|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-714 |
0e+00 |
|
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: 782.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 142 GDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCitetevtt 221
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 222 vitshdllpkfktlldkcplvktiiyiedqLQKTETTGfkegvkilpfnqvVKTGqdskfehvpPKGDDIAIIMYTSGST 301
Cdd:cd17639 73 ------------------------------LNETECSA-------------IFTD---------GKPDDLACIMYTSGST 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 302 GTPKGVLLSHKNCIATMKGFVDMVP--IYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLIDtssKIKRGCKG 379
Cdd:cd17639 101 GNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGCKG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 380 DATVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFLYQYKVKWVQRGYKTPLIDKLVFKKVAKLMGGKVRIIMS 459
Cdd:cd17639 178 DLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYMLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 460 GGAPLSADTHEQIKTCLClELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYrVTNKPYPQGEVLI 539
Cdd:cd17639 258 GGAPLSADTQEFLNIVLC-PVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGY-STDKPPPRGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 540 GGECVSQGYYKLPGKTNEDFfeeDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENIC 619
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAF---DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNIC 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 620 VYGDPTKQYTVALVVPNQNHLEELAQKHGLGDKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPD 699
Cdd:cd17639 413 VYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPE 492
|
570
....*....|....*
gi 442622933 700 MGLVTAAFKLKRKDI 714
Cdd:cd17639 493 NGLVTAAQKLKRKEI 507
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
95-727 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 699.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 95 ENIDTLEKVFNYVAKTYTSKRCLGTRQILSEEDEVQQNGRVFKKYNLGDYKWKTFTEAERTAANFGRGLRELGQKPRENI 174
Cdd:PLN02387 55 EGATTLAALFEQSCKKYSDKRLLGTRKLISREFETSSDGRKFEKLHLGEYEWITYGQVFERVCNFASGLVALGHNKEERV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 175 VIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPKFKTLLDKCPLVKTIIYIEDQLQK 254
Cdd:PLN02387 135 AIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETVKRVIYMDDEGVD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 255 TETTGFK-EGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVP-IYPDDV 332
Cdd:PLN02387 215 SDSSLSGsSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPkLGKNDV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 333 LIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLIDTSSKIKRGCKGDATVLKPTCMTSVPLILDRISKGINDKVNSGSA 412
Cdd:PLN02387 295 YLAYLPLAHILELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 413 FKKSLFKFLYQYKVKWVQ------RGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGL 486
Cdd:PLN02387 375 LAKKLFDIAYKRRLAAIEgswfgaWGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 487 TETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDF-FEEDGQ 565
Cdd:PLN02387 455 TETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYkVDERGM 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 566 RWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPNQNHLEELAQ 645
Cdd:PLN02387 535 RWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAK 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 646 KHGLGDKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQHDINRM 725
Cdd:PLN02387 615 KAGIDYSNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKL 694
|
..
gi 442622933 726 YA 727
Cdd:PLN02387 695 YE 696
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
142-727 |
3.22e-177 |
|
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: 517.54 E-value: 3.22e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 142 GDYKWKTFTEAERTAANFGRGLRELGQKPREN--IVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDgvahcitetev 219
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 220 ttvitshdllpkfktlldkcplvkTIIYIEDQlQKTETTGFKEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSG 299
Cdd:cd05927 70 ------------------------AIEYILNH-AEISIVFCDAGVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 300 STGTPKGVLLSHKNCIAT----MKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYST--PLTLIDtsski 373
Cdd:cd05927 125 TTGNPKGVMLTHGNIVSNvagvFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD----- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 374 krgckgDATVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFLYQYKVKWVQRG--YKTPLIDKLVFKKVAKLMG 451
Cdd:cd05927 200 ------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQALG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 452 GKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTnKP 531
Cdd:cd05927 274 GNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAK-DP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 532 YPQGEVLIGGECVSQGYYKLPGKTNEDFfEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKT 611
Cdd:cd05927 353 NPRGEVCIRGPNVFSGYYKDPEKTAEAL-DEDG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYAR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 612 CGIIENICVYGDPTKQYTVALVVPNQNHLEELAQKHGLGDKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITL 691
Cdd:cd05927 430 SPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHL 509
|
570 580 590
....*....|....*....|....*....|....*.
