQI-----------EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqaHQWLAGTGKL--EEGCEVVITALP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 334 LAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLlNRMYDKIFcqaDTPVkrwflefaakrkqaev 413
Cdd:PRK08751 263 LYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV-NTLFNGLL---NTPG---------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 414 rsgiirndsiWDELFFNKIQASLGGcvRMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHV 492
Cdd:PRK08751 323 ----------FDQIDFSSLKMTLGG--GMAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSI 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 493 GAPLPCNHIKLVDieELNYWTCKGE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHI 571
Cdd:PRK08751 385 GLPIPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDM 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1333574464 572 FkLAQGEYVAPEKIENIYIRSEPVAQIYVHG----DSLKAFLVGIVVPDP 617
Cdd:PRK08751 463 I-LVSGFNVYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
277-610 |
3.28e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 129.11 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 PKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFf 356
Cdd:PRK05677 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNI- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 357 qgdirLLSDdmkalcPTIFPVVPRLLNRMYDKIFCQADTpvkrwflEFAAkrkqaevrsgiIRNDSIWDELFFNKIQASL 436
Cdd:PRK05677 282 -----LISN------PRDLPAMVKELGKWKFSGFVGLNT-------LFVA-----------LCNNEAFRKLDFSALKLTL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 437 GGcvRMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIE--ELNYwtc 514
Cdd:PRK05677 333 SG--GMALQLATAER------WKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDgnELPL--- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 515 kGE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 593
Cdd:PRK05677 402 -GEvGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDVLAALP 479
|
330 340
....*....|....*....|....
gi 1333574464 594 PVAQ---IYV----HGDSLKAFLV 610
Cdd:PRK05677 480 GVLQcaaIGVpdekSGEAIKVFVV 503
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
281-627 |
6.20e-31 |
|
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: 126.41 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAH------MFERVIQsvvychGGRVG 354
Cdd:TIGR01923 112 QIATLMFTSGTTGKPKAVPHTFRNHYASAVG---SKENLGFTEDDNWLLS-LPLYHisglsiLFRWLIE------GATLR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 FFQGDIRLLsDDMKALCPTIFPVVPRLLNRMYDKifcqadtpvkrwflefaakrkqaevrsgiirndsiwdelffnkiqa 434
Cdd:TIGR01923 182 IVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE---------------------------------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 435 sLGGC--VRMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDIEE 508
Cdd:TIGR01923 215 -GGHNenLRKILLGGSAIPAPLI---EEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 509 lnywtckGEGEICVKGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 588
Cdd:TIGR01923 291 -------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETV 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1333574464 589 YIRSEPVAQIYV--HGDSL-----KAFLVGIVVPDPEVMPSWAQKR 627
Cdd:TIGR01923 362 LYQHPGIQEAVVvpKPDAEwgqvpVAYIVSESDISQAKLIAYLTEK 407
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
278-610 |
1.04e-30 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 127.48 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISfLPLAHMFERVIQSVVYCHGGRVGFFQ 357
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTA-LPLYHIFALTVNCLLFIELGGQNLLI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 GDIRLLSDDMKALcpTIFPVVprllnrmydkifcqADTPVKRWFlefaakrkQAEVrsgiirNDSIWDELFFNKIQASLG 437
Cdd:PRK08974 283 TNPRDIPGFVKEL--KKYPFT--------------AITGVNTLF--------NALL------NNEEFQELDFSSLKLSVG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 438 GcvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPLPCNHIKLVDiEELNYWTC 514
Cdd:PRK08974 333 G--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPP 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 515 KGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEP 594
Cdd:PRK08974 402 GEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPK 479
|
330 340
....*....|....*....|...
gi 1333574464 595 VAQIY-------VHGDSLKAFLV 610
Cdd:PRK08974 480 VLEVAavgvpseVSGEAVKIFVV 502
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
281-611 |
1.06e-30 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 123.38 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprqDDVLISFLPLAHMFErviqsvvYCHGGRVGFFQ 357
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLraaAAWADCADLTE-------DDRYLIINPFFHTFG-------YKAGIVACLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 GdirllsddmkalcPTIFPV----VPRLLNRMY-DKIFCQADTPVKRWFLEFAAKRKQAEVRSgiirndsiwdelffnki 432
Cdd:cd17638 67 G-------------ATVVPVavfdVDAILEAIErERITVLPGPPTLFQSLLDHPGRKKFDLSS----------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 qaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDiee 508
Cdd:cd17638 117 -------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 509 lnywtckgEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 588
Cdd:cd17638 186 --------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGA 256
|
330 340 350
....*....|....*....|....*....|
gi 1333574464 589 YIRSEPVAQIYV-------HGDSLKAFLVG 611
Cdd:cd17638 257 LAEHPGVAQVAVigvpderMGEVGKAFVVA 286
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-706 |
1.63e-30 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 129.20 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 89 ARTMYEVFRRGLSISGNGPCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACY 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 169 TYSMVVVPLydtLGPG-AIRYIINTADISTVIVDKPQKAVLLLEHVERKETpglklIILMEPFEEALKDR-GQECGVVIK 246
Cdd:PTZ00297 504 LYGFTTLPL---VGKGsTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAvARDLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 247 SMQTIEdcgQRNHRVPVvsssasgsllskPPKPSDLSIVCFT-------SGTTGNPKGAMLTHGNVVADFSgFLKVTEKV 319
Cdd:PTZ00297 576 PYEFVE---QKGRLCPV------------PLKEHVTTDTVFTyvvdnttSASGDGLAVVRVTHADVLRDIS-TLVMTGVL 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 320 IFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGffQGDIRLLSDDMKALCPTIFPVVPRLL--NRMYDKIFCQADTPV 397
Cdd:PTZ00297 640 PSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFstSRLQLSRANERYSAV 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 398 KRWFLEfaakrKQAEVRSGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTV-----LGFLRAALGCQVYe 468
Cdd:PTZ00297 718 YSWLFE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREVF- 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 469 gygQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDIEELNYWTCKGEGEICVKGpnvfkgylkDPDRTKEAldsdgwl 548
Cdd:PTZ00297 792 ---FLPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 549 htgdIGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKR 627
Cdd:PTZ00297 843 ----AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSH 917
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 628 GIEG--------TYVELCtnRELKKAILEDMVSLGKEGGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKK 699
Cdd:PTZ00297 918 CMGEgggparqlGWTELV--AYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSS 995
|
....*..
gi 1333574464 700 QIEDLYS 706
Cdd:PTZ00297 996 VIERFYS 1002
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
281-618 |
8.65e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 122.79 E-value: 8.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpRQDDVLISFLPLAHM---FERVIQSVVycHGGRV---- 353
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLT--FAGYYSARRFGL--GEDDVYLTVLPLFHInaqAVSVLAALS--VGATLvllp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 ----GFFQGDIRllsdDMKALCPTIFPVVPRLLnrmydkifcqADTPVKrwflefaAKRKQAEVRsgiirndsiwdelff 429
Cdd:cd05934 156 rfsaSRFWSDVR----RYGATVTNYLGAMLSYL----------LAQPPS-------PDDRAHRLR--------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 430 nkiqaslggcvrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIEel 509
Cdd:cd05934 200 --------------AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 510 NYWTCKGE-GEICVK---GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKI 585
Cdd:cd05934 264 GQELPAGEpGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEV 341
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1333574464 586 ENIYIRSEPVAQIYVHG-------DSLKAFlvgIVVPDPE 618
Cdd:cd05934 342 ERAILRHPAVREAAVVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
287-617 |
1.13e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 120.85 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 287 FTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEkvifprqDDVLISFLPLAHMFERVIqSVVYC--HGGRVGFFQgdir 361
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTE-------QDRLCIPVPLFHCFGSVL-GVLACltHGATMVFPS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 362 lLSDDMKAL--------CPTIFPVvPRllnrMYDKIFCQADtpvkrwFLEFAAKRkqaeVRSGIIrndsiwdelffnkiq 433
Cdd:cd05917 77 -PSFDPLAVleaiekekCTALHGV-PT----MFIAELEHPD------FDKFDLSS----LRTGIM--------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 aslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKLVDIEel 509
Cdd:cd05917 126 ------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVDPE-- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 510 nywTCK----GE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEK 584
Cdd:cd05917 192 ---GGIvppvGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPRE 267
|
330 340 350
....*....|....*....|....*....|...
gi 1333574464 585 IENIyirsepvaqIYVHGDSLKAFLVGivVPDP 617
Cdd:cd05917 268 IEEF---------LHTHPKVSDVQVVG--VPDE 289
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
220-590 |
5.03e-29 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 122.01 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 220 GLKLIILMEPFEEALKDRGQECGVVIksmQTIEDCGQRNHRVPVVSSSASGSLLSKPPKPSDLSIVCFTSGTTGNPKGAM 299
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTV---VTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVM 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 300 LTHGNVVADfsgflkVTEKV------IFPRQDDVLISFLPLAHMFErvIQSVVYChGGRVG--------FfqgDIRLLSD 365
Cdd:PLN02246 199 LTHKGLVTS------VAQQVdgenpnLYFHSDDVILCVLPMFHIYS--LNSVLLC-GLRVGaailimpkF---EIGALLE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 366 DMKALCPTIFPVVPrllnrmydkifcqadtPVkrwFLEFAakrKQAEVRSgiirndsiwDELffnkiqASlggcVRMIVT 445
Cdd:PLN02246 267 LIQRHKVTIAPFVP----------------PI---VLAIA---KSPVVEK---------YDL------SS----IRMVLS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 446 GAAPASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDIE---ELNYWT 513
Cdd:PLN02246 306 GAAPLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtgaSLPRNQ 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333574464 514 CkgeGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 590
Cdd:PLN02246 383 P---GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
275-619 |
5.60e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 122.05 E-value: 5.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 275 KPPK--PSDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKvtekvifPRQDDVLISF--LPLAHMFERVI 342
Cdd:PRK07059 197 KPVKlgPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYHIFALTV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 343 QSVVYCHGGRVGFF---QGDIRLLSDDMKALCPTIFPVVPRLLNRMYdkifcqadtpvkrwflefaakrkqaevrsgiir 419
Cdd:PRK07059 270 CGLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL--------------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 420 NDSIWDELFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLP 497
Cdd:PRK07059 317 NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 498 CNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQG 577
Cdd:PRK07059 388 STEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSG 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1333574464 578 EYVAPEKIENIyIRSEP----VAQIYVH----GDSLKAFlvgIVVPDPEV 619
Cdd:PRK07059 466 FNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-622 |
1.42e-28 |
|
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: 119.55 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACY----TYsmvvVPLYDTLGPGAIRYIINTADIS 196
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 197 TVIVDkpqkavlllehverketpglkliilmepfeealkdrgqecgvviksmqtiedcgqrnhrvpvvsssasgsllskp 276
Cdd:cd05930 87 LVLTD--------------------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 pkPSDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHG 350
Cdd:cd05930 92 --PDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdvsvweIF------GALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 351 GRVGFFQGDIRLLSDDMKALC----PTIFPVVPRLLNrmydkifcqadtpvkrwflefaakrkqaevrsgiirndsiwde 426
Cdd:cd05930 160 ATLVVLPEEVRKDPEALADLLaeegITVLHLTPSLLR------------------------------------------- 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 427 LFFNKIQASLGGCVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHI 501
Cdd:cd05930 197 LLLQELELAALPSLRLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 502 KLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEA-----LDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLA 575
Cdd:cd05930 277 YVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR 355
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1333574464 576 qGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 622
Cdd:cd05930 356 -GYRIELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-618 |
1.72e-28 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 120.32 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 122 SYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLgpgAIRYIINTADIST-VIV 200
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPQKAVLLLEHVERKeTPGLKLIILMEPFEEalkdrgqecgvvIKSMQTIEDCGQRNhrvpvvSSSASGSLLSKPP--- 277
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKED------------YKGYQCLYTFITQN------LPPGFNEYDFKPPsfd 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTEKVIF---PRQDDVLISFLPLAHMFERVIQSVVYCHGGRVG 354
Cdd:cd17642 182 RDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSH----ARDPIFgnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 ffqgdirllsddmkalcptifpvvprLLNRMYDKIFCQA--DTPVKRWFL-----EFAAKrkqaevrSGIIrndsiwdel 427
Cdd:cd17642 258 --------------------------LMYKFEEELFLRSlqDYKVQSALLvptlfAFFAK-------STLV--------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 428 ffNKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDI 506
Cdd:cd17642 296 --DKYDLS---NLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 EELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIE 586
Cdd:cd17642 371 DTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELE 449
|
490 500 510
....*....|....*....|....*....|..
gi 1333574464 587 NIYIRSEPVAQIYVHGdslkaflvgivVPDPE 618
Cdd:cd17642 450 SILLQHPKIFDAGVAG-----------IPDED 470
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-600 |
2.20e-28 |
|
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: 118.14 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 122 SYQEVADRAEFLGSGLLQHnCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVIV 200
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPqkavllleHVERKETPGLKLIILMEPFEEALKDRGQEcgvviksmqtiedcgqrnhrvpvvsssasgSLLSKPPKPS 280
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAALDDAPAP------------------------------PPPDAPSGPD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAH------MFerviqsVVYCHGGRVg 354
Cdd:TIGR01733 121 DLAYVIYTSGSTGRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSFdasveeIF------GALLAGATL- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 ffqgdirllsddmkalcptifpVVPRllnrmydkifcqaDTPVKRWFLEFAAKRKQAEVrsgiirndSIWDEL--FFNKI 432
Cdd:TIGR01733 190 ----------------------VVPP-------------EDEERDDAALLAALIAEHPV--------TVLNLTpsLLALL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 QASLGGC---VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKL 503
Cdd:TIGR01733 227 AAALPPAlasLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 504 VDiEELN---YWtckGEGEICVKGPNVFKGYLKDPDRTKEA-LDSDGWL-------HTGDIGKWLPAGTLKIIDRKKHIF 572
Cdd:TIGR01733 307 LD-DDLRpvpVG---VVGELYIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQV 382
|
490 500
....*....|....*....|....*...
gi 1333574464 573 KLaQGEYVAPEKIENIYIRSEPVAQIYV 600
Cdd:TIGR01733 383 KI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
117-569 |
1.80e-27 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 117.38 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 117 PYQWLSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNRpEWIIAELACYTYSMVVVPLydtlGPGAIRyiintadis 196
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTY--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 197 tvivDKPQKAVLLLEHVerKETPGLKLII----LMEPFEEALKDRGqECGVVIKSMQTIEDCGqRNHRVPvvsssasgsl 272
Cdd:cd05906 101 ----DEPNARLRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSG-LPGIRVLSIEELLDTA-ADHDLP---------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 273 lskPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflKVTEKVIFPrqDDVLISFLPLAHmfervIQSVVYCHggr 352
Cdd:cd05906 163 ---QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH-----VGGLVELH--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 vgffQGDIRLLSDDMKALCPTIFPVVPRLLNRMyDKIfcQADtpvKRW---FLeFAAKRKQAEVRSgiirnDSIWDelff 429
Cdd:cd05906 228 ----LRAVYLGCQQVHVPTEEILADPLRWLDLI-DRY--RVT---ITWapnFA-FALLNDLLEEIE-----DGTWD---- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 430 nkiqasLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLP 497
Cdd:cd05906 288 ------LSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIP 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333574464 498 CNHIKLVDIEElnywTCKGEGEIC---VKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKIIDRKK 569
Cdd:cd05906 362 GVSMRIVDDEG----QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
276-618 |
2.20e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 116.44 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSD-LSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlKVTEKVifprqdDVLISFLPLAHMFERV--IQSV--VYCHG 350
Cdd:PRK09088 130 PSIPPErVSLILFTSGTSGQPKGVMLSERNLQQTAHNF-GVLGRV------DAHSSFLCDAPMFHIIglITSVrpVLAVG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 351 GRV----GFFQG-DIRLLSDdmKALCPTIFPVVPRLLNRmydkifcqadtpvkrwflefaakrkqaevrsgiIRNDSIWD 425
Cdd:PRK09088 203 GSIlvsnGFEPKrTLGRLGD--PALGITHYFCVPQMAQA---------------------------------FRAQPGFD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 426 ELFFNKIQAslggcvrmIVTGAAP-ASPTVLGFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCN 499
Cdd:PRK09088 248 AAALRHLTA--------LFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 500 HIKLVDIEELNywtCK-GE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQG 577
Cdd:PRK09088 316 QTRVVDDQGND---CPaGVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGG 391
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1333574464 578 EYVAPEKIEniyirsepvAQIYVHGDSLKAFLVGivVPDPE 618
Cdd:PRK09088 392 ENVYPAEIE---------AVLADHPGIRECAVVG--MADAQ 421
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
277-625 |
4.40e-27 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 114.37 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 PKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEkvifprqDDVLISFLPLAHM--FERVIQSVVYchGG 351
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTE-------DDNWLCALPLFHIsgLSILMRSVIY--GM 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 352 RVGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYDKifcqadtpvkrwflefaakrkqaevrsgiirndsiwdelFFN 430
Cdd:cd05912 145 TVYLVDKfDAEQVLHLINSGKVTIISVVPTMLQRLLEI---------------------------------------LGE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 431 KIQASLggcvRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDIE 507
Cdd:cd05912 186 GYPNNL----RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 508 ELNYwtckGEGEICVKGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 587
Cdd:cd05912 260 QPPY----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEE 333
|
330 340 350
....*....|....*....|....*....|....*...
