|
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 ... |
141-745 |
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: 915.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 221 STVIVDKpqkavlllehverketpglkliilmdpfeealkergqkcGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCF 300
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVlisflplahmferviqsqwaptcadvHISYLPLAHMFERM 380
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDV--------------------------YISYLPLAHIFERV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 381 VQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGIIR 458
Cdd:cd05927 176 VEALFLYHGAKIGFYSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVR 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 459 NDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCN 538
Cdd:cd05927 256 ASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 539 HIKLVDVEELNYWA--CKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQG 616
Cdd:cd05927 336 EVKLVDVPEMNYDAkdPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 617 EYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWA-QKRGIEGTYADLCTSKDLKKAILEDMVRLGKE 695
Cdd:cd05927 416 EYVAPEKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKE 495
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1622946795 696 SGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 745
Cdd:cd05927 496 NGLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
97-745 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 694.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 97 RSViGSGPQLLTHY--YDDARTMYQVFRRGLSISGNGPCLGFRKPNQ----PYQWLSYQEVADRAEFLGSGLLQHNCK-- 168
Cdd:PLN02736 25 RSA-RSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTRIRVDgtvgEYKWMTYGEAGTARTAIGSGLVQHGIPkg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 169 ACtdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVdKPQKAVLLLEHVerKETPGLKL 248
Cdd:PLN02736 104 AC----VGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCL--SEIPSVRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 249 IILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkv 328
Cdd:PLN02736 177 IVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGS--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 329 tekvifprqdDVLISFLPlahmferviqsqwaptcADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKA 408
Cdd:PLN02736 254 ----------SLSTKFYP-----------------SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 409 LCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRKQAEVRSGiiRNDS-IWDELFFNKIQASLGGCVRMIVTG 485
Cdd:PLN02736 307 LRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 486 AAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKG---EGEICVR 562
Cdd:PLN02736 385 ASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 563 GPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGD 642
Cdd:PLN02736 465 GPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 643 SLKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLL 721
Cdd:PLN02736 545 SLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLL 624
|
650 660
....*....|....*....|....
gi 1622946795 722 TPTLKAKRPELREYFKKQIEELYS 745
Cdd:PLN02736 625 TPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
111-745 |
2.41e-174 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 513.11 E-value: 2.41e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 111 YDDARTMYQVFRRGLSISGNGPCLGfRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 190
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALR-EKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeealkeRGQKCGVVI 270
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV--RDELPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 271 KSMQAVEDCGQENHH------APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDDvlisf 344
Cdd:COG1022 155 LSLDELLALGREVADpaeleaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER-----LPLGPG----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 345 lplahmferviqsqwaptcaDVHISYLPLAHMFERMVQSVVYCHGGRVGfFQGDIRLLSDDMKALCPTIFPVVPRLLNRM 424
Cdd:COG1022 225 --------------------DRTLSFLPLAHVFERTVSYYALAAGATVA-FAESPDTLAEDLREVKPTFMLAVPRVWEKV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 425 YDKIFSQAN--TPLKRWLLEFA---AKRKQAEVRSGiiRNDSIW--------DELFFNKIQASLGGCVRMIVTGAAPASP 491
Cdd:COG1022 284 YAGIQAKAEeaGGLKRKLFRWAlavGRRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 492 TVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYL 571
Cdd:COG1022 362 ELARFFR-ALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYY 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 572 KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGI 651
Cdd:COG1022 430 KNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAAL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 652 VVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLGKesGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRP 730
Cdd:COG1022 509 IVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRK 586
|
650
....*....|....*
gi 1622946795 731 ELREYFKKQIEELYS 745
Cdd:COG1022 587 VILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
141-732 |
3.35e-157 |
|
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: 463.61 E-value: 3.35e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 221 STVIVDKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCF 300
Cdd:cd05907 79 KALFVEDP----------------------------------------------------------------DDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERviqsqwaptcadvhisylplahmfeRM 380
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFER-------------------------RA 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 381 VQSVVYCHGGRVGFFQgDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAkrkqaevrsgiirnd 460
Cdd:cd05907 146 GLYVPLLAGARIYFAS-SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV--------------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 461 siwdelffnkiqaslGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHI 540
Cdd:cd05907 210 ---------------GGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEV 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 541 KLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVA 620
Cdd:cd05907 274 RIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNIS 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 621 PEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGIEG-TYADLCTSKDLKKAILEDMVRLGKEsgLH 699
Cdd:cd05907 343 PEPIENALKASPLISQAVVIGDGRP-FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANAR--LS 419
|
570 580 590
....*....|....*....|....*....|...
gi 1622946795 700 SFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPEL 732
Cdd:cd05907 420 RYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-729 |
1.14e-150 |
|
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: 448.97 E-value: 1.14e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 142 PYQWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINT 217
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLvelgLKPGDK------VAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 218 ADISTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvpPQPDDLSI 297
Cdd:cd17639 76 TECSAIFTD---------------------------------------------------------------GKPDDLAC 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 298 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPrqddvlisflplahmferviqsqwaptcADVHISYLPLAHMF 377
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP----------------------------DDRYLAYLPLAHIF 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 378 ERMVQSVVYCHGGRVGFfqGDIRLLSDDMKALC--------PTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKR 447
Cdd:cd17639 145 ELAAENVCLYRGGTIGY--GSPRTLTDKSKRGCkgdltefkPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 448 KQAEVRSGIirnDS-IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDW 526
Cdd:cd17639 223 KLKALKEGP---GTpLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDL 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 527 TSGHVGAPLPCNHIKLVDVEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVI 604
Cdd:cd17639 299 ETGRVGPPLPCCEIKLVDWEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKII 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 605 DRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRG-IEGTYADLCTSKDLKK 683
Cdd:cd17639 379 DRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQK 458
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1622946795 684 AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKR 729
Cdd:cd17639 459 AVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
83-744 |
1.40e-147 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 446.77 E-value: 1.40e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 83 LMQSEEVEDSGGARRSVigsGPQLLTHYYDDA--------RTMYQVFRRGLSISGNGPCLGFR-----KPNQpYQWLSYQ 149
Cdd:PLN02614 8 IFQVEEGKEGSDGRPSV---GPVYRSIFAKDGfpnpiegmDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 150 EVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQ 229
Cdd:PLN02614 84 EVYDIVIKLGNSL--RSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE--E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 230 KAVLLLEHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPK 309
Cdd:PLN02614 160 KKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 310 GAMLTHGNVVADFSGFLKVTEKVifprqddvlisflplahmferviqsQWAPTCADVHISYLPLAHMFERMVQSVVYCHG 389
Cdd:PLN02614 240 GVMISNESIVTLIAGVIRLLKSA-------------------------NAALTVKDVYLSYLPLAHIFDRVIEECFIQHG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 390 GRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVRSGI--IRNDSIWDE 465
Cdd:PLN02614 295 AAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 466 LFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVD 544
Cdd:PLN02614 375 LVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGTVGPPVPNVDIRLES 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 545 VEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPE 622
Cdd:PLN02614 455 VPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 623 KIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFE 702
Cdd:PLN02614 534 NIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFE 613
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1622946795 703 QVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 744
Cdd:PLN02614 614 IIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
113-744 |
1.98e-147 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 445.80 E-value: 1.98e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 113 DARTMYQVFRRGLSISGNGPCLGFRKPNQ----PYQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIA 188
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPGSR--VGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 189 ELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV-DKPQKAVLlleHVERKETPGLKLIILMDPFEEALKERGQKCG 267
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELL---EPDCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 268 VVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfsgflkvtekVIFPRQDDVLISflpl 347
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAV-------------ATFVRGVDLFME---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 348 ahMFERVIqsqwapTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDK 427
Cdd:PLN02430 258 --QFEDKM------THDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 428 IFS--QANTPLKRWLLEFAAKRKQAEVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGC 503
Cdd:PLN02430 330 IQKalQELNPRRRLIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 504 QVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDVEELNY--WACKGEGEICVRGPNVFKGYLKDPDRTKEA 580
Cdd:PLN02430 410 FVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEV 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 581 LdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMP 660
Cdd:PLN02430 490 M-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTN 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 661 SWAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQI 740
Cdd:PLN02430 569 KWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEI 648
|
....
gi 1622946795 741 EELY 744
Cdd:PLN02430 649 DEMY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
142-745 |
1.63e-146 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 443.51 E-value: 1.63e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 142 PYQWLSYQEVADRAEFLGSGLLQ------HNCkactdqfiGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYII 215
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSrgvnpgDRC--------GIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 216 NTADISTVIVDKPQKAVLLleHVERKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPvPPQPDDL 295
Cdd:PLN02861 146 NHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 296 SIVCFTSGTTGNPKGAMLTHGNVVADF---SGFLKVTEKVIfpRQDDVLISFLPLAHMFERVIQSqwaptcadvhisylp 372
Cdd:PLN02861 223 CTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDRVA--TEEDSYFSYLPLAHVYDQVIET--------------- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 373 lahmfermvqsvvYC--HGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWLLEFAAKRK 448
Cdd:PLN02861 286 -------------YCisKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 449 QAEVRSGIIRNDS--IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDW 526
Cdd:PLN02861 353 LGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANV 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 527 TS--GHVGAPLPCNHIKLVDVEELNYWACKG--EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLK 602
Cdd:PLN02861 432 FSmvGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 603 VIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCTSKDLK 682
Cdd:PLN02861 511 IIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKAR 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946795 683 KAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 745
Cdd:PLN02861 591 KYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
104-745 |
2.66e-129 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 400.26 E-value: 2.66e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 104 PQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPNQ------------------PYQWLSYQEVADRAEFLGSGLLQ- 164
Cdd:PLN02387 47 PELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKLISrefetssdgrkfeklhlgEYEWITYGQVFERVCNFASGLVAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 165 -HNckacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQ--KAVLLLEHVERk 241
Cdd:PLN02387 127 gHN----KEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlkKLIDISSQLET- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 242 etpgLKLIILM-DPFEEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 320
Cdd:PLN02387 202 ----VKRVIYMdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 321 DFSGFLKVTEKVifprqddvlisflplahmferviqsqwapTCADVHISYLPLAHMFERMVQSVVYCHGGRVGFfqGDIR 400
Cdd:PLN02387 278 TVAGVMTVVPKL-----------------------------GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 401 LLSD-----------DMKALCPTIFPVVPRLLNRMYDKIFSQANTP--LKRWLLEFAAKRKQAEVR------SGIIRndS 461
Cdd:PLN02387 327 TLTDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--L 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 462 IWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIK 541
Cdd:PLN02387 405 LWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 542 LVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEA--LDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLA 614
Cdd:PLN02387 485 LVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQ 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 615 QGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSKDLKKAILEDMVRLG 693
Cdd:PLN02387 565 HGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAA 644
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 694 KESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYS 745
Cdd:PLN02387 645 KAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
142-614 |
1.49e-122 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 373.19 E-value: 1.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 142 PYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIS 221
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 222 TVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKergqkcgvviksMQAVEDCGQENHHAPVPPQPDDLSIVCFT 301
Cdd:pfam00501 96 VLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 302 SGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERViqsqwaptcadvhisylplahmferMV 381
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLS-------------------------LG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 382 QSVVYCHGGRVGFFQGDIRL----LSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwlleFAAKRKQAEVRSGii 457
Cdd:pfam00501 219 LLGPLLAGATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNML------------------LEAGAPKRALLSS-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 458 rndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAP 534
Cdd:pfam00501 279 ---------------------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 535 LPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLA 614
Cdd:pfam00501 338 LPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
88-744 |
2.56e-94 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 308.44 E-value: 2.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 88 EVEDSGGARRSVIGSGPQL--LTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPN--------------QPY-------- 143
Cdd:PTZ00216 40 ETENASAIYRIAGVTDEEHerLRNEWYYGPNFLQRLERICKERGDRRALAYRPVErvekevvkdadgkeRTMevthfnet 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 144 QWLSYQEVADRAEFLGSGL----LQHNCKactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTAD 219
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLaelgLTKGSN------VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 220 iSTVIVDKPQKAVLLLEHVERKETPGLKLIILmdpfeEALKERGQKCGVVIKSMQAVEDCG---QENHHAPVPPQPDDLS 296
Cdd:PTZ00216 194 -CKAIVCNGKNVPNLLRLMKSGGMPNTTIIYL-----DSLPASVDTEGCRLVAWTDVVAKGhsaGSHHPLNIPENNDDLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 297 IVCFTSGTTGNPKGAMLTHGNVVADFSGflkvtekvIFPRQDDVLISFLPLahmferviqsqwaptcaDVHISYLPLAHM 376
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILA--------LEDRLNDLIGPPEED-----------------ETYCSYLPLAHI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 377 FERMVQSVVYCHGGRVGFfqGDIRLLSD-------DMKALCPTIFPVVPRLLNRMydKIFSQANTP----LKRWLLEFAA 445
Cdd:PTZ00216 323 MEFGVTNIFLARGALIGF--GSPRTLTDtfarphgDLTEFRPVFLIGVPRIFDTI--KKAVEAKLPpvgsLKRRVFDHAY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 446 KRKQAEVRSGiiRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--CTAGCTFTtp 523
Cdd:PTZ00216 399 QSRLRALKEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvCCGGIQRT-- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 524 GDWTSGHVGAPLPCNHIKLVDVEELNYwACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTL 601
Cdd:PTZ00216 474 GDLEPNAVGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 602 KVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKRGIEGTYADLCT 677
Cdd:PTZ00216 553 RIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGIEGEYPAILK 630
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946795 678 SKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 744
Cdd:PTZ00216 631 DPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
141-730 |
1.32e-75 |
|
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: 251.89 E-value: 1.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 141 QPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 221 STVIVdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqENHhapvppqPDDLSIVCF 300
Cdd:cd17640 79 VALVV--------------------------------------------------------END-------SDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 301 TSGTTGNPKGAMLTHGNVVadfsgflkvtekvifpRQDDVLISFLPlahmferviqsqwaPTCADVHISYLPLAHMFERM 380
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLL----------------HQIRSLSDIVP--------------PQPGDRFLSILPIWHSYERS 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 381 VQSVVYCHGGRVGFfqGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQ--ANTPLKRWLLEFAAkrkqaevrsgiir 458
Cdd:cd17640 146 AEYFIFACGCSQAY--TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQvsKSSPIKQFLFLFFL------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 459 ndsiwdelffnkiqasLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCN 538
Cdd:cd17640 211 ----------------SGGIFKFGISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGT 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 539 HIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEY 618
Cdd:cd17640 274 EIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGEN 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 619 VAPEKIENIYIRSQPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKRGI---EGTYADLCTSKDLKKAILEDMVRLGKE 695
Cdd:cd17640 354 VEPQPIEEALMRSPFIEQIMVVGQDQK-RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEISNR 432
|
570 580 590
....*....|....*....|....*....|....*
gi 1622946795 696 SGLHSFEQVKAIHIHSDMFsVQNGLLTPTLKAKRP 730
Cdd:cd17640 433 PGFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-729 |
1.01e-74 |
|
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: 250.85 E-value: 1.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 143 YQWLSYQEVADRAEFLGSGLLQHNCKACTDqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 222
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 223 VIVDKpqkavllLEHVERKE--TPGLKLIILMDPFEEALKERGqkcgvviksMQAVEDCGQENHHAPvPPQPDDLSIVCF 300
Cdd:cd05932 82 LFVGK-------LDDWKAMApgVPEGLISISLPPPSAANCQYQ---------WDDLIAQHPPLEERP-TRFPEQLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 301 TSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIqsqwaptcadVHISYLplahmferm 380
Cdd:cd05932 145 TSGTTGQPKGVMLTFGS----FAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVF----------VEGGSL--------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 381 vqsvvycHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLL----NRMYDKIFSQAntpLKRWLlefaakrkQAEVRSGI 456
Cdd:cd05932 202 -------YGGVLVAFAESLDTFVEDVQRARPTLFFSVPRLWtkfqQGVQDKIPQQK---LNLLL--------KIPVVNSL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 457 IRndsiwdelffNKIQASLG-GCVRMIVTGAAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPL 535
Cdd:cd05932 264 VK----------RKVLKGLGlDQCRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 536 PCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQ 615
Cdd:cd05932 333 PGVEVRISE-----------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSK 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 616 GEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPDPEvmpswAQKRGIEGTYADLCTSkdlKKAILEDMvrlgkE 695
Cdd:cd05932 402 GKYVAPAPIENKLAEHDRVEMVCVIGSGLPA-PLALVVLSEE-----ARLRADAFARAELEAS---LRAHLARV-----N 467
|
570 580 590
....*....|....*....|....*....|....
gi 1622946795 696 SGLHSFEQVKAIHIHSDMFSVQNGLLTPTLKAKR 729
Cdd:cd05932 468 STLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
138-744 |
2.72e-68 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 235.71 E-value: 2.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 138 KPNQPYQWLSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIR 212
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRqaakaFLKLGLERFHG-------VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 213 YIINTADISTVIVDKPQKAVLLLEhvERKETPGLKLII-LMDPFEEalKERGQKcgvvikSMQAVEDCG----QENHHAP 287
Cdd:cd05933 74 YVAETSEANILVVENQKQLQKILQ--IQDKLPHLKAIIqYKEPLKE--KEPNLY------SWDEFMELGrsipDEQLDAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 288 VPPQ-PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIqsqwaptcaDV 366
Cdd:cd05933 144 ISSQkPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQIL---------DI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 367 hisYLPLAHmfermvqsvvychGGRVGFFQGDIR--LLSDDMKALCPTIFPVVPRLLNRMYDKI---FSQAnTPLKRWLL 441
Cdd:cd05933 215 ---WLPIKV-------------GGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 442 EFAaKRKQAEV-------RSGIIRNDSIWDELFFNKIQASLG--GCVRMIvTGAAPASPTVLGFLrAALGCQVYEGYGQT 512
Cdd:cd05933 278 SWA-KGVGLETnlklmggESPSPLFYRLAKKLVFKKVRKALGldRCQKFF-TGAAPISRETLEFF-LSLNIPIMELYGMS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 513 ECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEelnywaCKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 592
Cdd:cd05933 355 ETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 593 GKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQP-VAQIYVHGDSLKaFLVGIVV------PD---------P 656
Cdd:cd05933 429 GKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 657 EVMpSWAQKRGIEGTY-ADLCTSKDLK--KAILEDMVRLGKESGLHSFEQVKAIHIHSDmFSVQNGLLTPTLKAKRPELR 733
Cdd:cd05933 508 EAI-EFCRKLGSQATRvSEIAGGKDPKvyEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVA 585
|
650
....*....|.
gi 1622946795 734 EYFKKQIEELY 744
Cdd:cd05933 586 KKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
117-742 |
3.07e-64 |
|
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: 220.84 E-value: 3.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 117 MYQVFRRGLSISGNGPCLGFRkpnqpYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYS 196
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-----GRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 197 MVVVPLYDTLGPGAIRYIINTADISTVIVdkpqkAVLLlehverketpglkliilmdpfeealkergqkcgvviksmqav 276
Cdd:COG0318 74 AVVVPLNPRLTAEELAYILEDSGARALVT-----ALIL------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 277 edcgqenhhapvppqpddlsivcFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFerviq 356
Cdd:COG0318 107 -----------------------YTSGTTGRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVF----- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 357 sqwaptcADVHISYLPLAHmfermvqsvvychGGRV----GFfqgDIRLLSDDMKALCPTIFPVVPRLLNRMYDkifsqa 432
Cdd:COG0318 155 -------GLTVGLLAPLLA-------------GATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLR------ 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 433 ntplkrwllefAAKRKQAEVRSgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQT 512
Cdd:COG0318 206 -----------HPEFARYDLSS------------------------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLT 250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 513 ECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDVE--ELnywACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLH 588
Cdd:COG0318 251 ETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVDEDgrEL---PPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLR 326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 589 TGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPEvmps 661
Cdd:COG0318 327 TGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAF----VVLRPG---- 397
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 662 waqkrgiegtyADLcTSKDLKKAILEdmvRLGKesglhsFEQVKAIHIHSDMfsvqngLLTPTLKAKRPELREYFKKQIE 741
Cdd:COG0318 398 -----------AEL-DAEELRAFLRE---RLAR------YKVPRRVEFVDEL------PRTASGKIDRRALRERYAAGAL 450
|
.
gi 1622946795 742 E 742
Cdd:COG0318 451 E 451
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
143-695 |
1.70e-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: 222.30 E-value: 1.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 143 YQWLSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIST 222
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 223 VIVDKPQKAVLLLEHveRKETPGLKLIILMDPfeeaLKERGQKCGVVIKSMQAVEDcGQEnHHAPVPP---------QPD 293
Cdd:cd17641 87 VIAEDEEQVDKLLEI--ADRIPSVRYVIYCDP----RGMRKYDDPRLISFEDVVAL-GRA-LDRRDPGlyerevaagKGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFERVIQSQWAPTCadvhisylpl 373
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQMYSVGQALVC---------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 374 ahmfermvqsvvychGGRVGFFQgDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFS--QANTPLKRWL--------LEF 443
Cdd:cd17641 225 ---------------GFIVNFPE-EPETMMEDLREIGPTFVLLPPRVWEGIAADVRArmMDATPFKRFMfelgmklgLRA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 444 AAKRKQAEVRSGIIRNDS-IWDELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFT 521
Cdd:cd17641 289 LDRGKRGRPVSLWLRLASwLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 522 TP-GDWTSGHVGAPLPCNHIKLVDVeelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGT 600
Cdd:cd17641 367 HRdGDVDPDTVGVPFPGTEVRIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGH 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 601 LKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGIE-GTYADLCTSK 679
Cdd:cd17641 436 LVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRP 514
|
570
....*....|....*.
gi 1622946795 680 DLKKAILEDMVRLGKE 695
Cdd:cd17641 515 EVYELIRKEVEKVNAS 530
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
146-722 |
2.19e-61 |
|
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: 216.94 E-value: 2.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSgllQHNCKACTD--QFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:cd17632 68 ITYAELWERVGAVAA---AHDPEQPVRpgDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 224 IVDKPQKAV---LLLEHverketPGLKLIILMDPFEEALKER-----------GQKCGVVIKSMQAVEDCGQENHHAPVP 289
Cdd:cd17632 145 AVSAEHLDLaveAVLEG------GTPPRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 290 PQPDD-LSIVCFTSGTTGNPKGAMLTHgNVVADFsgFLKVtekviFPRQDDVLIsflplahmferviqsqwaptcADVHI 368
Cdd:cd17632 219 EPDDDpLALLIYTSGSTGTPKGAMYTE-RLVATF--WLKV-----SSIQDIRPP---------------------ASITL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 369 SYLPLAHMFERMVQSVVYCHGGrVGFFQG--DIRLLSDDMKALCPTIFPVVPRLlnrmYDKIFSQANTPLKRWL-----L 441
Cdd:cd17632 270 NFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSvagadA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 442 EFAAKRKQAEVRsgiirndsiwdelffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT 521
Cdd:cd17632 345 ETLAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 522 tpgdwtSGHVGAPlPCNHIKLVDVEELNYWACKG---EGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPA 598
Cdd:cd17632 405 ------DGVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 599 GTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGIVVPDPEVMpswaqkrgiegtyaDLCTS 678
Cdd:cd17632 478 DRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDAL--------------AGEDT 543
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1622946795 679 KDLKKAILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQNGLLT 722
Cdd:cd17632 544 ARLRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
146-729 |
2.63e-60 |
|
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: 210.76 E-value: 2.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLgSGLLQHNCKACTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTT 305
Cdd:cd05914 86 SDE----------------------------------------------------------------DDVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHGNVVADFSGfLKVTEKVifpRQDDVLISFLPLAHMFERVIqSQWAPTCADVHISYLplahmfERMVQSvv 385
Cdd:cd05914 102 GNSKGVMLTYRNIVSNVDG-VKEVVLL---GKGDKILSILPLHHIYPLTF-TLLLPLLNGAHVVFL------DKIPSA-- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 386 ychggrvgffqgdiRLLSDDMKALCPTIfpVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKrkqaevrsgIIRNDSIWdE 465
Cdd:cd05914 169 --------------KIIALAFAQVTPTL--GVPVPLVIEKIFKMDIIPKLTLKKFKFKLAK---------KINNRKIR-K 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 466 LFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPlpcnhIKLVDV 545
Cdd:cd05914 223 LAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 546 EELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIE 625
Cdd:cd05914 297 RIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIE 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 626 NIYIRSQPVA--QIYVHGDSLKAflvgIVVPDPEVMPSWAQKRgiegtyadlctsKDLKKAILEDmVRLGKESGLHSFEQ 703
Cdd:cd05914 377 AKINNMPFVLesLVVVQEKKLVA----LAYIDPDFLDVKALKQ------------RNIIDAIKWE-VRDKVNQKVPNYKK 439
|
570 580
....*....|....*....|....*.