gi 442622933 692 CKEVWSPDMGLVTAAFKLKRKDIQDRYQHDINRMYA 727
Cdd:cd05927 510 EPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
97-727 |
6.98e-150 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 451.09 E-value: 6.98e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 97 IDTLEKVFNYVAKTYTSKRCLGTRqilseedeVQQNGRVfkkynlGDYKWKTFTEA--ERTAAnfGRGLRELGQKPRENI 174
Cdd:PLN02736 43 IGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAgtARTAI--GSGLVQHGIPKGACV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 175 VIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPKFKTLLDKCPLVKTIIYI---EDQ 251
Cdd:PLN02736 107 GLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSEIPSVRLIVVVggaDEP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 252 LQKTETTgfkEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDD 331
Cdd:PLN02736 187 LPSLPSG---TGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 332 VLIGFLPLAHVFELVAESVCLMTGVPIGY--STPLTLIDtsskikrgckgDATVLKPTCMTSVPLILDRISKGINDKVNS 409
Cdd:PLN02736 264 VHISYLPLAHIYERVNQIVMLHYGVAVGFyqGDNLKLMD-----------DLAALRPTIFCSVPRLYNRIYDGITNAVKE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 410 GSAFKKSLFKFLYQYKVKWVQRGYK-TPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTE 488
Cdd:PLN02736 333 SGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 489 TTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEdFFEEDGqrWF 568
Cdd:PLN02736 413 TSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGYYKDEVQTRE-VIDEDG--WL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 569 KTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPNQNHLEELAQKHG 648
Cdd:PLN02736 490 HTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEG 569
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622933 649 LGDKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQHDINRMYA 727
Cdd:PLN02736 570 IKYEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
142-727 |
3.02e-137 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 416.81 E-value: 3.02e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 142 GDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFK-QAMPiVTVYATLGDDGVAHCItetevt 220
Cdd:COG1022 36 GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAaGAVT-VPIYPTSSAEEVAYIL------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 221 tvitSH-----------DLLPKFKTLLDKCPLVKTIIYIEDqlqktetTGFKEGVKILPFNQVVKTGQDSKFEH------ 283
Cdd:COG1022 109 ----NDsgakvlfvedqEQLDKLLEVRDELPSLRHIVVLDP-------RGLRDDPRLLSLDELLALGREVADPAelearr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTP 363
Cdd:COG1022 178 AAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAES 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 L-TLIDtsskikrgckgDATVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFL----YQY--------KVKWVQ 430
Cdd:COG1022 258 PdTLAE-----------DLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWAlavgRRYararlagkSPSLLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 431 RgYKTPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHE--QIktcLCLELIQGYGLTETTSGATVMDYRDMTYGRTGG 508
Cdd:COG1022 327 R-LKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARffRA---LGIPVLEGYGLTETSPVITVNRPGDNRIGTVGP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 509 PLTVCDIRLVnweegnyrvtnkpyPQGEVLIGGECVSQGYYKLPGKTNEDfFEEDGqrWFKTGDIGEIQADGVLKIIDRK 588
Cdd:COG1022 403 PLPGVEVKIA--------------EDGEILVRGPNVMKGYYKNPEATAEA-FDADG--WLHTGDIGELDEDGFLRITGRK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 589 KDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDpTKQYTVALVVPNQNHLEELAQKHGLGDKSFEELCSSPIIEKAIL 668
Cdd:COG1022 466 KDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGD-GRPFLAALIVPDFEALGEWAEENGLPYTSYAELAQDPEVRALIQ 544
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622933 669 KEIAEhARKcKLQKYEVPAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQHDINRMYA 727
Cdd:COG1022 545 EEVDR-ANA-GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
79-727 |
6.30e-136 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 416.68 E-value: 6.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 79 YRTTDPPRDVHVKMLQE--NIDTLEKVFNYVAKTYTSKRCLGTRQILSEEDEV--QQNG--RVFKKYNLGDYKWKTFTEA 152
Cdd:PTZ00216 48 YRIAGVTDEEHERLRNEwyYGPNFLQRLERICKERGDRRALAYRPVERVEKEVvkDADGkeRTMEVTHFNETRYITYAEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 153 ERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPKF 232
Cdd:PTZ00216 128 WERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 233 KTLLDKCPLVKT-IIYIeDQLQKTETTgfkEGVKILPFNQVVKTGQdSKFEHVPPKG----DDIAIIMYTSGSTGTPKGV 307
Cdd:PTZ00216 208 LRLMKSGGMPNTtIIYL-DSLPASVDT---EGCRLVAWTDVVAKGH-SAGSHHPLNIpennDDLALIMYTSGTTGDPKGV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 308 LLSHKNCIATMKGFVDMV-----PIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLIDTSSKIkrgcKGDAT 382
Cdd:PTZ00216 283 MHTHGSLTAGILALEDRLndligPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFARP----HGDLT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 383 VLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFLYQYKVKWVQRGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGA 462
Cdd:PTZ00216 359 EFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRAVLGGRVRAMLSGGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 463 PLSADTHEQIKTCLCLeLIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEgnYRVTNKPYPQGEVLIGGE 542
Cdd:PTZ00216 439 PLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEE--YKHTDTPEPRGEILLRGP 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 543 CVSQGYYKLPGKTNEdFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIEN--ICV 620
Cdd:PTZ00216 516 FLFKGYYKQEELTRE-VLDEDG--WFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngVCV 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 621 YGDPTKQYTVALVVPNQNHLEELAQKHGLGDkSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDM 700
Cdd:PTZ00216 593 LVHPARSYICALVLTDEAKAMAFAKEHGIEG-EYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPEN 671
|
650 660
....*....|....*....|....*..