gi 1333574464 588 IYIRSEPVAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 625
Cdd:cd05912 334 VLLSHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
280-600 |
4.81e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 116.23 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 280 SDLSIVCFTSGTTGNPKGAMLTHGNVVADF-SGFLKVTEKVIfprQDDVLISFLPLAHMF--ERVIQSVVYCHGGRVGFF 356
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRNLVANLcSSLFSVGPEMI---GQVVTLGLIPFFHIYgiTGICCATLRNKGKVVVMS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 357 QGDIRLLSDDMKALCPTIFPVVPRLLNRMydkifcqadtpVKrwflefaakrkqaevrsgiirnDSIWDELFFNKIQasl 436
Cdd:PLN02330 261 RFELRTFLNALITQEVSFAPIVPPIILNL-----------VK----------------------NPIVEEFDLSKLK--- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 437 ggcVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDIEE 508
Cdd:PLN02330 305 ---LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 509 LNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENI 588
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 1333574464 589 YIRSEPVAQIYV 600
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-602 |
5.03e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 116.03 E-value: 5.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVV---PLYDT------LGPGAIRYII- 190
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQP--GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRAseleyaLGQSGVRWVIc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 191 ----NTADISTVIVD-KPQKAVLLLEHVERKETPGLKLIILMEPFE-------EALKDRGQecGVvikSMQTIEDCGQRN 258
Cdd:PRK12583 124 adafKTSDYHAMLQElLPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARGE--TV---SREALAERQASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 259 HRVPVVSssasgsllskppkpsdlsiVCFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTEKvifprqdDVLISFLPLA 335
Cdd:PRK12583 199 DRDDPIN-------------------IQYTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 336 HMFERVIqSVVYC--HGGRVGF----FQGDIRLLSDDMKAlCPTIFPVvPRLLnrmydkiFCQADTPVKRWFlEFAAkrk 409
Cdd:PRK12583 253 HCFGMVL-ANLGCmtVGACLVYpneaFDPLATLQAVEEER-CTALYGV-PTMF-------IAELDHPQRGNF-DLSS--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 410 qaeVRSGIIrndsiwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-- 486
Cdd:PRK12583 319 ---LRTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdl 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 487 ---WTSghVGAPLPCNHIKLVDIEELNywTCKGE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTL 562
Cdd:PRK12583 369 errVET--VGRTQPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYV 444
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1333574464 563 KIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 602
Cdd:PRK12583 445 RIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
93-556 |
7.04e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 115.59 E-value: 7.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 93 YEVFRRGLSISGNGPCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHnckactdqfiGV--------FAQNRPEWIIAE 164
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL----------GVkkgdrvaiYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 165 LACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD----KPQKAVLLLEHVE--RKETPGLKLIIL---------ME- 228
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVvgrtgadvpMEg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 229 --PFEEALKDRGQECgvviksmqtieDCgqrnhrVPVvsssasgsllskppKPSDLSIVCFTSGTTGNPKGAMLTHGNVV 306
Cdd:COG0365 162 dlDWDELLAAASAEF-----------EP------EPT--------------DADDPLFILYTSGTTGKPKGVVHTHGGYL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 307 adfsGFLKVTEKVIF-PRQDDVL--------------ISFLPLAH-----MFERVIqsvVYCHGGRvgFFQgdirlLSDD 366
Cdd:COG0365 211 ----VHAATTAKYVLdLKPGDVFwctadigwatghsyIVYGPLLNgatvvLYEGRP---DFPDPGR--LWE-----LIEK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 367 MKalcPTIFPVVPRLLNRMydkifcqadtpvKRWFLEFAAKRKQAevrsgiirndsiwdelffnkiqaSLggcvRMIVTG 446
Cdd:COG0365 277 YG---VTVFFTAPTAIRAL------------MKAGDEPLKKYDLS-----------------------SL----RLLGSA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 447 AAPASPTVLGFLRAALGCQVYEGYGQTECtaGCTFTTPGDWTS---GHVGAPLPCNHIKLVDiEELNywTCKG--EGEIC 521
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVVD-EDGN--PVPPgeEGELV 389
|
490 500 510
....*....|....*....|....*....|....*....
gi 1333574464 522 VKG--PNVFKGYLKDPDRTKEAL--DSDGWLHTGDIGKW 556
Cdd:COG0365 390 IKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARR 428
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
276-617 |
7.57e-27 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 114.97 E-value: 7.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGN------VVADFSGFlkvtekvifpRQDDVLISFLPLAH---MFerVIQSVV 346
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNllsnalTLVDYWRF----------TPDDVLIHALPIFHthgLF--VATNVA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 347 YCHGGRVGFFQgdiRLLSDDMKALCP--TIFPVVPRLLNRMYDKifcqadtpvkRWFLEFAAKRkqaevrsgiirndsiw 424
Cdd:PRK07514 220 LLAGASMIFLP---KFDPDAVLALMPraTVMMGVPTFYTRLLQE----------PRLTREAAAH---------------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 425 delffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNHIK 502
Cdd:PRK07514 271 ---------------MRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 503 LVDIE---ELNywtcKGE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIfkLAQGE 578
Cdd:PRK07514 334 VTDPEtgaELP----PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGG 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1333574464 579 Y-VAPEKIENiYIRSEP-VAQIYVHGDSLKAF---LVGIVVPDP 617
Cdd:PRK07514 408 YnVYPKEVEG-EIDELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-600 |
1.66e-26 |
|
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: 113.24 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIstviv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 dkpqkavlllehverketpglKLIILMEPFeealkdrgqecgvviksmqtiedcGQRNHRvpvvsssasgsllskpPKPS 280
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPA----------------AMPD 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISfLPLAHmferviqsvvycHGGRVGFFqgdi 360
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAH------------QTGFVYGF---- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 361 rllsddmkaLCPTIFPVvPRLLNRMYDK------------IFCQADTPvkrwFLE--FAAKRKQAEVRSGIirndsiwde 426
Cdd:cd05903 154 ---------TLPLLLGA-PVVLQDIWDPdkalalmrehgvTFMMGATP----FLTdlLNAVEEAGEPLSRL--------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 427 lffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIK 502
Cdd:cd05903 211 --------------RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIK 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 503 LVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAP 582
Cdd:cd05903 275 VVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPV 351
|
490
....*....|....*...
gi 1333574464 583 EKIENIYIRSEPVAQIYV 600
Cdd:cd05903 352 LEVEDLLLGHPGVIEAAV 369
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
281-610 |
1.74e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 114.53 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKV------IFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVG 354
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqpLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 FFQGDIRLLSDDMKALCPTIFPVVPRLlNRMydkifcqadtpvkrwfleFAAKRKQAEVRSgiirndsiwdeLFFNKIQA 434
Cdd:PRK12492 288 VLITNPRDIPGFIKELGKWRFSALLGL-NTL------------------FVALMDHPGFKD-----------LDFSALKL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 435 SLGGcvrmivtGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDIE--ELNY 511
Cdd:PRK12492 338 TNSG-------GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVIDDDgnELPL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 512 wtckGE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 590
Cdd:PRK12492 410 ----GErGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVM 484
|
330 340
....*....|....*....|....*..
gi 1333574464 591 RSEPVAQIYV-------HGDSLKAFLV 610
Cdd:PRK12492 485 AHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
275-586 |
2.01e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 115.79 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 275 KPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDDVLISFLPLAHMFerviqsvvychGGRVG 354
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSF-----------GLTVT 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 FFqgdIRLLSDdMKALC---PTIFPVVPRLLNRMYDKIFCQADTpvkrwFLEFAAKRKQAEvrsgiirndsiwDELFfnk 431
Cdd:PRK08633 842 LW---LPLLEG-IKVVYhpdPTDALGIAKLVAKHRATILLGTPT-----FLRLYLRNKKLH------------PLMF--- 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 432 iqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWT-----SGHVGAPLPCNHI 501
Cdd:PRK08633 898 --ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAV 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 502 KLVD---IEELNYWTckgEGEICVKGPNVFKGYLKDPDRTKEAL---DSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLA 575
Cdd:PRK08633 972 RIVDpetFEELPPGE---DGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG 1048
|
330
....*....|.
gi 1333574464 576 qGEYVAPEKIE 586
Cdd:PRK08633 1049 -GEMVPLGAVE 1058
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
89-569 |
6.79e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 113.13 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 89 ARTMYEVFRRGLSISGNGPCLgfrkpnqpyqwlSYQEVADR---------AEFLG-----SGLLqHNCKACTDQFIGVFA 154
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPAL------------SFLLDADPldrpetwtyAELLAdvtrtANLL-HSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 155 QNRPEWIIAELACYTYSmVVVPLYDTLGPGAIRYIINTADISTVIVDKP-------QKAVLLLEHVerketPGLKLIILM 227
Cdd:PRK07529 91 PNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 228 epfeeALKDRGQECGVVIKSMQtiedcgQRNHRVPVV-------SSSASGSLLSKPPKPSDLSIVCFTSGTTGNPKGAML 300
Cdd:PRK07529 165 -----DLARYLPGPKRLAVPLI------RRKAHARILdfdaelaRQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 301 THGNVVAD-FSGFLkvtekVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR---VGFFQG--DIRLLSDDMK---ALC 371
Cdd:PRK07529 234 THGNEVANaWLGAL-----LLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAhvvLATPQGyrGPGVIANFWKiveRYR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 372 PTIFPVVPRLLNRMydkifcqADTPVKRWFLefaakrkqaevrsgiirndsiwdelffnkiqaslgGCVRMIVTGAAPAS 451
Cdd:PRK07529 309 INFLSGVPTVYAAL-------LQVPVDGHDI-----------------------------------SSLRYALCGAAPLP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 452 PTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDIEEL-NYWT-C-KGE-GEICVKGPN 526
Cdd:PRK07529 347 VEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLRdCaVDEvGVLCIAGPN 426
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1333574464 527 VFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK 569
Cdd:PRK07529 427 VFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-627 |
7.36e-26 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 111.61 E-value: 7.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 119 QWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 197
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 198 VIVDkpqkavlllehverketpglkliilmepfeEALKDRGQECGVVIksmqtiEDCGQRNHRVPVVSSSasgsllskPP 277
Cdd:cd12116 88 VLTD------------------------------DALPDRLPAGLPVL------LLALAAAAAAPAAPRT--------PV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVL--------IS----FLPLahmferviqsv 345
Cdd:cd12116 124 SPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM---RERLGLGPGDRLLavttyafdISllelLLPL----------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 346 vyCHGGRVGFFQGDI----RLLSDDMKALCPTIFpvvprllnrmydkifcQAdTPVKrWFLEFAAKrkqaevrsgiirnd 421
Cdd:cd12116 190 --LAGARVVIAPRETqrdpEALARLIEAHSITVM----------------QA-TPAT-WRMLLDAG-------------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 422 siWDELffnkiqASLggcvRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCN 499
Cdd:cd12116 236 --WQGR------AGL----TALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANT 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 500 HIKLVDiEELNYwTCKGE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTLKIIDRKKHI 571
Cdd:cd12116 301 QVYVLD-AALRP-VPPGVpGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQ 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1333574464 572 FKLaQGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 627
Cdd:cd12116 379 VKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-588 |
2.89e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 110.61 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 113 KPNQPYQWlSYQEVADRAEFLGSGLLQHNCKACTdqfigVFAQNRPEW---IIAELACYTYSMVVVPLYDTLGPGAIRYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 190 INTADISTVIVDKPQKAV--LLLEHVERKETPGLKLIILMEPFEEALKDrgqecgvvIKSMQTIEDCGQRNHRVPVvsss 267
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--------LSLSQIIADYEPLTTAITT---- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 268 asgsllskppKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHmferviqSVVY 347
Cdd:PRK06087 185 ----------HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH-------ATGF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 348 CHGGRVGFFQGDIRLLSDDMKAlcptifPVVPRLLNRmyDKIFCQ-ADTPVkrwflefaakrkqaevrsgiirndsIWDE 426
Cdd:PRK06087 244 LHGVTAPFLIGARSVLLDIFTP------DACLALLEQ--QRCTCMlGATPF-------------------------IYDL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 427 LFFNKIQASLGGCVRMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHI 501
Cdd:PRK06087 291 LNLLEKQPADLSALRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 502 KLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVA 581
Cdd:PRK06087 367 KVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENIS 444
|
....*..
gi 1333574464 582 PEKIENI 588
Cdd:PRK06087 445 SREVEDI 451
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-627 |
3.01e-25 |
|
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: 109.11 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPQKavlllehverketpglkliilmepfeealkdrgqecgvviksmqtiedcgqrnhrvpvvsssasgsllskppkps 280
Cdd:cd05935 80 GSELD--------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHM--FERVIQSVVYCHGGRVGFFQG 358
Cdd:cd05935 85 DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARW 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DIRLLSDDMKALCPTIFPVVPRLLNrmydkifcqadtpvkrwflefaakrkqaevrsgiirndsiwDELFFNKIQASLGG 438
Cdd:cd05935 161 DRETALELIEKYKVTFWTNIPTMLV-----------------------------------------DLLATPEFKTRDLS 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 439 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIEELNYWTCKGEG 518
Cdd:cd05935 200 SLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVG 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 519 EICVKGPNVFKGYLKDPDRTKEALDSDG---WLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPV 595
Cdd:cd05935 280 EIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI 358
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1333574464 596 AQIYV-------HGDSLKAFLVgiVVP------DPEVMPSWAQKR 627
Cdd:cd05935 359 *EVCVisvpderVGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-618 |
4.84e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 110.05 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 112 RKPNQPYQW-----LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAI 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 187 RYIINTADISTVIV-----DKPQKAV--LLLEHV-------ERKETPGLKLIILMEpfEEALKDRGQECGVViksmqTIE 252
Cdd:PRK08314 101 AHYVTDSGARVAIVgselaPKVAPAVgnLRLRHVivaqysdYLPAEPEIAVPAWLR--AEPPLQALAPGGVV-----AWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 253 DCGQRNHRVPVVSssasgsllskpPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEKVifprqDDVLISF 331
Cdd:PRK08314 174 EALAAGLAPPPHT-----------AGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANaVGSVLWSNSTP-----ESVVLAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 332 LPLAHM--FERVIQSVVYChGGRVgffqgdirllsddmkalcpTIFPvvprllnrmydkifcqadtpvkRWFLEFAAkrk 409
Cdd:PRK08314 238 LPLFHVtgMVHSMNAPIYA-GATV-------------------VLMP----------------------RWDREAAA--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 410 QAEVRSGIirndSIWD-------ELFFN-KIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTF 481
Cdd:PRK08314 273 RLIERYRV----THWTniptmvvDFLASpGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTH 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 482 TTPGDWT-SGHVGAPLPCNHIKLVDIEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWL 557
Cdd:PRK08314 348 SNPPDRPkLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMD 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333574464 558 PAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPE 618
Cdd:PRK08314 428 EEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
259-622 |
6.13e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 108.92 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 259 HRVPVVSSSASGSLLSKPPkPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHMF 338
Cdd:PRK07787 108 PHVPVRLHARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHVH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 339 E---------RVIQSVVycHGGRvgfF--QGDIRLLSDDmkalcPTIFPVVPRllnrMYDKIfcqADTPVkrwflefAAK 407
Cdd:PRK07787 183 GlvlgvlgplRIGNRFV--HTGR---PtpEAYAQALSEG-----GTLYFGVPT----VWSRI---AADPE-------AAR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 408 rkqaevrsgiirndsiwdelffnkiqaSLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 487
Cdd:PRK07787 239 ---------------------------ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGER 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 488 TSGHVGAPLPCNHIKLVDiEELNYWTCKGE--GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKII 565
Cdd:PRK07787 291 RPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIV 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 566 DR------KKHIFKLAQGEyvapekIENIYIRSEPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 622
Cdd:PRK07787 370 GRestdliKSGGYRIGAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
275-590 |
8.95e-25 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 109.16 E-value: 8.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 275 KPP-KPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKV-TEKVIFPRQDDVLISFLPLAHMFerviqsvvychgGR 352
Cdd:PLN02574 192 KPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFeASQYEYPGSDNVYLAALPMFHIY------------GL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 VGFFQGDIRL-----------LSDDMKAL---CPTIFPVVPRLLNRmydkifcqadtpvkrwfLEFAAKRKQAEVRsgii 418
Cdd:PLN02574 260 SLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPILMA-----------------LTKKAKGVCGEVL---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 419 rndsiwdelffnkiqaslgGCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGAP 495
Cdd:PLN02574 319 -------------------KSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 496 LPCNHIKLVDIEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLa 575
Cdd:PLN02574 380 APNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY- 458
|
330
....*....|....*
gi 1333574464 576 QGEYVAPEKIENIYI 590
Cdd:PLN02574 459 KGFQIAPADLEAVLI 473
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
276-616 |
1.01e-24 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 107.78 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRV 353
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIfsTLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 gFFQGDIRLLSDDMKALcpTIFPVVPRLLnrmydkifcqadtpvkrwflefaakrkqaevrsGIIRNDSiwdelFFNkiq 433
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSIL---------------------------------STLSPQD-----FPN--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 aslggcVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDiEELNY 511
Cdd:cd17653 211 ------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD-ADLQP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 512 WTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKI 585
Cdd:cd17653 280 VPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350
....*....|....*....|....*....|....