gi 1622946795 704 VKAIHIHSDMFSVqngllTPTLKAKR 729
Cdd:cd05914 440 ISKVKIVKEEFEK-----TPKGKIKR 460
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
146-666 |
1.24e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 198.97 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGK-GDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 -------DKPQKAVL-LLEHVERKETP-GLKLIILMDPFEEALkERGQkcgvviksmqavedcgQENHHAPVppQPDDLS 296
Cdd:PRK07656 109 lglflgvDYSATTRLpALEHVVICETEeDDPHTEKMKTFTDFL-AAGD----------------PAERAPEV--DPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 297 IVCFTSGTTGNPKGAMLTHGNV---VADFSGFLKVTEKvifprqDDVLISfLPLAHMFerviqsqwaptCADVHI----- 368
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLlsnAADWAEYLGLTEG------DRYLAA-NPFFHVF-----------GYKAGVnaplm 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 369 ---SYLPLAHmFErmVQSVvychggrvgffqgdIRLLSDDMkalcPTIFPVVPRLLNRMYDkifsqantplkrwllefAA 445
Cdd:PRK07656 232 rgaTILPLPV-FD--PDEV--------------FRLIETER----ITVLPGPPTMYNSLLQ-----------------HP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 446 KRKQAEVRSgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPG 524
Cdd:PRK07656 274 DRSAEDLSS------------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 525 D---WTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGT 600
Cdd:PRK07656 330 DdrkTVAGTIGTAIAGVENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGY 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 601 LKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV---GIVVPDPEVMpSWAQKR 666
Cdd:PRK07656 408 LYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAYVVlkpGAELTEEELI-AYCREH 481
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
294-657 |
1.04e-54 |
|
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: 191.34 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHMFerviqsqwaptcadvHIS--YL 371
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIG---------------GLFglLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 PLAHmfermvqsvvychGGRVGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqantplkrwllefaakRKQA 450
Cdd:cd04433 62 ALLA-------------GGTVVLLPKfDPEAALELIEREKVTILLGVPTLLARL----------------------LKAP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 451 EVRSgiiRNDSiwdelffnkiqaslggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--S 528
Cdd:cd04433 107 ESAG---YDLS----------------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 529 GHVGAPLPCNHIKLVDVEElNYWACKGEGEICVRGPNVFKGYLKDPDRTkEALDSDGWLHTGDIGKWLPAGTLKVIDRKK 608
Cdd:cd04433 168 GSVGRPVPGVEVRIVDPDG-GELPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLK 245
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622946795 609 HIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPE 657
Cdd:cd04433 246 DMIK-SGGENVYPAEVEAVLLGHPGVAEAAVVG-----------VPDPE 282
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
118-649 |
1.39e-54 |
|
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: 195.09 E-value: 1.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 118 YQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKaCTDQfIGVFAQNRPEWIIAELACYTYSM 197
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQ-PGDR-VALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 198 VVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmDPFEEALKergqkcgvviksmqave 277
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA--------------------------VSFTDLLA----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 278 dcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfpRQDDVLISFLPLAHMFerviqs 357
Cdd:cd05936 112 --AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAALPLFHVF------ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 358 qwAPTCAdvhisylplahmferMVQSVvychggRVGFFQ------GDIRLLsDDMKALCPTIFPVVPRLLNRmydkifsq 431
Cdd:cd05936 182 --GLTVA---------------LLLPL------ALGATIvliprfRPIGVL-KEIRKHRVTIFPGVPTMYIA-------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 432 antplkrwLLEFAAKRKqaEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQ 511
Cdd:cd05936 230 --------LLNAPEFKK--RDFSSL-----------------------RLCISGGAPLPVEVAERFEELTGVPIVEGYGL 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 512 TECTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTG 590
Cdd:cd05936 277 TETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTG 354
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 591 DIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 649
Cdd:cd05936 355 DIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAFVV 419
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
146-649 |
1.82e-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: 189.35 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPQKAVLLLehVERKETPGLKlIILMDPFEEALKERGQkcgvvikSMQAVedCGQENHHAPVPPQ--PDDLSIVCFTSG 303
Cdd:cd05911 89 DPDGLEKVKE--AAKELGPKDK-IIVLDDKPDGVLSIED-------LLSPT--LGEEDEDLPPPLKdgKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 304 TTGNPKGAMLTHGNVVADFSgFLKVTEKVIFPRqDDVLISFLPLAHMFerviqSQWAptcadVHISYLplahmfermvqs 383
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLS-QVQTFLYGNDGS-NDVILGFLPLYHIY-----GLFT-----TLASLL------------ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 384 vvycHGGRV----GFFqgdirllSDDMKALCP----TIFPVVPRLLNRMydkifsqANTPLkrwllefaakrkqaevrsg 455
Cdd:cd05911 213 ----NGATViimpKFD-------SELFLDLIEkykiTFLYLVPPIAAAL-------AKSPL------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 456 iirndsiwdelfFNKIQASlggCVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 534
Cdd:cd05911 256 ------------LDKYDLS---SLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 535 LPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLa 614
Cdd:cd05911 321 LPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY- 399
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1622946795 615 QGEYVAPEKIENIyIRSQP------VAQIY--VHGDSLKAFLV 649
Cdd:cd05911 400 KGFQVAPAELEAV-LLEHPgvadaaVIGIPdeVSGELPRAYVV 441
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
111-656 |
3.14e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 172.68 E-value: 3.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 111 YDDARTMYQVFRRGLSISGNGPCLGFRKPNqpyqwLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 190
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 191 ACytySM---VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDP----------- 254
Cdd:PRK06187 75 AV---PKigaVLHPINIRLKPEEIAYILNDAEDRVVLVDSE-----FVPLLAaiLPQLPTVRTVIVEGDgpaaplapevg 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 255 -FEEALKergqkcgvviksmqavedcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVI 333
Cdd:PRK06187 147 eYEELLA-------------------AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL---FLHSLAVCAWLK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 334 FpRQDDVLISFLPLAHMFErviqsqWaptcadvHISYLPLahmferMV-QSVVYchggrVGFFqgDIRLLSDDMKALCPT 412
Cdd:PRK06187 205 L-SRDDVYLVIVPMFHVHA------W-------GLPYLAL------MAgAKQVI-----PRRF--DPENLLDLIETERVT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 413 IFPVVPRLLNRMydkifSQANTPLKRWLlefaakrkqaevrSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPT 492
Cdd:PRK06187 258 FFFAVPTIWQML-----LKAPRAYFVDF-------------SSL-----------------------RLVIYGGAALPPA 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 493 VLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH------VGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGP 564
Cdd:PRK06187 297 LLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGP 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 565 NVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyirsqpvaqIYVHGDSL 644
Cdd:PRK06187 376 WLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA---------LYGHPAVA 444
|
570
....*....|..
gi 1622946795 645 KAFLVGivVPDP 656
Cdd:PRK06187 445 EVAVIG--VPDE 454
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
146-627 |
7.37e-39 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 150.94 E-value: 7.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSgLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05909 8 LTYRKLLTGAIALAR-KLAKMTKE--GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPQKAVLLLEHVERKETPgLKLIILmdpfeEALKER---GQKCGVVIKSMQAVEDCGQENHHAPVppQPDDLSIVCFTS 302
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYD-ARIVYL-----EDLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 303 GTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFERVIqSQWAPTCADVHISYLPLAHMFERMVQ 382
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFD----PNPEDVVFGALPFFHSFGLTG-CLWLPLLSGIKVVFHPNPLDYKKIPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 383 SVvychggrvgffqgdirllsDDMKAlcpTIFPVVPRLLnRMYdkifsqantplkrwllefaAKRKQAEVRSGIirndsi 462
Cdd:cd05909 232 LI-------------------YDKKA---TILLGTPTFL-RGY-------------------ARAAHPEDFSSL------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 463 wdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIK 541
Cdd:cd05909 264 -----------------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 542 LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAP 621
Cdd:cd05909 327 IVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSL 404
|
....*.
gi 1622946795 622 EKIENI 627
Cdd:cd05909 405 EAIEDI 410
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
241-745 |
3.94e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 152.18 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 241 KETPGLKLIILMDPFE---------EALKERGQKCGV-------VIKSMQAVEDCGQENhhapvppqPDDLSIVCFTSGT 304
Cdd:PTZ00342 244 NDLSNELEDISLGPLEydkeklekiKDLKEKAKKLGIsiilfddMTKNKTTNYKIQNED--------PDFITSIVYTSGT 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 305 TGNPKGAMLTHGNVvadFSGflkvtekvIFPRQD-DVLISFLPlahmferviqsqwaptcaDVHISYLPLAHMFERMVQS 383
Cdd:PTZ00342 316 SGKPKGVMLSNKNL---YNT--------VVPLCKhSIFKKYNP------------------KTHLSYLPISHIYERVIAY 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 384 VVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQAN--TPLKRWLlefaAKRKQAEVRSGIIRNDS 461
Cdd:PTZ00342 367 LSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFL----VKKILSLRKSNNNGGFS 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 462 IWDELFFN---KIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG-DWTSGHVGAPL-P 536
Cdd:PTZ00342 443 KFLEGITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAdDNNTESIGGPIsP 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 537 CNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAQG 616
Cdd:PTZ00342 522 NTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQG 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 617 EYVAPEKIENIYIRSQPVAQIYVHG-DSLKAFLvGIVVPDPEVM------PSWAQKRGI-EGTYADLCTSKDLKKAILED 688
Cdd:PTZ00342 602 EYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEKLTDETINNNIYVD 680
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 689 MVR-----LGKESGLHSFEQVKAIHIHSDMFSVQNgLLTPTLKAKRPEL-REY--FKKQIEELYS 745
Cdd:PTZ00342 681 YVKgkmleVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVfKDYafFIDQVKKIYK 744
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
146-660 |
1.66e-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: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIv 225
Cdd:cd05941 12 ITYADLVARAARL-ANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 dkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpdDLSIVCFTSGTT 305
Cdd:cd05941 90 --------------------------------------------------------------------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHGNVVADFsgflkvtekvifprqddvlisflplahmfeRVIQSQWAPTCADVHISYLPLAHmfermVQSVV 385
Cdd:cd05941 102 GRPKGVVLTHANLAANV------------------------------RALVDAWRWTEDDVLLHVLPLHH-----VHGLV 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 386 -------YChGGRV---GFFQGDIRLLSDDMKALcpTIFPVVPRllnrMYDKIFS--QANTPLKRWLLEFAAKRkqaevr 453
Cdd:cd05941 147 nallcplFA-GASVeflPKFDPKEVAISRLMPSI--TVFMGVPT----IYTRLLQyyEAHFTDPQFARAAAAER------ 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 454 sgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHV 531
Cdd:cd05941 214 -------------------------LRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTV 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 532 GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK-HI 610
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDI 346
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622946795 611 FKlAQGEYVAPEKIENIyIRSQP-VAQIYVHGDSLKAF---LVGIVVPDPEVMP 660
Cdd:cd05941 347 IK-SGGYKVSALEIERV-LLAHPgVSECAVIGVPDPDWgerVVAVVVLRAGAAA 398
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
121-656 |
2.41e-37 |
|
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: 145.45 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 121 FRRGLSISGNGPCLGFrkPNQPyqwLSYQEVADRAEFLGSGLlQHNCKACTDQfIGVFAQNRPEWIIAELACYTYSMVVV 200
Cdd:cd17631 1 LRRRARRHPDRTALVF--GGRS---LTYAELDERVNRLAHAL-RALGVAKGDR-VAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 201 PLYDTLGPGAIRYIINTADiSTVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcg 280
Cdd:cd17631 74 PLNFRLTPPEVAYILADSG-AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 281 qenhhapvppqpdDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekvIFPRQDDVLISFLPLAHmferviqsqwa 360
Cdd:cd17631 99 -------------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAA----LDLGPDDVLLVVAPLFH----------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 361 ptCADVHISYLPLAHmfermvqsvvycHGGRV----GFFQGDIRLLSDDMKAlcpTIFPVVPRLLNRMydkifsqANTPL 436
Cdd:cd17631 151 --IGGLGVFTLPTLL------------RGGTVvilrKFDPETVLDLIERHRV---TSFFLVPTMIQAL-------LQHPR 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 437 krwllefaakrkqaevrsgiirndsiWDELFFnkiqASLggcvRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTA 516
Cdd:cd17631 207 --------------------------FATTDL----SSL----RAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSP 251
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 517 GCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGK 594
Cdd:cd17631 252 GVTFLSPEDHRRklGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGR 329
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 595 WLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 656
Cdd:cd17631 330 LDEDGYLYIVDRKKDMII-SGGENVYPAEVEDV---------LYEHPAVAEVAVIG--VPDE 379
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
272-627 |
9.44e-36 |
|
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: 141.99 E-value: 9.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 272 SMQAVEDCGQENHHAPVPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifPRQDDVLISFLPLAH 349
Cdd:cd05904 135 SLSFSDLLFEADEAEPPVVVikQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 350 MFerviqsqwaptcadvhisylplahmfermvqsvvychgGRVGFFQGDIRL-----------LSDDMKALCP---TIFP 415
Cdd:cd05904 213 IY--------------------------------------GLSSFALGLLRLgatvvvmprfdLEELLAAIERykvTHLP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 416 VVPrllnrmydkifsqantPLkrwlleFAAKRKQAEVRSGIIRndsiwdelffnkiqaSLggcvRMIVTGAAPASPTVL- 494
Cdd:cd05904 255 VVP----------------PI------VLALVKSPIVDKYDLS---------------SL----RQIMSGAAPLGKELIe 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 495 GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYL 571
Cdd:cd05904 294 AFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYL 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 572 KDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENI 627
Cdd:cd05904 374 NNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
145-734 |
4.82e-33 |
|
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: 133.59 E-value: 4.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 145 WLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVI 224
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK--GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 225 VDKpqkaVLLLEHVERKETPGLkliilmdpfeeALKERGQKCGVVIKSMQAVEDCGQENHHAPV----PPQPDDLSIVCF 300
Cdd:cd05926 92 TPK----GELGPASRAASKLGL-----------AILELALDVGVLIRAPSAESLSNLLADKKNAksegVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 301 TSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvIFPrqDDVLISFLPLAHmferviqsqwaptcadVH--ISYL--PLAHm 376
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYK--LTP--DDRTLVVMPLFH----------------VHglVASLlsTLAA- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 377 fermvqsvvychGGRV----GFfqgDIRLLSDDMKALCPTIFPVVPRLLnrmydKIfsqantplkrwLLEFAAKRKQAEv 452
Cdd:cd05926 216 ------------GGSVvlppRF---SASTFWPDVRDYNATWYTAVPTIH-----QI-----------LLNRPEPNPESP- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 453 rsgiirndsiwdelfFNKIqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSG 529
Cdd:cd05926 264 ---------------PPKL--------RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 530 HVGAPlpcNHIKLVDVEElnywacKGE-------GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLK 602
Cdd:cd05926 320 SVGKP---VGVEVRILDE------DGEilppgvvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLF 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 603 VIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDP---EVMPSWAQKRgiEGTYADlctsk 679
Cdd:cd05926 391 LTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAVAFG-----------VPDEkygEEVAAAVVLR--EGASVT----- 451
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 680 dlKKAILEDMvrlgkESGLHSFEQVKAIHIhsdmfsVQNGLLTPTLKAKRPELRE 734
Cdd:cd05926 452 --EEELRAFC-----RKHLAAFKVPKKVYF------VDELPKTATGKIQRRKVAE 493
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
290-655 |
4.01e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 132.05 E-value: 4.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FSGFLKVTEkviFPRQDDVLISFLPLAHMFERVIQSQWAPTCadvhi 368
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANaAQGKAWVPG---LGDGPERVLAALPMFHAYGLTLCLTLAVSI----- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 369 sylplahmfermvqsvvychGGR-VGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrmYDKIfsqantplkrwlLEFAAKR 447
Cdd:PRK05605 288 --------------------GGElVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 448 kqaevrsGIirndsiwdelffnkiqaSLGGcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpg 524
Cdd:PRK05605 332 -------GV-----------------DLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD-- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 525 DWTSGHVGAPLPCNHIKLVDVEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKV 603
Cdd:PRK05605 385 DRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRI 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 604 IDRKKHIFkLAQGEYVAPEKIENIyirsqpVAQiyvHGDSLKAFLVGIVVPD 655
Cdd:PRK05605 464 VDRIKELI-ITGGFNVYPAEVEEV------LRE---HPGVEDAAVVGLPRED 505
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
175-666 |
4.00e-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: 127.18 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlllehVERKETPGLKLIILMDP 254
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL---------LEEKDFQADSLDRIEAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 255 FEEALKERGQKcgvviksmqavedcgqenhhapvppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIF 334
Cdd:TIGR01923 98 GRYETSLSASF-------------------------NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVG---SKENLGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 335 PRQDDVLISfLPLahmferviqsqwaptcadVHISYLPLahmferMVQSVVYchGGRVGFFQGDIRLLsDDMKALCPTIF 414
Cdd:TIGR01923 150 TEDDNWLLS-LPL------------------YHISGLSI------LFRWLIE--GATLRIVDKFNQLL-EMIANERVTHI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 415 PVVPRLLNRMYDKifSQANTPLKRWLLefaakrkqaevrsgiirndsiwdelffnkiqaslGGcvrmivtGAAPASptvl 494
Cdd:TIGR01923 202 SLVPTQLNRLLDE--GGHNENLRKILL----------------------------------GG-------SAIPAP---- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 495 gFLRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDVEElnywackGEGEICVRGPNVFKGY 570
Cdd:TIGR01923 235 -LIEEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 571 LkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV--HGDSL---- 644
Cdd:TIGR01923 307 L-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpKPDAEwgqv 384
|
490 500
....*....|....*....|...
gi 1622946795 645 -KAFLVGIVVPDPEVMPSWAQKR 666
Cdd:TIGR01923 385 pVAYIVSESDISQAKLIAYLTEK 407
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
147-633 |
6.11e-31 |
|
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: 125.84 E-value: 6.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 147 SYQEVADRAEFLGSGLLQHnCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVIV 225
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYPAErLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPqkavllleHVERKETPGLKLIILMDPFEEALkergqkcgvviksmqavEDCGQENHhAPVPPQPDDLSIVCFTSGTT 305
Cdd:TIGR01733 79 DSA--------LASRLAGLVLPVILLDPLELAAL-----------------DDAPAPPP-PDAPSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAHmferviqsqwaptcaDVHISYLPLAHMfermvqsvv 385
Cdd:TIGR01733 133 GRPKGVVVTHRSLVN----LLAWLARRYGLDPDDRVLQFASLSF---------------DASVEEIFGALL--------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 386 ycHGGRVgffqgdiRLLSDDMKAlcpTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwde 465
Cdd:TIGR01733 185 --AGATL-------VVPPEDEER---DDAALLAALIAEHPVTVLNLTPSLLALLAAA----------------------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 466 lffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNH 539
Cdd:TIGR01733 230 ------LPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 540 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA-LDSDGWL-------HTGDIGKWLPAGTLKVIDRKKHIF 611
Cdd:TIGR01733 304 LYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQV 382
|
490 500
....*....|....*....|..
gi 1622946795 612 KLaQGEYVAPEKIENIyIRSQP 633
Cdd:TIGR01733 383 KI-RGYRIELGEIEAA-LLRHP 402
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
280-649 |
8.30e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 127.96 E-value: 8.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 280 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGfLKVTEKVIFPRQDDVLISFLPLAHMFerviqsqw 359
Cdd:PRK05677 194 GAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIY-------- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 360 aptcadvhisylplAHMFERMVQSVVYCHGgrvgffqgdiRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTplkrw 439
Cdd:PRK05677 265 --------------AFTFHCMAMMLIGNHN----------ILISN------PRDLPAMVKELGKWKFSGFVGLNT----- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 440 llEFAAkrkqaevrsgiIRNDSIWDELFFNKIQASLGGcvRMIVTGAAPASptvlgfLRAALGCQVYEGYGQTECTAGCT 519
Cdd:PRK05677 310 --LFVA-----------LCNNEAFRKLDFSALKLTLSG--GMALQLATAER------WKEVTGCAICEGYGMTETSPVVS 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 520 FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAG 599
Cdd:PRK05677 369 VNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDG 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 600 TLKVIDRKKHIFkLAQGEYVAPEKIENIyIRSQP----VAQIYV----HGDSLKAFLV 649
Cdd:PRK05677 448 YMRIVDRKKDMI-LVSGFNVYPNELEDV-LAALPgvlqCAAIGVpdekSGEAIKVFVV 503
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
118-595 |
1.36e-30 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 127.15 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 118 YQVFRRGLSISGNGPCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHnckactdqfiGV--------FAQNRPEWIIAE 189
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL----------GVkkgdrvaiYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 190 LACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD----KPQKAVLLLEHVE--RKETPGLKLIILMD---------- 253
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglRGGKVIDLKEKVDeaLEELPSLEHVIVVGrtgadvpmeg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 254 --PFEEALKERGQKCgvviksmqavedcgqenhhAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEK 331
Cdd:COG0365 162 dlDWDELLAAASAEF-------------------EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYL----VHAATTAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 332 VIF-PRQDDVLISFLPLAhmferviqsqWAptcadVHISYL---PLAH-----MFERmvqSVVYCHGGRvgFFQgdirlL 402
Cdd:COG0365 219 YVLdLKPGDVFWCTADIG----------WA-----TGHSYIvygPLLNgatvvLYEG---RPDFPDPGR--LWE-----L 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 403 SDDMKalcPTIFPVVPRLLnRMydkifsqantpLKRWLLEFAAKRKQAevrsgiirndsiwdelffnkiqaSLggcvRMI 482
Cdd:COG0365 274 IEKYG---VTVFFTAPTAI-RA-----------LMKAGDEPLKKYDLS-----------------------SL----RLL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 483 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaGCTFTTPGDWTS---GHVGAPLPCNHIKLVDvEELNywACKG--EG 557
Cdd:COG0365 312 GSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVVD-EDGN--PVPPgeEG 386
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622946795 558 EICVRG--PNVFKGYLKDPDRTKEAL--DSDGWLHTGDIGKW 595
Cdd:COG0365 387 ELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARR 428
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
114-745 |
3.63e-30 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 128.43 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 114 ARTMYQVFRRGLSISGNGPCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACY 193
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRP--GDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 194 TYSMVVVPLydtLGPG-AIRYIINTADISTVIVDKPQKAVLLLEHVERKETpglklIILMDPFEEALKERGQK-CGVVIK 271
Cdd:PTZ00297 504 LYGFTTLPL---VGKGsTMRTLIDEHKIKVVFADRNSVAAILTCRSRKLET-----VVYTHSFYDEDDHAVARdLNITLI 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 272 SMQAVEdcgQENHHAPVPPQP--DDLSIVCFTSGTTGNPKGAML-----THGNVVADFSgFLKVTEKVIFPRQDDVLISF 344
Cdd:PTZ00297 576 PYEFVE---QKGRLCPVPLKEhvTTDTVFTYVVDNTTSASGDGLavvrvTHADVLRDIS-TLVMTGVLPSSFKKHLMVHF 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 345 LPLAHMFERV-IQSQWAPTCAdvhISYLPLAHMFERMVQsvvychggrvgfFQgdirllsddmkalcPTIFPVVPRLlnr 423
Cdd:PTZ00297 652 TPFAMLFNRVfVLGLFAHGSA---VATVDAAHLQRAFVK------------FQ--------------PTILVAAPSL--- 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 424 mydkiFSQANTPLKR----------WLLEfaakrKQAEVRSGII----RNDSIWDELFFNKIQASLGGCVRMIVTGAAPA 489
Cdd:PTZ00297 700 -----FSTSRLQLSRanerysavysWLFE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 490 SPTV-----LGFLRAALGCQVYegygQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDVEELNYWACKGEGEICVRGp 564
Cdd:PTZ00297 770 STSFsllehISVCYVPCLREVF----FLPSEGVFCVD----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG- 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 565 nvfkgylkDPDRTKEAldsdgwlhtgdIGKWLPAGTLKVIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSL 644
Cdd:PTZ00297 835 --------EPRRTLPI-----------AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPS 895
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 645 KAfLVGIVVPDPEVMP-SWAQKRGIE--GTYADLCTSKDLKK----AILEDMVRLGKESGLHSFEQVKAIHIHSDMFSVQ 717
Cdd:PTZ00297 896 RP-IIAIVSPNRDTVEfEWRQSHCMGegGGPARQLGWTELVAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDH 974
|
650 660
....*....|....*....|....*...
gi 1622946795 718 NGLLTPTLKAKRPELREYFKKQIEELYS 745
Cdd:PTZ00297 975 STFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
146-661 |
5.07e-30 |
|
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: 123.79 E-value: 5.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACY----TYsmvvVPLYDTLGPGAIRYIINTADIS 221
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGP--GDLVAVLLERSLEMVVAILAVLkagaAY----VPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 222 TVIVDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFT 301
Cdd:cd05930 87 LVLTD-----------------------------------------------------------------PDDLAYVIYT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 302 SGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLIsflplahmferviqsQWAPTCADVHIS--YLPLAHmfer 379
Cdd:cd05930 102 SGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVL---------------QFTSFSFDVSVWeiFGALLA---- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 380 mvqsvvychGGRVGFFQGDIRLLSDDMKALC----PTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaakrkqaevrsg 455
Cdd:cd05930 159 ---------GATLVVLPEEVRKDPEALADLLaeegITVLHLTPSLLRLLLQELELAALPSL------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 456 iirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV- 531
Cdd:cd05930 211 ------------------------RLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVp 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 532 -GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA-----LDSDGWLH-TGDIGKWLPAGTLKVI 604
Cdd:cd05930 267 iGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFL 345
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 605 DRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 661
Cdd:cd05930 346 GRIDDQVKIR-GYRIELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
288-649 |
6.47e-30 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 125.17 E-value: 6.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 288 VPPQ--PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkvtekvifprqddvlisflplahmferVIQSQWA--PTC 363
Cdd:PRK08974 199 VKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN--------------------------------LEQAKAAygPLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 364 ADVH---ISYLPLAHMFERMVQSVVYCHGGrvgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQANTPLKRWL 440
Cdd:PRK08974 247 HPGKelvVTALPLYHIFALTVNCLLFIELG------GQNLLITN------PRDIPGFVKELKKYPFTAITGVNTLFNALL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 441 lefaakrkqaevrsgiirNDSIWDELFFNKIQASLGGcvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AG 517
Cdd:PRK08974 315 ------------------NNEEFQELDFSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 518 CTFTTPGdwTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLP 597
Cdd:PRK08974 369 NPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDE 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946795 598 AGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIY-------VHGDSLKAFLV 649
Cdd:PRK08974 445 EGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
142-608 |
3.12e-29 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 122.78 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 142 PYQWLSYQEVADRAEFLGSGLLQHNCKAcTDQFIGVFAQNRpEWIIAELACYTYSMVVVPLydtlGPGAIRyiintadis 221
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL----TVPPTY--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 222 tvivDKPQKAVLLLEHVerKETPGLKLII----LMDPFEEALKERGQkCGVVIKSMQAVEDCGqENHHAPvPPQPDDLSI 297
Cdd:cd05906 101 ----DEPNARLRKLRHI--WQLLGSPVVLtdaeLVAEFAGLETLSGL-PGIRVLSIEELLDTA-ADHDLP-QSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 298 VCFTSGTTGNPKGAMLTHGNVVADFSGflKVtekVIFPRQDDvlisflplahmferviqsqwaptcaDVHISYLPLAHmf 377
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAG--KI---QHNGLTPQ-------------------------DVFLNWVPLDH-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 378 ermVQSVVYCHggrvgffQGDIRLLSDDMKALCPTIFPVVPRLLNRMyDKiFSQANTplkrWLLEFA-AK-RKQAEVRSg 455
Cdd:cd05906 220 ---VGGLVELH-------LRAVYLGCQQVHVPTEEILADPLRWLDLI-DR-YRVTIT----WAPNFAfALlNDLLEEIE- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 456 iirnDSIWDelffnkiqasLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWT 527
Cdd:cd05906 283 ----DGTWD----------LSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 528 SGH----VGAPLPCNHIKLVDVEElnywACKGEGEIC---VRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPAGT 600
Cdd:cd05906 349 QALefvsLGRPIPGVSMRIVDDEG----QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGN 423
|
....*...