gi 442622933 701 GLVTAAFKLKRKDIQDRYQHDINRMYA 727
Cdd:PTZ00216 672 GVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
84-727 |
3.85e-121 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 377.23 E-value: 3.85e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 84 PPRDvhvkmlqENIDTLEKVFNYVAKTYTSKRCLGTRQILSEEdevqqngrvfkkynLGDYKWKTFTEAERTAANFGRGL 163
Cdd:PLN02430 35 PPID-------SDITTAWDIFSKSVEKYPDNKMLGWRRIVDGK--------------VGPYMWKTYKEVYEEVLQIGSAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 164 RELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDllpKFKTLLD---KCP 240
Cdd:PLN02430 94 RASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK---KIKELLEpdcKSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 241 -LVKTIIYIEDQLQKTETTGFKEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMK 319
Cdd:PLN02430 171 kRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 320 GfVDMV------PIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPltliDTSSkikrgCKGDATVLKPTCMTSVP 393
Cdd:PLN02430 251 G-VDLFmeqfedKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHG----DLNA-----LRDDLMELKPTLLAGVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 394 LILDRISKGINDKVNSGSAFKKSLFKFLYQYKVKWVQRGYK----TPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTH 469
Cdd:PLN02430 321 RVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYShkkaSPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 470 EQIKTCLCLELIQGYGLTETTSGATVMDYRDMTY-GRTGGPLTVCDIRLVNWEEGNYRVTNKPyPQGEVLIGGECVSQGY 548
Cdd:PLN02430 401 EFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYDPLGEP-PRGEICVRGKCLFSGY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 549 YKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQY 628
Cdd:PLN02430 480 YKNPELTEEVM--KDG--WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSM 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 629 TVALVVPNQNHLEELAQKHGLgDKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTAAFK 708
Cdd:PLN02430 556 LVAVVVPNEENTNKWAKDNGF-TGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLK 634
|
650
....*....|....*....
gi 442622933 709 LKRKDIQDRYQHDINRMYA 727
Cdd:PLN02430 635 KRRNNLLKYYQVEIDEMYR 653
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
142-714 |
2.98e-117 |
|
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: 359.99 E-value: 2.98e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 142 GDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHcitetevtt 221
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAY--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 222 vitshdllpkfktLLDKCplvktiiyiedqlqktettgfkeGVKILpfnqvvktgqdskfehVPPKGDDIAIIMYTSGST 301
Cdd:cd05907 72 -------------ILNDS-----------------------EAKAL----------------FVEDPDDLATIIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 302 GTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVA-ESVCLMTGVPIGYSTPL-TLIDTSSKIKrgckg 379
Cdd:cd05907 100 GRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAgLYVPLLAGARIYFASSAeTLLDDLSEVR----- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 380 datvlkPTCMTSVPLILDRISKGIndKVNSGSAFKKSLFkflyqykvkwvqrgyktplidklvfkkvAKLMGGKVRIIMS 459
Cdd:cd05907 175 ------PTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLF----------------------------DLAVGGRLRFAAS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 460 GGAPLSADTHEQIKTcLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVnweegnyrvtnkpyPQGEVLI 539
Cdd:cd05907 219 GGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIA--------------DDGEILV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 540 GGECVSQGYYKLPGKTNEDFfEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENIC 619
Cdd:cd05907 284 RGPNVMLGYYKNPEATAEAL-DADG--WLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAV 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 620 VYGDpTKQYTVALVVPNQNHLEELAQKHGLGDKSFEELCSSPIIEKAILKEIaEHARKcKLQKYEVPAAITLCKEVWSPD 699
Cdd:cd05907 361 VIGD-GRPFLVALIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAV-EAANA-RLSRYEQIKKFLLLPEPFTIE 437
|
570
....*....|....*
gi 442622933 700 MGLVTAAFKLKRKDI 714