gi 1333574464 586 ENIYIRSEPVAQ---IYVHGDSLKAFlvgiVVPD 616
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
278-618 |
1.35e-24 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 108.01 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkviFPRQDDVL----ISF-LPLAHMFerviqsVVYCHGG- 351
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG---LTSESRVLqfasYTFdVSILEIF------TTLAAGGc 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 352 --------RVGFFQGDIRllsdDMKALCPTIFPVVPRLLNRmydkifcqADTPvkrwflefaakrkqaevrsgiirndsi 423
Cdd:cd05918 175 lcipseedRLNDLAGFIN----RLRVTWAFLTPSVARLLDP--------EDVP--------------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 424 wdelffnkiqaslggCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC---- 498
Cdd:cd05918 216 ---------------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAtcwv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 499 ----NHIKLVDIeelnywtckGE-GEICVKGPNVFKGYLKDPDRTKEA-LDSDGWLH------------TGDIGKWLPAG 560
Cdd:cd05918 279 vdpdNHDRLVPI---------GAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDG 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333574464 561 TLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP-----VAQIYVH-GDSLKAFLVGIVVPDPE 618
Cdd:cd05918 350 SLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
121-625 |
1.53e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 108.15 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 195
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 196 STVIVDK---PQKAVLLLEHVerketPGLKLIILMEPFEEalkdrGQECGVVIKSMQTiedcgqrnhrVPVVSSSAsgsl 272
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD-----GVDLLAAAAKFGP----------APLVAAAL---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 273 lskppkPSDLSIVCFTSGTTGNPKGAMLTHGNVV-------ADFSgflkvtekviFPRQddvlISFL---PLAH----MF 338
Cdd:PRK06188 167 ------PPDIAGLAYTGGTTGKPKGVMGTHRSIAtmaqiqlAEWE----------WPAD----PRFLmctPLSHaggaFF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 339 ERVIQ---SVVYCHGgrvgfFqgdirllsdDMKALCPTI--------FpVVPRLLNRMYDkifcqadtpvkrwflefaak 407
Cdd:PRK06188 227 LPTLLrggTVIVLAK-----F---------DPAEVLRAIeeqritatF-LVPTMIYALLD-------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 408 rkQAEVRSgiiRNDSiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW 487
Cdd:PRK06188 272 --HPDLRT---RDLS------------SL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDH 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 488 TSGHV------GAPLPCNHIKLVDiEELNYwTCKGE-GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAG 560
Cdd:PRK06188 331 DPDDPkrltscGRPTPGLRVALLD-EDGRE-VAQGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDG 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333574464 561 TLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 625
Cdd:PRK06188 408 FYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
156-610 |
1.74e-24 |
|
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: 106.65 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllehverketpglkliilmepfeealk 235
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 236 drgqecgvviksmqtiedcgqrnhrvpvvsssasgsllskppkpSDLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGF 312
Cdd:cd05972 81 --------------------------------------------EDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYW 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 313 LKVTEKVIFPRQDD------VLISFL-PLAHMFerviqSVVYCHGGRVgffqgdirllsDDMKALcptifpvvpRLLNRM 385
Cdd:cd05972 117 LGLRPDDIHWNIADpgwakgAWSSFFgPWLLGA-----TVFVYEGPRF-----------DAERIL---------ELLERY 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 386 YDKIFCQADTPVKRWFLEFAAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAALGCQ 465
Cdd:cd05972 172 GVTSFCGPPTAYRMLIKQDLSSYKFSHLRL---------------------------VVSAGEPLNPEVIEWWRAATGLP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 466 VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDiEELNYWTCKGEGEICVKGPNV--FKGYLKDPDRTKEALd 543
Cdd:cd05972 225 IRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI- 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333574464 544 SDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 610
Cdd:cd05972 303 RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-618 |
3.35e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 106.87 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 119 QWLSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 199 IVDKPQKAVLLLehverketpgLKLIILMEPFeealkdrgqecgVVIKSMQTIEDCGQRNhrvpvvsssasgsllSKPPK 278
Cdd:PRK06839 105 FVEKTFQNMALS----------MQKVSYVQRV------------ISITSLKEIEDRKIDN---------------FVEKN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVvadfsgFLKVTEKV--IFPRQDDVLISFLPLAHMferviqsvvychgGRVGFF 356
Cdd:PRK06839 148 ESASFIICYTSGTTGKPKGAVLTQENM------FWNALNNTfaIDLTMHDRSIVLLPLFHI-------------GGIGLF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 357 QgdirllsddmkalCPTIFP----VVPRLLNrmydkifcqadtPVKRwfLEFAAKRKQAEVRSGIIRNDSIWDELFFNKI 432
Cdd:PRK06839 209 A-------------FPTLFAggviIVPRKFE------------PTKA--LSMIEKHKVTVVMGVPTIHQALINCSKFETT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 QASlggCVRMIVTGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDiEE 508
Cdd:PRK06839 262 NLQ---SVRWFYNGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-EN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 509 LNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENI 588
Cdd:PRK06839 335 KNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV 412
|
490 500 510
....*....|....*....|....*....|
gi 1333574464 589 yirsepvaqIYVHGDSLKAFLVGivVPDPE 618
Cdd:PRK06839 413 ---------INKLSDVYEVAVVG--RQHVK 431
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-705 |
7.39e-24 |
|
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: 106.36 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 107 PCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTY---SMVVVPLYDTLGp 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 184 gairyiintADISTvivdkpqkavllLEHVERKETPGLKLIILMEPFEEALKDRGQECGVVIKSMQTIEDCGQRnHRVPV 263
Cdd:cd05921 89 ---------QDLAK------------LKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAI-SFAEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 264 VSSSASGSLLSKPPK--PSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD---VLISFLPLAHMF 338
Cdd:cd05921 147 AATPPTAAVDAAFAAvgPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT-----YPFFGEeppVLVDWLPWNHTF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 339 --ERVIQSVVYcHGGRV---------GFFQGDIRLLSDDMkalcPTIFPVVPRllnrmydkifcqadtpvkrWFLEFAAK 407
Cdd:cd05921 222 ggNHNFNLVLY-NGGTLyiddgkpmpGGFEETLRNLREIS----PTVYFNVPA-------------------GWEMLVAA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 408 rkqaevrsgiIRNDSIWDELFFNKiqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTECTAGCTF 481
Cdd:cd05921 278 ----------LEKDEALRRRFFKR--------LKLMFYAGAGLSQDVWDRLQAlavaTVGERIpmMAGLGATETAPTATF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 482 TTPGDWTSGHVGAPLPCNHIKLVdieelnywTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL---- 557
Cdd:cd05921 340 THWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpdd 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 558 PAGTLKIIDRKKHIFKLAQGEYVA--PekieniyIRSEPVAQI--YVHgDSL-----KAFLVGIVVPDPevmPSWAQKRG 628
Cdd:cd05921 412 PAKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALVFPDL---LACRRLVG 480
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333574464 629 IEGTYVELCTNRELKKAILEDMVSLGKEGGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEDLY 705
Cdd:cd05921 481 LQEASDAEVLRHAKVRAAFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLY 557
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
121-602 |
1.75e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 104.66 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DkpqkavlllEHVERKETPGLKLIilmepFEEALKDRGQEcgVVIKSMQTIEDcgqrnhrvpvvsssasgsllskppkps 280
Cdd:PRK03640 106 D---------DDFEAKLIPGISVK-----FAELMNGPKEE--AEIQEEFDLDE--------------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 dLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEKvifprqDDVLISfLPLAHM--FERVIQSVVYchGGRV-- 353
Cdd:PRK03640 143 -VATIMYTSGTTGKPKGVIQTYGNHWWSAVGSalnLGLTED------DCWLAA-VPIFHIsgLSILMRSVIY--GMRVvl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 --GFFQGDI-RLLSDDMKalcpTIFPVVPRLLNRMYdkifcqADTPVKRWflefaakrkqaevrsgiirNDSiwdelffn 430
Cdd:PRK03640 213 veKFDAEKInKLLQTGGV----TIISVVSTMLQRLL------ERLGEGTY-------------------PSS-------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 431 kiqaslggcVRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDi 506
Cdd:PRK03640 256 ---------FRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 eELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIE 586
Cdd:PRK03640 323 -DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIE 399
|
490
....*....|....*.
gi 1333574464 587 NIYIRSEPVAQIYVHG 602
Cdd:PRK03640 400 EVLLSHPGVAEAGVVG 415
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-622 |
2.52e-23 |
|
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: 103.67 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 173 VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehverketpglkliiLMEPFEEALKDRGqECGVVIkSMQTIE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG----------------------AADRLRDALPASP-DPGTVL-DADGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 253 DCGQRNHRVPVVsssasgsllskppkPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEkvifprqDDVLI 329
Cdd:cd05922 104 AARASAPAHEVS--------------HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITA-------DDRAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 330 SFLPLAhmferviqsvvYCHGGRV---GFFQGDIRLLS----------DDMKALCPTIFPVVP---RLLNRMydkIFCQA 393
Cdd:cd05922 163 TVLPLS-----------YDYGLSVlntHLLRGATLVLTndgvlddafwEDLREHGATGLAGVPstyAMLTRL---GFDPA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 394 DTPVKRWFLEFAAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgfLRAAL-GCQVYEGYGQ 472
Cdd:cd05922 229 KLPSLRYLTQAGGRLPQETIAR------------------------------------------LRELLpGAQVYVMYGQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 473 TECTAGCTFTTPG--DWTSGHVGAPLPCNHIklvDIEELNYWTCK-GE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWL 548
Cdd:cd05922 267 TEATRRMTYLPPEriLEKPGSIGLAIPGGEF---EILDDDGTPTPpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVL 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333574464 549 HTGDIGkWLPA-GTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 622
Cdd:cd05922 344 HTGDLA-RRDEdGFLFIVGRRDRMIKLF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-562 |
4.26e-23 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 105.32 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 119 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELA------CYtysmvvVPLyDTLGPGA-IRYIIN 191
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 192 TADISTVIVDkpqkavlllehverketpglkliilmepfeEALKDRGQECGVVIKSMQTIEDCGQRNHRVPVvsssasgs 271
Cdd:COG1020 571 DAGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPV-------- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 272 llskPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprQDDVL----ISF--------LPLah 336
Cdd:COG1020 613 ----PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGP------GDRVLqfasLSFdasvweifGAL-- 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 337 mferviqsvvyCHGGRVGFFQGDIRLLSDDMKALC----PTIFPVVPRLLNRMYDkifcqadtpvkrwflefAAKRKQAE 412
Cdd:COG1020 681 -----------LSGATLVLAPPEARRDPAALAELLarhrVTVLNLTPSLLRALLD-----------------AAPEALPS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 413 VRsgiirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF--TTPGDWTSG 490
Cdd:COG1020 733 LR--------------------------LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGG 786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 491 HV--GAPLPCNHIKLVDiEELN---YWTCkgeGEICVKGPNVFKGYLKDPDRTKEA-----LDSDG--WLHTGDIGKWLP 558
Cdd:COG1020 787 SVpiGRPIANTRVYVLD-AHLQpvpVGVP---GELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLP 862
|
....
gi 1333574464 559 AGTL 562
Cdd:COG1020 863 DGNL 866
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
280-610 |
9.16e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 102.80 E-value: 9.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 280 SDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLKVTEKVIFPRQDDVLISFLPLAHMF-ERVIQSVVYCHGGRVGFF-Q 357
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSN--TLMGVQWLYNCKEGEEVVLGVLPFFHVYgMTAVMNLSIMQGYKMVLIpK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 GDIRLLSDDMKALCPTIFPVVPRLLNRMYDkifcqadTPVkrwflefaakRKQAEVRSgiirndsiwdelffnkiqaslg 437
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIYIALLN-------SPL----------LKEYDISS---------------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 438 gcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHIKLVDIEELNYW 512
Cdd:PRK06710 325 --IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEAMIMSLETGEAL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 513 TCKGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRS 592
Cdd:PRK06710 399 PPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYEH 476
|
330 340
....*....|....*....|....*
gi 1333574464 593 EPVAQIYV-------HGDSLKAFLV 610
Cdd:PRK06710 477 EKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-554 |
1.37e-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: 102.32 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 120 WLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDTLGPGA---IRYIINTADIS 196
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 197 TVIVDKPQKAvLLLEHVERKETPGLKLIILMEPFEEALKDRGQECGvviksmqtiedcgqrnhrvpvvsssasgsllskp 276
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPS---------------------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 PKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvteKVIFPRQDDVLISFLPLAH---MFERVIQSVVYchGGRV 353
Cdd:cd05931 146 PDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIR----RAYGLDPGDVVVSWLPLYHdmgLIGGLLTPLYS--GGPS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 ------GFFQGDIRLLsddmkalcptifpvvpRLLNRmYDKIFCQADTpvkrwF-LEFAAKRKQAEVRSGIirndsiwdE 426
Cdd:cd05931 220 vlmspaAFLRRPLRWL----------------RLISR-YRATISAAPN-----FaYDLCVRRVRDEDLEGL--------D 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 427 LffnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------D 486
Cdd:cd05931 270 L----------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 487 WTSGHV----------------GAPLPCNHIKLVDIEelnywTCK-----GEGEICVKGPNVFKGYLKDPDRTKE----- 540
Cdd:cd05931 336 ALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPE-----TGRelpdgEVGEIWVRGPSVASGYWGRPEATAEtfgal 410
|
490
....*....|....*
gi 1333574464 541 -ALDSDGWLHTGDIG 554
Cdd:cd05931 411 aATDEGGWLRTGDLG 425
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
287-581 |
1.46e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 102.65 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 287 FTSGTTGNPKGAMLTHGNVVADFSGFLKVtekVIFPRQDD-VLISFLPLAHMF-ERVIQSVVYCHGGR---------VGF 355
Cdd:PRK08180 216 FTSGSTGLPKAVINTHRMLCANQQMLAQT---FPFLAEEPpVLVDWLPWNHTFgGNHNLGIVLYNGGTlyiddgkptPGG 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 356 FQGDIRLLsddmKALCPTIFPVVPRLlnrmydkifcqadtpvkrWFLEFAAKRKQAEVRsgiirndsiwdELFFNKiqas 435
Cdd:PRK08180 293 FDETLRNL----REISPTVYFNVPKG------------------WEMLVPALERDAALR-----------RRFFSR---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 436 lggcVRMIVTGAAPASPTVLGFL----RAALGCQVY--EGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDieel 509
Cdd:PRK08180 336 ----LKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVP---- 407
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 510 nywtCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKIIDRKKHIFKLAQGEYVA 581
Cdd:PRK08180 408 ----VGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGRIAEDFKLSSGTWVS 479
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
283-617 |
5.42e-22 |
|
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: 100.40 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 283 SIVCFTSGTTGNPKGAMLTHgnvvadfsgflkvtekvifpRQddvlisflplahmfeRVIQSVVYCHGGRVGFFQGDirl 362
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSH--------------------RS---------------LVLHAMAALLTDGLGLSESD--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 363 lsddmkalcpTIFPVVPrllnrMYDkifcqadtpVKRWFLEFAA-----------KRKQAEVRSGIIRND---------S 422
Cdd:cd12119 208 ----------VVLPVVP-----MFH---------VNAWGLPYAAamvgaklvlpgPYLDPASLAELIEREgvtfaagvpT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 423 IWDELF--FNKIQASLGGCVRMIVTGAAPASPTVLGFlrAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHV-------- 492
Cdd:cd12119 264 VWQGLLdhLEANGRDLSSLRRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETSPLGTVARP---PSEHSnlsedeql 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 493 ------GAPLPCNHIKLVDIE--ELNyWTCKGEGEICVKGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKI 564
Cdd:cd12119 339 alrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTI 416
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1333574464 565 IDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVhgdslkaflvgIVVPDP 617
Cdd:cd12119 417 TDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
279-627 |
8.09e-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: 97.55 E-value: 8.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQsvvychgGRVGFFQG 358
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN----AWMLALNSLFDPDDVLLCGLPLFHVNGSVVT-------LLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DIRLLSDDMKALCPTIFPVVPRLlnrmydkifcqadtpVKRWFLEFaakrkqaevrsgIIRNDSIWDELFFNKIQASLGG 438
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKL---------------VERYRITS------------LSTVPTVYAALLQVPVNADISS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 439 cVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DIEELNYWTCK 515
Cdd:cd05944 123 -LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 516 GE--GEICVKGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 593
Cdd:cd05944 202 PDevGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1333574464 594 PVAQIYVHG--DSLKAFL-VGIV--VPDPEVMP----SWAQKR 627
Cdd:cd05944 280 AVAFAGAVGqpDAHAGELpVAYVqlKPGAVVEEeellAWARDH 322
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
281-618 |
9.85e-22 |
|
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: 96.96 E-value: 9.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVA---DFSGFLKVTEkvifprqDDVLISFLPLAHMFERVIQSVVYCHGGR---VG 354
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAanlQLIHAMGLTE-------ADVYLNMLPLFHIAGLNLALATFHAGGAnvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 FFQGDIRL-LSDDMKAlcpTIFPVVPRLLNRMYDkifcqadtpvkrwflefAAKRKQAEVRSgiIRNdsiwdelffnkiq 433
Cdd:cd17637 74 KFDPAEALeLIEEEKV---TLMGSFPPILSNLLD-----------------AAEKSGVDLSS--LRH------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 aslggcvrmiVTGAApaSPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDieELNYWT 513
Cdd:cd17637 119 ----------VLGLD--APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 514 CKGE-GEICVKGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRK--KHIFKlAQGEYVAPEKIENIYI 590
Cdd:cd17637 184 PAGEtGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVIL 261
|
330 340
....*....|....*....|....*...