gi 1622946795 601 LKVIDRKK 608
Cdd:cd05906 424 LTITGRTK 431
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
286-658 |
3.30e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 122.82 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF--------SGFLKvtekvifPRQDDVLISflplahmferviqs 357
Cdd:PRK07059 197 KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNF-------------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 358 qwapTCAdvhisyLPLAHMFERMVQSVVYCHGGRVGFF---QGDIRLLSDDMKALCPTIFPVVPRLLNRMYdkifsqaNT 434
Cdd:PRK07059 256 ----VCA------LPLYHIFALTVCGLLGMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLYNALL-------NN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 435 PlkrwllEFaakrkqaevrsgiirndsiwDELFFNKIQASLGGcvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QT 512
Cdd:PRK07059 319 P------DF--------------------DKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsET 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 513 ECTAGCTFTTPGDWTsGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 592
Cdd:PRK07059 365 SPVATCNPVDATEFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDV 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622946795 593 GKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyIRSQP----VAQIYVH----GDSLKAFlvgIVVPDPEV 658
Cdd:PRK07059 443 GVMDERGYTKIVDRKKDMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
245-629 |
4.89e-29 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 122.40 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 245 GLKLIILMDPFEEALKERGQKCGVVIKSM-QAVEDC--------GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH 315
Cdd:PLN02246 122 GAKLIITQSCYVDKLKGLAEDDGVTVVTIdDPPEGClhfseltqADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 316 GNVVADfsgflkVTEKV------IFPRQDDVLISFLPLAHMFErviqsqwaptcadvhisylplahmfermVQSVVYChG 389
Cdd:PLN02246 202 KGLVTS------VAQQVdgenpnLYFHSDDVILCVLPMFHIYS----------------------------LNSVLLC-G 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 390 GRVG--------FfqgDIRLLSDDMKALCPTIFPVVPrllnrmydkifsqantPLkrwLLEFAakrKQAEVRSgiirnds 461
Cdd:PLN02246 247 LRVGaailimpkF---EIGALLELIQRHKVTIAPFVP----------------PI---VLAIA---KSPVVEK------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 462 iwDELffnkiqASlggcVRMIVTGAAPASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVG 532
Cdd:PLN02246 295 --YDL------SS----IRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 533 APLPCNHIKLVDVE---ELNYWACkgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKH 609
Cdd:PLN02246 360 TVVRNAELKIVDPEtgaSLPRNQP---GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKE 436
|
410 420
....*....|....*....|
gi 1622946795 610 IFKLaQGEYVAPEKIENIYI 629
Cdd:PLN02246 437 LIKY-KGFQVAPAELEALLI 455
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
147-657 |
6.54e-29 |
|
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: 121.87 E-value: 6.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 147 SYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLgpgAIRYIINTADIST-VIV 225
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLK--QNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY---NERELDHSLNISKpTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPQKAVLLLEHVERKeTPGLKLIILMDPFEEAlkeRGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTT 305
Cdd:cd17642 121 FCSKKGLQKVLNVQKK-LKIIKTIIILDSKEDY---KGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHGNVVADFSgflkvtekvifprqddvlisflplaHMFERVIQSQWAPTCAdvHISYLPLAHMFERMVQSVV 385
Cdd:cd17642 197 GLPKGVQLTHKNIVARFS-------------------------HARDPIFGNQIIPDTA--ILTVIPFHHGFGMFTTLGY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 386 YCHGGRVGF---FQGD--IRLLSD---DMKALCPTIFPVVPR--LLNRmYD----KIFSQANTPLKRWLLEFAAKRkqae 451
Cdd:cd17642 250 LICGFRVVLmykFEEElfLRSLQDykvQSALLVPTLFAFFAKstLVDK-YDlsnlHEIASGGAPLSKEVGEAVAKR---- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 452 vrsgiirndsiwdelfFNkiqaslggcvrmivtgaapasptvLGFLRaalgcqvyEGYGQTECTAGCTFTTPGDWTSGHV 531
Cdd:cd17642 325 ----------------FK------------------------LPGIR--------QGYGLTETTSAILITPEGDDKPGAV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 532 GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIF 611
Cdd:cd17642 357 GKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLI 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1622946795 612 KLaQGEYVAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDPE 657
Cdd:cd17642 437 KY-KGYQVPPAELESILLQ---------HPKIFDAGVAGI--PDED 470
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
280-656 |
1.53e-28 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 121.14 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 280 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvtekvifprqddvlisflplahmferviQSQW 359
Cdd:PRK08751 195 GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQ-------------------------------AHQW 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 360 APTCA------DVHISYLPLAHMFERMVQSVVYCHGGrvgffqGDIRLLSDdmkalcPTIFPVVPRLLNRMYDKIFSQAN 433
Cdd:PRK08751 244 LAGTGkleegcEVVITALPLYHIFALTANGLVFMKIG------GCNHLISN------PRDMPGFVKELKKTRFTAFTGVN 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 434 TPLKRWLlefaakrkqaevrsgiirNDSIWDELFFNKIQASLGGcvRMIVTGAapasptVLGFLRAALGCQVYEGYGQTE 513
Cdd:PRK08751 312 TLFNGLL------------------NTPGFDQIDFSSLKMTLGG--GMAVQRS------VAERWKQVTGLTLVEAYGLTE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 514 CT-AGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDI 592
Cdd:PRK08751 366 TSpAACINPLTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDI 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 593 GKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG----DSLKAFLVGIVVPDP 656
Cdd:PRK08751 445 ARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
146-639 |
1.95e-28 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 119.02 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADIstviv 225
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP--GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 dkpqkavlllehverketpglKLIILMDPFeealkergqkcgvviksmqavedcGQENHHApvppQPDDLSIVCFTSGTT 305
Cdd:cd05903 75 ---------------------KVFVVPERF------------------------RQFDPAA----MPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISfLPLAH-----------MFER---VIQSQWAPTCAdvhisyl 371
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAHqtgfvygftlpLLLGapvVLQDIWDPDKA------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 pLAHMFERmvqsvvychggRVGFFQGDIRLLSDDMKALcptifpvvprllnrmydkifSQANTPLKRwllefaakrkqae 451
Cdd:cd05903 175 -LALMREH-----------GVTFMMGATPFLTDLLNAV--------------------EEAGEPLSR------------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 452 vrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WT 527
Cdd:cd05903 210 ---------------------------LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLY 262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 528 SGhvGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRK 607
Cdd:cd05903 263 TD--GRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRS 338
|
490 500 510
....*....|....*....|....*....|..
gi 1622946795 608 KHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV 639
Cdd:cd05903 339 KDII-IRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-641 |
2.30e-28 |
|
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: 116.99 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVV--ADFSGF-LKVTEkvifprqDDVLISFLPLAHMFERVIQSQWAPT--CADV 366
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGErLGLTE-------QDRLCIPVPLFHCFGSVLGVLACLThgATMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 367 HIS--YLPLA--HMFERMVQSVVycHGgrvgffqgdirllsddmkalCPTIFPvvpRLLNRMydkifSQANTPLKRwlle 442
Cdd:cd05917 74 FPSpsFDPLAvlEAIEKEKCTAL--HG--------------------VPTMFI---AELEHP-----DFDKFDLSS---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 443 faakrkqaeVRSGIIrndsiwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFT 521
Cdd:cd05917 120 ---------LRTGIM---------------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQT 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 522 TPGDWTS---GHVGAPLPCNHIKLVDvEELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLP 597
Cdd:cd05917 164 RTDDSIEkrvNTVGRIMPHTEAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDE 242
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622946795 598 AGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 641
Cdd:cd05917 243 DGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
175-657 |
8.13e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 117.99 E-value: 8.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlllehverketpglkliilmdp 254
Cdd:PRK09088 50 LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAA----------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 255 feealkerGQKCGVVIKSMQAVEDCGQENHHAPVPPqpDDLSIVCFTSGTTGNPKGAMLTHGNvvadfsgflkvtekvif 334
Cdd:PRK09088 107 --------GRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKGVMLSERN----------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 335 prQDDVLISFLPLAHMferviqsqwaptcaDVHISYLPLAHMFE--RMVQSV--VYCHGGRV----GFFQG-DIRLLSDd 405
Cdd:PRK09088 160 --LQQTAHNFGVLGRV--------------DAHSSFLCDAPMFHiiGLITSVrpVLAVGGSIlvsnGFEPKrTLGRLGD- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 406 mKALCPTIFPVVPRLLNRmydkifsqantplkrwllefaakrkqaevrsgiIRNDSIWDELFFNKIQAslggcvrmIVTG 485
Cdd:PRK09088 223 -PALGITHYFCVPQMAQA---------------------------------FRAQPGFDAAALRHLTA--------LFTG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 486 AAP-ASPTVLGFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDVEELNYWAckGE-GE 558
Cdd:PRK09088 261 GAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--GVpGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 559 ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEniyirsqpvAQIY 638
Cdd:PRK09088 335 LLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE---------AVLA 404
|
490
....*....|....*....
gi 1622946795 639 VHGDSLKAFLVGivVPDPE 657
Cdd:PRK09088 405 DHPGIRECAVVG--MADAQ 421
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
146-641 |
8.28e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 118.72 E-value: 8.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVV---PLYDT------LGPGAIRYII- 215
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQP--GDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRAseleyaLGQSGVRWVIc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 216 ----NTADISTVIVD-KPQKAVLLLEHVERKETPGLKLIILMDPFE-------EALKERGQkcGVVIKSMQAVEdcGQEN 283
Cdd:PRK12583 124 adafKTSDYHAMLQElLPGLAEGQPGALACERLPELRGVVSLAPAPppgflawHELQARGE--TVSREALAERQ--ASLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 284 HHAPVPPQpddlsivcFTSGTTGNPKGAMLTHGNVV--ADFSG-FLKVTEKvifprqdDVLISFLPLAHMFERVIQSQwa 360
Cdd:PRK12583 200 RDDPINIQ--------YTSGTTGFPKGATLSHHNILnnGYFVAeSLGLTEH-------DRLCVPVPLYHCFGMVLANL-- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 361 pTCADV-------HISYLPLAHMFERMVQSVVYCHGgrvgffqgdirllsddmkalCPTIFpvvprllnrmydkiFSQAN 433
Cdd:PRK12583 263 -GCMTVgaclvypNEAFDPLATLQAVEEERCTALYG--------------------VPTMF--------------IAELD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 434 TPlKRWLLEFAAkrkqaeVRSGIIrndsiwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAALGC-QVYEGYGQT 512
Cdd:PRK12583 308 HP-QRGNFDLSS------LRTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 513 ECTAGCTFTTPGD-----WTSghVGAPLPCNHIKLVDVEELNywACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGW 586
Cdd:PRK12583 354 ETSPVSLQTTAADdlerrVET--VGRTQPHLEVKVVDPDGAT--VPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGW 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 587 LHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG 641
Cdd:PRK12583 430 MHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
479-650 |
9.51e-28 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 114.91 E-value: 9.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 479 VRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDveelnywack 554
Cdd:cd17638 117 LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD---------- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 555 gEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 634
Cdd:cd17638 186 -DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGV 263
|
170 180
....*....|....*....|...
gi 1622946795 635 AQIYV-------HGDSLKAFLVG 650
Cdd:cd17638 264 AQVAVigvpderMGEVGKAFVVA 286
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
114-608 |
2.41e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 117.75 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 114 ARTMYQVFRRGLSISGNGPCLgfrkpnqpyqwlSYQEVADR---------AEFLG-----SGLLqHNCKACTDQFIGVFA 179
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPAL------------SFLLDADPldrpetwtyAELLAdvtrtANLL-HSLGVGPGDVVAFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 180 QNRPEWIIAELACYTYSmVVVPLYDTLGPGAIRYIINTADISTVIVDKP-------QKAVLLLEHVerketPGLKLIILM 252
Cdd:PRK07529 91 PNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPfpgtdiwQKVAEVLAAL-----PELRTVVEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 253 D-------PFEEALKERGQKCGVVIKSMQAVEDCGQENHH-APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD-FS 323
Cdd:PRK07529 165 DlarylpgPKRLAVPLIRRKAHARILDFDAELARQPGDRLfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANaWL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 324 GFLkvtekVIFPRQDDVLISFLPLAHMFerviqsqwaptcADVHISYLPLAHMfermvQSVVYchGGRVGFfqGDIRLLS 403
Cdd:PRK07529 245 GAL-----LLGLGPGDTVFCGLPLFHVN------------ALLVTGLAPLARG-----AHVVL--ATPQGY--RGPGVIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 404 DDMK---ALCPTIFPVVPRLLNRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiwdelffnkIQASLGGCVR 480
Cdd:PRK07529 299 NFWKiveRYRINFLSGVPTVYAAL-------LQVP-----------------------------------VDGHDISSLR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 481 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDVEEL-NYW--ACKGE 556
Cdd:PRK07529 337 YALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDE 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1622946795 557 -GEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK 608
Cdd:PRK07529 417 vGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
294-657 |
2.97e-27 |
|
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: 115.08 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 294 DLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpRQDDVLISFLPLAHMFERVIQsqWAPtcADVHISYLPL 373
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLT--FAGYYSARRFGL--GEDDVYLTVLPLFHINAQAVS--VLA--ALSVGATLVL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 374 AHMFermvqsvvycHGGRvgfFQGDIRllsdDMKALCPTIFPVVPRLLnrmydkiFSQANTPlkrwllefaaKRKQAEVR 453
Cdd:cd05934 154 LPRF----------SASR---FWSDVR----RYGATVTNYLGAMLSYL-------LAQPPSP----------DDRAHRLR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 454 sgiirndsiwdelffnkiqaslggcvrmiVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA 533
Cdd:cd05934 200 -----------------------------AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 534 PLPCNHIKLVDVEelNYWACKGE-GEICVR---GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKH 609
Cdd:cd05934 251 PAPGYEVRIVDDD--GQELPAGEpGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKD 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 610 IFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFlvgIVVPDPE 657
Cdd:cd05934 328 MIR-RRGENISSAEVERAILRHPAVREAAVVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
144-666 |
1.27e-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: 113.93 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 144 QWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 223 VIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIksMQAVEDCGQENHHAPVPPQPDDLSIVCFTS 302
Cdd:cd12116 88 VLTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 303 GTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVL--------ISFLPLahmferviqsqwaptcadvhisYLPLa 374
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHSM---RERLGLGPGDRLLavttyafdISLLEL----------------------LLPL- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 375 hmfermvqsvvyCHGGRVGFFQGDI----RLLSDDMKALCPTIFpvvprllnrmydkifsQAnTP-LKRWLLefaakrkq 449
Cdd:cd12116 190 ------------LAGARVVIAPRETqrdpEALARLIEAHSITVM----------------QA-TPaTWRMLL-------- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 450 aevrsgiirnDSIWDELffnkiqASLggcvRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwT 527
Cdd:cd12116 233 ----------DAGWQGR------AGL----TALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-G 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 528 SGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGT 600
Cdd:cd12116 290 PIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGR 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 601 LKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 666
Cdd:cd12116 369 LEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGAAPDAAALR 435
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
183-656 |
1.46e-26 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 114.20 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 183 PEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkPQKAVLLLEHVERKETPGLkliilmdpfeEALKER 262
Cdd:PRK07514 64 PEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-PANFAWLSKIAAAAGAPHV----------ETLDAD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 263 GQkcGVViksMQAVEDCGQEnhHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN------VVADFSGFlkvtekvifpR 336
Cdd:PRK07514 133 GT--GSL---LEAAAAAPDD--FETVPRGADDLAAILYTSGTTGRSKGAMLSHGNllsnalTLVDYWRF----------T 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 337 QDDVLISFLPLAHmferviqsqwaptcadVHisylplaHMFermVQS-VVYCHGGRVGFFQgdiRLLSDDMKALCP--TI 413
Cdd:PRK07514 196 PDDVLIHALPIFH----------------TH-------GLF---VATnVALLAGASMIFLP---KFDPDAVLALMPraTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 414 FPVVPRLLNRMYdkifsqANTPLKRwllEFAAKrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTV 493
Cdd:PRK07514 247 MMGVPTFYTRLL------QEPRLTR---EAAAH--------------------------------MRLFISGSAPLLAET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 494 LGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNHIKLVDVE---ELNywacKGE-GEICVRGPNVF 567
Cdd:PRK07514 286 HREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLRVTDPEtgaELP----PGEiGMIEVKGPNVF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 568 KGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIfkLAQGEY-VAPEKIENiYIRSQP-VAQIYVHGDSLK 645
Cdd:PRK07514 360 KGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEG-EIDELPgVVESAVIGVPHP 436
|
490
....*....|....
gi 1622946795 646 AF---LVGIVVPDP 656
Cdd:PRK07514 437 DFgegVTAVVVPKP 450
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
280-649 |
1.59e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 114.92 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 280 GQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKV------IFPRQDDVLISFLPLAHMFer 353
Cdd:PRK12492 194 GRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqpLMKEGQEVMIAPLPLYHIY-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 354 viqsQWAPTCadvhisylplahmferMVQSVVYCHggrvgffqgdirllsddmkalcpTIFPVVPRLLNRMYDKifsqan 433
Cdd:PRK12492 272 ----AFTANC----------------MCMMVSGNH-----------------------NVLITNPRDIPGFIKE------ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 434 tpLKRWLLE--------FAAKRKQAEVRSgiirndsiwdeLFFNKIQASLGGcvrmivtGAAPASPTVLGFlRAALGCQV 505
Cdd:PRK12492 303 --LGKWRFSallglntlFVALMDHPGFKD-----------LDFSALKLTNSG-------GTALVKATAERW-EQLTGCTI 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 506 YEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD 584
Cdd:PRK12492 362 VEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAE 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 585 GWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 649
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
290-664 |
1.82e-26 |
|
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: 112.83 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF---LKVTEkvifprqDDVLISFLPlahMFerviqsqwaptcadv 366
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalnLGLTE-------DDNWLCALP---LF--------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 367 HISYLPLahmferMVQSVVYchGGRVGFFQG-DIRLLSDDMKALCPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLefaa 445
Cdd:cd05912 129 HISGLSI------LMRSVIY--GMTVYLVDKfDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL---- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 446 krkqaevrsgiirndsiwdelffnkiqaslggcvrmivtGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPG 524
Cdd:cd05912 197 ---------------------------------------GGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 525 DWTS--GHVGAPLPCNHIKLVDVEELNYwackGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLK 602
Cdd:cd05912 236 DALNkiGSAGKPLFPVELKIEDDGQPPY----EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLY 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 603 VIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflVGIvvPDPEvmpsWAQ 664
Cdd:cd05912 311 VLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGV---------VGI--PDDK----WGQ 356
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
137-657 |
4.76e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 113.13 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 137 RKPNQPYQW-----LSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAI 211
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERL-AGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 212 RYIINTADISTVIV-----DKPQKAV--LLLEHV-------ERKETPGLKLIILMDpfEEALKERGQKCGVViksmqAVE 277
Cdd:PRK08314 101 AHYVTDSGARVAIVgselaPKVAPAVgnLRLRHVivaqysdYLPAEPEIAVPAWLR--AEPPLQALAPGGVV-----AWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 278 DCGQENHHA-PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfsgflkvtekvifprqddvlisflplahMFERVIQ 356
Cdd:PRK08314 174 EALAAGLAPpPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTV-------------------------------MANAVGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 357 SQWAP-TCADVHISYLPLAHM--FERMVQSVVYChGGRVgffqgdirllsddmkalcpTIFP-----VVPRLLNRMydKI 428
Cdd:PRK08314 223 VLWSNsTPESVVLAVLPLFHVtgMVHSMNAPIYA-GATV-------------------VLMPrwdreAAARLIERY--RV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 429 FSQANTPlkRWLLEFAAKRKQAEvrsgiiRNDSiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEG 508
Cdd:PRK08314 281 THWTNIP--TMVVDFLASPGLAE------RDLS------------SL----RYIGGGGAAMPEAVAERLKELTGLDYVEG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 509 YGQTEcTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSD 584
Cdd:PRK08314 337 YGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGK 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 585 GWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFlvgiVVPDPE 657
Cdd:PRK08314 416 RFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
144-666 |
4.82e-26 |
|
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: 114.95 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELA------CYtysmvvVPLyDTLGPGA-IRYIIN 216
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGP--GDLVGVCLERSLEMVVALLAvlkagaAY------VPL-DPAYPAErLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 217 TADISTVIVDkpqkavlllehverketpglkliilmdpfeEALKERGQKCGVVIKSMQAVEDCGQENHHAPVPPQPDDLS 296
Cdd:COG1020 571 DAGARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 297 IVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLKVTEkvifprQDDVLisflplahmferviqsQWAPTCADVHIS--YL 371
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVnllAWMQRRYGLGP------GDRVL----------------QFASLSFDASVWeiFG 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 PLahmfermvqsvvyCHGGRVGFFQGDIRLLSDDMKALC----PTIFPVVPRLLNRMYDkifsqantplkrwllefAAKR 447
Cdd:COG1020 679 AL-------------LSGATLVLAPPEARRDPAALAELLarhrVTVLNLTPSLLRALLD-----------------AAPE 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 448 KQAEVRsgiirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF--TTPGD 525
Cdd:COG1020 729 ALPSLR--------------------------LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPD 782
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 526 WTSGHV--GAPLPCNHIKLVDvEELN---YWACkgeGEICVRGPNVFKGYLKDPDRTKEA-----LDSDG--WLHTGDIG 593
Cdd:COG1020 783 ADGGSVpiGRPIANTRVYVLD-AHLQpvpVGVP---GELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLA 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 594 KWLPAGTLKVIDRKKHifklaQ----------GEyvapekIENIyIRSQP-VAQIYV--HGDSL-KAFLVGIVVPDPEVM 659
Cdd:COG1020 859 RWLPDGNLEFLGRADD-----QvkirgfrielGE------IEAA-LLQHPgVREAVVvaREDAPgDKRLVAYVVPEAGAA 926
|
....*..
gi 1622946795 660 PSWAQKR 666
Cdd:COG1020 927 AAAALLR 933
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
138-627 |
5.62e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 112.92 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 138 KPNQPYQWlSYQEVADRAEFLGSGLLQHNCKACTdqfigVFAQNRPEW---IIAELACYTYSMVVVPLYDTLGPGAIRYI 214
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPGD-----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 215 INTADISTVIVDKPQKAV--LLLEHVERKETPGLKLIILMDPFEEALKErgqkcgvvIKSMQAVEDcgQENHHAPVPPQP 292
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQTrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--------LSLSQIIAD--YEPLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLisflplahmferviqsqWAPTcadvhisylP 372
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVF-----------------MMPA---------P 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 373 LAHmfermvqSVVYCHGGRVGFFQGDIRLLSDDMKAlcptifPVVPRLLNRmyDKI-FSQANTPLkrwllefaakrkqae 451
Cdd:PRK06087 237 LGH-------ATGFLHGVTAPFLIGARSVLLDIFTP------DACLALLEQ--QRCtCMLGATPF--------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 452 vrsgiirndsIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTECTAGcTFTTPGD---W 526
Cdd:PRK06087 287 ----------IYDLLNLLEKQPADLSALRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPH-AVVNLDDplsR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 527 TSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDR 606
Cdd:PRK06087 353 FMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGR 431
|
490 500
....*....|....*....|.