Cdd:cd05907 438 NGELTPTLKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
93-727 |
8.03e-112 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 352.99 E-value: 8.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 93 LQENIDTLEKVFNYVAKTYTSKRCLGTRQILseedevqqNGRVfkkynlGDYKWKTFTEAERTAANFGRGLRELGQKPRE 172
Cdd:PLN02861 38 LPADIDSPWQFFSDAVKKYPNNQMLGRRQVT--------DSKV------GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 173 NIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPKFKTLLDKC-PLVKTIIYIED- 250
Cdd:PLN02861 104 RCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKCsSNLKTIVSFGDv 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 251 -QLQKTETTgfKEGVKILPFNQVVKTG-QDSKfehVPPK-GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKG-----FV 322
Cdd:PLN02861 184 sSEQKEEAE--ELGVSCFSWEEFSLMGsLDCE---LPPKqKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLStdhllKV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 323 DMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYstpltlidTSSKIkRGCKGDATVLKPTCMTSVPLILDRISKG 402
Cdd:PLN02861 259 TDRVATEEDSYFSYLPLAHVYDQVIETYCISKGASIGF--------WQGDI-RYLMEDVQALKPTIFCGVPRVYDRIYTG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 403 INDKVNSGSAFKKSLFKFLYQYKVKWVQRGYK----TPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCL 478
Cdd:PLN02861 330 IMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKqeeaSPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 479 ELIQGYGLTETTSGA--TVMDYRDMTyGRTGGPLTVCDIRLVNWEEGNYRVTNKpYPQGEVLIGGECVSQGYYKLPGKTN 556
Cdd:PLN02861 410 VLSQGYGLTESCGGCftSIANVFSMV-GTVGVPMTTIEARLESVPEMGYDALSD-VPRGEICLRGNTLFSGYHKRQDLTE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 557 EDFFeeDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPN 636
Cdd:PLN02861 488 EVLI--DG--WFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPD 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 637 QNHLEELAQKHGLGDkSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTAAFKLKRKDIQD 716
Cdd:PLN02861 564 RQALEDWAANNNKTG-DFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLK 642
|
650
....*....|.
gi 442622933 717 RYQHDINRMYA 727
Cdd:PLN02861 643 YYKDCIDQLYS 653
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
95-728 |
1.84e-106 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 338.92 E-value: 1.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 95 ENIDTLEKVFNYVAKTYTSKRCLGTRQILseedevqqNGRVfkkynlGDYKWKTFTEAERTAANFGRGLRELGQKPRENI 174
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRREIV--------DGKP------GKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 175 VIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPK-FKTLLDKCPLVKTIIYIE--DQ 251
Cdd:PLN02614 108 GIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISElFKTCPNSTEYMKTVVSFGgvSR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 252 LQKTETTGFkeGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMV-----P 326
Cdd:PLN02614 188 EQKEEAETF--GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksanaA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 327 IYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPltliDTSSKIKrgckgDATVLKPTCMTSVPLILDRISKGINDK 406
Cdd:PLN02614 266 LTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRG----DVKLLIE-----DLGELKPTIFCAVPRVLDRVYSGLQKK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 407 VNSGSAFKKSLFKFLYQYKVKWVQRGYK----TPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQ 482
Cdd:PLN02614 337 LSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 483 GYGLTETTSG--ATVMDYRDMtYGRTGGPLTVCDIRLVNWEEGNYRVTNKPyPQGEVLIGGECVSQGYYKLPGKTNEDFF 560
Cdd:PLN02614 417 GYGLTESCAGtfVSLPDELDM-LGTVGPPVPNVDIRLESVPEMEYDALAST-PRGEICIRGKTLFSGYYKREDLTKEVLI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 561 eeDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPNQNHL 640
Cdd:PLN02614 495 --DG--WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQIL 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 641 EELAQKHGL-GDksFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQ 719
Cdd:PLN02614 571 ERWAAENGVsGD--YNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQ 648
|
....*....