gi 1333574464 591 RSEPVAQIYVHGdslkaflvgivVPDPE 618
Cdd:cd17637 262 EHPAIAEVCVIG-----------VPDPK 278
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
277-617 |
1.58e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 98.97 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 PKPSDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFLPLAHMferviqsvvychggrVGFF 356
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYAERLGL-GADDVILMASPMAHQ---------------TGFM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 357 QGDIRLLSDDMKALCPTIFPVVprllnRMYDKI------FCQADTPvkrwFLEFAAkRKQAEVRSGIirndsiwdelffn 430
Cdd:PRK13295 255 YGLMMPVMLGATAVLQDIWDPA-----RAAELIrtegvtFTMASTP----FLTDLT-RAVKESGRPV------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 431 kiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDIE 507
Cdd:PRK13295 312 ---SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDAD 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 508 --ELNYWTckgEGEICVKGPNVFKGYLKDPDRTkeALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKI 585
Cdd:PRK13295 384 gaPLPAGQ---IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEI 457
|
330 340 350
....*....|....*....|....*....|...
gi 1333574464 586 ENIYIRSEPVAQiyvhgdslkaflVGIV-VPDP 617
Cdd:PRK13295 458 EALLYRHPAIAQ------------VAIVaYPDE 478
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
121-618 |
2.31e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 98.57 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGA-GDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 dkpQKAVL-LLEHVeRKETPgLKLII-------------LMEPFEeaLKDRGQECGVVIKSMQTIEDCGQRnhrvpvvss 266
Cdd:PRK06178 137 ---LDQLApVVEQV-RAETS-LRHVIvtsladvlpaeptLPLPDS--LRAPRLAAAGAIDLLPALRACTAP--------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 267 sasgsLLSKPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPlahMFerviqsvv 346
Cdd:PRK06178 201 -----VPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVG---GEDSVFLSFLP---EF-------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 347 YCHGGRVGFfqgdirllsddmkalcptIFPvvprllnrmydkIFCQAdTPV--KRW----FLEFAAKRKqaeVRSGIIRN 420
Cdd:PRK06178 262 WIAGENFGL------------------LFP------------LFSGA-TLVllARWdavaFMAAVERYR---VTRTVMLV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 421 DSIwDELF---------FNKIQASlgGCVRMIvtgaAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFTTpGDWTSG 490
Cdd:PRK06178 308 DNA-VELMdhprfaeydLSSLRQV--RVVSFV----KKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA-GFQDDD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 491 H--------VGAPLPCNHIKLVDIEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTL 562
Cdd:PRK06178 380 FdllsqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFL 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 563 KIIDRKKHIFKLaQGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFLVGivVPDPE 618
Cdd:PRK06178 459 HYLGRRKEMLKV-NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
281-697 |
2.81e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 95.48 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHM--FERVIQSVVycHGGRVGFFQG 358
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG---LHSRLGFGGGDSWLLS-LPLYHVggLAILVRSLL--AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DiRLLSDDMKALCPTIFPVVPRLLNRMYDKIfcQADTPVKRwflefaakrkqaevrsgiirndsiwdelffnkiqaslgg 438
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDSG--QGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 439 cVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDieelnywtck 515
Cdd:cd17630 113 -LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE---------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 516 gEGEICVKGPNVFKGYLKDPdrTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepv 595
Cdd:cd17630 178 -DGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE--------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 596 AQIYVHGDSLKAFLVGivVPDPEvmpsWAQKrgIEGTYVelcTNRELKKAILEDMVSlgkeGGLHSFEQVKAIHIhsdmf 675
Cdd:cd17630 245 AALAAHPAVRDAFVVG--VPDEE----LGQR--PVAVIV---GRGPADPAELRAWLK----DKLARFKLPKRIYP----- 304
|
410 420
....*....|....*....|..
gi 1333574464 676 sVQNGLLTPTLKAKRPELREYF 697
Cdd:cd17630 305 -VPELPRTGGGKVDRRALRAWL 325
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
279-619 |
3.08e-21 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 97.32 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVAdFS----GFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVVYC--HGGr 352
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVS-FTnwmlSDFPLGP-------GDVFLNQAPFS--FDLSVMDLYPAlaSGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 vgffqgdirllsddmkalcpTIFPVvPRLLnrmydkifcQADtpVKRWFlEFAAKRKQAEVRSgiirNDSIWDELF---- 428
Cdd:cd05945 165 --------------------TLVPV-PRDA---------TAD--PKQLF-RFLAEHGITVWVS----TPSFAAMCLlspt 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 429 FNkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKL 503
Cdd:cd05945 208 FT--PESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 504 VDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSD---GWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYV 580
Cdd:cd05945 286 LD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRI 363
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1333574464 581 APEKIENIYIRSEPVAQIYV----HGDSlKAFLVGIVVPDPEV 619
Cdd:cd05945 364 ELEEIEAALRQVPGVKEAVVvpkyKGEK-VTELIAFVVPKPGA 405
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-627 |
1.23e-20 |
|
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: 95.86 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 111 FRKPNQPY-----QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA 185
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 186 -IRYIINTADISTVIVDKPQKAVLLlehverketpGLKLIILMEpfEEALKDRGQEcgvviksmqtiedcgqrNHRVPVv 264
Cdd:cd17655 85 rIQYILEDSGADILLTQSHLQPPIA----------FIGLIDLLD--EDTIYHEESE-----------------NLEPVS- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 265 sssasgsllskppKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekVIFPRQDDVL----ISF-LPLAHMFE 339
Cdd:cd17655 135 -------------KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKV---IYQGEHLRVAlfasISFdASVTEIFA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 340 RVIQSVVYCHGGRVGFFQGD-IRLLSDDMKALCPTIFPVVPRLLNRMYDKIFCqadtPVKRwflefaakrkqaevrsgii 418
Cdd:cd17655 199 SLLSGNTLYIVRKETVLDGQaLTQYIRQNRITIIDLTPAHLKLLDAADDSEGL----SLKH------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 419 rndsiwdelffnkiqaslggcvrMIVTGAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--G 493
Cdd:cd17655 256 -----------------------LIVGGEALSTELAKKIIeLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 494 APLPCNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDR 567
Cdd:cd17655 313 KPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGR 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333574464 568 KKHIFKLaQGEYVAPEKIENIYIRSEPVAQ---IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 627
Cdd:cd17655 392 IDHQVKI-RGYRIELGEIEARLLQHPDIKEavvIARKDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
276-610 |
1.27e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 95.90 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpRQDDVLISFLPLAHMFerviqsvvychggrvgf 355
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL--RDDDVYLTVMPAFHID----------------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 356 FQgdirlLSDDMKAlcptiFPVVPRLLnrMYDKifcqadtpvkrwfleFAAKRKQAEVRsgiirndsiwdelffnKIQAS 435
Cdd:PRK08008 228 CQ-----CTAAMAA-----FSAGATFV--LLEK---------------YSARAFWGQVC----------------KYRAT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 436 LGGCVRMIVTG--AAPASPT--------VLGFLRAA----------LGCQVYEGYGQTECTAGCTFTTPGD---WTSghV 492
Cdd:PRK08008 265 ITECIPMMIRTlmVQPPSANdrqhclreVMFYLNLSdqekdafeerFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--I 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 493 GAPLPCNHIKLVDieELNYWTCKGE-GEICVKG---PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRK 568
Cdd:PRK08008 343 GRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRR 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1333574464 569 KHIFKLAqGEYVAPEKIENIyIRSEP-VAQIYVHG--DSL-----KAFLV 610
Cdd:PRK08008 421 CNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
121-620 |
3.26e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 94.88 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVV---PLYDTlgpGAIRYIINTADIST 197
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEK-GDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 198 -VIVDK--------------PQKAVLLLEHVERKETPGLKLIILMepfeealkdrGQECGVVIKSMQTIEDCGQRNHRVP 262
Cdd:PRK08315 119 lIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFL----------GDEKHPGMLNFDELLALGRAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 263 VVSSSASGsllskppKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTEKVIFPRQDDVLISfLPLAHMFERVI 342
Cdd:PRK08315 189 LAARQATL-------DPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAMKLTEEDRLCIP-VPLYHCFGMVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 343 qSVVYC--HGgrvgffqgdirllsddmkalCPTIFPVV---PRLLNRMYDKIFCQADTPVKRWFLefaakrkqAEVrsgi 417
Cdd:PRK08315 258 -GNLACvtHG--------------------ATMVYPGEgfdPLATLAAVEEERCTALYGVPTMFI--------AEL---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 418 irndsiwDELFFNKIQASlggCVRmivTGAAPASPtvlgflraalgC------QVYE---------GYGQTECTAGCTFT 482
Cdd:PRK08315 305 -------DHPDFARFDLS---SLR---TGIMAGSP-----------CpievmkRVIDkmhmsevtiAYGMTETSPVSTQT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 483 TPGD------WTsghVGAPLPCNHIKLVDIEelnywTCK----GE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTG 551
Cdd:PRK08315 361 RTDDplekrvTT---VGRALPHLEVKIVDPE-----TGEtvprGEqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTG 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333574464 552 DIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP----EVM 620
Cdd:PRK08315 433 DLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VPDEkygeEVC 493
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
156-602 |
4.38e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 94.46 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 156 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehverketpglkliilMEPFEEALK 235
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA-----------------------LAPVATAVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 236 DRGQECGVVIKSMQTIEDcgqrnhrvPVVSSSASGSLLSKPPKPSDL-----SIVCFTSGTTGNPKGAMLTHGNVVADFS 310
Cdd:PRK07786 133 DIVPLLSTVVVAGGSSDD--------SVLGYEDLLAEAGPAHAPVDIpndspALIMYTSGTTGRPKGAVLTHANLTGQAM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 311 GFLKVTEkviFPRQDDVLISFLPLAHmfervIQSVvychGGRVGFFQGDIRLLSDDMKALCPTIFPVVprLLNRMYDKIF 390
Cdd:PRK07786 205 TCLRTNG---ADINSDVGFVGVPLFH-----IAGI----GSMLPGLLLGAPTVIYPLGAFDPGQLLDV--LEAEKVTGIF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 391 CqadTPVKrWFLEFAAKRKQAevrsgiiRNDSIwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAAL-GCQVYEG 469
Cdd:PRK07786 271 L---VPAQ-WQAVCAEQQARP-------RDLAL-----------------RVLSWGAAPASDTLLRQMAATFpEAQILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 470 YGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDiEELNYwTCKGE-GEICVKGPNVFKGYLKDPDRTKEALDSd 545
Cdd:PRK07786 323 FGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVAARVVD-ENMND-VPVGEvGEIVYRAPTLMSGYWNNPEATAEAFAG- 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1333574464 546 GWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 602
Cdd:PRK07786 399 GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-588 |
7.05e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 95.03 E-value: 7.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGsGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKP--QKAVL--LLEHVERketpGLKLIILmEPFEE----ALKDRGqecgvVIKSmqtiedcgqrnhRVPVVSSsasgsl 272
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYL-EDVRAqiglADKIKG-----LLAG------------RFPLVYF------ 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 273 lsKPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSgflKVTEKVIFPRQDDVLiSFLPLAHMFerviqsvvychggr 352
Cdd:PRK06814 788 --CNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRA---QVAARIDFSPEDKVF-NALPVFHSF-------------- 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 vGFFQGDIRLLSDDMKAL---CPTIFPVVPRLLnrmYD---KIFCQADTpvkrwFLefaakrkqaevrSGIIRNDSIWDe 426
Cdd:PRK06814 848 -GLTGGLVLPLLSGVKVFlypSPLHYRIIPELI---YDtnaTILFGTDT-----FL------------NGYARYAHPYD- 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 427 lFFNkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDI 506
Cdd:PRK06814 906 -FRS---------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPV 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 EELNywtcKGeGEICVKGPNVFKGYLK-DPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKI 585
Cdd:PRK06814 976 PGID----EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAV 1048
|
...
gi 1333574464 586 ENI 588
Cdd:PRK06814 1049 EEL 1051
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
281-622 |
3.19e-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: 90.98 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFP-RQDDVLISflpLAHMFerviqsVVYCHGGRVGF--FQ 357
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAH----RDPLLFADAMAREALGlTPGDRVFS---SAKMF------FGYGLGNSLWFplAV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 GDIRLLSDD----------MKALCPTIFPVVPRLLNRMYDkifcQADTPvkrwflefaakrkQAEVRSgiIRndsiwdel 427
Cdd:cd05919 159 GASAVLNPGwptaervlatLARFRPTVLYGVPTFYANLLD----SCAGS-------------PDALRS--LR-------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 428 ffnkiqaslggcvrmIVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKLV 504
Cdd:cd05919 212 ---------------LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVPGYEIRLV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 505 DiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEK 584
Cdd:cd05919 275 D-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVE 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1333574464 585 IENIYIRSEPVAQIYV----HGDSL---KAFlvgiVVPDPEVMPS 622
Cdd:cd05919 352 VESLIIQHPAVAEAAVvavpESTGLsrlTAF----VVLKSPAAPQ 392
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
279-630 |
7.11e-19 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 89.80 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGFlkvtekVIFPRQDDVLISFLPLAHMferviqsvvychGGRVG 354
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPF------NLFPRDGDLYWTPADWAWI------------GGLLD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 ffqgdirllsddmkALCPTIFPVVPRLLNRMY----DKIF-CQADTPVKRWFLEFAAKRkqaevrsgIIRNDSIWDELFF 429
Cdd:cd05971 149 --------------VLLPSLYFGVPVLAHRMTkfdpKAALdLMSRYGVTTAFLPPTALK--------MMRQQGEQLKHAQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 430 NKIQAslggcvrmIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPLPCNHIKLVDi 506
Cdd:cd05971 207 VKLRA--------IATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 EELNYWTCKGEGEICVKGPN--VFKGYLKDPDRTKEALDSDgWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEK 584
Cdd:cd05971 276 DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAE 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1333574464 585 IENIYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPEVMPSWAQKRGIE 630
Cdd:cd05971 354 IEECLLKHPAVLMAAVvgipdpiRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
287-617 |
1.66e-18 |
|
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: 89.28 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 287 FTSGTTGNPKGAMLTHGnvvadfSGFLKVTEKVIFPRQDD--VLISFLPLAHmferviqsvvyCHGGrvGFFQGdirlls 364
Cdd:cd12118 140 YTSGTTGRPKGVVYHHR------GAYLNALANILEWEMKQhpVYLWTLPMFH-----------CNGW--CFPWT------ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 365 ddMKALCPTIF---PVVPRLLnrmYDKI-------FCQADTpvkrwflefaakrkqaeVRSGIIRNDSIWdelffnkiQA 434
Cdd:cd12118 195 --VAAVGGTNVclrKVDAKAI---YDLIekhkvthFCGAPT-----------------VLNMLANAPPSD--------AR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 435 SLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKLVDI 506
Cdd:cd12118 245 PLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLEEV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 EELNYWTCK-----GE--GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEY 579
Cdd:cd12118 322 DVLDPETMKpvprdGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGEN 399
|
330 340 350
....*....|....*....|....*....|....*...
gi 1333574464 580 VAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 617
Cdd:cd12118 400 ISSVEVEGV---------LYKHPAVLEAAVVA--RPDE 426
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
279-602 |
3.09e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 88.70 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVAdfSGFLKVTekVIFPRQDDVLISFLPLAHMFErvIQSVVY------CHggr 352
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIV--QSLAKIA--IVGYGEDDVYLHTAPLCHIGG--LSSALAmlmvgaCH--- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 VGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrMYDKIfcqadtpvkrwflefaakrkqaevrsGIIRNDSIWDElffnki 432
Cdd:PLN02860 242 VLLPKFDAKAALQAIKQHNVTSMITVPAM---MADLI--------------------------SLTRKSMTWKV------ 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 qaslGGCVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SG 490
Cdd:PLN02860 287 ----FPSVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 491 H------VGAPLPcnHIKL-VDIEELNYwtckgEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLK 563
Cdd:PLN02860 359 HqpqgvcVGKPAP--HVELkIGLDESSR-----VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLW 431
|
330 340 350
....*....|....*....|....*....|....*....
gi 1333574464 564 IIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 602
Cdd:PLN02860 432 LIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
150-622 |
4.50e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 88.02 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlLLEHVERKET-PGLKLIILME 228
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA------DGPHDRAEPTtRWWPLTVNVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 229 PfeealkDRGQECGVViksMQTIEDCGQRNHRVPVVSSSasgsllskppKPSDLSIVcFTSGTTGNPKGAMLTHGNVVAD 308
Cdd:PRK05852 145 G------DSGPSGGTL---SVHLDAATEPTPATSTPEGL----------RPDDAMIM-FTGGTTGLPKMVPWTHANIASS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 309 FSGFlkVTEKVIFPRqdDVLISFLPLAH---MFERVIQSVVycHGGRV-----GFFQGdiRLLSDDMKALCPTIFPVVPr 380
Cdd:PRK05852 205 VRAI--ITGYRLSPR--DATVAVMPLYHghgLIAALLATLA--SGGAVllparGRFSA--HTFWDDIKAVGATWYTAVP- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 381 llnrmydkifcqadtPVKRWFLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRA 460
Cdd:PRK05852 276 ---------------TIHQILLERAATEPSGRKPAAL-----------------------RFIRSCSAPLTAETAQALQT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 461 ALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DIEELnywTCKGEGEICVKGPNVFK 529
Cdd:PRK05852 318 EFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPL---PAGAVGEVWLRGTTVVR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 530 GYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAF- 608
Cdd:PRK05852 393 GYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYg 470
|
490
....*....|....*.
gi 1333574464 609 --LVGIVVPDPEVMPS 622
Cdd:PRK05852 471 eaVAAVIVPRESAPPT 486
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
279-586 |
1.14e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 86.97 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISFLPLAH-MferviqsvvychgGRVGFfq 357
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGNLYANAEA---MFVAAEFDVETDVMVSWLPLFHdM-------------GMVGF-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 gdirlLSDDMKALC------PTIFPVVPRLLNRMYDKiFCQADTPVKRWFLEFAAKR--KQAEvrsgiirnDSIWDElff 429
Cdd:PRK07768 213 -----LTVPMYFGAelvkvtPMDFLRDPLLWAELISK-YRGTMTAAPNFAYALLARRlrRQAK--------PGAFDL--- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 430 nkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD------------- 486
Cdd:PRK07768 276 --------SSLRFALNGAEPIDPADVedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadlla 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 487 -------WTSGHV------GAPLPCNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLkDPDRTKEALDSDGWLHTGDI 553
Cdd:PRK07768 344 alrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDL 421
|
330 340 350
....*....|....*....|....*....|...