gi 1622946795 607 KKHIFkLAQGEYVAPEKIENI 627
Cdd:PRK06087 432 KKDII-VRGGENISSREVEDI 451
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-661 |
5.78e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 111.76 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 198 VVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVErketpgLKLIILMDPfeealkergqkcGVVIKsmqaVE 277
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG-----AADRLR------DALPASPDP------------GTVLD----AD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 278 DCGQENHHAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSG---FLKVTEkvifprqDDVLISFLPLAHMFEr 353
Cdd:cd05922 101 GIRAARASAPaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaeYLGITA-------DDRALTVLPLSYDYG- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 354 viQSQwaptcadVHISYLPLAhmfermvqSVVYCHGGRVGffqgdiRLLSDDMKALCPTIFPVVP---RLLNRMydkIFS 430
Cdd:cd05922 173 --LSV-------LNTHLLRGA--------TLVLTNDGVLD------DAFWEDLREHGATGLAGVPstyAMLTRL---GFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 431 QANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgfLRAAL-GCQVYEGY 509
Cdd:cd05922 227 PAKLPSLRYLTQAGGRLPQETIAR------------------------------------------LRELLpGAQVYVMY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 510 GQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIklvDVEELNYWACK-GE-GEICVRGPNVFKGYLKDPDRTKEALDSDG 585
Cdd:cd05922 265 GQTEATRRMTYLPPEriLEKPGSIGLAIPGGEF---EILDDDGTPTPpGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 586 WLHTGDIGkWLPA-GTLKVIDRKKHIFKLAqGEYVAPEKIENIyIRSQP---VAQIYVHGDSLKAFLVGIVVPDPEVMPS 661
Cdd:cd05922 342 VLHTGDLA-RRDEdGFLFIVGRRDRMIKLF-GNRISPTEIEAA-ARSIGliiEAAAVGLPDPLGEKLALFVTAPDKIDPK 418
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
146-664 |
8.79e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 112.00 E-value: 8.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADI 220
Cdd:PRK06188 38 LTYGQLADRISryiqaFEALGLGTGDA-------VALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 221 STVIVDK---PQKAVLLLEHVerketPGLKLIILMDPFEEalkerGQKCGVVIKSMQavedcgqenhHAPVPP--QPDDL 295
Cdd:PRK06188 111 STLIVDPapfVERALALLARV-----PSLKHVLTLGPVPD-----GVDLLAAAAKFG----------PAPLVAaaLPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 296 SIVCFTSGTTGNPKGAMLTHGNVVAdfsgflkvtekvifprqddvlisflplahmferviQSQWAptCAD----VHISYL 371
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIAT-----------------------------------MAQIQ--LAEwewpADPRFL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 ---PLAHMFERMVQSVVYchggRVGFFqgdIRLLSDDMKALCPTI--------FpVVPRLLNRmydkifsqantplkrwL 440
Cdd:PRK06188 214 mctPLSHAGGAFFLPTLL----RGGTV---IVLAKFDPAEVLRAIeeqritatF-LVPTMIYA----------------L 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 441 LEFAAKRKqaevrsgiiRNDSiwdelffnkiqaSLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF 520
Cdd:PRK06188 270 LDHPDLRT---------RDLS------------SL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITY 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 521 TTPGDWTSGHV------GAPLPCNHIKLVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIG 593
Cdd:PRK06188 325 LRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVA-QGEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVA 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 594 KWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 664
Cdd:PRK06188 402 REDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
146-666 |
9.78e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 110.65 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05935 2 LTYLELLEVVKKLASFL--SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPQkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTT 305
Cdd:cd05935 80 GSEL---------------------------------------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHGNVVADFSGflkvtekvifprqddvlisflpLAHMFerviqsqwAPTCADVHISYLPLAHM--FERMVQS 383
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQ----------------------SAVWT--------GLTPSDVILACLPLFHVtgFVGSLNT 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 384 VVYCHGGRVGFFQGDIRLLSDDMKALCPTIFPVVPRLLNRMydkifsqANTPlkrwllefaakrkqaevrsgiirndsiw 463
Cdd:cd05935 147 AVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL-------LATP---------------------------- 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 464 delffnKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLV 543
Cdd:cd05935 192 ------EFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVI 265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 544 DVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDG---WLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVA 620
Cdd:cd05935 266 DIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVW 344
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946795 621 PEKIENIYIRSQPVAQIYV-------HGDSLKAFLVgiVVP------DPEVMPSWAQKR 666
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVisvpderVGEEVKAFIV--LRPeyrgkvTEEDIIEWAREQ 401
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
187-625 |
1.42e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 113.48 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 187 IAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllEHVERKETPGLKLIILMDP---FEEALKER- 262
Cdd:PRK08633 680 LANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSR--------KFLEKLKNKGFDLELPENVkviYLEDLKAKi 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 263 --GQKC--GVVIKSMQAVEDCGQENHhapvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQD 338
Cdd:PRK08633 752 skVDKLtaLLAARLLPARLLKRLYGP----TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRND 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 339 DVLISFLPLAHMFERVIqSQWAPTCADVHISYLP-------LAHMFERmvqsvvycHGGRVgffqgdirllsddmkaLC- 410
Cdd:PRK08633 824 DVILSSLPFFHSFGLTV-TLWLPLLEGIKVVYHPdptdalgIAKLVAK--------HRATI----------------LLg 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 411 -PTIFpvvprllnRMYdkifsqantplkrwllefaakrkqaevrsgiIRNDSIWDELFfnkiqASLggcvRMIVTGAAPA 489
Cdd:PRK08633 879 tPTFL--------RLY-------------------------------LRNKKLHPLMF-----ASL----RLVVAGAEKL 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 490 SPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWT-----SGHVGAPLPCNHIKLVDVEELNYWACKGEGEI 559
Cdd:PRK08633 911 KPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLI 990
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946795 560 CVRGPNVFKGYLKDPDRTKEAL---DSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIE 625
Cdd:PRK08633 991 LIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
273-639 |
6.33e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 109.68 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 273 MQAVEDCGQENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF-SGFLKVTEKVIfprQDDVLISFLPLAHMF 351
Cdd:PLN02330 166 LEAADRAGDTSDNEEI--LQTDLCALPFSSGTTGISKGVMLTHRNLVANLcSSLFSVGPEMI---GQVVTLGLIPFFHIY 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 352 erviqsqwaptcadvHISYLPLAHMFERmvqsvvychGGRVGFFQGDIRLLSDDMKALCPTIFPVVPrllnrmydkifsq 431
Cdd:PLN02330 241 ---------------GITGICCATLRNK---------GKVVVMSRFELRTFLNALITQEVSFAPIVP------------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 432 antPLKRWLLEfaakrkqaevrsgiirnDSIWDELFFNKIQaslggcVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYG 510
Cdd:PLN02330 284 ---PIILNLVK-----------------NPIVEEFDLSKLK------LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 511 QTECTagCTFTTPGDWTSGH-------VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDS 583
Cdd:PLN02330 338 LTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDE 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 584 DGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV 639
Cdd:PLN02330 416 DGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
285-661 |
7.13e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 108.92 E-value: 7.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 285 HAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifprQDDVLISFLPLAHmferviqsqwaptca 364
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFH--------------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 365 dVHISYL----PLahmfeRMVQSVVycHGGRvgfF--QGDIRLLSDDmkalcPTIFPVVPRllnrMYDKIfsqantplkr 438
Cdd:PRK07787 181 -VHGLVLgvlgPL-----RIGNRFV--HTGR---PtpEAYAQALSEG-----GTLYFGVPT----VWSRI---------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 439 wllefAAKRKQAEVRSGiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGC 518
Cdd:PRK07787 231 -----AADPEAARALRG-----------------------ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 519 TFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL 596
Cdd:PRK07787 283 STRADGERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVD 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622946795 597 PAGTLKVIDR------KKHIFKLAQGEyvapekIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 661
Cdd:PRK07787 362 PDGMHRIVGRestdliKSGGYRIGAGE------IETALLGHPGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
286-629 |
1.63e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 108.39 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 286 APVPPQpDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvtekvifprqddvlisflplahmFErviQSQWA-PTCA 364
Cdd:PLN02574 192 KPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVR-----------------------FE---ASQYEyPGSD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 365 DVHISYLPLAHMFermvqsvvychgGRVGFFQGDIRL-----------LSDDMKAL---CPTIFPVVPRLLNRMYDKIFS 430
Cdd:PLN02574 245 NVYLAALPMFHIY------------GLSLFVVGLLSLgstivvmrrfdASDMVKVIdrfKVTHFPVVPPILMALTKKAKG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 431 QANTPLKrwllefaakrkqaevrsgiirndsiwdelffnkiqaslggCVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGY 509
Cdd:PLN02574 313 VCGEVLK----------------------------------------SLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGY 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 510 GQTECTAGCT--FTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL 587
Cdd:PLN02574 353 GMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL 432
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622946795 588 HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYI 629
Cdd:PLN02574 433 RTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAVLI 473
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
137-620 |
1.69e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 108.81 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 137 RKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPL---YDTLG--PGAI 211
Cdd:PRK08180 61 RGADGGWRRLTYAEALERVRAIAQALLDRGLSA--ERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 212 RYIINTADISTVIVDKPQK-----AVLLLEHVE----RKETPGLKLIilmdPFEEALKERGQKcgvviksmqAVEDcgqe 282
Cdd:PRK08180 139 RHVLELLTPGLVFADDGAAfaralAAVVPADVEvvavRGAVPGRAAT----PFAALLATPPTA---------AVDA---- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 283 nHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekVIFPRQDD-VLISFLPLAHMFErviqsqwap 361
Cdd:PRK08180 202 -AHAAV--GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQT---FPFLAEEPpVLVDWLPWNHTFG--------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 362 TCADVHIS-------YL----PLAHMFERMVqsvvychggrvgffqgdirllsDDMKALCPTIFPVVPRLlnrmydkifs 430
Cdd:PRK08180 267 GNHNLGIVlynggtlYIddgkPTPGGFDETL----------------------RNLREISPTVYFNVPKG---------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 431 qantplkrWLLEFAAKRKQAEVRsgiirndsiwdELFFNKiqaslggcVRMIVTGAAPASPTVLGFL----RAALGCQVY 506
Cdd:PRK08180 315 --------WEMLVPALERDAALR-----------RRFFSR--------LKLLFYAGAALSQDVWDRLdrvaEATCGERIR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 507 --EGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEelnywackGEGEICVRGPNVFKGYLKDPDRTKEALDSD 584
Cdd:PRK08180 368 mmTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEE 439
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1622946795 585 GWLHTGDIGKWL----PAGTLKVIDRKKHIFKLAQGEYVA 620
Cdd:PRK08180 440 GYYRSGDAVRFVdpadPERGLMFDGRIAEDFKLSSGTWVS 479
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
146-641 |
4.97e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 106.20 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVK--KGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DkpqkavlllehverketpglkliilmDPFEEALKERGQkcgVVIKSMQAvedcGQENHHAPVPPQP-DDLSIVCFTSGT 304
Cdd:PRK03640 106 D--------------------------DDFEAKLIPGIS---VKFAELMN----GPKEEAEIQEEFDlDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 305 TGNPKGAMLTHGNVVADFSGF---LKVTEKvifprqDDVLISfLPlahMFerviqsqwaptcadvHISYLPLahmferMV 381
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSAVGSalnLGLTED------DCWLAA-VP---IF---------------HISGLSI------LM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 382 QSVVYchGGRV----GFFQGDI-RLLSDDMKalcpTIFPVVPRLLNRMYDKIfSQANTPlkrwllefaakrkqaevrsgi 456
Cdd:PRK03640 202 RSVIY--GMRVvlveKFDAEKInKLLQTGGV----TIISVVSTMLQRLLERL-GEGTYP--------------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 457 irnDSiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGA 533
Cdd:PRK03640 254 ---SS-----------------FRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGK 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 534 PL-PCNhIKLVDveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFk 612
Cdd:PRK03640 312 PLfPCE-LKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI- 386
|
490 500
....*....|....*....|....*....
gi 1622946795 613 LAQGEYVAPEKIENIYIRSQPVAQIYVHG 641
Cdd:PRK03640 387 ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
132-744 |
6.02e-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: 106.75 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 132 PCLGFRKPNQPYQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTY---SMVVVPLYDTLGp 208
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMS- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 209 gairyiintADISTvivdkpqkavllLEHVERKETPGLKLIILMDPFEEALKE-----------RGQKCG---VVIKSMQ 274
Cdd:cd05921 89 ---------QDLAK------------LKHLFELLKPGLVFAQDAAPFARALAAifplgtplvvsRNAVAGrgaISFAELA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 275 AVEDCGQ-ENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDD---VLISFLPlahm 350
Cdd:cd05921 148 ATPPTAAvDAAFAAV--GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT-----YPFFGEeppVLVDWLP---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 351 ferviqsqWAPTCADVHISYLPLAHmfermvQSVVYCHGGR--VGFFQGDIRLLSDDMkalcPTIFPVVPrllnrmydki 428
Cdd:cd05921 217 --------WNHTFGGNHNFNLVLYN------GGTLYIDDGKpmPGGFEETLRNLREIS----PTVYFNVP---------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 429 fsqantplKRWllefaakrkqaEVRSGIIRNDSIWDELFFNKiqaslggcVRMIVTGAAPASPTVLGFLRA----ALGCQ 504
Cdd:cd05921 269 --------AGW-----------EMLVAALEKDEALRRRFFKR--------LKLMFYAGAGLSQDVWDRLQAlavaTVGER 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 505 V--YEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVdveelnywACKGEGEICVRGPNVFKGYLKDPDRTKEALD 582
Cdd:cd05921 322 IpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFD 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 583 SDGWLHTGDIGKWL----PAGTLKVIDRKKHIFKLAQGEYVA--PekieniyIRSQPVAQI--YVHgDSL-----KAFLV 649
Cdd:cd05921 394 EEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVG 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 650 GIVVPDPEVMPswAQKRGIEGTYADLCTSKDLKKAILEDMVRLGKESGLHSFEQVKAIhIHSDMFSVQNGLLTPTLKAKR 729
Cdd:cd05921 466 ALVFPDLLACR--RLVGLQEASDAEVLRHAKVRAAFRDRLAALNGEATGSSSRIARAL-LLDEPPSIDKGEITDKGYINQ 542
|
650
....*....|....*
gi 1622946795 730 PELREYFKKQIEELY 744
Cdd:cd05921 543 RAVLERRAALVERLY 557
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
181-649 |
8.02e-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: 105.11 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 181 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlllehverketpglkliilmdpfeealk 260
Cdd:cd05972 34 RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 261 ergqkcgvviksmqavedcgqenhhapvppqpDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDv 340
Cdd:cd05972 81 --------------------------------EDPALIYFTSGTTGLPKGVLHTHSY----PLGHIPTAAYWLGLRPDD- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 341 lisflplahMFERVIQSQWApTCADVHIsYLPLAHMFermvqSVVYCHGGRVgffqgdirllsDDMKALcptifpvvpRL 420
Cdd:cd05972 124 ---------IHWNIADPGWA-KGAWSSF-FGPWLLGA-----TVFVYEGPRF-----------DAERIL---------EL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 421 LNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGFLRAA 500
Cdd:cd05972 168 LERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRL---------------------------VVSAGEPLNPEVIEWWRAA 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 501 LGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNV--FKGYLKDPDRTK 578
Cdd:cd05972 221 TGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTE 299
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 579 EALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 649
Cdd:cd05972 300 ASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
144-657 |
3.57e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 103.79 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 144 QWLSYQEVADRAEFLgSGLLQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:PRK06839 26 EEMTYKQLHEYVSKV-AAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 224 IVDKP-QKAVLLLEHVERKETPglkliilmdpfeealkergqkcgVVIKSMQAVEDCGQENHhapVPPQPDDLSIVCFTS 302
Cdd:PRK06839 105 FVEKTfQNMALSMQKVSYVQRV-----------------------ISITSLKEIEDRKIDNF---VEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 303 GTTGNPKGAMLTHGNvvadfsgflkvtekvifprqddvlisflplahMFERVIQSQWAP--TCADVHISYLPLAHMferm 380
Cdd:PRK06839 159 GTTGKPKGAVLTQEN--------------------------------MFWNALNNTFAIdlTMHDRSIVLLPLFHI---- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 381 vqsvvychgGRVGFFQgdirllsddmkalCPTIFP----VVPRLLNRmyDKIFSQANTplKRWLLEFAAKRKQAEVRSGI 456
Cdd:PRK06839 203 ---------GGIGLFA-------------FPTLFAggviIVPRKFEP--TKALSMIEK--HKVTVVMGVPTIHQALINCS 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 457 IRNDSIWDElffnkiqaslggcVRMIVTGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVG 532
Cdd:PRK06839 257 KFETTNLQS-------------VRWFYNGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 533 APLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFk 612
Cdd:PRK06839 321 KPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI- 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622946795 613 LAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 657
Cdd:PRK06839 398 ISGGENIYPLEVEQV---------INKLSDVYEVAVVG--RQHVK 431
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
145-593 |
4.13e-23 |
|
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: 104.24 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 145 WLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDTLGPGA---IRYIINTADIS 221
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 222 TVIVDKPQKAvLLLEHVERKETPGLKLIILMDPFEEALKERGQkcgvviksmqavedcgqenhhaPVPPQPDDLSIVCFT 301
Cdd:cd05931 101 VVLTTAAALA-AVRAFAASRPAAGTPRLLVVDLLPDTSAADWP----------------------PPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 302 SGTTGNPKGAMLTHGNVVADFSGFLkvteKVIFPRQDDVLISFLPLAHmferviqsqwaptcaDVHISYLPLAHMFermv 381
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIR----RAYGLDPGDVVVSWLPLYH---------------DMGLIGGLLTPLY---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 382 qsvvycHGGRVGFFQgdirllsddmkalcPTIFpvvprlLNRmydkifsqantPLkRWL-----------------LEFA 444
Cdd:cd05931 215 ------SGGPSVLMS--------------PAAF------LRR-----------PL-RWLrlisryratisaapnfaYDLC 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 445 AKRKQAEVRSGIirndsiwdELffnkiqaslgGCVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTEC 514
Cdd:cd05931 257 VRRVRDEDLEGL--------DL----------SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 515 TAGCTFTTPG----------DWTSGHV----------------GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFK 568
Cdd:cd05931 315 TLFVSGGPPGtgpvvlrvdrDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVAS 394
|
490 500 510
....*....|....*....|....*....|.
gi 1622946795 569 GYLKDPDRTKE------ALDSDGWLHTGDIG 593
Cdd:cd05931 395 GYWGRPEATAEtfgalaATDEGGWLRTGDLG 425
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
289-655 |
5.17e-23 |
|
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: 102.39 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 289 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFerviqsqWAptCADVHI 368
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--F-------DA--CIGEIF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 369 SYLplahmfermvqsvvyCHGGRVgFFQGDIRLLSDDMKALcpTIFPVVPRLLNRMYDKIFSQantplkrwllefaakrk 448
Cdd:cd17653 166 STL---------------CNGGTL-VLADPSDPFAHVARTV--DALMSTPSILSTLSPQDFPN----------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 449 qaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDW 526
Cdd:cd17653 211 ------------------------------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 527 TsgHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGT 600
Cdd:cd17653 259 V--TIGKPIPNSTCYILD-ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGG 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 601 LKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ---IYVHGDSLKAFlvgiVVPD 655
Cdd:cd17653 336 LEFLGREDNQVKV-RGFRINLEEIEEVVLQSQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
146-656 |
1.60e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 101.93 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKK-GDR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DkpqkaVLLLEHVErketPGLKLIiLMDPFEEALKERGQkcgVVIKSMQAVEDC--GQENHHAPVPPQPDDLSIVCFTSG 303
Cdd:PRK08316 115 D-----PALAPTAE----AALALL-PVDTLILSLVLGGR---EAPGGWLDFADWaeAGSVAEPDVELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 304 TTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHmferviqsqwaptCADVHISYLPlahmfermvqs 383
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDM----SADDIPLHALPLYH-------------CAQLDVFLGP----------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 384 VVYCHGGRVGFFQGDIRLLSDDMKALCPTIFpvvprllnrmydkifsqantplkrwlleFAAKrkqaevrsgiirndSIW 463
Cdd:PRK08316 234 YLYVGATNVILDAPDPELILRTIEAERITSF----------------------------FAPP--------------TVW 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 464 DELF----FNKIQASlggCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP---- 534
Cdd:PRK08316 272 ISLLrhpdFDTRDLS---SLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsag 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 535 LPCNHI--KLVDvEELNYWAcKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIF 611
Cdd:PRK08316 345 RPVLNVetRVVD-DDGNDVA-PGEvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMI 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622946795 612 KLAqGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 656
Cdd:PRK08316 422 KTG-GENVASREVEEA---------LYTHPAVAEVAVIG--LPDP 454
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
181-627 |
1.76e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 102.16 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 181 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQKAVLLLEhvERKETPGLKLIILMDP------ 254
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCG-AHVVVTEAALAPVATA--VRDIVPLLSTVVVAGGssddsv 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 255 --FEEALKERGQKcgvviksmqavedcgqenhHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkv 332
Cdd:PRK07786 153 lgYEDLLAEAGPA-------------------HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 333 iFPRQDDVLISFLPLahmferviqsqwaptcadVHISYL-PLAHMFERMVQSVVYchggRVGFFqgDIRLLSDDMKALCP 411
Cdd:PRK07786 212 -ADINSDVGFVGVPL------------------FHIAGIgSMLPGLLLGAPTVIY----PLGAF--DPGQLLDVLEAEKV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 412 TIFPVVPrllnrmydkifsqantplKRWLLEFAAKRKQAevrsgiiRNDSIwdelffnkiqaslggcvRMIVTGAAPASP 491
Cdd:PRK07786 267 TGIFLVP------------------AQWQAVCAEQQARP-------RDLAL-----------------RVLSWGAAPASD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 492 TVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVF 567
Cdd:PRK07786 305 TLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLM 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 568 KGYLKDPDRTKEALDSdGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENI 627
Cdd:PRK07786 383 SGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENV 440
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
291-657 |
1.88e-22 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 101.47 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvtekvIFPRQDDVlisflplahmfeRVIQSqwAPTCADVHIsy 370
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGR-----ALGLTSES------------RVLQF--ASYTFDVSI-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 371 lplAHMFermvqsVVYCHGG---------RVGFFQGDIRllsdDMKALCPTIFPVVPRLLNRmydkifsqANTPlkrwll 441
Cdd:cd05918 163 ---LEIF------TTLAAGGclcipseedRLNDLAGFIN----RLRVTWAFLTPSVARLLDP--------EDVP------ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 442 efaakrkqaevrsgiirndsiwdelffnkiqaslggCVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT 521
Cdd:cd05918 216 ------------------------------------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 522 TPG-DWTSGHVGAPLPC--------NHIKLVDVeelnywackGE-GEICVRGPNVFKGYLKDPDRTKEA-LDSDGWLH-- 588
Cdd:cd05918 258 PVVpSTDPRNIGRPLGAtcwvvdpdNHDRLVPI---------GAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqe 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 589 ----------TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENiYIRSQP------VAQIYVH-GDSLKAFLVGI 651
Cdd:cd05918 329 gsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQRVELGEIEH-HLRQSLpgakevVVEVVKPkDGSSSPQLVAF 406
|
....*.
gi 1622946795 652 VVPDPE 657
Cdd:cd05918 407 VVLDGS 412
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
146-659 |
2.50e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 101.81 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVV---PLYDTlgpGAIRYIINTADIST 222
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEK-GDR-VGIWAPNVPEWVLTQFATAKIGAILVtinPAYRL---SELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 223 -VIVDK--------------PQKAVLLLEHVERKETPGLKLIILMDpfeeALKERGqkcgvvIKSMQAVEDCGQENHHAP 287
Cdd:PRK08315 119 lIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLG----DEKHPG------MLNFDELLALGRAVDDAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 288 VPP-----QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsGFLkVTEKVIFPRQDDVLISfLPLAHMF----------- 351
Cdd:PRK08315 189 LAArqatlDPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAMKLTEEDRLCIP-VPLYHCFgmvlgnlacvt 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 352 --------------ERVIQSQWAPTCADVH------ISylPLAH-MFERMVQSVVychggRVGFFQGdirllsddmkALC 410
Cdd:PRK08315 265 hgatmvypgegfdpLATLAAVEEERCTALYgvptmfIA--ELDHpDFARFDLSSL-----RTGIMAG----------SPC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 411 PTifPVVPRLLNRMYdkifsqantplkrwllefaakrkQAEVrsgiirndSIwdelffnkiqaslggcvrmivtgaapas 490
Cdd:PRK08315 328 PI--EVMKRVIDKMH-----------------------MSEV--------TI---------------------------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 491 ptvlgflraalgcqvyeGYGQTECTAGCTFTTPGD------WTsghVGAPLPCNHIKLVDVEelnywacKGE-------G 557
Cdd:PRK08315 347 -----------------AYGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-------TGEtvprgeqG 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 558 EICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkwlpagtlkVIDrkkhifklAQGeYVapeKI------------E 625
Cdd:PRK08315 400 ELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLA---------VMD--------EEG-YV---NIvgrikdmiirggE 458
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1622946795 626 NIYIRsqpvaQI----YVHGDSLKAFLVGivVPDP----EVM 659
Cdd:PRK08315 459 NIYPR-----EIeeflYTHPKIQDVQVVG--VPDEkygeEVC 493
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
181-649 |
8.25e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 99.76 E-value: 8.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 181 NRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpQKAVLLLEHVERKETPGLKLIILMDPFEEALK 260
Cdd:PRK08008 71 NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPADD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 261 ergqkcGVV----IKSMQAVEDCgqenhHAPvPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKVIfpR 336
Cdd:PRK08008 149 ------GVSsftqLKAQQPATLC-----YAP-PLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCAL--R 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 337 QDDVLISFLPlahmferviqsqwaptcaDVHISylplahmfermvqsvvychggrvgfFQgdirllsddmkalCPTIFPV 416
Cdd:PRK08008 213 DDDVYLTVMP------------------AFHID-------------------------CQ-------------CTAAMAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 417 vprllnrmydkiFSQANTPLkrwLLE-FAAKRKQAEVRsgiirndsiwdelffnKIQASLGGCVRMIVTG--AAPASPT- 492
Cdd:PRK08008 237 ------------FSAGATFV---LLEkYSARAFWGQVC----------------KYRATITECIPMMIRTlmVQPPSANd 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 493 -------VLGFLRAA----------LGCQVYEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDveELNYWA 552
Cdd:PRK08008 286 rqhclreVMFYLNLSdqekdafeerFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 553 CKGE-GEICVRG---PNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIy 628
Cdd:PRK08008 362 PAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI- 439
|
490 500
....*....|....*....|....*....
gi 1622946795 629 IRSQP-VAQIYVHG--DSL-----KAFLV 649
Cdd:PRK08008 440 IATHPkIQDIVVVGikDSIrdeaiKAFVV 468
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
288-649 |
9.81e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 99.72 E-value: 9.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 288 VPPQPD-DLSIVCFTSGTTGNPKGAMLTHGNVVADfsgflkvtekvifprqddvlisflplahmfeRVIQSQWAPTCAD- 365
Cdd:PRK06710 200 VPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN-------------------------------TLMGVQWLYNCKEg 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 366 --VHISYLPLAHMF-ERMVQSVVYCHGGRVGFF-QGDIRLLSDDMKALCPTIFPVVPRLLnrmydkiFSQANTPLkrwll 441
Cdd:PRK06710 249 eeVVLGVLPFFHVYgMTAVMNLSIMQGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIY-------IALLNSPL----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 442 efaakRKQAEVRSgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfT 521
Cdd:PRK06710 317 -----LKEYDISS------------------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----V 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 522 TPGDW-----TSGHVGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWL 596
Cdd:PRK06710 364 THSNFlwekrVPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMD 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 597 PAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV-------HGDSLKAFLV 649
Cdd:PRK06710 443 EDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
136-666 |
1.16e-21 |
|
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: 98.94 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 136 FRKPNQPY-----QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA 210
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPI-DPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 211 -IRYIINTADISTVIVDKPQKAVLLlehverketpGLKLIILMDpfEEALKERGQkcgvviksmqavedcgqENHHAPVp 289
Cdd:cd17655 85 rIQYILEDSGADILLTQSHLQPPIA----------FIGLIDLLD--EDTIYHEES-----------------ENLEPVS- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 290 pQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtEKVIFPRQDDVLISFLPLAhmFERVIQSQWAP--TCADVH 367
Cdd:cd17655 135 -KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA----NKVIYQGEHLRVALFASIS--FDASVTEIFASllSGNTLY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 368 ISYLPLAHMFERMVQSVvychggrvgffqgdirllsDDMKALCPTIFPVVPRLLNRMYDKIFSqantPLKRwllefaakr 447
Cdd:cd17655 208 IVRKETVLDGQALTQYI-------------------RQNRITIIDLTPAHLKLLDAADDSEGL----SLKH--------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 448 kqaevrsgiirndsiwdelffnkiqaslggcvrMIVTGAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTF--TTPG 524
Cdd:cd17655 256 ---------------------------------LIVGGEALSTELAKKIIeLFGTNPTITNAYGPTETTVDASIyqYEPE 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 525 DWTSGHV--GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWL 596
Cdd:cd17655 303 TDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWL 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946795 597 PAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ---IYVHGDSLKAFLVGIVVPDPEVMPSWAQKR 666
Cdd:cd17655 382 PDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEavvIARKDEQGQNYLCAYIVSEKELPVAQLREF 453
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
490-657 |
2.13e-21 |
|
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: 96.18 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 490 SPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFK 568
Cdd:cd17637 124 APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAGEtGEIVVRGPLVFQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 569 GYLKDPDRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRK--KHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYVHGdslk 645
Cdd:cd17637 201 GYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV-ILEHPaIAEVCVIG---- 273
|
170
....*....|..