gi 442622933 720 HDINRMYAS 728
Cdd:PLN02614 649 SVIDEMYKT 657
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
139-595 |
1.38e-93 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 297.30 E-value: 1.38e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 139 YNLGDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETE 218
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 219 VTTV-ITSHDLLPKFKTLLDKCPLVKTIIYIEdqlqktettgFKEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYT 297
Cdd:pfam00501 94 AKVLiTDDALKLEELLEALGKLEVVKLVLVLD----------RDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 298 SGSTGTPKGVLLSHKNCIATMKGFVDMVP----IYPDDVLIGFLPLAHVFELVAE-SVCLMTGVPIGYSTPLTLIDTssk 372
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGFPALDP--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 373 ikRGCKGDATVLKPTCMTSVPLILDRIskgindkVNSGsAFKKSLFkflyqykvkwvqrgyktplidklvfkkvaklmgG 452
Cdd:pfam00501 241 --AALLELIERYKVTVLYGVPTLLNML-------LEAG-APKRALL---------------------------------S 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 453 KVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATV---MDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTN 529
Cdd:pfam00501 278 SLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTplpLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPG 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622933 530 KPypqGEVLIGGECVSQGYYKLPGKTNEDFFEEdgqRWFKTGDIGEIQADGVLKIIDRKKDLVKLQ 595
Cdd:pfam00501 358 EP---GELCVRGPGVMKGYLNDPELTAEAFDED---GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
142-711 |
1.33e-71 |
|
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: 240.72 E-value: 1.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 142 GDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGcfkqAMPIVTVYATLGDDgvahcitetevtt 221
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQG----IMALGAVDVVRGSD------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 222 vITSHDLLpkfktlldkcplvktiiYIedqlqktettgfkegvkilpFNQVvktgqDSKFEHVPPKGDDIAIIMYTSGST 301
Cdd:cd17640 64 -SSVEELL-----------------YI--------------------LNHS-----ESVALVVENDSDDLATIIYTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 302 GTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLidtsskikrgcKGDA 381
Cdd:cd17640 101 GNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTL-----------KDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 382 TVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFLyqykvkwvqrgyktplidklvfkkvakLMGGKVRIIMSGG 461
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF---------------------------LSGGIFKFGISGG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 462 A--PLSADT-HEQIKtclcLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNwEEGNyrVTNKPYPQGEVL 538
Cdd:cd17640 223 GalPPHVDTfFEAIG----IEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVD-PEGN--VVLPPGEKGIVW 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 539 IGGECVSQGYYKLPGKTNEdFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENI 618
Cdd:cd17640 296 VRGPQVMKGYYKNPEATSK-VLDSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQI 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 619 CVYGDPTKQYTvALVVPNQNHLEELAQKHGLG-DKSFEELCSSPIIEKAILKEIAEHARKCKLQK-YEVPAAITLCKEVW 696
Cdd:cd17640 373 MVVGQDQKRLG-ALIVPNFEELEKWAKESGVKlANDRSQLLASKKVLKLYKNEIKDEISNRPGFKsFEQIAPFALLEEPF 451
|
570
....*....|....*
gi 442622933 697 SPDmGLVTAAFKLKR 711
Cdd:cd17640 452 IEN-GEMTQTMKIKR 465
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
148-719 |
1.33e-60 |
|
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: 210.82 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCitetevttvitshd 227
Cdd:COG0318 26 TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYI-------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 228 llpkfktlLDKCplvktiiyiedqlqktettgfkeGVKILpfnqVVktgqdskfehvppkgddiAIIMYTSGSTGTPKGV 307
Cdd:COG0318 92 --------LEDS-----------------------GARAL----VT------------------ALILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 308 LLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESV-CLMTG---VPIGYSTPLTLIDTsskIKRGckgdatv 383
Cdd:COG0318 119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLaPLLAGatlVLLPRFDPERVLEL---IERE------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 384 lKPTCMTSVPLILDRIskgindkvnsgsafkkslfkflyqykvkwvqrgYKTPLIDKLVFkkvaklmgGKVRIIMSGGAP 463
Cdd:COG0318 189 -RVTVLFGVPTMLARL---------------------------------LRHPEFARYDL--------SSLRLVVSGGAP 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 464 LSADTHEQIKTCLCLELIQGYGLTETTSGATV--MDYRDMTYGRTGGPLTVCDIRLVNwEEGNyrvtnkPYPQ---GEVL 538
Cdd:COG0318 227 LPPELLERFEERFGVRIVEGYGLTETSPVVTVnpEDPGERRPGSVGRPLPGVEVRIVD-EDGR------ELPPgevGEIV 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 539 IGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSLGKVESELKTCGIIENI 618
Cdd:COG0318 300 VRGPNVMKGYWNDPEATAEAF--RDG--WLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAHPGVAEA 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 619 CVYGDPTKQY---TVALVVPNQNHLEELAqkhglgdksfeelcsspiiekailkEIAEHARKcKLQKYEVPAAITLCKEV 695
Cdd:COG0318 375 AVVGVPDEKWgerVVAFVVLRPGAELDAE-------------------------ELRAFLRE-RLARYKVPRRVEFVDEL 428
|
570 580
....*....|....*....|....