gi 1333574464 554 GKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIE 586
Cdd:PRK07768 422 GYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
280-653 |
1.14e-17 |
|
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: 85.00 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 280 SDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfprQDDVLISFLPLAHMFERV-IQSVVYCHGGRVGFfqG 358
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWV---VGDVTYLPLPATHIGGLWwILTCLIHGGLCVTG--G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DIRLLSDDMKAL---CPTIFPVVPRLLNRMYDKIFCQADTPVKRWFLEFAAKRkqaevrsgIIRNDSIWDELFFNkiqas 435
Cdd:cd17635 76 ENTTYKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR--------AIAADVRFIEATGL----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 436 lggcvrmivtgaapasptvlgflraalgCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDIEELNYWTc 514
Cdd:cd17635 143 ----------------------------TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 515 KGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEP 594
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAEGVSG 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333574464 595 V--AQIYVHGDSLKAFLVGIVVpdpeVMPSWAQKRGIEGtyVELCTNRELKKAILEDMVSL 653
Cdd:cd17635 272 VqeCACYEISDEEFGELVGLAV----VASAELDENAIRA--LKHTIRRELEPYARPSTIVI 326
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
276-617 |
1.70e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 86.09 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTekvifprQDDVLISFLPLAHMFERVIQSV-VYCHGG 351
Cdd:PRK06145 145 AVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLT-------ASERLLVVGPLYHVGAFDLPGIaVLWVGG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 352 RvgffqgdIRLLSD-DMKALCPTIfpvvprllnrMYDKIFCQADTPVKRWFLEFAAKRKQAEVrsgiirndsiwdelffn 430
Cdd:PRK06145 218 T-------LRIHREfDPEAVLAAI----------ERHRLTCAWMAPVMLSRVLTVPDRDRFDL----------------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 431 kiqASLGGCVrmivtGAAPASPT--VLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPcnHIKLVDI 506
Cdd:PRK06145 264 ---DSLAWCI-----GGGEKTPEsrIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALA--HVEIRIA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 EELNYWTCKG-EGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKI 585
Cdd:PRK06145 334 DGAGRWLPPNmKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEV 411
|
330 340 350
....*....|....*....|....*....|....*
gi 1333574464 586 EN-IYIRSE--PVAQIYVHGDSLKAFLVGIVVPDP 617
Cdd:PRK06145 412 ERvIYELPEvaEAAVIGVHDDRWGERITAVVVLNP 446
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-619 |
2.22e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 85.72 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGAIRYIINTAD 194
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 195 ISTVIVDkpqkavlllehverketpglkliilmepfeEALKDRGQECGVVIKSMQTIEDCGQRNHRVPVvsssasgslls 274
Cdd:cd12117 95 AKVLLTD------------------------------RSLAGRAGGLEVAVVIDEALDAGPAGNPAVPV----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 275 kppKPSDLSIVCFTSGTTGNPKGAMLTHGNV---VADfSGFLKVTEkvifprqDDVLISFLPL---AHMFErviqsvVY- 347
Cdd:cd12117 134 ---SPDDLAYVMYTSGSTGRPKGVAVTHRGVvrlVKN-TNYVTLGP-------DDRVLQTSPLafdASTFE------IWg 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 348 --CHGGRVgffqgdirllsddmkALCPTIFPVVPRLLnrmydkifcqadtpvkrwflefaakrkQAEVRSGIIrnDSIWd 425
Cdd:cd12117 197 alLNGARL---------------VLAPKGTLLDPDAL---------------------------GALIAEEGV--TVLW- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 426 eL---FFNKI----QASLGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV 492
Cdd:cd12117 232 -LtaaLFNQLadedPECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSI 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 493 --GAPLPcN--------HIKLVDIEELnywtckgeGEICVKGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKW 556
Cdd:cd12117 307 piGRPIA-NtrvyvldeDGRPVPPGVP--------GELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARW 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 557 LPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEV 619
Cdd:cd12117 378 LPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
279-618 |
2.33e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 85.44 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTEKVIFPRQDDVLISFLPLAHMFerviqSV-----VYCHGGRV 353
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVweiwgALLHGGRL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 GFFQGDIRLLSDDMkalcptifpvvPRLLNRMYDKIFCQadTPVKrwFLEFAakrkQAEVRsgiirndsiwdelfFNKIQ 433
Cdd:cd17643 163 VVVPYEVARSPEDF-----------ARLLRDEGVTVLNQ--TPSA--FYQLV----EAADR--------------DGRDP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 ASLggcvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLVD 505
Cdd:cd17643 210 LAL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVLD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 506 iEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGE 578
Cdd:cd17643 286 -ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGF 363
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1333574464 579 YVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 618
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-602 |
3.50e-17 |
|
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: 84.87 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 dkpqkavllleHVERKETPGLKLIILMEPFEEALKDRGQECgvviKSMQTIEDcgqrnhrvpvvsssasgsllsKPPKPS 280
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPE----SAGPLIED---------------------PPREPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHgNVVADFSGFLKVTEKVIFPRQDdVLISFLPLAHMferviqsvvychggrVGFFQgdi 360
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQ-RAAESRVLFMSTQAGLRHGRHN-VVLGLMPLYHV---------------IGFFA--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 361 rLLSDDMkALCPTIFPVvprllnrmydkifcQADTPVKrwflefAAKRKQAEVRSGIIRNDSIWDELFFNKIQASLG-GC 439
Cdd:cd05923 211 -VLVAAL-ALDGTYVVV--------------EEFDPAD------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 440 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVDI-EELNYWTCKG-E 517
Cdd:cd05923 269 LRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRIgGSPDEALANGeE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 518 GEICVK--GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 595
Cdd:cd05923 346 GELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGV 423
|
....*..
gi 1333574464 596 AQIYVHG 602
Cdd:cd05923 424 TEVVVIG 430
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-617 |
8.45e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 83.83 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKK-GDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DkpqkaVLLLEHVErketPGLKLIiLMEPFEEALKDRGQECGvviKSMQTIEDCGQRNHRVPVvsssasgsllSKPPKPS 280
Cdd:PRK08316 115 D-----PALAPTAE----AALALL-PVDTLILSLVLGGREAP---GGWLDFADWAEAGSVAEP----------DVELADD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFER--VIQSVVYCHGGRVGFFQG 358
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDM----SADDIPLHALPLYHCAQLdvFLGPYLYVGATNVILDAP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DIRLLSDDMKALCPTIFpvvprllnrmydkiFCqadtPVKRWFlefaakrkqaevrsGIIRNDSiwdelfFNKIQASlgg 438
Cdd:PRK08316 248 DPELILRTIEAERITSF--------------FA----PPTVWI--------------SLLRHPD------FDTRDLS--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 439 CVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDiEELNY 511
Cdd:PRK08316 287 SLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVD-DDGND 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 512 WTcKGE-GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIyi 590
Cdd:PRK08316 362 VA-PGEvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA-- 436
|
490 500
....*....|....*....|....*..
gi 1333574464 591 rsepvaqIYVHGDSLKAFLVGivVPDP 617
Cdd:PRK08316 437 -------LYTHPAVAEVAVIG--LPDP 454
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-621 |
1.05e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 83.47 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPQkavlllehvERKETPGLKLIILMEPFEEALKDRgqecgvviksmqtiedcgqrnhrVPVvsssasgsllskPPKPS 280
Cdd:cd12114 91 DGPD---------AQLDVAVFDVLILDLDALAAPAPP-----------------------PPV------------DVAPD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHG---NVVADFSGFLKVTEkvifprqDDVLISFLPLAHMFerviqSV-----VYCHGGR 352
Cdd:cd12114 127 DLAYVIFTSGSTGTPKGVMISHRaalNTILDINRRFAVGP-------DDRVLALSSLSFDL-----SVydifgALSAGAT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 VgffqgdirllsddmkalcptifpVVPRllnrmydkifCQADTPVKRWflefaakrKQAEVRSGIirndSIWdelffNKI 432
Cdd:cd12114 195 L-----------------------VLPD----------EARRRDPAHW--------AELIERHGV----TLW-----NSV 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 QASLGgcvrMIVTgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAGCTF----TTPGDWTS 489
Cdd:cd12114 225 PALLE----MLLD-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIWSIYhpidEVPPDWRS 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 490 GHVGAPLPCNHIKLVD--IEELNYWTckgEGEICVKGPNVFKGYLKDPDRTKEAL--DSDG--WLHTGDIGKWLPAGTLK 563
Cdd:cd12114 300 IPYGRPLANQRYRVLDprGRDCPDWV---PGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLE 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 564 IIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 621
Cdd:cd12114 377 FLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
433-617 |
1.40e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.53 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 QASLGGCVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------ 499
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 500 HIKLVDIEELNYWTC-------KGEGEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIF 572
Cdd:PLN03102 368 ILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1333574464 573 kLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGIvvPDP 617
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
279-627 |
1.78e-16 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 82.52 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqddvlISFLPLAHMferviqsvvychggRVGFFQG 358
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASF--------------SFDVFAG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DI--RLLSDDMKALCPTIFPVVPRLLNRMYDK--IFCQADTP-VKRWFLEFAAKRKQ--AEVRSGIIRNDSIWDElFFNK 431
Cdd:cd17650 152 DFarSLLNGGTLVICPDEVKLDPAALYDLILKsrITLMESTPaLIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQ-DFKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 432 IQASLGGCVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwtsghVGAPLPCNHIKLVDiEELNY 511
Cdd:cd17650 231 LAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 512 WTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKI 585
Cdd:cd17650 291 QPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEI 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1333574464 586 ENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEvmPSWAQKR 627
Cdd:cd17650 370 ESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
152-617 |
3.39e-16 |
|
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: 82.16 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 152 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKavlLLEHVE--RKETPGLKLIILMEP 229
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN---IPEEIEkaAPECPSKPKLVWVGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 230 FE-EALKDRGQECGVVIKSMQTIEDCGQrnhrvpvvsssasgsllskpPKPSDLSIVCFTSGTTGNPKgaMLTHgnvvaD 308
Cdd:cd05970 154 PVpEGWIDFRKLIKNASPDFERPTANSY--------------------PCGEDILLVYFSSGTTGMPK--MVEH-----D 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 309 FSgflkvtekvifprqddvlisfLPLAHmfervIQSVVYCHGGRvgffQGDIRLLSDDM---KAlcptifpvvprllnrM 385
Cdd:cd05970 207 FT---------------------YPLGH-----IVTAKYWQNVR----EGGLHLTVADTgwgKA---------------V 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 386 YDKIFCQ--ADTPV-----KRW----FLEFAAKRKQAE------VRSGIIRND-SIWDelfFNKIqaslggcvRMIVTGA 447
Cdd:cd05970 242 WGKIYGQwiAGAAVfvydyDKFdpkaLLEKLSKYGVTTfcapptIYRFLIREDlSRYD---LSSL--------RYCTTAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 448 APASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDIEELnywTCKG--EGEICV-- 522
Cdd:cd05970 311 EALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGR---SCEAgeEGEIVIrt 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 523 -KGPNV--FKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIY 599
Cdd:cd05970 387 sKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECA 464
|
490
....*....|....*...
gi 1333574464 600 VHGdslkaflvgivVPDP 617
Cdd:cd05970 465 VTG-----------VPDP 471
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-621 |
4.84e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 81.71 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTlgpgaiRYiiNTADISTvIV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV-NT------RY--RSHEVAH-IL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPQKAVLLLEhverketPGLKLIILMEPFEEALKD---RGQECGVVIKSMQTIED-CGQRNHRVPVVSSSASGSLLSKP 276
Cdd:PRK06164 104 GRGRARWLVVW-------PGFKGIDFAAILAAVPPDalpPLRAIAVVDDAADATPApAPGARVQLFALPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 PKPSDLSIVCFT-SGTTGNPK------GAMLTHGNVVADFSGFlkvtekvifpRQDDVLISFLPLahmferviqSVVYCH 349
Cdd:PRK06164 177 AADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF---------CGVFGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 350 GGRVGFFQGDIRLLSDDMKALCPTIfpvvpRLL-----------NRMYDKIFCQADTPVkrwflEFAAKRkqaevRSGIi 418
Cdd:PRK06164 238 STLLGALAGGAPLVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----LFGF- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 419 rndsiwdelffnkiqASLggcvrmivtgaAPASPTVLGFLRAAlGCQVYEGYGQTECTA---GCTFTTPgdWTSGHVGAP 495
Cdd:PRK06164 302 ---------------ASF-----------APALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPATDP--VSVRIEGGG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 496 LPCN---HIKLVDIEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIF 572
Cdd:PRK06164 353 RPASpeaRVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSL 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1333574464 573 KLAqGEYVAPEKIENIYIRSEPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 621
Cdd:PRK06164 433 RLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
276-628 |
8.43e-16 |
|
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: 80.85 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRV 353
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLA----NLVAWQARASSLGPGARTLQFAGLG--FDVSVQEIfsTLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 GFFQGDIRLLSDDMKALCptifpvvprllnrmydkifcqADTPVKRWFLEFAAKRKQAEVrsgiirndsiwdelffNKIQ 433
Cdd:cd17651 206 VLPPEEVRTDPPALAAWL---------------------DEQRISRVFLPTVALRALAEH----------------GRPL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 ASLGGCVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDiE 507
Cdd:cd17651 249 GVRLAALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLD-A 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 508 ELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 581
Cdd:cd17651 328 ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIE 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1333574464 582 PEKIENIYIRSEPVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKRG 628
Cdd:cd17651 407 LGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELRA 456
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-621 |
1.12e-15 |
|
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: 80.05 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DkpqkavlllehverketpglkliilmepfeealkdrgqecgvviksmqtiedcgqrnhrvpvvsssasgsllskppkPS 280
Cdd:cd12115 103 D-----------------------------------------------------------------------------PD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVA------------DFSGFLKVTEkVIFprqdDVLI--SFLPLahmferviqsvv 346
Cdd:cd12115 106 DLAYVIYTSGSTGRPKGVAIEHRNAAAflqwaaaafsaeELAGVLASTS-ICF----DLSVfeLFGPL------------ 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 347 yCHGGRVGFFQGDIRLLsdDMKALCP-TIFPVVPrllnrmydkifcqadtpvkrwflefaakrkqaevrsgiirndSIWD 425
Cdd:cd12115 169 -ATGGKVVLADNVLALP--DLPAAAEvTLINTVP------------------------------------------SAAA 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 426 ELF-FNKIQASlggcVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHI 501
Cdd:cd12115 204 ELLrHDALPAS----VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQA 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 502 KLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLa 575
Cdd:cd12115 280 YVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV- 357
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1333574464 576 QGEYVAPEKIENIYIRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 621
Cdd:cd12115 358 RGFRIELGEIEAALRSIPGVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
279-590 |
1.52e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 80.25 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviqsvvychggrvGFfqG 358
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS----PKEDDVMMSFLPPFHAY---------------GF--N 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DIRLLSddMKALCPTIF---PVVPRLLNRMYD--KIFCQADTPVkrwFLEF---AAKRKQA---EVRSGIIRNDSIWDEL 427
Cdd:PRK06334 241 SCTLFP--LLSGVPVVFaynPLYPKKIVEMIDeaKVTFLGSTPV---FFDYilkTAKKQESclpSLRFVVIGGDAFKDSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 428 FfnkiqaslggcvrmivTGAAPASPTVlgflraalgcQVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLV 504
Cdd:PRK06334 316 Y----------------QEALKTFPHI----------QLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 505 DiEELNYWTCKGE-GEICVKGPNVFKGYL-KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAP 582
Cdd:PRK06334 368 S-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSL 445
|
....*...
gi 1333574464 583 EKIENIYI 590
Cdd:PRK06334 446 EALESILM 453
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
287-580 |
2.11e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 80.09 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 287 FTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD----VLISFLPLAHM------FERVIQS--VVYCHGGR-- 352
Cdd:PRK12582 227 FTSGSTGMPKAVINTQRMMCANIAMQEQL-----RPREPDppppVSLDWMPWNHTmggnanFNGLLWGggTLYIDDGKpl 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 VGFFQGDIRLLSDdmkaLCPTIFPVVPRLLNRMYDKIfcQADTPVKRWFLefaaKRKQAEVRSGIIRNDSIWDelffnKI 432
Cdd:PRK12582 302 PGMFEETIRNLRE----ISPTVYGNVPAGYAMLAEAM--EKDDALRRSFF----KNLRLMAYGGATLSDDLYE-----RM 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 QAslggcvrmiVTGAAPASPTVLgflraalgcqvYEGYGQTEcTAGCTFTTpgDWTS---GHVGAPLPCNHIKLVDIEEl 509
Cdd:PRK12582 367 QA---------LAVRTTGHRIPF-----------YTGYGATE-TAPTTTGT--HWDTervGLIGLPLPGVELKLAPVGD- 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333574464 510 NYwtckgegEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL----PAGTLKIIDRKKHIFKLAQGEYV 580
Cdd:PRK12582 423 KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
276-606 |
2.66e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 79.75 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFSgflkvtekvifPRqdDVLISFLPLAHMFerviqsvv 346
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADFT-----------PN--DRFMSALPLFHSF-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 347 ychGGRVGFFQGdirLLSDDMKALCPTI--FPVVPRLLnrmYDK----IFCQADtpvkrwFLEFAAKrkqaevrsgiirn 420
Cdd:PRK08043 420 ---GLTVGLFTP---LLTGAEVFLYPSPlhYRIVPELV---YDRnctvLFGTST------FLGNYAR------------- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 421 dsiwdelFFNKIQASLggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNH 500
Cdd:PRK08043 472 -------FANPYDFAR---LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMD 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 501 IKLVD---IEElnywtckgEGEICVKGPNVFKGYLK--DPDRTK-------EALDSDGWLHTGDIGKWLPAGTLKIIDRK 568
Cdd:PRK08043 542 ARLLSvpgIEQ--------GGRLQLKGPNIMNGYLRveKPGVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQGRA 613
|
330 340 350
....*....|....*....|....*....|....*...