gi 1622946795 646 aflvgivVPDPE 657
Cdd:cd17637 274 -------VPDPK 278
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
290-656 |
2.20e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 98.59 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadFSGFLKVTEKVIFpRQDDVLISFLPLAH----MF----------ERVI 355
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYAERLGL-GADDVILMASPMAHqtgfMYglmmpvmlgaTAVL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 356 QSQWAPTcadvhisylplahmfeRMVQSVvycHGGRVGFFQGDIRLLSD--DMKALCPTifpVVPRLlnrmydKIFSQAN 433
Cdd:PRK13295 270 QDIWDPA----------------RAAELI---RTEGVTFTMASTPFLTDltRAVKESGR---PVSSL------RTFLCAG 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 434 TPLKRWLLEFAakrkqaevrsgiirndsiwdelffnkiqaslggcvrmivtgaapasptvlgflRAALGCQVYEGYGQTE 513
Cdd:PRK13295 322 APIPGALVERA-----------------------------------------------------RAALGAKIVSAWGMTE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 514 CTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTkeALDSDGWLHTG 590
Cdd:PRK13295 349 NGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTG 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946795 591 DIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQiyvhgdslkaflVGIV-VPDP 656
Cdd:PRK13295 425 DLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQ------------VAIVaYPDE 478
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
245-625 |
2.23e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 98.53 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 245 GLKLIILMDPFEEA---LKERGQKcgvviksMQAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAD 321
Cdd:PRK07768 108 GAKAVVVGEPFLAAapvLEEKGIR-------VLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 322 FSGflkVTEKVIFPRQDDVLISFLPLAH-MferviqsqwaptcadvhisylplahmfermvqsvvychgGRVGFfqgdir 400
Cdd:PRK07768 181 AEA---MFVAAEFDVETDVMVSWLPLFHdM---------------------------------------GMVGF------ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 401 lLSDDMKALC------PTIFPVVPRLLNRMYDKiFSQANTPLKRWLLEFAAKR--KQAEvrsgiirnDSIWDElffnkiq 472
Cdd:PRK07768 213 -LTVPMYFGAelvkvtPMDFLRDPLLWAELISK-YRGTMTAAPNFAYALLARRlrRQAK--------PGAFDL------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 473 aslgGCVRMIVTGAAPASPTVL----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD----------------- 525
Cdd:PRK07768 276 ----SSLRFALNGAEPIDPADVedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrr 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 526 ---WTSGHV------GAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLkDPDRTKEALDSDGWLHTGDIGKWL 596
Cdd:PRK07768 348 avpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLT 425
|
410 420
....*....|....*....|....*....
gi 1622946795 597 PAGTLKVIDRKKHIFKLAqGEYVAPEKIE 625
Cdd:PRK07768 426 EEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
146-657 |
2.26e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 98.57 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKAcTDQfIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGA-GDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 dkpQKAVL-LLEHVeRKETPgLKLII---LMD--------PFEEALKERGQKCGVVIKSMQAVEDCGQENhhAPVPPQPD 293
Cdd:PRK06178 137 ---LDQLApVVEQV-RAETS-LRHVIvtsLADvlpaeptlPLPDSLRAPRLAAAGAIDLLPALRACTAPV--PLPPPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPlahMFerviqsqWaptcadvhISylpl 373
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVG---GEDSVFLSFLP---EF-------W--------IA---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 374 ahmfermvqsvvychGGRVGFfqgdirllsddmkalcptIFPvvprllnrmydkIFSQANTPL-KRW-LLEFAAKRKQAE 451
Cdd:PRK06178 265 ---------------GENFGL------------------LFP------------LFSGATLVLlARWdAVAFMAAVERYR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 452 VRSGIIRNDSIwDELF---------FNKIQASlgGCVRMIvtgaAPASPTVLGFLRAALGCQVYEG-YGQTECTAGCTFT 521
Cdd:PRK06178 300 VTRTVMLVDNA-VELMdhprfaeydLSSLRQV--RVVSFV----KKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 522 TpGDWTSGH--------VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIG 593
Cdd:PRK06178 373 A-GFQDDDFdllsqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622946795 594 KWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGivVPDPE 657
Cdd:PRK06178 451 KIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQ---------HPAVLGSAVVG--RPDPD 502
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
147-656 |
2.36e-21 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 98.47 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 147 SYQEVADRAEFLGSGLlqHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVD 226
Cdd:cd12119 27 TYAEVAERARRLANAL--RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 227 K---PQKAVLL--LEHVERketpglklIILMDPFEEALKERGQKcgvVIKSMQAVEDcgqenhHAPVPPQPD----DLSI 297
Cdd:cd12119 105 RdflPLLEAIAprLPTVEH--------VVVMTDDAAMPEPAGVG---VLAYEELLAA------ESPEYDWPDfdenTAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 298 VCFTSGTTGNPKGAMLTHGNVV--------ADFSGFlkvtekvifpRQDDVLISFLPLAHMferviqSQW-----APTCA 364
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHRSLVlhamaallTDGLGL----------SESDVVLPVVPMFHV------NAWglpyaAAMVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 365 ------DVHISYLPLAHMFERmvQSVVYCHGgrvgffqgdirllsddmkalCPTIfpvvprllnrmydkifsqantplkr 438
Cdd:cd12119 232 aklvlpGPYLDPASLAELIER--EGVTFAAG--------------------VPTV------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 439 WLLEFAA-KRKQAEVRSGiirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAG 517
Cdd:cd12119 265 WQGLLDHlEANGRDLSSL------------------------RRVVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTETSPL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 518 CTFTTPgdwTSGHV--------------GAPLPCNHIKLVDVE--ELNyWACKGEGEICVRGPNVFKGYLKDPDRTkEAL 581
Cdd:cd12119 320 GTVARP---PSEHSnlsedeqlalrakqGRPVPGVELRIVDDDgrELP-WDGKAVGELQVRGPWVTKSYYKNDEES-EAL 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 582 DSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVhgdslkaflvgIVVPDP 656
Cdd:cd12119 395 TEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
146-658 |
5.88e-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: 96.55 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADISTVI 224
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDA--GDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAErIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 225 VDkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFTSGT 304
Cdd:cd05945 94 AD-----------------------------------------------------------------GDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 305 TGNPKGAMLTHGNVVAdfsgflkvtekvifprqddvlisflplahmFERVIQSQWAPTCADVHISYLPLAhmFERMVQSV 384
Cdd:cd05945 109 TGRPKGVQISHDNLVS------------------------------FTNWMLSDFPLGPGDVFLNQAPFS--FDLSVMDL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 385 VYC--HGGrvgffqgdirllsddmkalcpTIFPVvPRLLNRMYDKIFSQ-ANTPLKRWLlefaakrkqaevrsgiiRNDS 461
Cdd:cd05945 157 YPAlaSGA---------------------TLVPV-PRDATADPKQLFRFlAEHGITVWV-----------------STPS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 462 IWDELF----FNkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVG 532
Cdd:cd05945 198 FAAMCLlsptFT--PESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIG 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 533 APLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD---GWLHTGDIGKWLPAGTLKVIDRKKH 609
Cdd:cd05945 276 YAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDF 354
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1622946795 610 IFKLaQGEYVAPEKIENIYIRSQPVAQIYV----HGDSlKAFLVGIVVPDPEV 658
Cdd:cd05945 355 QVKL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEK-VTELIAFVVPKPGA 405
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-666 |
8.86e-20 |
|
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: 91.77 E-value: 8.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADfsgfLKVTEKVIFPRQDDVLISFLPLAHMFERVIQsqwaptcadvhisyl 371
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN----AWMLALNSLFDPDDVLLCGLPLFHVNGSVVT--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 pLAHMFERMVQSVVYCHGGRVGffqgdirllsddmkalcPTIFPVVPRLLNRMYDKIFSQANTPLkrwllefaAKRKQAE 451
Cdd:cd05944 62 -LLTPLASGAHVVLAGPAGYRN-----------------PGLFDNFWKLVERYRITSLSTVPTVY--------AALLQVP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 452 VRSGIirndsiwdelffnkiqaslgGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGH 530
Cdd:cd05944 116 VNADI--------------------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 531 VGAPLPCNHIKLV--DVEELNYWACKGE--GEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDR 606
Cdd:cd05944 176 VGLRLPYARVRIKvlDGVGRLLRDCAPDevGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGR 254
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946795 607 KKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYVHG--DSLKAFL-VGIV--VPDPEVMP----SWAQKR 666
Cdd:cd05944 255 AKDLI-IRGGHNIDPALIEEALLRHPAVAFAGAVGqpDAHAGELpVAYVqlKPGAVVEEeellAWARDH 322
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
175-669 |
1.06e-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: 92.50 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDkpqkavlllehverketpglkliilmdp 254
Cdd:cd05971 34 VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD---------------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 255 feealkergqkcgvviksmqavedcgqenhhapvppQPDDLSIVCFTSGTTGNPKGAMLTH----GNVVADFSGFlkvte 330
Cdd:cd05971 86 ------------------------------------GSDDPALIIYTSGTTGPPKGALHAHrvllGHLPGVQFPF----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 331 kVIFPRQDDVLISFLPLAhmferviqsqWAPTCADVHISYL----P-LAHMFERmvqsvvychggrvgfFQGD--IRLLS 403
Cdd:cd05971 125 -NLFPRDGDLYWTPADWA----------WIGGLLDVLLPSLyfgvPvLAHRMTK---------------FDPKaaLDLMS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 404 D---DMKALCPTIFpvvprllnrmydKIFSQANTPLKRWLLEfaakrkqaevrsgiirndsiwdelffnkiqaslggcVR 480
Cdd:cd05971 179 RygvTTAFLPPTAL------------KMMRQQGEQLKHAQVK------------------------------------LR 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 481 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPLPCNHIKLVDvEELNYWACKGEG 557
Cdd:cd05971 211 AIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEVG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 558 EICVRGPN--VFKGYLKDPDRTKEALDSDgWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVA 635
Cdd:cd05971 288 EIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVL 365
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1622946795 636 QIYV-------HGDSLKAFlvgiVVPDPEVMPSWAQKRGIE 669
Cdd:cd05971 366 MAAVvgipdpiRGEIVKAF----VVLNPGETPSDALAREIQ 402
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
294-661 |
1.41e-19 |
|
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: 90.47 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHM--FERVIQSQWAPTCADVHISYL 371
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG---LHSRLGFGGGDSWLLS-LPLYHVggLAILVRSLLAGAELVLLERNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 PLAHMFERmvqsvvychggrvgffqGDIRLLSddmkalcptifpVVPRLLNRMYDKifSQANTPLKRwllefaakrkqae 451
Cdd:cd17630 77 ALAEDLAP-----------------PGVTHVS------------LVPTQLQRLLDS--GQGPAALKS------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 452 vrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTS 528
Cdd:cd17630 113 ---------------------------LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 529 GHVGAPLPCNHIKLVDveelnywackgEGEICVRGPNVFKGYLKDPdrTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKK 608
Cdd:cd17630 162 GGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRAD 228
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946795 609 HIFkLAQGEYVAPEKIENIyIRSQP-VAQIYVHG---DSLKAFLVGIVVPDPEVMPS 661
Cdd:cd17630 229 NMI-ISGGENIQPEEIEAA-LAAHPaVRDAFVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
146-627 |
5.14e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 92.34 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGsGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKP--QKAVL--LLEHVERketpGLKLIILMDPFEE---ALKERGqkcgVVIKSMQAVEDCGqenhhapvpPQPDDLSIV 298
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLEDVRAQiglADKIKG----LLAGRFPLVYFCN---------RDPDDPAVI 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 299 CFTSGTTGNPKGAMLTHGNVVADFSgflKVTEKVIFPRQDDVLiSFLPLAHMFE----RVIqsqwaPTCADVHIsYL--- 371
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLANRA---QVAARIDFSPEDKVF-NALPVFHSFGltggLVL-----PLLSGVKV-FLyps 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 PLAHmfeRMVQSVVYchggrvgffqgdirllsdDMKAlcpTIfpvvprllnrmydkIFSqANTPLkrwllefaakrkqae 451
Cdd:PRK06814 869 PLHY---RIIPELIY------------------DTNA---TI--------------LFG-TDTFL--------------- 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 452 vrSGIIRNDSIWDelFFNkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV 531
Cdd:PRK06814 895 --NGYARYAHPYD--FRS---------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTV 961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 532 GAPLPCNHIKLVDVEELNywacKGeGEICVRGPNVFKGYLK-DPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHI 610
Cdd:PRK06814 962 GRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRF 1035
|
490
....*....|....*..
gi 1622946795 611 FKLAqGEYVAPEKIENI 627
Cdd:PRK06814 1036 AKIA-GEMISLAAVEEL 1051
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
292-641 |
1.00e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 90.24 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfSGFLKVTekVIFPRQDDVLISFLPLahmferviqsqwaptcadVHISYL 371
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIV--QSLAKIA--IVGYGEDDVYLHTAPL------------------CHIGGL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 PLAhMFERMVQSvvyCHggrVGFFQGDIRLLSDDMKALCPTIFPVVPRLlnrMYDkifsqantplkrwLLEFAAKRKqae 451
Cdd:PLN02860 229 SSA-LAMLMVGA---CH---VLLPKFDAKAALQAIKQHNVTSMITVPAM---MAD-------------LISLTRKSM--- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 452 vrsgiirndsIWDElffnkiqaslGGCVRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDW 526
Cdd:PLN02860 283 ----------TWKV----------FPSVRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 527 T-----------------SGH------VGAPLPcnHIKLvdveELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDS 583
Cdd:PLN02860 339 TlespkqtlqtvnqtkssSVHqpqgvcVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSN 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 584 DGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG 641
Cdd:PLN02860 413 DGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
175-661 |
2.66e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 88.79 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKpqkavlLLEHVERKET-PGLKLIILMD 253
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA------DGPHDRAEPTtRWWPLTVNVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 254 PfeealkERGQKCGVVIKSMqaveDCGQENHHAPVPPQ---PDDLSIVcFTSGTTGNPKGAMLTHGNVVADFSGFlkVTE 330
Cdd:PRK05852 145 G------DSGPSGGTLSVHL----DAATEPTPATSTPEglrPDDAMIM-FTGGTTGLPKMVPWTHANIASSVRAI--ITG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 331 KVIFPRqdDVLISFLPLAHmferviqsqwaptcadvhiSYLPLAHMFERMVQsvvychGGRV-----GFFQGdiRLLSDD 405
Cdd:PRK05852 212 YRLSPR--DATVAVMPLYH-------------------GHGLIAALLATLAS------GGAVllparGRFSA--HTFWDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 406 MKALCPTIFPVVPrllnrmydkifsqantPLKRWLLEFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTG 485
Cdd:PRK05852 263 IKAVGATWYTAVP----------------TIHQILLERAATEPSGRKPAAL-----------------------RFIRSC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 486 AAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DVEELNYWACk 554
Cdd:PRK05852 304 SAPLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLPLPAGAV- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 555 geGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPV 634
Cdd:PRK05852 381 --GEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNV 456
|
490 500 510
....*....|....*....|....*....|
gi 1622946795 635 AQIYVHGDSLKAF---LVGIVVPDPEVMPS 661
Cdd:PRK05852 457 MEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
146-658 |
3.68e-18 |
|
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: 88.03 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELA------CYtysmvvVPLYDTLGPGAIRYIINTAD 219
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGP--GDVVGVLAERSPELVVALLAvlkagaAY------VPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 220 ISTVIVDKPQKAVLLLehverketPGLKLIILMDPFEEALKErgqkcgvviksmqavedcgqenhhAPVPPQPDDLSIVC 299
Cdd:cd12117 95 AKVLLTDRSLAGRAGG--------LEVAVVIDEALDAGPAGN------------------------PAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 300 FTSGTTGNPKGAMLTHGNVV--ADFSGFLKVTEkvifprqDDVLISFLPL---AHMFErvIqsqWAPtcadvhisylpla 374
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVrlVKNTNYVTLGP-------DDRVLQTSPLafdASTFE--I---WGA------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 375 hmfermvqsvvYCHGGRVgffqgdirllsddmkALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkQAEVRS 454
Cdd:cd12117 198 -----------LLNGARL---------------VLAPKGTLLDPDAL---------------------------GALIAE 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 455 GIIrnDSIWdeL---FFNKI----QASLGGcVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT---- 522
Cdd:cd12117 225 EGV--TVLW--LtaaLFNQLadedPECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvv 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 523 -PGDWTSGHV--GAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDI 592
Cdd:cd12117 297 tELDEVAGSIpiGRPIANTRVYVLD--EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDL 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 593 GKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPEV 658
Cdd:cd12117 375 ARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAA-LRAHPgVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
177-656 |
4.23e-18 |
|
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: 88.32 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 177 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKavlLLEHVE--RKETPGL-KLIILMD 253
Cdd:cd05970 77 LTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDN---IPEEIEkaAPECPSKpKLVWVGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 254 PFEEALKERGQKCgvviksMQAVEDCgqENHHAPVPPQPDDLSIVCFTSGTTGNPKgaMLTHgnvvaDFSGFLK--VTEK 331
Cdd:cd05970 154 PVPEGWIDFRKLI------KNASPDF--ERPTANSYPCGEDILLVYFSSGTTGMPK--MVEH-----DFTYPLGhiVTAK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 332 VIFPRQDDVLisflplaHMfeRVIQSQWAPTC-ADVHISYLPLAHMFermvqsvVYCHGGrvgFFQGDI--RLLSDDMKA 408
Cdd:cd05970 219 YWQNVREGGL-------HL--TVADTGWGKAVwGKIYGQWIAGAAVF-------VYDYDK---FDPKALleKLSKYGVTT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 409 LC--PTIFpvvprllnrmydkifsqantplkRWLlefaakrkqaeVRSGIIRNDsiwdelfFNKIqaslggcvRMIVTGA 486
Cdd:cd05970 280 FCapPTIY-----------------------RFL-----------IREDLSRYD-------LSSL--------RYCTTAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 487 APASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDVEELnywACKG--EGEICVRG 563
Cdd:cd05970 311 EALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGR---SCEAgeEGEIVIRT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 564 PN-----VFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIY 638
Cdd:cd05970 387 SKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECA 464
|
490
....*....|....*...
gi 1622946795 639 VHGdslkaflvgivVPDP 656
Cdd:cd05970 465 VTG-----------VPDP 471
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
274-674 |
1.30e-17 |
|
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: 85.98 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 274 QAVEDCGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKVIFP-RQDDVLIS--------- 343
Cdd:cd05919 72 DDYAYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAH----RDPLLFADAMAREALGlTPGDRVFSsakmffgyg 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 344 -----FLPLAHMFERVIQSQWaPTCADVhisylplahmFERMVQsvvycHGgrvgffqgdirllsddmkalcPTIFPVVP 418
Cdd:cd05919 148 lgnslWFPLAVGASAVLNPGW-PTAERV----------LATLAR-----FR---------------------PTVLYGVP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 419 RllnrMYDKIFSQANTPlkrwllefaakrkQAEVRSgiIRndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLG-FL 497
Cdd:cd05919 191 T----FYANLLDSCAGS-------------PDALRS--LR-----------------------LCVSAGEALPRGLGeRW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 498 RAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDP 574
Cdd:cd05919 229 MEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVPGYEIRLVD--EEGHTIPPGEeGDLLVRGPSAAVGYWNNP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 575 DRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYV----HGDSL---KAF 647
Cdd:cd05919 305 EKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVvavpESTGLsrlTAF 382
|
410 420
....*....|....*....|....*..
gi 1622946795 648 lvgiVVPDPEVMPSWAQKRGIEGTYAD 674
Cdd:cd05919 383 ----VVLKSPAAPQESLARDIHRHLLE 405
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
95-639 |
4.14e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 85.20 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 95 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKAcTDQf 174
Cdd:PRK06155 1 GEPLGAGLAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGG-----TRWTYAEAARAAAAAAHALAAAGVKR-GDR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPqkavlLLEHVERKETPGLKL--IILM 252
Cdd:PRK06155 74 VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA-----LLAALEAADPGDLPLpaVWLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 253 DPFEEALKERGQKCGVVIKSMQAVedcgqenhhAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHgnvvADFSGFLKVTEKV 332
Cdd:PRK06155 149 DAPASVSVPAGWSTAPLPPLDAPA---------PAAAVQPGDTAAILYTSGTTGPSKGVCCPH----AQFYWWGRNSAED 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 333 IFPRQDDVLISFLPLAHmferviqsqwapTCAdvhisylpLAHMFERMVQSVVYCHGGRV---GFFqgdirllsDDMKAL 409
Cdd:PRK06155 216 LEIGADDVLYTTLPLFH------------TNA--------LNAFFQALLAGATYVLEPRFsasGFW--------PAVRRH 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 410 CPTIFpvvpRLLNRMYDKIFSQANTPLKRwllefaakrkqaevrsgiirndsiwdelffnkiqaslGGCVRMIVTGAAPA 489
Cdd:PRK06155 268 GATVT----YLLGAMVSILLSQPARESDR-------------------------------------AHRVRVALGPGVPA 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 490 SptVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTSGHVGAPLPCNHIKLVDVEELNYWAckGE-GEICVRG--PNV 566
Cdd:PRK06155 307 A--LHAAFRERFGVDLLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPD--GEpGELLLRAdePFA 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 567 F-KGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIyIRSQP-VAQIYV 639
Cdd:PRK06155 382 FaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
472-656 |
5.23e-17 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 84.66 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 472 QASLGGCVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKL- 542
Cdd:cd12118 243 ARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLe 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 543 -VDVEELNY-----WACKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQG 616
Cdd:cd12118 320 eVDVLDPETmkpvpRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGG 397
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622946795 617 EYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDP 656
Cdd:cd12118 398 ENISSVEVEGV---------LYKHPAVLEAAVVA--RPDE 426
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
146-660 |
6.52e-17 |
|
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: 83.91 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqenhhapvppqPDDLSIVCFTSGTT 305
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHGNVVAdfsgFLKVTEKViFPRQDdvlisflpLAhmfeRVIQSqwAPTCADVHI--SYLPLahmfermvqs 383
Cdd:cd12115 118 GRPKGVAIEHRNAAA----FLQWAAAA-FSAEE--------LA----GVLAS--TSICFDLSVfeLFGPL---------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 384 vvyCHGGRVGFFQGDIRLLsdDMKALCP-TIFPVVPRLLnrmydkifsqantplkRWLLEFaakrkqaevrsgiirndsi 462
Cdd:cd12115 169 ---ATGGKVVLADNVLALP--DLPAAAEvTLINTVPSAA----------------AELLRH------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 463 wdelffNKIQASlggcVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNH 539
Cdd:cd12115 209 ------DALPAS----VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQ 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 540 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKL 613
Cdd:cd12115 279 AYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV 357
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1622946795 614 aQGEYVAPEKIENIyIRSQP-VAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 660
Cdd:cd12115 358 -RGFRIELGEIEAA-LRSIPgVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
175-656 |
6.68e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 84.17 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVLLLEHverketpglKLIILMDP 254
Cdd:PRK06145 55 VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALET---------PKIVIDAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 255 FEEALKERGQKcgvviksmqavedcgqenhHAPVPPQ----PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSGFLK 327
Cdd:PRK06145 126 AQADSRRLAQG-------------------GLEIPPQaavaPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 328 VTekvifprQDDVLISFLPLAHmferviqsqwaptcadVHISYLP-LAhmfermvqsvVYCHGGRVGF---FQGDIRLLS 403
Cdd:PRK06145 187 LT-------ASERLLVVGPLYH----------------VGAFDLPgIA----------VLWVGGTLRIhreFDPEAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 404 DDMKALCPTIFpvVPRLLNRMYdkifsQANTPLK------RWLLefAAKRKQAEVRsgiIRNdsiwdelffnkiqaslgg 477
Cdd:PRK06145 234 IERHRLTCAWM--APVMLSRVL-----TVPDRDRfdldslAWCI--GGGEKTPESR---IRD------------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 478 cvrmivtgaapasptvlgFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKG 555
Cdd:PRK06145 284 ------------------FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNM 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 556 EGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN-IYIRSQ-- 632
Cdd:PRK06145 345 KGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPEva 422
|
490 500
....*....|....*....|....