gi 442622933 696 wsPdmglVTAAFKLKRKDIQDRYQ 719
Cdd:COG0318 429 --P----RTASGKIDRRALRERYA 446
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-718 |
8.29e-58 |
|
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: 204.62 E-value: 8.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 143 DYKWKTFTEAERTAANFgrgLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTV 222
Cdd:cd05932 6 EFTWGEVADKARRLAAA---LRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 223 itshdllpkFKTLLDKCP---------LVKTIIYIEDQLQKTETtgfkegvkilpFNQVVKTGQDSKfEHVPPKGDDIAI 293
Cdd:cd05932 83 ---------FVGKLDDWKamapgvpegLISISLPPPSAANCQYQ-----------WDDLIAQHPPLE-ERPTRFPEQLAT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 294 IMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVA-ESVCLMTGVPIGYSTPLtliDT-SS 371
Cdd:cd05932 142 LIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAESL---DTfVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 372 KIKRGckgdatvlKPTCMTSVPLILDRISKGINDKVnsgsafkkslfkflyqyKVKWVQRGYKTPLIDKLVFKKVAKLMG 451
Cdd:cd05932 219 DVQRA--------RPTLFFSVPRLWTKFQQGVQDKI-----------------PQQKLNLLLKIPVVNSLVKRKVLKGLG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 452 -GKVRIIMSGGAPLSADTHEQIKTcLCLELIQGYGLTEtTSGATVMDY--RDMTyGRTGGPLTVCDIRLVnweegnyrvt 528
Cdd:cd05932 274 lDQCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTE-NFAYSHLNYpgRDKI-GTVGNAGPGVEVRIS---------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 529 nkpyPQGEVLIGGECVSQGYYKLPGKTNEDfFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESE 608
Cdd:cd05932 341 ----EDGEILVRSPALMMGYYKDPEATAEA-FTADG--FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENK 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 609 LKTCGIIENICVYGDPTKQyTVALVVPNQN-HLEELAQKHGLGDKSFeelcsspiieKAILKEIAEHarkckLQKYEVPA 687
Cdd:cd05932 414 LAEHDRVEMVCVIGSGLPA-PLALVVLSEEaRLRADAFARAELEASL----------RAHLARVNST-----LDSHEQLA 477
|
570 580 590
....*....|....*....|....*....|.
gi 442622933 688 AITLCKEVWSPDMGLVTAAFKLKRKDIQDRY 718
Cdd:cd05932 478 GIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
290-645 |
3.66e-52 |
|
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: 184.03 E-value: 3.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTG---VPIGYSTPLTL 366
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGgtvVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 367 IDTsskIKRgckgdatvLKPTCMTSVPLILDRISKGINDKVNSGSAfkkslfkflyqykvkwvqrgyktplidklvfkkv 446
Cdd:cd04433 81 LEL---IER--------EKVTILLGVPTLLARLLKAPESAGYDLSS---------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 447 aklmggkVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVM--DYRDMTYGRTGGPLTVCDIRLVNwEEGN 524
Cdd:cd04433 116 -------LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGppDDDARKPGSVGRPVPGVEVRIVD-PDGG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 525 YRVTNKPypqGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGK 604
Cdd:cd04433 188 ELPPGEI---GELVVRGPSVMKGYWNNPEATAAVD--EDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSG-GENVYPAE 259
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 442622933 605 VESELKTC-GIIEnICVYG--DPTK-QYTVALVVPNQNH---LEELAQ 645
Cdd:cd04433 260 VEAVLLGHpGVAE-AAVVGvpDPEWgERVVAVVVLRPGAdldAEELRA 306
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
289-646 |
7.65e-50 |
|
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: 181.49 E-value: 7.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFElvaesvCLMTGV-PIGYSTPLTLI 367
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYP------LTFTLLlPLLNGAHVVFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 D--TSSKIKRGCKGDatvLKPTCMTSVPLILDRISKgiNDKVNsgsafKKSLFKFLYQYKVKWVQRGyktplIDKLVFKK 445
Cdd:cd05914 163 DkiPSAKIIALAFAQ---VTPTLGVPVPLVIEKIFK--MDIIP-----KLTLKKFKFKLAKKINNRK-----IRKLAFKK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 446 VAKLMGGKVRIIMSGGAPLSADTHEQIKTcLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRlvnweegny 525
Cdd:cd05914 228 VHEAFGGNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVR--------- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 526 rvTNKPYPQ---GEVLIGGECVSQGYYKLPGKTNEdFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSL 602
Cdd:cd05914 298 --IDSPDPAtgeGEIIVRGPNVMKGYYKNPEATAE-AFDKDG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYP 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 442622933 603 GKVESEL--KTCGIIENICVygdpTKQYTVALVVPNQNHLEELAQK 646
Cdd:cd05914 373 EEIEAKInnMPFVLESLVVV----QEKKLVALAYIDPDFLDVKALK 414
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
148-647 |
2.36e-48 |
|
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: 177.79 E-value: 2.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHD 227
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 228 LLPKFKTLLDKCPLVKTIIYIEDQLQKtettgfkegvkILPFNQVVKTGQDSKFEHVPP----KGDDIAIIMYTSGSTGT 303