gi 1333574464 569 KHIFKLAqGEYVAPEKIENIYIRSEPVAQiyvHGDSLK 606
Cdd:PRK08043 614 KRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
279-695 |
2.70e-15 |
|
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: 79.07 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHmferviqsvvychggRVGFFQG 358
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH---------------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DIRLLSDDMKA-LCPT-IFPVVPRLLNRMYDK----IFCQADTPVKrWFLEFAAKRKQAEvrsgiirndsiWDElffnki 432
Cdd:cd05908 166 HLAPLIAGMNQyLMPTrLFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPEKAND-----------WDL------ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 qaslgGCVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF--------------------- 481
Cdd:cd05908 228 -----SSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthge 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 482 -------TTPGDWTSGHVGAPLPCNHIKLVDieELNYWTCKGE-GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 553
Cdd:cd05908 299 pepevdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 554 GkWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVaqiyvhgdslkafLVGIVVpdpevmpswaqkrgIEGTY 633
Cdd:cd05908 377 G-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV-------------ELGRVV--------------ACGVN 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333574464 634 VELCTNRE-----LKKAILEDMVSLGKEGGLHsFEQVKAIHIHsDMFSVQNGLLTPTLKAKRPELRE 695
Cdd:cd05908 428 NSNTRNEEifcfiEHRKSEDDFYPLGKKIKKH-LNKRGGWQIN-EVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
288-618 |
3.52e-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: 78.52 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 288 TSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV---IQSVVYChGGRVgffqgdirLLS 364
Cdd:cd05920 147 SGGTTGTPKLIPRTH----NDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAcpgVLGTLLA-GGRV--------VLA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 365 DDmkALCPTIFPVVPRllnrmyDKIFCQADTP--VKRWfLEFAAKRKQAEvrsgiirndsiwdelffnkiqASLggcvRM 442
Cdd:cd05920 214 PD--PSPDAAFPLIER------EGVTVTALVPalVSLW-LDAAASRRADL---------------------SSL----RL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 443 IVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDiEELNYWTCKGEGEI 520
Cdd:cd05920 260 LQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEGEL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 521 CVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsepvaQIYV 600
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------LLLR 408
|
330
....*....|....*...
gi 1333574464 601 HGDSLKAFLVGivVPDPE 618
Cdd:cd05920 409 HPAVHDAAVVA--MPDEL 424
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
277-615 |
1.03e-14 |
|
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: 77.12 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 277 PKPSDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERV--IQSVVychggrvg 354
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPAlgLTSVI-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 ffqgdirllsDDMKALCPTifPVVPRllnrmydkifcqadtpvkrwFLEFAAKRKQAevrSGIIRNDSIWDEL--FFNKI 432
Cdd:cd05910 150 ----------PDMDPTRPA--RADPQ--------------------KLVGAIRQYGV---SIVFGSPALLERVarYCAQH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 QASLGGcVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNH 500
Cdd:cd05910 195 GITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 501 IKLVDI--EELNYWTCKGE------GEICVKGPNVFKGYLKDPDRTKEALDSDG----WLHTGDIGKWLPAGTLKIIDRK 568
Cdd:cd05910 274 VRIIEIddEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1333574464 569 KHIFKLAQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 615
Cdd:cd05910 354 AHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
281-622 |
1.94e-14 |
|
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: 75.98 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGR--VGFFQG 358
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGAsgVLLEEA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 359 DIRLLSDDMKALCPTIFPVVPRllnrMYDKIFCQADTpvkrwflefaakrkqaevrsgiirndsiwdelffnkiQASLGG 438
Cdd:cd05958 175 TPDLLLSAIARYKPTVLFTAPT----AYRAMLAHPDA-------------------------------------AGPDLS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 439 CVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDieELNYWTCKGE 517
Cdd:cd05958 214 SLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD--DEGNPVPDGT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 518 -GEICVKGPNVFKgYLKDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVA 596
Cdd:cd05958 291 iGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVA 366
|
330 340
....*....|....*....|....*....
gi 1333574464 597 QIYVHGDSLKAFLV---GIVVPDPEVMPS 622
Cdd:cd05958 367 ECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
469-625 |
2.38e-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: 74.65 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 469 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDIE--ELNywtcKGE-GEICVKGPNVFKGYLKDPDRTKEALdSD 545
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 546 GWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSEP-VAQIYVhgdslkaflvgIVVPDp 617
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 1333574464 618 evmPSWAQ 625
Cdd:cd17636 276 ---PRWAQ 280
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
287-629 |
1.41e-13 |
|
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: 73.94 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 287 FTSGTTGNPKGAMLTHGNVVADFSGFLKvteKVIFPRQDDVLIS--------------FLPLAH------MFERVIQSVV 346
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSaaklffayglgnslTFPLSVgattvlMPERPTPAAV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 347 YchggrvgffqgdirllsDDMKALCPTIFPVVPRLLNRMYdkifcQADTPVKRWFLEfaakrkqaevrsgiirndsiwde 426
Cdd:cd05959 247 F-----------------KRIRRYRPTVFFGVPTLYAAML-----AAPNLPSRDLSS----------------------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 427 lffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNHIKLV 504
Cdd:cd05959 282 -------------LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 505 DiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEK 584
Cdd:cd05959 347 D-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFE 423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1333574464 585 IENIYIRSEPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPSWAQKRGI 629
Cdd:cd05959 424 VESALVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDSEALEEEL 471
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
276-618 |
1.49e-13 |
|
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: 73.46 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF-----LKVTEKVIF--PRQDDVLIS--FLPLAHMfERViqsVV 346
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMqdeypLGPGDRVLQktPLSFDVSVWelFWPLVAG-ARL---VV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 347 YCHGGRvgffqGDIRLLSDDMKALCPTIFPVVPRLLnrmydkifcqadtpvkRWFLEFAAKRKQAEVRsgiirndsiwde 426
Cdd:cd17646 210 ARPGGH-----RDPAYLAALIREHGVTTCHFVPSML----------------RVFLAEPAAGSCASLR------------ 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 427 lffnkiqaslggcvRMIVTGAAPASPTVLGFlRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIKL 503
Cdd:cd17646 257 --------------RVFCSGEALPPELAARF-LALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLYV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 504 VDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKIIDRKKHIFKLaQG 577
Cdd:cd17646 322 LD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RG 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1333574464 578 EYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 618
Cdd:cd17646 400 FRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
432-600 |
2.50e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 72.60 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 432 IQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDIE 507
Cdd:cd05974 191 IQQDLASFdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 508 ElnywTCKGEGEICV-----KGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAP 582
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1333574464 583 EKIENIYIRSEPVAQIYV 600
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
278-610 |
2.68e-13 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 72.88 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGN----VVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQ-SVVYCHggR 352
Cdd:cd05928 172 GSQEPMAIYFTSGTTGSPKMAEHSHSSlglgLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQgACVFVH--H 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 VGFFQGDIRLlsddmKALcpTIFPVvprllnrmydKIFCQADTpVKRWFLEFAAKRKQAEvrsgiirndsiwdelffnki 432
Cdd:cd05928 250 LPRFDPLVIL-----KTL--SSYPI----------TTFCGAPT-VYRMLVQQDLSSYKFP-------------------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 qaSLGGCVrmivTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDiEELNYW 512
Cdd:cd05928 292 --SLQHCV----TGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 513 TCKGEGEICVK-GPN----VFKGYLKDPDRTKEALDSDGWLhTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIEN 587
Cdd:cd05928 365 PPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVES 442
|
330 340 350
....*....|....*....|....*....|
gi 1333574464 588 IYIRSEPVAQIYV-------HGDSLKAFLV 610
Cdd:cd05928 443 ALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
121-618 |
1.08e-12 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 70.61 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKACTDQFigVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYiintadistviv 200
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVF--VLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRD------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 dkpqkavlllehveRKETPGLKLIILmepfEEALKDRGQecgvviksmqtiedcgqrnhrvpvvsssasgsllskppkPS 280
Cdd:cd05969 67 --------------RLENSEAKVLIT----TEELYERTD---------------------------------------PE 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflkVTEKVIFP-RQDDvlisflplahmferviqsvVYCHGGRVGFFQGd 359
Cdd:cd05969 90 DPTLLHYTSGTTGTPKGVLHVHDAMIFYY-----FTGKYVLDlHPDD-------------------IYWCTADPGWVTG- 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 360 irllsddmkalcpTIFPVVPRLLNRMYDKIFcQADTPVKRWFlefaakrkqaevrsGIIRND--SIW------------- 424
Cdd:cd05969 145 -------------TVYGIWAPWLNGVTNVVY-EGRFDAESWY--------------GIIERVkvTVWytaptairmlmke 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 425 -DELFFNKIQASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIK 502
Cdd:cd05969 197 gDELARKYDLSSL----RFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGVKAA 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 503 LVDiEELNYWTCKGEGEICVKG--PNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYV 580
Cdd:cd05969 273 VVD-ENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRV 349
|
490 500 510
....*....|....*....|....*....|....*...
gi 1333574464 581 APEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 618
Cdd:cd05969 350 GPFEVESALMEHPAVAEAGVIG-----------KPDPL 376
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
88-600 |
1.08e-12 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 70.94 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 88 DARTMYEVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELAC 167
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKR-GDR-VALMCGNRIEFLDVFLGC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 168 YTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkAVLLLEHVERKETPGLKLIILMEPFEEALkDRGQECGVVIKS 247
Cdd:PRK06155 92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA--LLAALEAADPGDLPLPAVWLLDAPASVSV-PAGWSTAPLPPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 248 MQTIeDCGqrnhrvpvvsssasgsllskPPKPSDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFPRQDDV 327
Cdd:PRK06155 169 DAPA-PAA--------------------AVQPGDTAAILYTSGTTGPSKGVCCPH----AQFYWWGRNSAEDLEIGADDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 328 LISFLPLAH-----MFervIQSVVycHGGRV---------GFFqgdirllsDDMKALCPTIFpvvpRLLNRMYDKIFCQA 393
Cdd:PRK06155 224 LYTTLPLFHtnalnAF---FQALL--AGATYvleprfsasGFW--------PAVRRHGATVT----YLLGAMVSILLSQP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 394 DTPVKRwflefaakrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPASptVLGFLRAALGCQVYEGYGQT 473
Cdd:PRK06155 287 ARESDR-------------------------------------AHRVRVALGPGVPAA--LHAAFRERFGVDLLDGYGST 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 474 ECTAGCtFTTPGDWTSGHVGAPLPCNHIKLVDiEELNYWTCKGEGEICVKG--PNVF-KGYLKDPDRTKEALdSDGWLHT 550
Cdd:PRK06155 328 ETNFVI-AVTHGSQRPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHT 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1333574464 551 GDIGKWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIyIRSEP-VAQIYV 600
Cdd:PRK06155 405 GDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
441-618 |
1.91e-12 |
|
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: 70.17 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 441 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-PCNHIKLVDIEelnywtck 515
Cdd:COG1021 303 RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsPDDEVRIVDED-------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 516 GE-------GEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKK-HIFKlaQGEYVAPEKIEN 587
Cdd:COG1021 372 GNpvppgevGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVEN 449
|
170 180 190
....*....|....*....|....*....|.
gi 1333574464 588 iyirsepvaQIYVHGDSLKAFLVGivVPDPE 618
Cdd:COG1021 450 ---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
287-600 |
3.62e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 69.13 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 287 FTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHmferVI-QSVVY---CHGGRVGFfqGDIRL 362
Cdd:PRK09029 142 LTSGSTGLPKAAVHTAQAHLASAEG---VLSLMPFTAQDSWLLS-LPLFH----VSgQGIVWrwlYAGATLVV--RDKQP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 363 LSDDMK-----ALCPTifpVVPRLLNrmYDkifcQADTPVKRwFLefaakrkqaevrsgiirndsiwdelffnkiqasLG 437
Cdd:PRK09029 212 LEQALAgcthaSLVPT---QLWRLLD--NR----SEPLSLKA-VL---------------------------------LG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 438 GCvrMIvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLVDieelnywtckge 517
Cdd:PRK09029 249 GA--AI--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------------ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 518 GEICVKGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQ 597
Cdd:PRK09029 305 GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQ 381
|
...
gi 1333574464 598 IYV 600
Cdd:PRK09029 382 VFV 384
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
516-571 |
4.11e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.21 E-value: 4.11e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1333574464 516 GE--GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHI 571
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
275-610 |
4.77e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 69.10 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 275 KPPKPSDLSIVC-FTSGTTGNPKGAMLTH-GNVVADFSGFLkvtekvIFPRQDD-VLISFLPLAHmferviqsvvyCHGG 351
Cdd:PLN02479 189 KPPADEWQSIALgYTSGTTASPKGVVLHHrGAYLMALSNAL------IWGMNEGaVYLWTLPMFH-----------CNGW 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 352 rvgffqgdirLLSDDMKALCPTIFPVVPRLLNRMYDKI-------FCQAdtPVkrwflefaakrkqaeVRSGIIrNDSIW 424
Cdd:PLN02479 252 ----------CFTWTLAALCGTNICLRQVTAKAIYSAIanygvthFCAA--PV---------------VLNTIV-NAPKS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 425 DELFfnkiqaSLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH 500
Cdd:PLN02479 304 ETIL------PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQ 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 501 -IKLVDIEELNYWTCKGE----------GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKK 569
Cdd:PLN02479 375 gVRYIGLEGLDVVDTKTMkpvpadgktmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSK 453
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1333574464 570 HIFkLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLV 610
Cdd:PLN02479 454 DII-ISGGENISSLEVENV---------VYTHPAVLEASVV 484
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
287-617 |
6.05e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 68.53 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 287 FTSGTTGNPKGAMLTHG-------NVVADfsgflkvtekvIFP--RQDDVLISFLPLAHMfERVIQSVVYCHGGRVgffq 357
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGqmafvitNHLAD-----------LMPgtTEQDASLVVAPLSHG-AGIHQLCQVARGAAT---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 gdIRLLSDDMKAlcptifPVVPRLLNRMYDKIFCQADTPVKrWFLEFAAkrkqaevrsgIIRNDsiwdelffnkiQASLg 437
Cdd:PRK07470 234 --VLLPSERFDP------AEVWALVERHRVTNLFTVPTILK-MLVEHPA----------VDRYD-----------HSSL- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 438 gcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH--------IKLV 504
Cdd:PRK07470 283 ---RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmevqIQDD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 505 DIEELNywtcKGE-GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPE 583
Cdd:PRK07470 357 EGRELP----PGEtGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPR 430
|
330 340 350
....*....|....*....|....*....|....
gi 1333574464 584 KIENiyirsepvaQIYVHGDSLKAFLVGivVPDP 617
Cdd:PRK07470 431 EIEE---------KLLTHPAVSEVAVLG--VPDP 453
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
278-627 |
9.36e-12 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 67.85 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQS--VVYCHGGRVGF 355
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLV----NLSHGLIKEYGITSSDRVLQFASIA--FDVAAEEiyVTLLSGATLVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 356 FQGDIRLLSDDMKAlcptifpvvprllnrmydkiFCQadtpvkrwflefaakRKQAEVRSgiiRNDSIWDELFFNKIQAS 435
Cdd:cd17644 178 RPEEMRSSLEDFVQ--------------------YIQ---------------QWQLTVLS---LPPAYWHLLVLELLLST 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 436 LGG--CVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIKLVDi 506
Cdd:cd17644 220 IDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 EELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLH--------TGDIGKWLPAGTLKIIDRKKHIFKLaQGE 578
Cdd:cd17644 299 ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGF 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1333574464 579 YVAPEKIENIYIRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 627
Cdd:cd17644 378 RIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPSTVELR 429
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
150-619 |
1.25e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 67.78 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 150 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLllehveRKETPGLKLIILMEP 229
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELL------DGLDPGVRVINVDSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 230 FEEALKDrgqecgvviksmqtiedcGQRNHRVPvvsssasgsllSKPPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVadF 309
Cdd:PRK07867 131 AWADELA------------------AHRDAEPP-----------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--S 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 310 SGflkvtekvifprqddvlisfLPLAHMFERVIQSVVYC-----HGGRVgffqgdirllsddMKALCPTIFpvvprllnr 384
Cdd:PRK07867 180 AG--------------------VMLAQRFGLGPDDVCYVsmplfHSNAV-------------MAGWAVALA--------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 385 mydkifCQADTPVKRwflEFAAKRKQAEVRS-GIIrndsiwdelFFNKIqaslGGCVRMIVtgAAP-------------- 449
Cdd:PRK07867 218 ------AGASIALRR---KFSASGFLPDVRRyGAT---------YANYV----GKPLSYVL--ATPerpddadnplrivy 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 450 ---ASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDIE--------------ELNYW 512
Cdd:PRK07867 274 gneGAPGDIARFARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNAD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 513 TCKGEgEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRS 592
Cdd:PRK07867 350 EAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRY 426
|
490 500
....*....|....*....|....*..