gi 1622946795 633 PVAQIYVHGDSLKAFLVGIVVPDP 656
Cdd:PRK06145 423 EAAVIGVHDDRWGERITAVVVLNP 446
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
291-657 |
7.44e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 83.90 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkvTEKVIFPRQDDVLISFLPLAHMFerviqSQWAptcadvhiSY 370
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA----TQRWFGFNEDDVWTLFHSYAFDF-----SVWE--------IW 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 371 LPLAHmfermvqsvvychGGRVGFFQGDIRLLSDDMkalcptifpvvPRLLNRMYDKIFSQanTPLkrwllefAAKRKQA 450
Cdd:cd17643 154 GALLH-------------GGRLVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQ--TPS-------AFYQLVE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 451 EVRSGIIRNDSIwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGC---QVYEGYGQTECTAGCTFT--TPGD 525
Cdd:cd17643 201 AADRDGRDPLAL-----------------RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRplDAAD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 526 W---TSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-------ALDSDGWLHTGDIGKW 595
Cdd:cd17643 264 LpaaAASPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARR 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 596 LPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPE 657
Cdd:cd17643 343 LPDGELEYLGRADEQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
287-667 |
8.22e-17 |
|
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: 83.93 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 287 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgflkvtekviFPRQDDVLISFLPLAHMferviqSQWAPTCADV 366
Cdd:cd17651 130 DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN-------------LVAWQARASSLGPGART------LQFAGLGFDV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 367 hisylplahmferMVQSV--VYCHGGRVGFFQGDIRLLSDDMKALCPTifpvvpRLLNRMYdkifsqANTPLKRWLLEfA 444
Cdd:cd17651 191 -------------SVQEIfsTLCAGATLVLPPEEVRTDPPALAAWLDE------QRISRVF------LPTVALRALAE-H 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 445 AKRKQAEvrsgiirndsiwdelffnkiqaslGGCVRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCT 519
Cdd:cd17651 245 GRPLGVR------------------------LAALRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 520 FTTPGDWTS-GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWL------HTGDI 592
Cdd:cd17651 301 PGDPAAWPApPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 593 GKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV------HGDslkAFLVGIVVPDPEVMPSWAQKR 666
Cdd:cd17651 380 ARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVDAAELR 455
|
.
gi 1622946795 667 G 667
Cdd:cd17651 456 A 456
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
291-666 |
1.21e-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: 83.29 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvtekvifpRQDDVLISFlPLAHMferviqsQWAPTCADVHISY 370
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW----------RREYELDSF-PVRLL-------QMASFSFDVFAGD 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 371 LPLAhmfermvqsvvYCHGGRVGFFQGDIRLlsdDMKALCptifpvvpRLLNRmyDKIFSQANTP-LKRWLLEFAAKRKQ 449
Cdd:cd17650 153 FARS-----------LLNGGTLVICPDEVKL---DPAALY--------DLILK--SRITLMESTPaLIRPVMAYVYRNGL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 450 --AEVRSGIIRNDSIWDElFFNKIQASLGGCVRMIvtgaapaspTVLGFLRAALGCQVYEGYGQTECTAGctfTTPgdwt 527
Cdd:cd17650 209 dlSAMRLLIVGSDGCKAQ-DFKTLAARFGQGMRII---------NSYGVTEATIDSTYYEEGRDPLGDSA---NVP---- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 528 sghVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPAGTL 601
Cdd:cd17650 272 ---IGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNV 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 602 KVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYV---HGDSLKAFLVGIVVPDPEvmPSWAQKR 666
Cdd:cd17650 348 ELLGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAAT--LNTAELR 412
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
146-660 |
2.47e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 82.32 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVR--PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPQkavlllehvERKETPGLKLIILMDPFEEALKERgqkcgvviksmqavedcgqenhhAPVPPQPDDLSIVCFTSGTT 305
Cdd:cd12114 91 DGPD---------AQLDVAVFDVLILDLDALAAPAPP-----------------------PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHG---NVVADFSGFLKVTEkvifprqDDVLISFLPLAH------MFerviqsqwAPTCAdvhisylplahm 376
Cdd:cd12114 139 GTPKGVMISHRaalNTILDINRRFAVGP-------DDRVLALSSLSFdlsvydIF--------GALSA------------ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 377 fermvqsvvychGGRVgffqgdirllsddmkalcptifpVVPRLlnrmydkifSQANTPlKRWllefaakrKQAEVRSGI 456
Cdd:cd12114 192 ------------GATL-----------------------VLPDE---------ARRRDP-AHW--------AELIERHGV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 457 irndSIWdelffNKIQASLGgcvrMIVTgAAPASPTVLGFLRAAL-------------------GCQVYEGYGQTECTAG 517
Cdd:cd12114 219 ----TLW-----NSVPALLE----MLLD-VLEAAQALLPSLRLVLlsgdwipldlparlralapDARLISLGGATEASIW 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 518 CTF----TTPGDWTSGHVGAPLPCNHIKLVD--VEELNYWackGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG--WL 587
Cdd:cd12114 285 SIYhpidEVPPDWRSIPYGRPLANQRYRVLDprGRDCPDW---VPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLY 361
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 588 HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 660
Cdd:cd12114 362 RTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
508-664 |
1.28e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 78.88 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 508 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVE--ELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSD 584
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYWNRPEVNARRT-RG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 585 GWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqgeyvapekIENIY-------IRSQP-VAQIYVhgdslkaflvgIVVPDp 656
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 1622946795 657 evmPSWAQ 664
Cdd:cd17636 276 ---PRWAQ 280
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
294-627 |
1.46e-15 |
|
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: 78.84 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 294 DLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIfprQDDVLISFLPLAHMFerviQSQWAPTCadvhisylpl 373
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWV---VGDVTYLPLPATHIG----GLWWILTC---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 374 ahmfermvqsvVYCHGGRVGFfqGDIRLLSDDMKAL---CPTIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRkqa 450
Cdd:cd17635 65 -----------LIHGGLCVTG--GENTTYKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 451 evrsgIIRNDSIWDELFFNkiqaslggcvrmivtgaapasptvlgflraalgCQVYEGYGQTECTAGCTFTTPGDWTS-G 529
Cdd:cd17635 129 -----AIAADVRFIEATGL---------------------------------TNTAQVYGLSETGTALCLPTDDDSIEiN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 530 HVGAPLPCNHIKLVDVEELNYWAcKGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKH 609
Cdd:cd17635 171 AVGRPYPGVDVYLAATDGIAGPS-ASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSE 248
|
330
....*....|....*...
gi 1622946795 610 IFKLAqGEYVAPEKIENI 627
Cdd:cd17635 249 SINCG-GVKIAPDEVERI 265
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
146-656 |
1.85e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.06 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKacTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNIT--KNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKP-----QKAVLLLEHVERKETPGLKLIILMD----PFE-----EALKERGQKCGVVIKSMQAVEDcgqenHHAPVPpq 291
Cdd:PLN03102 118 DRSfeplaREVLHLLSSEDSNLNLPVIFIHEIDfpkrPSSeeldyECLIQRGEPTPSLVARMFRIQD-----EHDPIS-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 pddlsiVCFTSGTTGNPKGAMLTH-GNVVADFSGFLKvTEKVIFPrqddVLISFLPLAHMferviqSQWAPTCADVhisy 370
Cdd:PLN03102 191 ------LNYTSGTTADPKGVVISHrGAYLSTLSAIIG-WEMGTCP----VYLWTLPMFHC------NGWTFTWGTA---- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 371 lplahmfERMVQSVVYCHGGRVGFFQgDIRLLSDDMKALCPTIFpvvprllnrmydkifsqantplkRWLLEfaAKRKQA 450
Cdd:PLN03102 250 -------ARGGTSVCMRHVTAPEIYK-NIEMHNVTHMCCVPTVF-----------------------NILLK--GNSLDL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 451 EVRSGIIRndsiwdelffnkiqaslggcvrmIVTGAAPAsPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSg 529
Cdd:PLN03102 297 SPRSGPVH-----------------------VLTGGSPP-PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 530 hvgapLPCN------------HIKLVDVEELNYWAC-------KGEGEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTG 590
Cdd:PLN03102 352 -----LPENqqmelkarqgvsILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTG 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 591 DIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGIvvPDP 656
Cdd:PLN03102 426 DVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
146-657 |
1.96e-15 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 79.80 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActdqfiG--VFAQ--NRPEWIIAELACYtySMVVVPLYdTLgPG----AIRYIINT 217
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRP------GdrVVVQlpNVAEFVIVFFALF--RAGAIPVF-AL-PAhrraEISHFAEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 218 ADISTVIVDKpqkAVLLLEHVE-----RKETPGLKLIILMDPFEEalkergqkcgvviksMQAVEDCGQENHHAPVP-PQ 291
Cdd:COG1021 121 SEAVAYIIPD---RHRGFDYRAlarelQAEVPSLRHVLVVGDAGE---------------FTSLDALLAAPADLSEPrPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDlsiVCF---TSGTTGNPKGAMLTHG----NVV--ADFSGFlkvtekvifpRQDDVLISFLPLAHMFerviqsqwaPT 362
Cdd:COG1021 183 PDD---VAFfqlSGGTTGLPKLIPRTHDdylySVRasAEICGL----------DADTVYLAALPAAHNF---------PL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 363 CADVhisylplahmfermVQSVVYcHGGRVgffqgdirLLSDDMKALcpTIFP-----------VVPRLLNRMydkifsq 431
Cdd:COG1021 241 SSPG--------------VLGVLY-AGGTV--------VLAPDPSPD--TAFPlierervtvtaLVPPLALLW------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 432 antplkrwlLEFAAKRKQAevrsgiirndsiwdeLffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQ 511
Cdd:COG1021 289 ---------LDAAERSRYD---------------L------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGM 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 512 TEctaG-CTFTTPGD--WTSGH-VGAPL-PCNHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYLKDPDRTKEA 580
Cdd:COG1021 335 AE---GlVNYTRLDDpeEVILTtQGRPIsPDDEVRIVDedgnpVPP-------GEvGELLTRGPYTIRGYYRAPEHNARA 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 581 LDSDGWLHTGDIGKWLPAGTLKVIDRKK-HIFKlaQGEYVAPEKIENiyirsqpvaQIYVHGDSLKAFLVGivVPDPE 657
Cdd:COG1021 405 FTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVEN---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
284-645 |
2.53e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 80.14 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 284 HHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTH----GNV-----VADFSgflkvtekvifPRqdDVLISFLPLAHMFERV 354
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHksllANVeqiktIADFT-----------PN--DRFMSALPLFHSFGLT 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 355 IqSQWAP--TCADVHISYLPLAHmfeRMVQSVVYCHGGRVGFfqGDIRLLSDDMKALCPtifpvvprllnrmYDkifsqa 432
Cdd:PRK08043 423 V-GLFTPllTGAEVFLYPSPLHY---RIVPELVYDRNCTVLF--GTSTFLGNYARFANP-------------YD------ 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 433 ntplkrwlleFAAkrkqaevrsgiirndsiwdelffnkiqaslggcVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQT 512
Cdd:PRK08043 478 ----------FAR---------------------------------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVT 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 513 ECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDVEELNywacKGeGEICVRGPNVFKGYLK--DPDRTK-------EALDS 583
Cdd:PRK08043 515 ECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE----QG-GRLQLKGPNIMNGYLRveKPGVLEvptaenaRGEME 589
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 584 DGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQiyvHGDSLK 645
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ---HATAIK 647
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
287-639 |
3.84e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 78.37 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 287 PVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGflkVTEKVIFPRQDDVLISfLPLAHMFERVIQSQWAPTCADV 366
Cdd:PRK09029 129 AVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEG---VLSLMPFTAQDSWLLS-LPLFHVSGQGIVWRWLYAGATL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 367 HisyLPLAHMFERMVQSVVYChggrvgffqgdirllsddmkALCPTifpVVPRLLNRmydkifSQANTPLKRWLLefaak 446
Cdd:PRK09029 205 V---VRDKQPLEQALAGCTHA--------------------SLVPT---QLWRLLDN------RSEPLSLKAVLL----- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 447 rkqaevrsgiirndsiwdelffnkiqaslGGCvrMIvtgaapasPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDW 526
Cdd:PRK09029 248 -----------------------------GGA--AI--------PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 527 TSGhVGAPLPCNHIKLVDveelnywackgeGEICVRGPNVFKGYLKDpDRTKEALDSDGWLHTGDIGKWLpAGTLKVIDR 606
Cdd:PRK09029 288 LAG-VGSPLPGREVKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGR 352
|
330 340 350
....*....|....*....|....*....|...
gi 1622946795 607 KKHIFkLAQGEYVAPEKIENIYIRSQPVAQIYV 639
Cdd:PRK09029 353 LDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-655 |
4.65e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.82 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 52 ATTLVSMGALAAILAYW--FTHRPKAlQPPCNL----LMQSEEVedsggaRRSVIGSGPqllTHYYDDARTMYQVFRRGL 125
Cdd:PRK12467 453 ATDLFEATTIERLATHWrnLLEAIVA-EPRRRLgelpLLDAEER------ARELVRWNA---PATEYAPDCVHQLIEAQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 126 SISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDT 205
Cdd:PRK12467 523 RQHPERPALVFGE-----QVLSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 206 LGPGAIRYIINTADISTVIVDKPQKAVLLLehverkeTPGLKLIILMDPfeealkergqkcgvviksmqAVEDCGQENHH 285
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPV-------PAGLRSLCLDEP--------------------ADLLCGYSGHN 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVvadfSGFLKVTEKVIFPRQDDVLISFLPLAhmferviqsqwaptcAD 365
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSMLMVSTFA---------------FD 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 366 VHIS--YLPLahmfermvqsvvyCHGGRVgffqgdirLLSDDMKALCPTIFpvvprllnrmYDKIFSQANTPLKrwllef 443
Cdd:PRK12467 710 LGVTelFGAL-------------ASGATL--------HLLPPDCARDAEAF----------AALMADQGVTVLK------ 752
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 444 aakrkqaevrsgiiRNDSIWDELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTT- 522
Cdd:PRK12467 753 --------------IVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYEl 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 523 ---PGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDI 592
Cdd:PRK12467 819 sdeERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDL 897
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 593 GKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-------VAQIYVHGDSLKAFLVGIVVPD 655
Cdd:PRK12467 898 ARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEAR-LLAQPgvreavvLAQPGDAGLQLVAYLVPAAVAD 965
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
146-657 |
7.31e-15 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 77.70 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd17646 24 LTYRELDERANRLAHLLRARGVGP--EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPQKAVLllehverketPGLKLIILMDPfeealkergqkcgvviksmqavEDCGQENHHAP-VPPQPDDLSIVCFTSGT 304
Cdd:cd17646 102 TADLAARL----------PAGGDVALLGD----------------------EALAAPPATPPlVPPRPDNLAYVIYTSGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 305 TGNPKGAMLTHGNVVADFSGFlkvtekvifprQDDvlisfLPLAHMfERVIQSqwAPTCADVHIS--YLPLAHMfERMVq 382
Cdd:cd17646 150 TGRPKGVMVTHAGIVNRLLWM-----------QDE-----YPLGPG-DRVLQK--TPLSFDVSVWelFWPLVAG-ARLV- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 383 svVYCHGGRvgffqGDIRLLSDDMKALCPTIFPVVPRLLnrmydkifsqantplkrwllefaakrkqaevrsgiirndsi 462
Cdd:cd17646 209 --VARPGGH-----RDPAYLAALIREHGVTTCHFVPSML----------------------------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 463 wdELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNH 539
Cdd:cd17646 241 --RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 540 IKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH------TGDIGKWLPAGTLKVIDRKKHIFKL 613
Cdd:cd17646 319 LYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622946795 614 aQGEYVAPEKIENIyIRSQP-VAQIYV---HGDSLKAFLVGIVVPDPE 657
Cdd:cd17646 398 -RGFRVEPGEIEAA-LAAHPaVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
146-668 |
1.11e-14 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 77.41 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQhnckactdqfIGVFAQNR--------PEWIIAELACYTYSMVVVPLYDTLGPGAIRYIInt 217
Cdd:cd05959 30 LTYAELEAEARRVAGALRA----------LGVKREERvllimldtVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 218 ADI-STVIVDKPQKAVLLLEHVERKEtPGLKLIILMDPFEEALKErgqkcgvviksMQAVEDCGQENHH-APVPPQPDDL 295
Cdd:cd05959 98 EDSrARVVVVSGELAPVLAAALTKSE-HTLVVLIVSGGAGPEAGA-----------LLLAELVAAEAEQlKPAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 296 SIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKvteKVIFPRQDDVLIS--------------FLPLAH------MFERVi 355
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSaaklffayglgnslTFPLSVgattvlMPERP- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 356 qsqwAPtcadvhisylplAHMFERMVQsvvychgGRvgffqgdirllsddmkalcPTIFPVVPRLLNRMydkifsqantp 435
Cdd:cd05959 242 ----TP------------AAVFKRIRR-------YR-------------------PTVFFGVPTLYAAM----------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 436 lkrwlleFAAKRKQAEVRSGIirndsiwdelffnkiqaslggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEct 515
Cdd:cd05959 269 -------LAAPNLPSRDLSSL-----------------------RLCVSAGEALPAEVGERWKARFGLDILDGIGSTE-- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 516 AGCTF--TTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSdGWLHTGDIG 593
Cdd:cd05959 317 MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKY 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 594 KWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFlvgiVVPDPEVMPSWAQKR 666
Cdd:cd05959 395 VRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAVVGvededglTKPKAF----VVLRPGYEDSEALEE 469
|
..
gi 1622946795 667 GI 668
Cdd:cd05959 470 EL 471
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
146-641 |
1.46e-14 |
|
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: 76.78 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRP--GQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 dkpqkavllleHVERKETPGLKLIILMDPFEEALKERGQKC--GVVIKsmqavedcgqenhhaPVPPQPDDLSIVCFTSG 303
Cdd:cd05923 107 -----------AVDAQVMDAIFQSGVRVLALSDLVGLGEPEsaGPLIE---------------DPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 304 TTGNPKGAMLTHGNVvadfsgflkvTEKVIFprqddvlisflpLAHmferviQSQWAPTCADVHISYLPLAHMfermvqs 383
Cdd:cd05923 161 TTGLPKGAVIPQRAA----------ESRVLF------------MST------QAGLRHGRHNVVLGLMPLYHV------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 384 vvychggrVGFFQgdirLLSDDMkALCPTIFPVvprllnrmydKIFSQANtplkrwllefAAKRKQAEVRSGIIRNDSIW 463
Cdd:cd05923 206 --------IGFFA----VLVAAL-ALDGTYVVV----------EEFDPAD----------ALKLIEQERVTSLFATPTHL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 464 DELFFNKIQASLG-GCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKL 542
Cdd:cd05923 253 DALAAAAEFAGLKlSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 543 VDV-EELNYWACKG-EGEICVR--GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEY 618
Cdd:cd05923 330 VRIgGSPDEALANGeEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGEN 407
|
490 500
....*....|....*....|...
gi 1622946795 619 VAPEKIENIYIRSQPVAQIYVHG 641
Cdd:cd05923 408 IHPSEIERVLSRHPGVTEVVVIG 430
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
480-657 |
1.58e-14 |
|
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: 76.60 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 480 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDvEELNYWACKGEG 557
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 558 EICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENiyirsqpvaQI 637
Cdd:cd05920 337 ELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------LL 406
|
170 180
....*....|....*....|
gi 1622946795 638 YVHGDSLKAFLVGivVPDPE 657
Cdd:cd05920 407 LRHPAVHDAAVVA--MPDEL 424
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
292-722 |
1.79e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.01 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVtekviFPRQDDVLISflplahmferviqsqwaptcadVHISYL 371
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQL-----RPREPDPPPP----------------------VSLDWM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 PLAHMFermvqsvvychGGRVGFfQGDIR----LLSDDMKALcPTIFPVVPRLLNRMYDKIFsqANTPLKRWLLEFAAKR 447
Cdd:PRK12582 272 PWNHTM-----------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVY--GNVPAGYAMLAEAMEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 448 KQAEVRSgiirndsiwdelFFNKIqaslggcvRMIVTGAAPASPTVLGFLRA----ALGCQV--YEGYGQTEcTAGCTFT 521
Cdd:PRK12582 337 DDALRRS------------FFKNL--------RLMAYGGATLSDDLYERMQAlavrTTGHRIpfYTGYGATE-TAPTTTG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 522 TpgDWTS---GHVGAPLPCNHIKLVDVEElNYwackgegEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWL-- 596
Cdd:PRK12582 396 T--HWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdp 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 597 --PAGTLKVIDRKKHIFKLAQGEYV--APEKIENIYIRSQPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKRGieGTY 672
Cdd:PRK12582 466 ddPEKGLIFDGRVAEDFKLSTGTWVsvGTLRPDAVAACSPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAP 542
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622946795 673 ADLCTSKDLKKAILEDMVRLGKESGLHSfEQVKAIHIHSDMFSVQNGLLT 722
Cdd:PRK12582 543 EDVVKHPAVLAILREGLSAHNAEAGGSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
146-660 |
3.29e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 75.94 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNckACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPQKAVLL---LEHVERKETPGLKLIILMDPFEEALKERGQKCGVviksmQAVEDCGQENHHAPVPPQ-PDDLSIVCFT 301
Cdd:PRK06164 114 WPGFKGIDFaaiLAAVPPDALPPLRAIAVVDDAADATPAPAPGARV-----QLFALPDPAPPAAAGERAaDPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 302 -SGTTGNPK------GAMLTHGNVVADFSGFlkvtekvifpRQDDVLISFLPLahmferviqsqwaptCAdvhisylpla 374
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPF---------------CG---------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 375 hmfermvqsvVYCHGGRVGFFQGDIRLLSDDMKALCPTIfpvvpRLL-----------NRMYDKIFSQANTPLkrwllEF 443
Cdd:PRK06164 234 ----------VFGFSTLLGALAGGAPLVCEPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 444 AAKRkqaevRSGIirndsiwdelffnkiqASLggcvrmivtgaAPASPTVLGFLRAAlGCQVYEGYGQTECTA---GCTF 520
Cdd:PRK06164 294 PSAR-----LFGF----------------ASF-----------APALGELAALARAR-GVPLTGLYGSSEVQAlvaLQPA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 521 TTPgdWTSGHVGAPLPCN---HIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLP 597
Cdd:PRK06164 341 TDP--VSVRIEGGGRPASpeaRVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRG 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946795 598 AGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSL--KAFLVGIVVPDPEVMP 660
Cdd:PRK06164 419 DGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
471-639 |
8.88e-14 |
|
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: 74.14 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 471 IQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDVE 546
Cdd:cd05974 191 IQQDLASFdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 547 ElnywACKGEGEICV-----RGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAP 621
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1622946795 622 EKIENIYIRSQPVAQIYV 639
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
292-629 |
1.35e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 74.08 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAHMFErVIQSQWAPTCADVHI--S 369
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS----PKEDDVMMSFLPPFHAYG-FNSCTLFPLLSGVPVvfA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 370 YLPLAHmfERMVQSVvychggrvgffqgdirllsDDMKAlcpTIFPVVPRLLNrmydkifsqantplkrWLLEFAAKRKQ 449
Cdd:PRK06334 257 YNPLYP--KKIVEMI-------------------DEAKV---TFLGSTPVFFD----------------YILKTAKKQES 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 450 A--EVRSGIIRNDSIWDELFfnkiqaslggcvrmivTGAAPASPTVlgflraalgcQVYEGYGQTECTAGCTFTT---PG 524
Cdd:PRK06334 297 ClpSLRFVVIGGDAFKDSLY----------------QEALKTFPHI----------QLRQGYGTTECSPVITINTvnsPK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 525 DwtSGHVGAPLPCNHIKLVDvEELNYWACKGE-GEICVRGPNVFKGYL-KDPDRTKEALDSDGWLHTGDIGKWLPAGTLK 602
Cdd:PRK06334 351 H--ESCVGMPIRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELF 427
|
330 340
....*....|....*....|....*..
gi 1622946795 603 VIDRKKHIFKLAqGEYVAPEKIENIYI 629
Cdd:PRK06334 428 LKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
293-661 |
1.49e-13 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 73.28 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvTEKVIFPRQDDVLISFLPLAHMFER--VIQSQWAPTCADVhisy 370
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRY---AVNVLRLREDDRFVGSPPLAFTFGLggVLLFPFGVGASGV---- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 371 lplahMFERMVQSVVYCHGGRVGffqgdirllsddmkalcPTIFPVVPRllnrMYdkifsqantplkRWLLEFAAKRKQa 450
Cdd:cd05958 170 -----LLEEATPDLLLSAIARYK-----------------PTVLFTAPT----AY------------RAMLAHPDAAGP- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 451 evrsgiirndsiwdelffnkiqasLGGCVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSG 529
Cdd:cd05958 211 ------------------------DLSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 530 HVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKgYLKDPDRTKEAldSDGWLHTGDIGKWLPAGTLKVIDRKK 608
Cdd:cd05958 266 ATGKPVPGYEAKVVD--DEGNPVPDGTiGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSD 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 609 HIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLV---GIVVPDPEVMPS 661
Cdd:cd05958 341 DMIVSG-GYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
292-634 |
3.08e-13 |
|
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: 72.91 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKvifpRQDDVLISFLPLAHMFErVIQSQWAPTCADVHISYL 371
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTHDMG-LIAFHLAPLIAGMNQYLM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 PLAhmfermvqsvvychggrvgffqgdirllsddmkalcptIFPVVPRLLNRMYDK----IFSQANTPLKrWLLEFAAKR 447
Cdd:cd05908 180 PTR--------------------------------------LFIRRPILWLKKASEhkatIVSSPNFGYK-YFLKTLKPE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 448 KQAEvrsgiirndsiWDElffnkiqaslgGCVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAG 517
Cdd:cd05908 221 KAND-----------WDL-----------SSIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 518 CTF----------------------------TTPGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFK 568
Cdd:cd05908 275 ASLpkaqspfktitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTP 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 569 GYLKDPDRTKEALDSDGWLHTGDIGkWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 634
Cdd:cd05908 353 GYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
483-649 |
4.60e-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: 72.50 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 483 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVR 562
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 563 -GPN----VFKGYLKDPDRTKEALDSDGWLhTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQI 637
Cdd:cd05928 376 vKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170
....*....|....*....
gi 1622946795 638 YV-------HGDSLKAFLV 649
Cdd:cd05928 454 AVvsspdpiRGEVVKAFVV 472
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
177-656 |
6.12e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.00 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 177 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV--DKPqkavlllEHVE--RKETPGLKLIILM 252
Cdd:PRK07470 62 VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIChaDFP-------EHAAavRAASPDLTHVVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 253 D--PFEEAlkergqkcgvviksmqaVEDCGQENHHAPVPPQP---DDLSIVCFTSGTTGNPKGAMLTHG-------NVVA 320
Cdd:PRK07470 135 GgaRAGLD-----------------YEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGqmafvitNHLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 321 DfsgflkvtekvIFP--RQDDVLISFLPLAHmferviqsqwaptCADVHiSYLPLAhmfeRMVQSVVychggrvgffqgd 398
Cdd:PRK07470 198 D-----------LMPgtTEQDASLVVAPLSH-------------GAGIH-QLCQVA----RGAATVL------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 399 irLLSDDMKAlcptifPVVPRLLNRMYDKIFSQANTPLKrWLLEFAAkrkqaevrsgIIRNDsiwdelffnkiQASLggc 478
Cdd:PRK07470 236 --LPSERFDP------AEVWALVERHRVTNLFTVPTILK-MLVEHPA----------VDRYD-----------HSSL--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 479 vRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH--------IKLVDV 545
Cdd:PRK07470 283 -RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmevqIQDDEG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 546 EELNywacKGE-GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKI 624
Cdd:PRK07470 359 RELP----PGEtGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREI 432
|
490 500 510
....*....|....*....|....*....|..