Cdd:cd05911 92 GLEKVKEAAKELGPKDKIIVLDDKPDG-----------VLSIEDLLSPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 304 PKGVLLSHKNCIATMK--GFVDMVPIYPDDVLIGFLPLAHvfelvaesvclMTGVPIGYSTPLtlidtsskikRGCkgda 381
Cdd:cd05911 161 PKGVCLSHRNLIANLSqvQTFLYGNDGSNDVILGFLPLYH-----------IYGLFTTLASLL----------NGA---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 382 TVLKPTCMTSVPLiLDRISKgindkvnsgsafkkslfkflyqYKVKW-------VQRGYKTPLIDKlvfkkvAKLmgGKV 454
Cdd:cd05911 216 TVIIMPKFDSELF-LDLIEK----------------------YKITFlylvppiAAALAKSPLLDK------YDL--SSL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 455 RIIMSGGAPLSADTHEQIKTCLCL-ELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTNKPyp 533
Cdd:cd05911 265 RVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEP-- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 534 qGEVLIGGECVSQGYYKLPGKTNEDFFEEDgqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCG 613
Cdd:cd05911 343 -GEICVRGPQVMKGYYNNPEATKETFDEDG---WLHTGDIGYFDEDGYLYIVDRKKELIKYK-GFQVAPAELEAVLLEHP 417
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 442622933 614 IIENICVYG--DPTK-QYTVALVVPNQN------HLEELAQKH 647
Cdd:cd05911 418 GVADAAVIGipDEVSgELPRAYVVRKPGekltekEVKDYVAKK 460
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
146-718 |
1.12e-47 |
|
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: 177.61 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 146 WKTFT--EAERTAANFGRGLRELGQKPRENIVIFAETRAEW---MIAAHGCfkQAMPiVTVYATLGDDGVA----HCITE 216
Cdd:cd17641 9 WQEFTwaDYADRVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAI--GALS-LGIYQDSMAEEVAyllnYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 217 TEVTTVITSHDllpKFKTLLDKCPLVKTIIYIEdqlqKTETTGFKEGvKILPFNQVVKTGQDSKFEHvpP---------- 286
Cdd:cd17641 86 VVIAEDEEQVD---KLLEIADRIPSVRYVIYCD----PRGMRKYDDP-RLISFEDVVALGRALDRRD--Pglyerevaag 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 287 KGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFE-LVAESVCLMTGVPIGY-STPL 364
Cdd:cd17641 156 KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEqMYSVGQALVCGFIVNFpEEPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 365 TLidtsskikrgcKGDATVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFLYQYKVKWVQRGYKTP-------- 436
Cdd:cd17641 236 TM-----------MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRpvslwlrl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 437 ---LIDKLVFKKVAKLMG-GKVRIIMSGGAPLSADTHEQIKTcLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTV 512
Cdd:cd17641 305 aswLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 513 CDIRLVNweegnyrvtnkpypQGEVLIGGECVSQGYYKLPGKTNEDfFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLV 592
Cdd:cd17641 384 TEVRIDE--------------VGEILVRSPGVFVGYYKNPEATAED-FDEDG--WLHTGDAGYFKENGHLVVIDRAKDVG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 593 KLQAGEYVSLGKVESELKTCGIIENICVYGDpTKQYTVALVVPNQNHLEELAQKHGLGDKSFEELCSSPIIEKAILKEI- 671
Cdd:cd17641 447 TTSDGTRFSPQFIENKLKFSPYIAEAVVLGA-GRPYLTAFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVYELIRKEVe 525
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 442622933 672 ---AEHARKCKLQKYevpaaITLCKEVwSPDMGLVTAAFKLKRKDIQDRY 718
Cdd:cd17641 526 kvnASLPEAQRIRRF-----LLLYKEL-DADDGELTRTRKVRRGVIAEKY 569
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
225-718 |
2.21e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 167.29 E-value: 2.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 225 SHDLLPKFKTLLDKCPLVKTIIYIEDqlqkteTTGFKEGVKILPFNQVVKtGQDSKFEHVPPKGDDIAIIMYTSGSTGTP 304
Cdd:PRK06187 110 DSEFVPLLAAILPQLPTVRTVIVEGD------GPAAPLAPEVGEYEELLA-AASDTFDFPDIDENDAAAMLYTSGTTGHP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 305 KGVLLSHKN-------CIATMKgfvdmvpIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGY------STPLTLIDTss 371
Cdd:PRK06187 183 KGVVLSHRNlflhslaVCAWLK-------LSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIprrfdpENLLDLIET-- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 372 kikrgckgdatvLKPTCMTSVPLILDRISKgindkvnsgsafkkslfkflyqykvkwvqrgYKTPlidklVFKKVAKLmg 451
Cdd:PRK06187 254 ------------ERVTFFFAVPTIWQMLLK-------------------------------APRA-----YFVDFSSL-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 452 gkvRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGR------TGGPLTVCDIRLVNwEEGNy 525
Cdd:PRK06187 284 ---RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVD-DDGD- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 526 RVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKV 605
Cdd:PRK06187 359 ELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETI--DGG--WLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPREL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 606 ESELKTCGIIENICVYGDPTKQY---TVALVVPnqnhleelaqKHGlgdksfeelcsspiiEKAILKEIAEHARKcKLQK 682
Cdd:PRK06187 434 EDALYGHPAVAEVAVIGVPDEKWgerPVAVVVL----------KPG---------------ATLDAKELRAFLRG-RLAK 487
|
490 500 510
....*....|....*....|....*....|....*.