gi 1333574464 593 EPVAQIYVHGdslkaflvgivVPDPEV 619
Cdd:PRK07867 427 PDATEVAVYA-----------VPDPVV 442
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-616 |
1.48e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.26 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 27 ATTLVSMGALAAILAYW--FTHRPKAlQPPCNL----LMQSEEVkdsggaRRSVIGDGPqllTHYYDDARTMYEVFRRGL 100
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEER------ARELVRWNA---PATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 101 SISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDT 180
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 181 LGPGAIRYIINTADISTVIVDKPQKAVLLLehverkeTPGLKLIILMEPFEEalkdrgqecgvviksmqtIEDCGQRNHR 260
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------PAGLRSLCLDEPADL------------------LCGYSGHNPE 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 261 VPVvsssasgsllskppKPSDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTEKVIFPRQDDVLISFLPLAHMFER 340
Cdd:PRK12467 651 VAL--------------DPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFAFDLGV 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 341 VIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP----TIFPVVPRLLnrmydKIFCQADtpvkrwflefaakrKQAEVRsg 416
Cdd:PRK12467 713 TELFGALASGATLHLLPPDCARDAEAFAALMAdqgvTVLKIVPSHL-----QALLQAS--------------RVALPR-- 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 417 iirndsiwdelffnkiqaslgGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT----PGDWTSGHV 492
Cdd:PRK12467 772 ---------------------PQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPI 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 493 GAPLPCNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKII 565
Cdd:PRK12467 831 GQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYL 909
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1333574464 566 DRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYV------HGDSLKAFLVGIVVPD 616
Cdd:PRK12467 910 GRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaqpgdAGLQLVAYLVPAAVAD 965
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-618 |
3.29e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 66.49 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACytySMVvvplydtlgpGAIRYIINTAdistviV 200
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNHRGFVLALYAA---GKV----------GARIILLNTG------F 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DKPQkavlLLEHVERKetpGLKLIILMEPFEEALKDRGQECGVVIKSMQTIEDCGQRNHRVPVVSSSASGSLLSKPPKPS 280
Cdd:PRK07788 134 SGPQ----LAEVAARE---GVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DL-SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISflplAHMFerviqsvvycHGgrVGFFQGD 359
Cdd:PRK07788 207 KPgGIVILTSGTTGTPKGAPRPEPSPLAPLAGLL---SRVPFRAGETTLLP----APMF----------HA--TGWAHLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 360 I-----------------RLLSDDMKALCPTIFpVVPRLLNRMYDKIfcqadtpvkrwflefaakrkqAEVRSgiirnds 422
Cdd:PRK07788 268 LamalgstvvlrrrfdpeATLEDIAKHKATALV-VVPVMLSRILDLG---------------------PEVLA------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 423 iwdelffnKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPCNH 500
Cdd:PRK07788 319 --------KYDTS---SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKGVT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 501 IKLVDiEELNYWTCKGEGEICVKGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYV 580
Cdd:PRK07788 387 VKILD-ENGNEVPRGVVGRIFVGNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENV 460
|
490 500 510
....*....|....*....|....*....|....*...
gi 1333574464 581 APEKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 618
Cdd:PRK07788 461 FPAEVEDLLAGHPDVVEAAVIG-----------VDDEE 487
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
440-615 |
4.04e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 66.08 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 440 VRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSGH---VGAPLPCNHIKLVDI- 506
Cdd:PRK09274 290 LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGAgicVGRPVDGVEVRIIAIs 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 -EELNYWT-----CKGE-GEICVKGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGkWL-PAGTLKIIDRKKHIFKL 574
Cdd:PRK09274 370 dAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVET 448
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1333574464 575 AQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 615
Cdd:PRK09274 449 AGGTLY-----------TIPCERIFnTHPGVKRSALVGVGVP 479
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
447-618 |
5.74e-11 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 65.48 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 447 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDIEELNYWTckgEGEICVK 523
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVLGKvHILDEDGNEVPPGE---IGEVYFA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 524 GPNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsepvaqiyvHG 602
Cdd:cd05929 329 NGPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HP 396
|
170
....*....|....*.
gi 1333574464 603 DSLKAFLVGivVPDPE 618
Cdd:cd05929 397 KVLDAAVVG--VPDEE 410
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
121-626 |
2.18e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 63.65 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLlQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 D---KPQKAVLLlehverKETPGLKLIILMEPFEEALKDRGQECGVVIKSMQTIEDCGQRNHRVPVVsssasgsllskpp 277
Cdd:PRK05620 118 DprlAEQLGEIL------KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPEL------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNvvadfsgflkvtekvifprqddvlisfLPLAHMFERVIQSVVYCHGgrVGFFq 357
Cdd:PRK05620 179 DETTAAAICYSTGTTGAPKGVVYSHRS---------------------------LYLQSLSLRTTDSLAVTHG--ESFL- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 gdirllsddmkaLCPTIFPV----VPrLLNRMydkifcqADTPvkrwfLEFAAKRKQAEVRSGIIRND---------SIW 424
Cdd:PRK05620 229 ------------CCVPIYHVlswgVP-LAAFM-------SGTP-----LVFPGPDLSAPTLAKIIATAmprvahgvpTLW 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 425 DELFFNKIQ-----ASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA----- 494
Cdd:PRK05620 284 IQLMVHYLKnpperMSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvs 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 495 ----PLPCNHiKLVDIEELNYWTCKGEGEICVKGPNVFKGYLKDP----------------DRTKEALDSDGWLHTGDIG 554
Cdd:PRK05620 360 qgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVG 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333574464 555 KWLPAGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK 626
Cdd:PRK05620 439 SVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
281-604 |
2.51e-10 |
|
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: 63.26 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVT-EKVIFPRQDDVLiSFLPLAhmFERVIQSVV--YCHGGRvgffq 357
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFErEKTNINFSDKVL-QFATCS--FDVCYQEIFstLLSGGT----- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 358 gdIRLLSDDMKALCPTIFPVVPRllNRMYDKIFcqadtPVKrwFLEFAAKRKQaevrsgiirndsiwdelFFNkiqaSLG 437
Cdd:cd17656 197 --LYIIREETKRDVEQLFDLVKR--HNIEVVFL-----PVA--FLKFIFSERE-----------------FIN----RFP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 438 GCVRMIVTGAAP--ASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDiEELNYW 512
Cdd:cd17656 245 TCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 513 TCKGEGEICVKGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIE 586
Cdd:cd17656 323 PQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIE 401
|
330 340
....*....|....*....|
gi 1333574464 587 NIYIRSEPVAQ--IYVHGDS 604
Cdd:cd17656 402 AQLLNHPGVSEavVLDKADD 421
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
441-622 |
3.28e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.18 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 441 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDiEELNYWTCKGEG 518
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 519 EICVKGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 595
Cdd:PRK12406 352 EIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGV 427
|
170 180 190
....*....|....*....|....*....|
gi 1333574464 596 AQIYVHGDSLKAF---LVGIVVPDPEVMPS 622
Cdd:PRK12406 428 HDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
283-596 |
4.31e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 283 SIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVgFFQG---D 359
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKL-VLPGpdlD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 360 IRLLSDDMKALCPTIFPVVPR----LLNRMydkifcqadtpvkrwflefaakrKQAEVRSGIIRndsiwdelffnkiqas 435
Cdd:PRK07008 256 GKSLYELIEAERVTFSAGVPTvwlgLLNHM-----------------------REAGLRFSTLR---------------- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 436 lggcvRMIVTGAApASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------I 501
Cdd:PRK07008 297 -----RTVIGGSA-CPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdM 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 502 KLVDIE--ELNyWTCKGEGEICVKGPNVFKGYLKdpdRTKEALDsDGWLHTGDIGKWLPAGTLKIIDRKKHIFKlAQGEY 579
Cdd:PRK07008 368 KIVGDDgrELP-WDGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEW 441
|
330
....*....|....*..
gi 1333574464 580 VAPEKIENIYIRSEPVA 596
Cdd:PRK07008 442 ISSIDIENVAVAHPAVA 458
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
463-626 |
1.46e-09 |
|
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: 60.65 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 463 GCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEA 541
Cdd:cd17645 234 GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 542 LDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPV---AQIYVHGDSLKAFLVGI 612
Cdd:cd17645 313 FIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIelaAVLAKEDADGRKYLVAY 391
|
170
....*....|....*...
gi 1333574464 613 VVP----DPEVMPSWAQK 626
Cdd:cd17645 392 VTApeeiPHEELREWLKN 409
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-617 |
3.59e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 59.90 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 200
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 201 DK---PQKAVLLlehverKETPGLKLIILME------------PFEEALKDRGQECGVViksmqtiedcgqrnhrvpvvs 265
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVEdgsgndllpgavDYEDALAAGSPERDFG--------------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 266 ssasgsllskPPKPSDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTEKVIfprQDDVLIS----------FLPL 334
Cdd:PRK07798 160 ----------ERSPDDLYLLY-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPI---EDEEELAkraaagpgmrRFPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 335 AHMFERVIQSVVYchggrVGFFQGDIRLLSDDMKalcptifpVVPRLLNRMYDK-----IFCQADTpvkrwfleFAAKRK 409
Cdd:PRK07798 226 PPLMHGAGQWAAF-----AALFSGQTVVLLPDVR--------FDADEVWRTIERekvnvITIVGDA--------MARPLL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 410 QAevrsgiIRNDSIWDelffnkiqaslGGCVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTFTTPGDwt 488
Cdd:PRK07798 285 DA------LEARGPYD-----------LSSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSGTVAKG-- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 489 SGHVGAPL--PCNHIKLVDiEELNYWTcKGEGEICV--KGPNVFKGYLKDPDRTKEALDS-DG--WLHTGDIGKWLPAGT 561
Cdd:PRK07798 346 AVHTGGPRftIGPRTVVLD-EDGNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRARVEADGT 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 562 LKIIDRKKHIFKLAqGEYVAPEKIENIyIRSepvaqiyvHGDSLKAFLVGivVPDP 617
Cdd:PRK07798 424 ITLLGRGSVCINTG-GEKVFPEEVEEA-LKA--------HPDVADALVVG--VPDE 467
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
279-621 |
4.12e-09 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 59.34 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTEkvifprqDDVLISFLplAHMFE-RVIQSVVYCHGGR 352
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNG-------DEAVLFFS--NYVFDfFVEQMTLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 353 vgffqgDIRLLSDDMKALCPTIfpvvPRLLNRmyDKIFCQADTPVKRWFLEFAakrkqaevrsgiirndsiwdelffnki 432
Cdd:cd17648 164 ------KLVVPPDEMRFDPDRF----YAYINR--EKVTYLSGTPSVLQQYDLA--------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 qaSLGGCVRMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDiEELN 510
Cdd:cd17648 205 --RLPHLKRVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 511 YWTCKGEGEICVKGPNVFKGYLKDPDRTKE-------------ALDSDGWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQ 576
Cdd:cd17648 281 RVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-R 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1333574464 577 GEYVAPEKIENIY-----IRSEPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 621
Cdd:cd17648 360 GQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
286-602 |
4.35e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 59.38 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 286 CFTSGTTGNPKGAMLTHgnvvadfsgflkvtekvifpRQDdvlisflplahmferVIQSVVYCHGGRVGFFQGDirllsd 365
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSH--------------------RSN---------------VLHALMANNGDALGTSAAD------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 366 dmkalcpTIFPVVPrllnrMYdkifcQADTpvkrWFLEFAAKRKQAEVRSGIIRND--SIWDELFFNKIQASLG------ 437
Cdd:PRK06018 222 -------TMLPVVP-----LF-----HANS----WGIAFSAPSMGTKLVMPGAKLDgaSVYELLDTEKVTFTAGvptvwl 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 438 -------------GCVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV-- 492
Cdd:PRK06018 281 mllqymekeglklPHLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqk 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 493 -GAPLPCNHIKLVDIE--ELNyWTCKGEGEICVKGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKIIDRKK 569
Cdd:PRK06018 358 qGYPPFGVEMKITDDAgkELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSK 433
|
330 340 350
....*....|....*....|....*....|...
gi 1333574464 570 HIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 602
Cdd:PRK06018 434 DVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
440-618 |
4.36e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 59.53 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 440 VRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVDiEELNYWTC 514
Cdd:PRK08276 264 LRVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELPP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 515 KGEGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 593
Cdd:PRK08276 338 GEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHP 415
|
170 180
....*....|....*....|....*
gi 1333574464 594 PVAQIYVHGdslkaflvgivVPDPE 618
Cdd:PRK08276 416 KVADVAVFG-----------VPDEE 429
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
279-627 |
5.02e-09 |
|
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: 59.19 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTH---GNVVADFSGFLKVTEkvifprqDDVLISFLPLAhmFERVIQSVV--YCHGGRV 353
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHrglANLAAAQIAAFDVGP-------GSRVLQFASPS--FDASVWELLmaLLAGATL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 GFFQGDIRLLSDDMKALCP----TIFPVVPRLLNRMYDkifcqadtpvkrwflefaakrkqaevrsgiirndsiwdelff 429
Cdd:cd17652 163 VLAPAEELLPGEPLADLLRehriTHVTLPPAALAALPP------------------------------------------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 430 nkiqASLGGCVRMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDiEE 508
Cdd:cd17652 201 ----DDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-AR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 509 LNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVA 581
Cdd:cd17652 273 LRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIE 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1333574464 582 PEKIENIYIRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 627
Cdd:cd17652 352 LGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
150-619 |
8.36e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 58.50 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 150 IGVFAQNRPEWII----AELACYTysmvVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlLLEHVErkeTPGLKLII 225
Cdd:PRK13388 55 VGVLLGNTPEMLFwlaaAALGGYV----LVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 226 LMEP-FEEALKDRGQEcgvviksmqtiedcgqrnhrVPVvsssasgsllsKPPKPSDLSIVCFTSGTTGNPKGAMLTHGN 304
Cdd:PRK13388 126 VDTPaYAELVAAAGAL--------------------TPH-----------REVDAMDPFMLIFTSGTTGAPKAVRCSHGR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 305 VVadFSGFLkVTEKVIFPRqDDVLISFLPLAH----MferVIQSVVYCHGGRVGF--------FQGDIRLLSddmkalcP 372
Cdd:PRK13388 175 LA--FAGRA-LTERFGLTR-DDVCYVSMPLFHsnavM---AGWAPAVASGAAVALpakfsasgFLDDVRRYG-------A 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 373 TIFPVVPRLL-------NRMYDkifcqADTPVKRWFLEFAAKRKQAEvrsgiirndsiwdelffnkiqaslggcvrmivt 445
Cdd:PRK13388 241 TYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPRDIAE--------------------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 446 gaapasptvlgFLRAaLGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLPcnHIKLVDIEELNywTC----------- 514
Cdd:PRK13388 283 -----------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP--GVAIYNPETLT--ECavarfdahgal 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 515 ----KGEGEICVK-GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIY 589
Cdd:PRK13388 345 lnadEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERIL 422
|
490 500 510
....*....|....*....|....*....|
gi 1333574464 590 IRSEPVAQIYVHGdslkaflvgivVPDPEV 619
Cdd:PRK13388 423 LRHPAINRVAVYA-----------VPDERV 441
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
279-625 |
1.06e-08 |
|
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: 58.15 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPL----AHmfERVIQSVVycHGGRVg 354
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFnfdgAH--EQLLPPLI--CGACV- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 ffqgdirlLSDDMKALCPtifpvvPRLLNRMYDKIFCQ-ADTPVKRWFlEFAAkrkqaEVRSGIIRNDsiwdelffnkiq 433
Cdd:cd17649 164 --------VLRPDELWAS------ADELAEMVRELGVTvLDLPPAYLQ-QLAE-----EADRTGDGRP------------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 434 aslgGCVRMIVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGAPLPCNHIKLVDi 506
Cdd:cd17649 212 ----PSLRLYIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGRPLGGRSAYILD- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 507 EELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEAL--DSDG-----WLHTGDIGKWLPAGTLKIIDRKKHIFKLaQGEY 579
Cdd:cd17649 284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFR 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1333574464 580 VAPEKIENIYIRSEPVAQIYV---HGDSLKAfLVGIVVP-DPEVMPSWAQ 625
Cdd:cd17649 363 IELGEIEAALLEHPGVREAAVvalDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
440-633 |
1.14e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 58.10 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 440 VRMIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDIEELNYWTC 514
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 515 KGE-----GEICVKGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIy 589
Cdd:PRK05857 367 GAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI- 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1333574464 590 irSEPVAQI-----YVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 633
Cdd:PRK05857 444 --AEGVSGVreaacYEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-628 |
3.64e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 86 YDDARTMYEVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 165
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 166 ACYTYSMVVVPLYDTLGPGAIRYIINTADIStvivdkpqkavLLLEHveRKETPGLKLIilmepfeealkdRGQECGVVI 245
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIE-----------LLLTQ--SHLQARLPLP------------DGLRSLVLD 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 246 KSMQTIEDCGQRNhrvPVVSssasgsllskpPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQD 325
Cdd:PRK12467 1698 QEDDWLEGYSDSN---PAVN-----------LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAA 1759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 326 DVLISFLPLAhmFERVIQSVVY--CHGGRVgffqgdirLLSDDMKALCPtifpvvprllNRMYDKIFCQADTpvkrwFLE 403
Cdd:PRK12467 1760 DVVLQFTSFA--FDVSVWELFWplINGARL--------VIAPPGAHRDP----------EQLIQLIERQQVT-----TLH 1814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 404 FAAKRKQAevrsgiirndsiwdelfFNKIQASLGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAG-- 478
Cdd:PRK12467 1815 FVPSMLQQ-----------------LLQMDEQVEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDvt 1877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 479 ---CTFTTPGDWTSGHVGAPLPCNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEAL------DSDGWLH 549
Cdd:PRK12467 1878 hwtCRRKDLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLY 1956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 550 -TGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENiYIRSEP----VAQIYVHGDSLKAfLVGIVVPDPEVMPSWA 624
Cdd:PRK12467 1957 rTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAYVVPTDPGLVDDD 2033
|
....