gi 1622946795 625 ENiyirsqpvaQIYVHGDSLKAFLVGivVPDP 656
Cdd:PRK07470 433 EE---------KLLTHPAVSEVAVLG--VPDP 453
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
146-657 |
1.17e-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: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKACTDQFigVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYiintadistviv 225
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVF--VLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRD------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 dkpqkavlllehveRKETPGLKLIILmdpfEEALKERgqkcgvviksmqavedcgqenhhapvpPQPDDLSIVCFTSGTT 305
Cdd:cd05969 67 --------------RLENSEAKVLIT----TEELYER---------------------------TDPEDPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 306 GNPKGAMLTHGNVVADFsgflkVTEKVIFPRQDDvlisflplaHMFERVIQSQWapTCADVHISYLPLAHmferMVQSVV 385
Cdd:cd05969 102 GTPKGVLHVHDAMIFYY-----FTGKYVLDLHPD---------DIYWCTADPGW--VTGTVYGIWAPWLN----GVTNVV 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 386 YchGGRVgffqgDIRLLSDDMKALCPTIFPVVPRLLnRMydkifsqantpLKRWLLEFAAKrkqaevrsgiirndsiWDE 465
Cdd:cd05969 162 Y--EGRF-----DAESWYGIIERVKVTVWYTAPTAI-RM-----------LMKEGDELARK----------------YDL 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 466 lffnkiqASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVD 544
Cdd:cd05969 207 -------SSL----RFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGVKAAVVD 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 545 vEELNYWACKGEGEICVRG--PNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPE 622
Cdd:cd05969 276 -ENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPF 352
|
490 500 510
....*....|....*....|....*....|....*
gi 1622946795 623 KIENIYIRSQPVAQIYVHGdslkaflvgivVPDPE 657
Cdd:cd05969 353 EVESALMEHPAVAEAGVIG-----------KPDPL 376
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
175-658 |
1.23e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 70.87 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAVL--LLEHVERKETPGLKLIILM 252
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLdgLDPGVRVINVDSPAWADEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 253 DPFEEALKErgqkcgvviksmqavedcgqenhhaPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLKVTEKV 332
Cdd:PRK07867 137 AAHRDAEPP-------------------------FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 333 IFPrqDDVLISFLPLAHmfERVIQSQWAPTCAdvhisylplahmfermvqsvvyCHGGRV--------GFFqgdirllsD 404
Cdd:PRK07867 190 LGP--DDVCYVSMPLFH--SNAVMAGWAVALA----------------------AGASIAlrrkfsasGFL--------P 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 405 DMKALCPTIFPVVPRLLNrmYdkIFS------QANTPLKrwllefaakrkqaevrsgiirndsiwdelffnkiqaslggc 478
Cdd:PRK07867 236 DVRRYGATYANYVGKPLS--Y--VLAtperpdDADNPLR----------------------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 479 vrmIVTGAAPASPTVLGFlRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDVE------------ 546
Cdd:PRK07867 271 ---IVYGNEGAPGDIARF-ARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedad 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 547 --ELNYWACKGEgEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKI 624
Cdd:PRK07867 343 grLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPI 419
|
490 500 510
....*....|....*....|....*....|....
gi 1622946795 625 ENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 658
Cdd:PRK07867 420 ERILLRYPDATEVAVYA-----------VPDPVV 442
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
555-610 |
3.22e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.59 E-value: 3.22e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 555 GE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHI 610
Cdd:PRK08162 385 GEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
146-687 |
5.65e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 69.04 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLlQHNCKACTDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK05620 39 TTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 D---KPQKAVLLlehverKETPGLKLIILMDPFEEALKERGQKCGVVIKSMQAVEDcGQENHHaPVPPQP-DDLSIVCFT 301
Cdd:PRK05620 118 DprlAEQLGEIL------KECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDeTTAAAICYS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 302 SGTTGNPKGAMLTHGNVVADfSGFLKVTEKviFPRQDDVliSFL---PLAHMFerviqsQWAptcadvhisyLPLAhmfe 378
Cdd:PRK05620 190 TGTTGAPKGVVYSHRSLYLQ-SLSLRTTDS--LAVTHGE--SFLccvPIYHVL------SWG----------VPLA---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 379 rmvqsvvychggrvGFFQGdirllsddmkalCPTIFP----VVPRLLnrmydKIFSqanTPLKRwllefaakrkqaeVRS 454
Cdd:PRK05620 245 --------------AFMSG------------TPLVFPgpdlSAPTLA-----KIIA---TAMPR-------------VAH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 455 GIirnDSIWDELFFNKIQ-----ASLggcvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSG 529
Cdd:PRK05620 278 GV---PTLWIQLMVHYLKnpperMSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 530 HVGA---------PLPCNHiKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDP----------------DRTKEALDSD 584
Cdd:PRK05620 351 EARWayrvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTAD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 585 GWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKIENIYIRSQPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQ 664
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGE 493
|
570 580 590
....*....|....*....|....*....|.
gi 1622946795 665 K--------RGIEGTYAdlcTSKDLKKAILE 687
Cdd:PRK05620 494 RplavtvlaPGIEPTRE---TAERLRDQLRD 521
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
144-650 |
9.05e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.22 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGA-IRYIINTADIST 222
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGP--EVRVAIAAERSFELVVALLAVLKAGGAYVPL-DPNYPAErLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 223 VIVDKPQKAVLLLehverkeTPGLKLIILMDPfeEALKERGQkcgvviksmqavedcgqenHHAPVPPQPDDLSIVCFTS 302
Cdd:PRK12316 2104 LLTQRHLLERLPL-------PAGVARLPLDRD--AEWADYPD-------------------TAPAVQLAGENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 303 GTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFErVIQSQWaptcadvhisYLPLahmfermvq 382
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVA----HCQAAGERYELSPADCELQFMSFS--FD-GAHEQW----------FHPL--------- 2209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 383 svvyCHGGRVgffqgdirLLSDDMKalcptifpvvpRLLNRMYDKIFSQANTplkrwLLEFAAKRKQAEVRsgiirndsi 462
Cdd:PRK12316 2210 ----LNGARV--------LIRDDEL-----------WDPEQLYDEMERHGVT-----ILDFPPVYLQQLAE--------- 2252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 463 wdelffnkiQASLGGC---VRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTEctagcTFTTPGDWTSGH-------- 530
Cdd:PRK12316 2253 ---------HAERDGRppaVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTE-----AVVTPLLWKCRPqdpcgaay 2318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 531 --VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH-------TGDIGKWLPAGTL 601
Cdd:PRK12316 2319 vpIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVV 2397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 602 KVIDRKKHIFKLaQGEYVAPEKIENiYIRSQP-------VAQIYVHGDSLKAFLVG 650
Cdd:PRK12316 2398 EYLGRIDHQVKI-RGFRIELGEIEA-RLQAHPavreavvVAQDGASGKQLVAYVVP 2451
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
479-649 |
1.07e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.95 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 479 VRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH---------IKLVDV 545
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryiglegLDVVDT 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 546 EELNYWACKGE--GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEK 623
Cdd:PLN02479 390 KTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLE 467
|
170 180
....*....|....*....|....*.
gi 1622946795 624 IENIyirsqpvaqIYVHGDSLKAFLV 649
Cdd:PLN02479 468 VENV---------VYTHPAVLEASVV 484
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
146-656 |
1.42e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 67.60 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTVIV 225
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DK---PQKAVLLlehverKETPGLKLIILMD------------PFEEALKErgqkcgvviksmqavedcgQENHHAPVPP 290
Cdd:PRK07798 107 ERefaPRVAEVL------PRLPKLRTLVVVEdgsgndllpgavDYEDALAA-------------------GSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 291 QPDDLSIVCfTSGTTGNPKGAMLTHGNV-VADFSGFLKVTEKVIfprQDDVLISFLPLAHMFERviqsqWAPTCadvhis 369
Cdd:PRK07798 162 SPDDLYLLY-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPI---EDEEELAKRAAAGPGMR-----RFPAP------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 370 ylPLAHmfeRMVQSVVYchggrVGFFQGDIRLLSDDMKalcptifpvvprllnrmydkiFSQANtplkrwLLEFAAKRKq 449
Cdd:PRK07798 227 --PLMH---GAGQWAAF-----AALFSGQTVVLLPDVR---------------------FDADE------VWRTIEREK- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 450 aeVRSGIIRNDS----IWDELffnkiqASLGG----CVRMIVTGAAPASPTV-LGFLRAALGCQVYEGYGQTECTAGCTF 520
Cdd:PRK07798 269 --VNVITIVGDAmarpLLDAL------EARGPydlsSLFAIASGGALFSPSVkEALLELLPNVVLTDSIGSSETGFGGSG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 521 TTPGDwtSGHVGAPL--PCNHIKLVDvEELNYWAcKGEGEICV--RGPNVFKGYLKDPDRTKEALDS-DG--WLHTGDIG 593
Cdd:PRK07798 341 TVAKG--AVHTGGPRftIGPRTVVLD-EDGNPVE-PGSGEIGWiaRRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRA 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946795 594 KWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyIRSQPvaqiyvhgDSLKAFLVGivVPDP 656
Cdd:PRK07798 417 RVEADGTITLLGRGSVCINTG-GEKVFPEEVEEA-LKAHP--------DVADALVVG--VPDE 467
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
486-657 |
2.00e-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: 67.02 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 486 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPcNHIKLVDvEELNYWACKGEGEICVRG 563
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 564 PNVFKgYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRsqpvaqiyvHGD 642
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVG-YLDEdGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 1622946795 643 SLKAFLVGivVPDPE 657
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
177-320 |
6.30e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 65.69 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 177 VFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADiSTVIVDKPQkavlLLEHVERKETPGLKLIILMDPFE 256
Cdd:PRK04319 103 IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDV 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622946795 257 EAlkerGQKCGVVIKSMQAVEDcgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVA 320
Cdd:PRK04319 178 EE----GPGTLDFNALMEQASD-----EFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-654 |
6.51e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 65.17 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 290 PQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQsqwaptcadvhis 369
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGIRPGEVDLATFPLFALFGPALG------------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 370 ylplahmfermVQSVVychggrvgffqgdirllsDDMKALCPTifPVVPRllnrmydKIFSqantPLKRWllefaakrkq 449
Cdd:cd05910 145 -----------LTSVI------------------PDMDPTRPA--RADPQ-------KLVG----AIRQY---------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 450 aEVrSGIIRNDSIWDEL--FFNKIQASLGGcVRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------ 519
Cdd:cd05910 173 -GV-SIVFGSPALLERVarYCAQHGITLPS-LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrel 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 520 FTTPGDWTSGH----VGAPLPCNHIKLV--DVEELNYWACKGE------GEICVRGPNVFKGYLKDPDRTKEALDSDG-- 585
Cdd:cd05910 250 LATTTAATSGGagtcVGRPIPGVRVRIIeiDDEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNse 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 586 --WLHTGDIGKWLPAGTLKVIDRKKHIFKLAQGEYVapekieniyirSQPVAQIY-VHGDSLKAFLVGIVVP 654
Cdd:cd05910 330 gfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
291-666 |
7.60e-11 |
|
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: 65.15 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 291 QPDDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQsQWAPTCADVHISY 370
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLV----NLSHGLIKEYGITSSDRVLQFASIA--FDVAAE-EIYVTLLSGATLV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 371 LPLAHMFERMVQSVVYCHggrvgffQGDIRLLSddmkalCPTifpvvprllnrmydkifsqantplkrwllefaakrkqa 450
Cdd:cd17644 177 LRPEEMRSSLEDFVQYIQ-------QWQLTVLS------LPP-------------------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 451 evrsgiirndSIWDELFFNKIQASLGG--CVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDW 526
Cdd:cd17644 206 ----------AYWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 527 TSGH-----VGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLH--------TGDIG 593
Cdd:cd17644 276 TERNitsvpIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLA 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946795 594 KWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 666
Cdd:cd17644 355 RYLPDGNIEYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPSTVELR 429
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
111-690 |
1.75e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.80 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAEL 190
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGE-----QELTYGELNRRANRLAHRLIALGVGP--EVLVGIAVERSLEMVVGLL 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADIStvivdkpqkavLLLEHveRKETPGLKLIilmdpfeealkeRGQKCgVVI 270
Cdd:PRK12467 1643 AILKAGGAYVPLDPEYPRERLAYMIEDSGIE-----------LLLTQ--SHLQARLPLP------------DGLRS-LVL 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 271 KSMQAVEDcGQENHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFsgflKVTEKVIFPRQDDVLISFLPLAHM 350
Cdd:PRK12467 1697 DQEDDWLE-GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL----CATQEAYQLSAADVVLQFTSFAFD 1771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 351 FerviqSQWAptcadvhiSYLPLahmfermvqsvvyCHGGRVgffqgdirLLSDDMKALCPtifpvvprllNRMYDKIFS 430
Cdd:PRK12467 1772 V-----SVWE--------LFWPL-------------INGARL--------VIAPPGAHRDP----------EQLIQLIER 1807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 431 QANTplkrwLLEFAAKRKQAevrsgiirndsiwdelfFNKIQASLGGC--VRMIVTGAAPASPTVLGFLRAALG-CQVYE 507
Cdd:PRK12467 1808 QQVT-----TLHFVPSMLQQ-----------------LLQMDEQVEHPlsLRRVVCGGEALEVEALRPWLERLPdTGLFN 1865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 508 GYGQTECTAG-----CTFTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL- 581
Cdd:PRK12467 1866 LYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFv 1944
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 582 -----DSDGWLH-TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGI 651
Cdd:PRK12467 1945 adpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGgvreAVVIAQDGANGKQ-LVAY 2021
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1622946795 652 VVPDPEVMPSWAQKRgieGTYADlcTSKDLKKAILED-MV 690
Cdd:PRK12467 2022 VVPTDPGLVDDDEAQ---VALRA--ILKNHLKASLPEyMV 2056
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-649 |
1.87e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.98 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 28 TQEILRILRLPELGDLGQFfrSLSATTLVSMGALAAILAYWFTHRPKAL-----QPPCNLLMQS--------EEVEDSGG 94
Cdd:PRK12316 2959 QLPGLHIESFAWDGAATQF--DLALDTWESAEGLGASLTYATDLFDARTverlaRHWQNLLRGMvenpqrsvDELAMLDA 3036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 95 ARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQHNCKActDQF 174
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGE-----QRLSYAELNRRANRLAHRLIERGVGP--DVL 3109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWIIAELACYTYSMVVVPLyDTLGPGAiryiintaDISTVIVDKPQKAVLLLEHVERKETPGLKlIILMDP 254
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPL-DPEYPEE--------RLAYMLEDSGAQLLLSQSHLRLPLAQGVQ-VLDLDR 3179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 255 FEEALKErgqkcgvviksmqavedcgqenHHAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNvvadFSGFLKVTEKVIF 334
Cdd:PRK12316 3180 GDENYAE----------------------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYG 3233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 335 PRQDDVLISFLPLAhmFErviqsqwaptcADVHISYLPLAhmfermvqsvvycHGGRVgfFQGDIRLLSDdmkalcptif 414
Cdd:PRK12316 3234 LGVGDRVLQFTTFS--FD-----------VFVEELFWPLM-------------SGARV--VLAGPEDWRD---------- 3275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 415 pvvPRLLNRMYDKifSQANTPLKRWllefaakrkqaevrsgiirndSIWDELFFNKIQASLGGCVRMIVTGAAPASPtvl 494
Cdd:PRK12316 3276 ---PALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTSLKRIVCGGEALPAD--- 3326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 495 GFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH--VGAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLK 572
Cdd:PRK12316 3327 LQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHN 3405
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 573 DPDRTKEALDSDGW------LHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPV---AQIYVHGDS 643
Cdd:PRK12316 3406 RPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVreaVVLAVDGRQ 3484
|
....*.
gi 1622946795 644 LKAFLV 649
Cdd:PRK12316 3485 LVAYVV 3490
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
480-661 |
2.02e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.95 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 480 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDvEELNYWACKGEG 557
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 558 EICVRGPNV--FKgYLKDPDRTKEaLDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 634
Cdd:PRK12406 352 EIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVG-YLDAdGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGV 427
|
170 180 190
....*....|....*....|....*....|
gi 1622946795 635 AQIYVHGDSLKAF---LVGIVVPDPEVMPS 661
Cdd:PRK12406 428 HDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
286-618 |
2.03e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 63.76 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFlkvteKVIFP-RQDDVLISFLPLAHMFerviqsqwAPTCA 364
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL-----REDYGiEPGEIDLPTFPLFALF--------GPALG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 365 dvhisylplahmfermVQSVVychggrvgffqgdirllsDDMKALCP-TIFPvvprllnrmyDKIFSQ----------AN 433
Cdd:PRK09274 234 ----------------MTSVI------------------PDMDPTRPaTVDP----------AKLFAAierygvtnlfGS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 434 TPLKRWLLEFAAKRKQaevrsgiirndsiwdelffnkiqaSLGGCVRMIVTGAaPASPTVLGFLRAAL--GCQVYEGYGQ 511
Cdd:PRK09274 270 PALLERLGRYGEANGI------------------------KLPSLRRVISAGA-PVPIAVIERFRAMLppDAEILTPYGA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 512 TECTAGCT-------FTTPGDWTSGH---VGAPLPCNHIKLVDV--EELNYWA-----CKGE-GEICVRGPNVFKGYLKD 573
Cdd:PRK09274 325 TEALPISSiesreilFATRAATDNGAgicVGRPVDGVEVRIIAIsdAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNR 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622946795 574 PDRTKEA--LDSDG--WLHTGDIGkWL-PAGTLKVIDRKKHIFKLAQGEY 618
Cdd:PRK09274 405 PEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
146-657 |
2.22e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 63.79 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACytySMVvvplydtlgpGAIRYIINTAdistviV 225
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRA--GDGVAVLARNHRGFVLALYAA---GKV----------GARIILLNTG------F 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 226 DKPQkavlLLEHVERKetpGLKLIILMDPFEE---ALKERGQKCGVVIKSMQAVEDC------------GQENHHAPVPP 290
Cdd:PRK07788 134 SGPQ----LAEVAARE---GVKALVYDDEFTDllsALPPDLGRLRAWGGNPDDDEPSgstdetlddliaGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 291 QPDdlSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLkvtEKVIFPRQDDVLISflplAHMFERVIQSQWAPTCAdvHISY 370
Cdd:PRK07788 207 KPG--GIVILTSGTTGTPKGAPRPEPSPLAPLAGLL---SRVPFRAGETTLLP----APMFHATGWAHLTLAMA--LGST 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 371 LPLAHMF--ERMVQSVVychggrvgffqgdirllsdDMKAlcpTIFPVVPRLLNRMYDkifsqantplkrwLLEfaakrk 448
Cdd:PRK07788 276 VVLRRRFdpEATLEDIA-------------------KHKA---TALVVVPVMLSRILD-------------LGP------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 449 qaEVRSgiirndsiwdelffnKIQASlggCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT- 527
Cdd:PRK07788 315 --EVLA---------------KYDTS---SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAe 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 528 -SGHVGAPLPCNHIKLVD-----VEElnywackGE-GEICVRGPNVFKGYlKDPdRTKEALdsDGWLHTGDIGKWLPAGT 600
Cdd:PRK07788 374 aPGTVGRPPKGVTVKILDengneVPR-------GVvGRIFVGNGFPFEGY-TDG-RDKQII--DGLLSSGDVGYFDEDGL 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946795 601 LKVIDRKKHIFkLAQGEYVAPEKIENIyirsqpvaqIYVHGDSLKAFLVGivVPDPE 657
Cdd:PRK07788 443 LFVDGRDDDMI-VSGGENVFPAEVEDL---------LAGHPDVVEAAVIG--VDDEE 487
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
146-636 |
2.31e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAEFLGSGLLQHncKACTDQFIGVFAQNrPEWIIAELACYTYSMVVVPLYDtlgPGAIR--------YIINT 217
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQAR--ASFGDRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYP---PESARrhhqerllSIIAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 218 ADISTVIVDKP-QKAVLLLEHVERKETPGLkliILMDPFEEALKERGQKCGVviksmqavedcgqenhhapvppQPDDLS 296
Cdd:PRK05691 115 AEPRLLLTVADlRDSLLQMEELAAANAPEL---LCVDTLDPALAEAWQEPAL----------------------QPDDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 297 IVCFTSGTTGNPKGAMLTHGNVVADFS----GFlkvtekVIFPRQDDVLISFLPLAHMFErVIQSQWAPTCADVHISYLP 372
Cdd:PRK05691 170 FLQYTSGSTALPKGVQVSHGNLVANEQlirhGF------GIDLNPDDVIVSWLPLYHDMG-LIGGLLQPIFSGVPCVLMS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 373 LAHMFERMVQSVvychgGRVGFFQGDIRLLSDDMKALCPtifpvvprllNRMYDKIFSQANtpLKRWLLEFAAkrkqaev 452
Cdd:PRK05691 243 PAYFLERPLRWL-----EAISEYGGTISGGPDFAYRLCS----------ERVSESALERLD--LSRWRVAYSG------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 453 rSGIIRNDSIwdELFFNKIQ----------ASLG-GCVRMIVTGAAPA-SPTVLGFLRAALGCQVYEGyGQTECTAGCTF 520
Cdd:PRK05691 299 -SEPIRQDSL--ERFAEKFAacgfdpdsffASYGlAEATLFVSGGRRGqGIPALELDAEALARNRAEP-GTGSVLMSCGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 521 TTPGdwtsghvgaplpcNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGkWLP 597
Cdd:PRK05691 375 SQPG-------------HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLR 440
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622946795 598 AGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPVAQ 636
Cdd:PRK05691 441 DGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
175-658 |
7.05e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 62.35 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 175 IGVFAQNRPEWII----AELACYTysmvVVPLYDTLGPGAIRYIINTADISTVIVDKPQKAvlLLEHVErkeTPGLKLII 250
Cdd:PRK13388 55 VGVLLGNTPEMLFwlaaAALGGYV----LVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 251 LMDPfeealkergqkcgvviKSMQAVEDCGQENHHAPVppQPDDLSIVCFTSGTTGNPKGAMLTHGNVVadFSGFLkVTE 330
Cdd:PRK13388 126 VDTP----------------AYAELVAAAGALTPHREV--DAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRA-LTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 331 KVIFPRqDDVLISFLPLAHmfERVIQSQWAPTCADvhisylplahmfermvqsvvychGGRVGF--------FQGDIRLL 402
Cdd:PRK13388 185 RFGLTR-DDVCYVSMPLFH--SNAVMAGWAPAVAS-----------------------GAAVALpakfsasgFLDDVRRY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 403 SddmkalcPTIFPVVPRLLNrmYdkIFSQ------ANTPLKRWLLEFAAKRKQAEvrsgiirndsiwdelffnkiqaslg 476
Cdd:PRK13388 239 G-------ATYFNYVGKPLA--Y--ILATperpddADNPLRVAFGNEASPRDIAE------------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 477 gcvrmivtgaapasptvlgFLRAaLGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLPcnHIKLVDVEE--------- 547
Cdd:PRK13388 283 -------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP--GVAIYNPETltecavarf 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 548 ------LNywACKGEGEICVR-GPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVA 620
Cdd:PRK13388 339 dahgalLN--ADEAIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLS 414
|
490 500 510
....*....|....*....|....*....|....*...
gi 1622946795 621 PEKIENIYIRSQPVAQIYVHGdslkaflvgivVPDPEV 658
Cdd:PRK13388 415 AAPIERILLRHPAINRVAVYA-----------VPDERV 441
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
285-670 |
2.38e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.13 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 285 HAP-VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFErVIQSQWaptc 363
Cdd:PRK12316 4685 HDPaVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN----HLHATGERYELTPDDRVLQFMSFS--FD-GSHEGL---- 4753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 364 advhisYLPLahmfermvqsvvyCHGGRVgffqgdirLLSDDMKALcPTifpvvpRLLNRMYDKIFSQANTPLKRW--LL 441
Cdd:PRK12316 4754 ------YHPL-------------INGASV--------VIRDDSLWD-PE------RLYAEIHEHRVTVLVFPPVYLqqLA 4799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 442 EFAAKRKQ-AEVRsgiirndsiwdelffnkiQASLGGcvrmivTGAAPASPTVLgfLRAALGCQVYEGYGQTECTAGCT- 519
Cdd:PRK12316 4800 EHAERDGEpPSLR------------------VYCFGG------EAVAQASYDLA--WRALKPVYLFNGYGPTETTVTVLl 4853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 520 FTTPGDWTSG----HVGAPLPCNHIKLVDVEeLNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH- 588
Cdd:PRK12316 4854 WKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYr 4932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 589 TGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIEnIYIRSQP-------VAQIYVHGdslkAFLVGIVVP-DPEVMP 660
Cdd:PRK12316 4933 TGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPqDPALAD 5006
|
410
....*....|
gi 1622946795 661 SWAQKRGIEG 670
Cdd:PRK12316 5007 ADEAQAELRD 5016
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
480-656 |
2.50e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 60.39 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 480 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 542
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 543 vdveelnywackgeGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHifklaQ----GEY 618
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622946795 619 VAPEKIENIYIRsqpvaqiyvHGDSLKAFLVGIvvPDP 656
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
479-657 |
2.50e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 60.30 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 479 VRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNhIKLVDvEELNYWAC 553
Cdd:PRK08276 264 LRVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNELPP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 554 KGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGkWLPA-GTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQ 632
Cdd:PRK08276 338 GEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHP 415
|
170 180
....*....|....*....|....*
gi 1622946795 633 PVAQIYVHGdslkaflvgivVPDPE 657
Cdd:PRK08276 416 KVADVAVFG-----------VPDEE 429
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
502-665 |
2.82e-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: 59.88 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 502 GCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEA 580
Cdd:cd17645 234 GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 581 LDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENI---YIRSQPVAQIYVHGDSLKAFLVGI 651
Cdd:cd17645 313 FIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFlmnHPLIELAAVLAKEDADGRKYLVAY 391
|
170
....*....|....*...