gi 1333574464 625 QKRG 628
Cdd:PRK12467 2034 EAQV 2037
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
276-569 |
3.64e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.55 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPLAH-MferviqsvvychgGRVG 354
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKV---RPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 FF------QgdirlLSDDmkaLCPT-IFPVVP----RLLNRMYDKIfcqADTPVkrwF-LEFAAKRkqAEVRSGIIRNDS 422
Cdd:PRK09192 236 FLltpvatQ-----LSVD---YLPTrDFARRPlqwlDLISRNRGTI---SYSPP---FgYELCARR--VNSKDLAELDLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 423 IWdelffnkiqaslggcvRMIVTGAAPASPTVL----------GF-LRAALGCqvyegYGQTECTAGCTFTTPG------ 485
Cdd:PRK09192 300 CW----------------RVAGIGADMIRPDVLhqfaeafapaGFdDKAFMPS-----YGLAEATLAVSFSPLGsgivve 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 486 ----DWTSGH------------------VGAPLPCNHIKLVDI--EELNYwtcKGEGEICVKGPNVFKGYLKDPDRTKeA 541
Cdd:PRK09192 359 evdrDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-V 434
|
330 340
....*....|....*....|....*...
gi 1333574464 542 LDSDGWLHTGDIGkWLPAGTLKIIDRKK 569
Cdd:PRK09192 435 LAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
441-617 |
4.53e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 56.15 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 441 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 503
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 504 vdieelnywtckgeGEICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHifklaQ----GEY 579
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 1333574464 580 VAPEKIENIYIRsepvaqiyvHGDSLKAFLVGIvvPDP 617
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
283-619 |
4.93e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 283 SIVCFTSGTTGNPKG--------AMLTHGN-VVADFSGFLKVTEKvifprqdDVLISFLPLAHMFERVIQSVVYCHGGRV 353
Cdd:PRK13390 151 AVMLYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDISES-------DIYYSSAPIYHAAPLRWCSMVHALGGTV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 GFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYdkifcqadtpvkrwflefaakRKQAEVRSgiiRNDSiwdelffnki 432
Cdd:PRK13390 224 VLAKRfDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT---RYDV---------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 433 qASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDIEEL 509
Cdd:PRK13390 270 -SSL----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 510 NywtcKGE-GEICVKGPNVFKGYLKDPDRTKEALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIE 586
Cdd:PRK13390 344 P----AGRiGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETE 418
|
330 340 350
....*....|....*....|....*....|...
gi 1333574464 587 NIYIRSEPVAQIYVHGdslkaflvgivVPDPEV 619
Cdd:PRK13390 419 NALTMHPAVHDVAVIG-----------VPDPEM 440
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
278-597 |
1.27e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 278 KPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFS----GFlkvtekVIFPRQDDVLISFLPLAHMFERV------IQSVVY 347
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYHDMGLIggllqpIFSGVP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 348 CHGGRVGFF--------------QGDIRLLSDDMKALCPtifpvvprllNRMYDKIFCQADtpVKRWFLEFAAkrkqaev 413
Cdd:PRK05691 238 CVLMSPAYFlerplrwleaiseyGGTISGGPDFAYRLCS----------ERVSESALERLD--LSRWRVAYSG------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 414 rSGIIRNDSIwdELFFNKIQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTF 481
Cdd:PRK05691 299 -SEPIRQDSL--ERFAEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGR 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 482 TTPGdwtsghvgaplpcNHIKLVDIEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGkWLP 558
Cdd:PRK05691 375 SQPG-------------HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLR 440
|
330 340 350
....*....|....*....|....*....|....*....
gi 1333574464 559 AGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQ 597
Cdd:PRK05691 441 DGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
276-588 |
1.78e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.39 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISFLPLAH-Mferviqsvvychggrvg 354
Cdd:PRK05851 148 PPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG---LNARVGLDAATDVGCSWLPLYHdM----------------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 355 ffqGDIRLLSDDMKA----LCPT-IFPVVP-RLLNRMYDKIFCQADTPVKRWFLEFAAKRKQAEVRSGIIRndsiwdelf 428
Cdd:PRK05851 208 ---GLAFLLTAALAGaplwLAPTtAFSASPfRWLSWLSDSRATLTAAPNFAYNLIGKYARRVSDVDLGALR--------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 429 fnkiQASLGG----C--VRMIVTGAAPasptvLGFLRAALGcqvyEGYGQTECTAGCTFTTPG-----------DWTSGH 491
Cdd:PRK05851 276 ----VALNGGepvdCdgFERFATAMAP-----FGFDAGAAA----PSYGLAESTCAVTVPVPGiglrvdevttdDGSGAR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 492 ----VGAPLPCNHIKLVDIEELNYWTCKGEGEICVKGPNVFKGYLKDPdrtkeALDSDGWLHTGDIGkWLPAGTLKIIDR 567
Cdd:PRK05851 343 rhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLG-YLVDGGLVVCGR 416
|
330 340
....*....|....*....|.
gi 1333574464 568 KKHIFKLAqGEYVAPEKIENI 588
Cdd:PRK05851 417 AKELITVA-GRNIFPTEIERV 436
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
287-602 |
2.45e-07 |
|
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: 53.18 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 287 FTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPLAH-MFERVIQSVVYCHGGRVGFFQGDIRLLSD 365
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF----VCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 366 DMKALCPTIFPVVPRLLNRMYdkifcQADTPVkrwflefaakrkqAEVRSgIIRNDSIWDELFFNKIQAslggcvrmivt 445
Cdd:cd17633 83 KINQYNATVIYLVPTMLQALA-----RTLEPE-------------SKIKS-IFSSGQKLFESTKKKLKN----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 446 gaapasptvlGFLRAALgcqvYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDIEElnywtcKGEGEICVKG 524
Cdd:cd17633 133 ----------IFPKANL----IEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVKS 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333574464 525 PNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYVHG 602
Cdd:cd17633 192 EMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
279-610 |
3.14e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 53.88 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIV--------CFTSGTTGNPKGAMLTHGNVVADFSGF----LKVTEKVIFPRQDDVLISF-------LPLAHMFE 339
Cdd:PRK06060 136 PGGYEPMggdalayaTYTSGTTGPPKAAIHRHADPLTFVDAMcrkaLRLTPEDTGLCSARMYFAYglgnsvwFPLATGGS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 340 RVIQSVVYchGGRVGffqgdiRLLSDDMKalcPTIFPVVPRLLNRMYDKifCQADTpvkrwflefaakrkqaeVRSgiir 419
Cdd:PRK06060 216 AVINSAPV--TPEAA------AILSARFG---PSVLYGVPNFFARVIDS--CSPDS-----------------FRS---- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 420 ndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPL 496
Cdd:PRK06060 262 --------------------LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 497 PCNHIKLVDIEELNYWTcKGEGEICVKGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkiidrKKHI 571
Cdd:PRK06060 320 PPYEIRVVAPDGTTAGP-GVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADD 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1333574464 572 FKLAQGEYVAPEKIENIYIRSEPVAQIYVHG-------DSLKAFLV 610
Cdd:PRK06060 390 TEVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
441-625 |
3.60e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.07 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 441 RMIVTGAAPASPTVLGF-----LRAALGcqvyegYGQTEcTAG--CTFTtPGDWTSG--HVGAPLPcnHIKlVDIeelny 511
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQarqlqLRLAPT------YGMTE-TASqiATLK-PDDFLAGnnSSGQVLP--HAQ-ITI----- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 512 wTCKGEGEICVKGPNVFKGYLkdPdrtkEALDSDGWLHTGDIGKWLPAGTLKIIDR--KKHIfklAQGEYVAPEKIENIY 589
Cdd:PRK07445 297 -PANQTGNITIQAQSLALGYY--P----QILDSQGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAI 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 1333574464 590 IRSEPVAQIYVHGdslkaflvgivVPDPEvmpsWAQ 625
Cdd:PRK07445 367 LATGLVQDVCVLG-----------LPDPH----WGE 387
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
152-307 |
3.96e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 53.36 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 152 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQkavlLLEHVERKETPGLKLIILM---- 227
Cdd:PRK04319 103 IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVgedv 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 228 --EP----FEEALKDRGQECgvviksmqTIEDCgqrnhrvpvvsssasgsllskppKPSDLSIVCFTSGTTGNPKGAMLT 301
Cdd:PRK04319 178 eeGPgtldFNALMEQASDEF--------DIEWT-----------------------DREDGAILHYTSGSTGKPKGVLHV 226
|
....*.
gi 1333574464 302 HGNVVA 307
Cdd:PRK04319 227 HNAMLQ 232
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
279-651 |
4.47e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQSV--VYCHGGRVgff 356
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FDGSHEGLyhPLINGASV--- 4763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 357 qgdirLLSDDMKALcPTifpvvpRLLNRMYDKIFCQADTPVKRWFLEFAAKRKQAEVRSgiirndsiwdelffnkiqasl 436
Cdd:PRK12316 4764 -----VIRDDSLWD-PE------RLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPS--------------------- 4810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 437 ggcVRMIVTGA---APASPTVLgfLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKLVDiEE 508
Cdd:PRK12316 4811 ---LRVYCFGGeavAQASYDLA--WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLD-GQ 4884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 509 LNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAGTLKIIDRKKHI-----FKLAQ 576
Cdd:PRK12316 4885 LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQvkirgFRIEL 4964
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333574464 577 GEYVAPEKiENIYIRSEPVaqIYVHGdSLKAFLVGIVVP-DPEVMPSWAQKRGIEGtyvELctNRELKKAILEDMV 651
Cdd:PRK12316 4965 GEIEARLR-EHPAVREAVV--IAQEG-AVGKQLVGYVVPqDPALADADEAQAELRD---EL--KAALRERLPEYMV 5031
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
287-336 |
1.33e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.48 E-value: 1.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1333574464 287 FTSGTTGNPKGAMLTHGNVVADF----SGFLKVTEKVifPRQDDVLISFLPLAH 336
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWLPFYH 218
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
495-555 |
2.25e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333574464 495 PLPCNHIK-----LVDIEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 555
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
429-702 |
6.12e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 49.39 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 429 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKlVDIEE 508
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQ-VRICN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 509 LNYWTC-KGE-GEICVKGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIE 586
Cdd:PRK07638 323 EAGEEVqKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 587 NIYIRSEPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyvelCTNRELKKAILEDmvslgkeggLHSFEQ 664
Cdd:PRK07638 401 SVLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQLKSFCLQR---------LSSFKI 452
|
250 260 270
....*....|....*....|....*....|....*...
gi 1333574464 665 VKAIHIhsdmfsVQNGLLTPTLKAKRPELREYFKKQIE 702
Cdd:PRK07638 453 PKEWHF------VDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
276-337 |
1.10e-05 |
|
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: 48.44 E-value: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVVAdFSGFLKVTeKVifpRQDDVLISFLPLAHM 337
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLC-GV---TADDVIYITLPLYHS 196
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
443-627 |
1.17e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 48.12 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 443 IVTGAAPASPTVLgflRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDieelnywtckgeGEI 520
Cdd:PRK07824 156 VLVGGGPAPAPVL---DAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED------------GRI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 521 CVKGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLPAGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQI 598
Cdd:PRK07824 211 ALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADC 284
|
170 180 190
....*....|....*....|....*....|..
gi 1333574464 599 YVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 627
Cdd:PRK07824 285 AVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-336 |
1.43e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 48.33 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 121 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELAcytysmvVVPLydtlgpGAIryiinTADI 195
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLG-------LAKL------GAV-----VALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 196 STVIVDKPqkavllLEHVERKETPglKLIILMEPFEEALKDRGQEcgVVIKSMQTIEDCGQRNHRVPVVSSSASGSLLSK 275
Cdd:PRK08279 118 NTQQRGAV------LAHSLNLVDA--KHLIVGEELVEAFEEARAD--LARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333574464 276 PPKPS-------DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAH 336
Cdd:PRK08279 188 TNPASrsgvtakDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
281-618 |
2.49e-05 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 47.35 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 281 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKvtekvifprQDDVLISFLPLAHMfERVIQSVVYC--HGGRV 353
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGAL---------PSDVLYTCLPLYHS-TALIVGWSAClaSGATL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 354 GF--------FQGDIRllsddmKALCpTIFPVVPRLLnrmydkifcqadtpvkRWFLefAAKRKQAEVRsgiirndsiwd 425
Cdd:cd05940 152 VIrkkfsasnFWDDIR------KYQA-TIFQYIGELC----------------RYLL--NQPPKPTERK----------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 426 elffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-I 501
Cdd:cd05940 196 ----HKVRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 502 KLV--DIEELNYWT-----C----KGE-----GEICVKGPnvFKGYLKDPDRTKEAL-----DSDGWLHTGDIGKWLPAG 560
Cdd:cd05940 260 ALVkyDLESGEPIRdaegrCikvpRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEG 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333574464 561 TLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGDSL-----KAFLVGIVVPDPE 618
Cdd:cd05940 338 FWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
279-610 |
2.90e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 279 PSDLSIVCFTSGTTGNPKGAMLT-HGNVVADFSG--FLKVTEKVIFPRQ-----DDVLISFLPlAHMFerviqsvvychG 350
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEqRGMLNNQLSKvpYLALSEADVIAQTasqsfDISVWQFLA-APLF-----------G 3935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 351 GRVGFFQGDIrllSDDMKALCP-------TIFPVVPRLLNRMydkifcqadtpvkrwflefaakrkqaevrsgiIRNDsi 423
Cdd:PRK05691 3936 ARVEIVPNAI---AHDPQGLLAhvqaqgiTVLESVPSLIQGM--------------------------------LAED-- 3978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 424 wdelffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLP 497
Cdd:PRK05691 3979 ---------RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTD 4047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 498 CNHIKLVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKEAL-------DSDGWLHTGDIGKWLPAGTLKIIDRKKH 570
Cdd:PRK05691 4048 NNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDH 4126
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1333574464 571 I-----FKLAQGEYVApEKIENIYIRSEPVA-QIYVHGDSLKAFLV 610
Cdd:PRK05691 4127 QvkirgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
439-693 |
3.11e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 43.83 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 439 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGcTFTTPG---DWTSGhVGAPLPCNHIKLVDIEELNYWTcK 515
Cdd:PRK13383 293 QLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPVGP-R 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 516 GEGEICVKGPNVFKGYlkdPDRTKEALdSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 595
Cdd:PRK13383 370 VTGRIFVGGELAGTRY---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAV 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 596 AQIYVHGDSLKAF---LVGIVVPDPevmpswaqkrgieGTYVELCTNRELkkaiLEDMVSlgkegglhSFEQVKAIHIHS 672
Cdd:PRK13383 445 ADNAVIGVPDERFghrLAAFVVLHP-------------GSGVDAAQLRDY----LKDRVS--------RFEQPRDINIVS 499
|
250 260
....*....|....*....|.
gi 1333574464 673 DMFSvqngllTPTLKAKRPEL 693
Cdd:PRK13383 500 SIPR------NPTGKVLRKEL 514
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
437-619 |
3.12e-04 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 43.98 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 437 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDIE--ELNy 511
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 512 wtcKGE-GEICVKGPNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 590
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLA 459
|
170 180 190
....*....|....*....|....*....|....*.
gi 1333574464 591 RSEPVAQIYV-------HGDSLKAFlvgiVVPDPEV 619
Cdd:PRK13382 460 THPDVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
441-626 |
3.73e-04 |
|
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: 43.52 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 441 RMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL-PCNHIKLVDIEELNYWTCK--G 516
Cdd:cd05924 137 FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFtRANPDTVVLDDDGRVVPPGsgG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 517 EGEICVKGpNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGEYVAPEKIEniyirse 593
Cdd:cd05924 214 VGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVE------- 284
|
170 180 190
....*....|....*....|....*....|...
gi 1333574464 594 pvAQIYVHGDSLKAFLVGivVPDPEvmpsWAQK 626
Cdd:cd05924 285 --EALKSHPAVYDVLVVG--RPDER----WGQE 309
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
430-588 |
5.99e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 43.19 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 430 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 502
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 503 LVDIEELNYWTCKGEGE----ICVKGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKIIDRKKHIFKLAqGE 578
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|
gi 1333574464 579 YVAPEKIENI 588
Cdd:cd05915 421 WISSVDLENA 430
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
276-306 |
8.29e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.72 E-value: 8.29e-04
10 20 30
....*....|....*....|....*....|.
gi 1333574464 276 PPKPSDLSIVCFTSGTTGNPKGAMLTHGNVV 306
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
426-611 |
9.73e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 426 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIK 502
Cdd:PRK05691 1376 QLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCR 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 503 LVDiEELNYWTCKGEGEICVKGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKIIDRKKHIFKLa 575
Cdd:PRK05691 1456 VLD-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL- 1533
|
170 180 190
....*....|....*....|....*....|....*...
gi 1333574464 576 QGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVG 611
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
529-617 |
2.70e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.18 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333574464 529 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSEP-VAQIYVH 601
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 1333574464 602 -----------GDSLKafLVGIVVPDP 617
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| |