gi 1622946795 652 VVP----DPEVMPSWAQK 665
Cdd:cd17645 392 VTApeeiPHEELREWLKN 409
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
144-664 |
3.54e-09 |
|
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: 59.69 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 144 QWLSYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIINTADISTV 223
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGP--EVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 224 IvdkpqkavlllehverketpglkliilmdpfeealkergqkcgvviksmqavedcgqeNHHapvppqPDDLSIVCFTSG 303
Cdd:cd17649 89 L----------------------------------------------------------THH------PRQLAYVIYTSG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 304 TTGNPKGAMLTHGNVVAdfsgFLKVTEKVIFPRQDDVLISFLPLAhmFERVIQsQWAPTC---ADVHISYLPLAhmferm 380
Cdd:cd17649 105 STGTPKGVAVSHGPLAA----HCQATAERYGLTPGDRELQFASFN--FDGAHE-QLLPPLicgACVVLRPDELW------ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 381 vqsvvychggrvgffqGDIRLLSDDMKALCPTIFPVVPRLLNRmydkifsqantpLKRWLLEFAAKRKQAevrsgiirnd 460
Cdd:cd17649 172 ----------------ASADELAEMVRELGVTVLDLPPAYLQQ------------LAEEADRTGDGRPPS---------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 461 siwdelffnkiqaslggcVRMIVTGAAPASPTvlgFLRAALGCQVY--EGYGQTECTAGCT-FTTPGD----WTSGHVGA 533
Cdd:cd17649 214 ------------------LRLYIFGGEALSPE---LLRRWLKAPVRlfNAYGPTEATVTPLvWKCEAGaaraGASMPIGR 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 534 PLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL--DSDG-----WLHTGDIGKWLPAGTLKVIDR 606
Cdd:cd17649 273 PLGGRSAYILD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGR 351
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946795 607 KKHIFKLaQGEYVAPEKIENiYIRSQP----VAQIYVHGDSLKAfLVGIVVP-DPEVMPSWAQ 664
Cdd:cd17649 352 VDHQVKI-RGFRIELGEIEA-ALLEHPgvreAAVVALDGAGGKQ-LVAYVVLrAAAAQPELRA 411
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
291-666 |
4.59e-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: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 291 QPDDLSIVCFTSGTTGNPKGAMLTH---GNVVADFSGFLKVTekvifPRQddvlisflplahmfeRVIQsqWAPTCADVH 367
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHrglANLAAAQIAAFDVG-----PGS---------------RVLQ--FASPSFDAS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 368 ISYLPLAhmfermvqsvvYCHGGRvgffqgdirllsddmkaLCptifpVVPRLLnrmydkifSQANTPLKRWLlefaakr 447
Cdd:cd17652 149 VWELLMA-----------LLAGAT-----------------LV-----LAPAEE--------LLPGEPLADLL------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 448 kQAEVRSGIIRNDSIWDELffnkIQASLGGCVRMIVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDW 526
Cdd:cd17652 181 -REHRITHVTLPPAALAAL----PPDDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 527 TSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSD------GWLH-TGDIGKWLPAG 599
Cdd:cd17652 253 GVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADG 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 600 TLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQKR 666
Cdd:cd17652 332 QLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
286-649 |
5.71e-09 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 59.08 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGN--VVADFSGflkvtEKVIFPRQDDVLIS--------------FLPLAH 349
Cdd:TIGR02262 154 KPAATQADDPAFWLYSSGSTGMPKGVVHTHSNpyWTAELYA-----RNTLGIREDDVCFSaaklffayglgnalTFPMSV 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 350 MFERVIQSQwAPTCADVhisylplahmFERmvqsvvychggrvgffqgdirllsddMKALCPTIFPVVPRLlnrmYDKIF 429
Cdd:TIGR02262 229 GATTVLMGE-RPTPDAV----------FDR--------------------------LRRHQPTIFYGVPTL----YAAML 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 430 SQANTPlkrwllefaaKRKQAEVRsgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVLGF-LRAALGCQVYEG 508
Cdd:TIGR02262 268 ADPNLP----------SEDQVRLR----------------------------LCTSAGEALPAEVGQrWQARFGVDIVDG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 509 YGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKLVDveELNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEALDSdG 585
Cdd:TIGR02262 310 IGSTE--MLHIFLSnlPGDVRYGTSGKPVPGYRLRLVG--DGGQDVADGEpGELLISGPSSATMYWNNRAKSRDTFQG-E 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946795 586 WLHTGDigKWL--PAGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG----DSL---KAFLV 649
Cdd:TIGR02262 385 WTRSGD--KYVrnDDGSYTYAGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGvadeDGLikpKAFVV 454
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
293-625 |
1.15e-08 |
|
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: 58.25 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVadfsGFLKVT-EKVIFPRQDDVLisflplahmferviqsQWAPTCADVhiSYl 371
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV----NLLHFErEKTNINFSDKVL----------------QFATCSFDV--CY- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 plahmfermvQSVV--YCHGGRvgffqgdIRLLSDDMKALCPTIFPVVPRllNRMYDKIFSQAntplkrwLLEFAAKRKQ 449
Cdd:cd17656 185 ----------QEIFstLLSGGT-------LYIIREETKRDVEQLFDLVKR--HNIEVVFLPVA-------FLKFIFSERE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 450 aevrsgiirndsiwdelFFNkiqaSLGGCVRMIVTGAAP--ASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGD 525
Cdd:cd17656 239 -----------------FIN----RFPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGpsETHVVTTYTINPEAE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 526 WTS-GHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGW------LHTGDIGKWLPA 598
Cdd:cd17656 297 IPElPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPD 375
|
330 340
....*....|....*....|....*..
gi 1622946795 599 GTLKVIDRKKHIFKLaQGEYVAPEKIE 625
Cdd:cd17656 376 GNIEFLGRADHQVKI-RGYRIELGEIE 401
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
480-635 |
1.40e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 58.18 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 480 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKLVDV 545
Cdd:PRK07008 296 RRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKIVGD 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 546 E--ELNyWACKGEGEICVRGPNVFKGYLKdpdRTKEALDsDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEK 623
Cdd:PRK07008 373 DgrELP-WDGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSID 446
|
170
....*....|..
gi 1622946795 624 IENIYIRSQPVA 635
Cdd:PRK07008 447 IENVAVAHPAVA 458
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
289-608 |
3.17e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.94 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 289 PPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVifpRQDDVLISFLPLAH------MFerviqsqWAPT 362
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKV---RPGDRCVSWLPFYHdmglvgFL-------LTPV 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 363 CADVHISYLPLAHMFERMVQSvvychggrvgffqgdIRLLSDDMK--ALCPTI-FPVVPRllnRMYDKifSQANTPLKRW 439
Cdd:PRK09192 242 ATQLSVDYLPTRDFARRPLQW---------------LDLISRNRGtiSYSPPFgYELCAR---RVNSK--DLAELDLSCW 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 440 LLefaakrkqAEVRSGIIRNDSIwdELFFNKIqaslggcvrmivtgaAPAsptvlGF-LRAALGCqvyegYGQTECTAGC 518
Cdd:PRK09192 302 RV--------AGIGADMIRPDVL--HQFAEAF---------------APA-----GFdDKAFMPS-----YGLAEATLAV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 519 TFTTPG----------DWTSGH------------------VGAPLPCNHIKLVDV--EELNYwacKGEGEICVRGPNVFK 568
Cdd:PRK09192 347 SFSPLGsgivveevdrDRLEYQgkavapgaetrrvrtfvnCGKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMS 423
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622946795 569 GYLKDPDRTKeALDSDGWLHTGDIGkWLPAGTLKVIDRKK 608
Cdd:PRK09192 424 GYFRDEESQD-VLAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
293-666 |
3.22e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.21 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 293 DDLSIVCFTSGTTGNPKGAMLTHGNVVA------DFSG-----FLKVTEKVIFPRQddVLIsflplahmfeRVIQSQWAP 361
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTAsadathDRLGgpgqwLLALPAHHIAGLQ--VLV----------RSVIAGSEP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 362 TCADVHISYLPLAhmFERMVQSVvychggrvgffQGDIRLLSddmkaLCPTifpvvpRLLNRMYDKIFSQAntplkrwLL 441
Cdd:PRK07824 103 VELDVSAGFDPTA--LPRAVAEL-----------GGGRRYTS-----LVPM------QLAKALDDPAATAA-------LA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 442 EFAAkrkqaevrsgiirndsiwdelffnkiqaslggcvrmIVTGAAPASPTVlgfLRAA--LGCQVYEGYGQTECTAGCT 519
Cdd:PRK07824 152 ELDA------------------------------------VLVGGGPAPAPV---LDAAaaAGINVVRTYGMSETSGGCV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 520 FTtpgdwtsghvGAPLPCNHIKLVDveelnywackgeGEICVRGPNVFKGY--LKDPDrtkeALDSDGWLHTGDIGKwLP 597
Cdd:PRK07824 193 YD----------GVPLDGVRVRVED------------GRIALGGPTLAKGYrnPVDPD----PFAEPGWFRTDDLGA-LD 245
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 598 AGTLKVIDRKKHIFKLAqGEYVAPEKIENIYIRSQPVAQIYVHG---DSLKAFLVGIVVPDPEVMPSWAQKR 666
Cdd:PRK07824 246 DGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
292-660 |
3.76e-08 |
|
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: 56.64 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMLTHGNVV---ADFSG--FLKVTEkvifprqDDVLISFLplAHMFErviqsqwaptcadv 366
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSEryFGRDNG-------DEAVLFFS--NYVFD-------------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 367 hisylplaHMFERMVQSVVYCHggrvgffqgDIRLLSDDMKALCPTIfpvvPRLLNRmyDKIFSQANTPLKRWLLEFAak 446
Cdd:cd17648 150 --------FFVEQMTLALLNGQ---------KLVVPPDEMRFDPDRF----YAYINR--EKVTYLSGTPSVLQQYDLA-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 447 rkqaevrsgiirndsiwdelffnkiqaSLGGCVRMIVTGAAPASPtVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPG 524
Cdd:cd17648 205 ---------------------------RLPHLKRVDAAGEEFTAP-VFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 525 DWTSGHVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-------------ALDSDGWLH-TG 590
Cdd:cd17648 257 QRFDKSLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTG 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 591 DIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIY-----IRSQPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 660
Cdd:cd17648 336 DLVRWLPSGELEYLGRNDFQVKI-RGQRIEPGEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
480-641 |
8.57e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 55.53 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 480 RMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV---GAPLPCNHIKLVDVE 546
Cdd:PRK06018 297 KMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqkqGYPPFGVEMKITDDA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 547 --ELNyWACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKlAQGEYVAPEKI 624
Cdd:PRK06018 374 gkELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDL 448
|
170
....*....|....*..
gi 1622946795 625 ENIYIRSQPVAQIYVHG 641
Cdd:PRK06018 449 ENLAVGHPKVAEAAVIG 465
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
479-672 |
1.61e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 54.63 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 479 VRMIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDVEELNYWAC 553
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 554 KGE-----GEICVRGPNVFKGYLKDPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIY 628
Cdd:PRK05857 367 GAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIA 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622946795 629 IRSQPV--AQIYVHGDSLKAFLVGI-VVPDPEVMPSWAQ--KRGIEGTY 672
Cdd:PRK05857 445 EGVSGVreAACYEIPDEEFGALVGLaVVASAELDESAARalKHTIAARF 493
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
509-627 |
1.90e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.39 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 509 YGQTECTAGCTFTTPG-----------DWTSGH----VGAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKD 573
Cdd:PRK05851 310 YGLAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ 389
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622946795 574 PdrtkeALDSDGWLHTGDIGkWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENI 627
Cdd:PRK05851 390 A-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
467-649 |
2.28e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 467 FFNKIqasLGGC-------VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLP 536
Cdd:PRK06060 246 FFARV---IDSCspdsfrsLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 537 CNHIKLVDVEELNYwACKGEGEICVRGPNVFKGYLKDPDrtkEALDSDGWLHTGDIGK-----WLPAGTlkvidrKKHIF 611
Cdd:PRK06060 321 PYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCidsdgWVTYRC------RADDT 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622946795 612 KLAQGEYVAPEKIENIYIRSQPVAQIYVHG-------DSLKAFLV 649
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLV 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
111-666 |
2.43e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.58 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 111 YDDARTMYQVFRRGLSISGNGPCLGFRKpnqpyQWLSYQEVADRAEFLGSGLLQhnCKACTDQFIGVFAQNRPEWIIAEL 190
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGE-----ETLDYAELNRRANRLAHALIE--RGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 191 ACYTYSMVVVPLYDTLGPGAIRYIINTADIstvivdkpqkAVLLLEHVERKETP---GLKLIILMDP--FEEALKERGQK 265
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGV----------QLLLSQSHLGRKLPlaaGVQVLDLDRPaaWLEGYSEENPG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 266 CGVViksmqavedcgqenhhapvppqPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifprqddvlisfL 345
Cdd:PRK12316 650 TELN----------------------PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYG--------------L 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 346 PLAhmfERVIQSqwAPTCADVHIS--YLPLAhmfermvqsvvycHGGRVgffqgdirllsddmkalcptifPVVPRLLNR 423
Cdd:PRK12316 694 GVG---DTVLQK--TPFSFDVSVWefFWPLM-------------SGARL----------------------VVAAPGDHR 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 424 MYDKIFSQANTPLKRwLLEFAAKRKQAEVRSGIIrndsiwdelffnkiqASLGGCVRMIVTGAAPASPTVLGFLRAALGC 503
Cdd:PRK12316 734 DPAKLVELINREGVD-TLHFVPSMLQAFLQDEDV---------------ASCTSLRRIVCSGEALPADAQEQVFAKLPQA 797
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 504 QVYEGYGQTECTAGCTFTTPGDWTSGHV--GAPLPCNHIKLVDVeELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL 581
Cdd:PRK12316 798 GLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERF 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 582 ------DSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAfLVGIVVPD 655
Cdd:PRK12316 877 vpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLE 954
|
570
....*....|....*..
gi 1622946795 656 ------PEVMPSWAQKR 666
Cdd:PRK12316 955 seggdwREALKAHLAAS 971
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
473-657 |
2.52e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 53.68 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 473 ASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC-TAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDvEELNY 550
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVhAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 551 WACKGEGEICV---RGPNV-FKGYLKDPDRTKealdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIEN 626
Cdd:cd05973 280 LGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|.
gi 1622946795 627 IYIRSQPVAQIYVhgdslkaflvgIVVPDPE 657
Cdd:cd05973 355 ALIEHPAVAEAAV-----------IGVPDPE 374
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
146-349 |
3.56e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 53.72 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 146 LSYQEVADRAE-----FLGSGLLQHNCkactdqfIGVFAQNRPEWIIAELACyTYSMVVVPLYDT-LGPGAIRYIINTAD 219
Cdd:PRK08279 63 ISYAELNARANryahwAAARGVGKGDV-------VALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 220 ISTVIVDKPqkavlLLEHVE--RKETPGLKLIILMDPFEEALKERgqkcgvVIKSMQAVEDCGQENHHAPVPPQPDDLSI 297
Cdd:PRK08279 135 AKHLIVGEE-----LVEAFEeaRADLARPPRLWVAGGDTLDDPEG------YEDLAAAAAGAPTTNPASRSGVTAKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622946795 298 VCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEkvifPRQDDVLISFLPLAH 349
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
292-649 |
4.96e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMlthgnvvadfsgflkVTEKVIFPRQddvlISFLPLAHMFERVIQSQWAPTCADVHISYL 371
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVM---------------VEQRGMLNNQ----LSKVPYLALSEADVIAQTASQSFDISVWQF 3928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 372 PLAHMFermvqsvvychGGRVGFFQGDIrllSDDMKALCP-------TIFPVVPRLLNRMydkifsqantplkrwllefa 444
Cdd:PRK05691 3929 LAAPLF-----------GARVEIVPNAI---AHDPQGLLAhvqaqgiTVLESVPSLIQGM-------------------- 3974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 445 akrkqaevrsgiIRNDsiwdelffnkiQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF---- 520
Cdd:PRK05691 3975 ------------LAED-----------RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvd 4031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 521 --TTPGDWTSghVGAPLPCNHIKLVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-------DSDGWLHTGD 591
Cdd:PRK05691 4032 laSTRGSYLP--IGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGD 4108
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622946795 592 IGKWLPAGTLKVIDRKKHI-----FKLAQGEYVApEKIENIYIRSQPVA-QIYVHGDSLKAFLV 649
Cdd:PRK05691 4109 LARRRSDGVLEYVGRIDHQvkirgYRIELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
479-658 |
6.26e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 479 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDVEELNywackg 555
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP------ 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 556 EGEIcvrGPNVFK------GYLKDPDRTKEALDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENI 627
Cdd:PRK13390 345 AGRI---GTVYFErdrlpfRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENA 420
|
170 180 190
....*....|....*....|....*....|.
gi 1622946795 628 YIRSQPVAQIYVHGdslkaflvgivVPDPEV 658
Cdd:PRK13390 421 LTMHPAVHDVAVIG-----------VPDPEM 440
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
251-350 |
7.07e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 52.68 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 251 LMDPFEE---ALKERGQKCGVVIKSM--QAVEDCGQENHHAPVPPQPDDLS---------IVCFTSGTTGNPKGAMLTHG 316
Cdd:cd05938 88 LQEAVEEvlpALRADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRahvtikspaLYIYTSGTTGLPKAARISHL 167
|
90 100 110
....*....|....*....|....*....|....
gi 1622946795 317 NVVAdFSGFLKVTeKVifpRQDDVLISFLPLAHM 350
Cdd:cd05938 168 RVLQ-CSGFLSLC-GV---TADDVIYITLPLYHS 196
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
286-349 |
1.35e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.87 E-value: 1.35e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622946795 286 APVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADF----SGFLKVTEKVifPRQDDVLISFLPLAH 349
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWLPFYH 218
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
534-594 |
2.65e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.66 E-value: 2.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946795 534 PLPCNHIK-----LVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEAL-DSDGW--LHTGDIGK 594
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY 385
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
479-626 |
1.64e-05 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 47.40 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 479 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDVEElnywacKGE 556
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GEI 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 557 GEICVRGPNVFKGYLKDPDRTKealdsDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 626
Cdd:cd17633 185 GKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIES 248
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
476-658 |
4.86e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 46.68 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 476 GGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDVE--ELNy 550
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 551 wacKGE-GEICVRGPNVFKGYlkDPDRTKEAldSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIyI 629
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKT-L 458
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622946795 630 RSQP-VAQIYV-------HGDSLKAFlvgiVVPDPEV 658
Cdd:PRK13382 459 ATHPdVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
480-665 |
5.40e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 46.22 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 480 RMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL-PCNHIKLVDVEELNYWACK--G 555
Cdd:cd05924 137 FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFtRANPDTVVLDDDGRVVPPGsgG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 556 EGEICVRGpNVFKGYLKDPDRTKEA---LDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGEYVAPEKIENIyIRSQ 632
Cdd:cd05924 214 VGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVEEA-LKSH 290
|
170 180 190
....*....|....*....|....*....|....
gi 1622946795 633 P-VAQIYVHGdslkaflvgivVPDPEvmpsWAQK 665
Cdd:cd05924 291 PaVYDVLVVG-----------RPDER----WGQE 309
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
468-746 |
1.07e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 468 FNKIQASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDVEE 547
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 548 LNYWACKGE-GEICVRGPNVFKGYLKDPDRTKEaLDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIEN 626
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 627 IYIRSQPVAQIYVHGdslkaflvgivVPDpevmPSWAQKRG--IEGTyadlCTSKDLKKAILEDmvrlgkesgLHSFEQV 704
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPD----SYWGEKPVaiIKGS----ATKQQLKSFCLQR---------LSSFKIP 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622946795 705 KAIHIhsdmfsVQNGLLTPTLKAKRPELreyfKKQIEELYSI 746
Cdd:PRK07638 454 KEWHF------VDEIPYTNSGKIARMEA----KSWIENQEKI 485
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
469-633 |
1.47e-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: 45.11 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 469 NKIQASLGGCVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 541
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 542 LVDVEELNYWACKGEGE----ICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLAqGE 617
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170
....*....|....*.
gi 1622946795 618 YVAPEKIENIyIRSQP 633
Cdd:cd05915 421 WISSVDLENA-LMGHP 435
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
294-657 |
3.41e-04 |
|
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: 43.88 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 294 DLSIVCFTSGTTGNPKGAMLTH-----GNVVADFSGFLKvtekvifprQDDVLISFLPLAHMFERVIqsqwAPTCADVHI 368
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrrawrGGAFFAGSGGAL---------PSDVLYTCLPLYHSTALIV----GWSACLASG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 369 SYLPLAHMFErmvqsvvychggrVGFFQGDIRllsddmKALCpTIFPVVPRLLnrmydkifsqantplkRWLLefAAKRK 448
Cdd:cd05940 149 ATLVIRKKFS-------------ASNFWDDIR------KYQA-TIFQYIGELC----------------RYLL--NQPPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 449 QAEVRsgiirndsiwdelffNKIQASLGGCVRmivtgaapasPTVLGFLRAALGC-QVYEGYGQTECTAGCT--FTTPGd 525
Cdd:cd05940 191 PTERK---------------HKVRMIFGNGLR----------PDIWEEFKERFGVpRIAEFYAATEGNSGFInfFGKPG- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 526 wTSGHVGAPLPCNH-IKLV--DVEELNYW---------ACKGE-----GEICVRGPnvFKGYLKDPDRTKEAL-----DS 583
Cdd:cd05940 245 -AIGRNPSLLRKVApLALVkyDLESGEPIrdaegrcikVPRGEpglliSRINPLEP--FDGYTDPAATEKKILrdvfkKG 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946795 584 DGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVAQIYVHGDSL-----KAFLVGIVVPDPE 657
Cdd:cd05940 322 DAWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
147-316 |
5.74e-04 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 43.33 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 147 SYQEVADRAEFLGSGLLQHNCKActDQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGAIRYIIntADISTVIVd 226
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKK--GDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRI--IDSSSRLL- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 227 kpqkaVLLLEHVERKETPGLKLIIlmdpfEEALKERGQKC-GVVIKSMQAVEDCGQEN--------------HHAPVPPQ 291
Cdd:cd17634 161 -----ITADGGVRAGRSVPLKKNV-----DDALNPNVTSVeHVIVLKRTGSDIDWQEGrdlwwrdliakaspEHQPEAMN 230
|
170 180
....*....|....*....|....*
gi 1622946795 292 PDDLSIVCFTSGTTGNPKGAMLTHG 316
Cdd:cd17634 231 AEDPLFILYTSGTTGKPKGVLHTTG 255
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
478-649 |
5.88e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 43.06 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 478 CVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGcTFTTPG---DWTSGhVGAPLPCNHIKLVDVEELNYwACK 554
Cdd:PRK13383 293 QLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIG-ALATPAdlrDAPET-VGKPVAGCPVRILDRNNRPV-GPR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 555 GEGEICVRGPNVFKGYlkdPDRTKEALdSDGWLHTGDIGKWLPAGTLKVIDRKKHIFkLAQGEYVAPEKIENIYIRSQPV 634
Cdd:PRK13383 370 VTGRIFVGGELAGTRY---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAV 444
|
170 180
....*....|....*....|..
gi 1622946795 635 AQIYV-------HGDSLKAFLV 649
Cdd:PRK13383 445 ADNAVigvpderFGHRLAAFVV 466
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
288-319 |
6.22e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.49 E-value: 6.22e-04
10 20 30
....*....|....*....|....*....|..
gi 1622946795 288 VPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVV 319
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
465-650 |
1.38e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 465 ELFFNKIQASLGGCVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIK 541
Cdd:PRK05691 1376 QLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCR 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 542 LVDvEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKE-----ALDSDG--WLHTGDIGKWLPAGTLKVIDRKKHIFKLa 614
Cdd:PRK05691 1456 VLD-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL- 1533
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622946795 615 QGEYVAPEKIENIYIRSQPVAQ--IYVHGDSLKAFLVG 650
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
568-656 |
2.48e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 568 KGYLKDPDRTKEALDSDGWL------HTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIyIRSQP-VAQIYVH 640
Cdd:PRK10252 814 QGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRA-MQALPdVEQAVTH 891
|
90 100
....*....|....*....|....*..
gi 1622946795 641 -----------GDSLKafLVGIVVPDP 656
Cdd:PRK10252 892 acvinqaaatgGDARQ--LVGYLVSQS 916
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
505-641 |
3.39e-03 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 40.49 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 505 VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL--------VDVEELNYW----------ACKGE-GEICVRGPN 565
Cdd:cd05937 229 IGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvkMDPETDDPIrdpktgfcvrAPVGEpGEMLGRVPF 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 566 V----FKGYLKDPDRTKEAL------DSDGWLHTGDIGKWLPAGTLKVIDRKKHIFKLaQGEYVAPEKIENIYIRSQPVA 635
Cdd:cd05937 309 KnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIA 387
|
....*.
gi 1622946795 636 QIYVHG 641
Cdd:cd05937 388 EANVYG 393
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
138-319 |
4.00e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 40.26 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 138 KPNQP-YQWL----SYQEVADRAEFLGSGLLQHncKACTDQFIGVFAQNRPEWIIAELAC----YTYsmvvVPLYDTLGP 208
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSL--KLPDKSPIIVFGHMSPEMLATFLGAvkagHAY----IPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946795 209 GAIRYIINTADISTVI--VDKPqkavlllehVERKETPGLKLIILMDPFEEalkergqkcGVVIKSMQAVEDcgqenhha 286
Cdd:PRK04813 89 ERIEMIIEVAKPSLIIatEELP---------LEILGIPVITLDELKDIFAT---------GNPYDFDHAVKG-------- 142
|
170 180 190
....*....|....*....|....*....|...
gi 1622946795 287 pvppqpDDLSIVCFTSGTTGNPKGAMLTHGNVV 319
Cdd:PRK04813 143 ------DDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
|
| |