gi 442622933 683 YEVPAAITLCKEVwsPDmglvTAAFKLKRKDIQDRY 718
Cdd:PRK06187 488 FKLPKRIAFVDEL--PR----TSVGKILKRVLREQY 517
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
263-711 |
4.93e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 169.51 E-value: 4.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 263 GVKILPFNQVVKTgQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVD--MVPIYPDDVLIGFLPLA 340
Cdd:PTZ00342 279 GISIILFDDMTKN-KTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKhsIFKKYNPKTHLSYLPIS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 341 HVFELVAESVCLMTGVPIgystpltliDTSSK-IKRGCKgDATVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFK 419
Cdd:PTZ00342 358 HIYERVIAYLSFMLGGTI---------NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 420 FLYQYKvKWVQRGYKTPLIDKL--VFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMD 497
Cdd:PTZ00342 428 KILSLR-KSNNNGGFSKFLEGIthISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQH 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 498 YRDMTYGRTGGPLTV-CDIRLVNWEegNYRVTNKPyPQGEVLIGGECVSQGYYkLPGKTNEDFFEEDGqrWFKTGDIGEI 576
Cdd:PTZ00342 507 ADDNNTESIGGPISPnTKYKVRTWE--TYKATDTL-PKGELLIKSDSIFSGYF-LEKEQTKNAFTEDG--YFKTGDIVQI 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 577 QADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPNQN----HLEE--LAQKHGLG 650
Cdd:PTZ00342 581 NKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYllfkCLKDdnMLESTGIN 660
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622933 651 DKSFEELCSSPIIEKAI----LKE-IAEHARKCKLQKYEVPAAITLCKEVWspDM-GLVTAAFKLKR 711
Cdd:PTZ00342 661 EKNYLEKLTDETINNNIyvdyVKGkMLEVYKKTNLNRYNIINDIYLTSKVW--DTnNYLTPTFKVKR 725
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
145-690 |
3.63e-43 |
|
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: 162.73 E-value: 3.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 145 KWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHcitetevttvit 224
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEH------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 225 shdllpkfktLLDKCplvktiiyiedqlqktettGFKEGVKILPFNQVVKTGQDSKFEhVPPKGDDIAIIMYTSGSTGTP 304
Cdd:cd05936 91 ----------ILNDS-------------------GAKALIVAVSFTDLLAAGAPLGER-VALTPEDVAVLQYTSGTTGVP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 305 KGVLLSHKN-------CIATMKGFVDmvpiyPDDVLIGFLPLAHVFELvaeSVCLMTGVPIGYS-------TPLTLIDTs 370
Cdd:cd05936 141 KGAMLTHRNlvanalqIKAWLEDLLE-----GDDVVLAALPLFHVFGL---TVALLLPLALGATivliprfRPIGVLKE- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 371 skIKRGckgdatvlKPTCMTSVPLILDRIskgindkVNSgSAFKKSLFKflyqykvkwvqrgyktplidklvfkkvaklm 450
Cdd:cd05936 212 --IRKH--------RVTIFPGVPTMYIAL-------LNA-PEFKKRDFS------------------------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 451 ggKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTY-GRTGGPLTVCDIRLVNwEEGNyrvTN 529
Cdd:cd05936 243 --SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKpGSIGIPLPGTEVKIVD-DDGE---EL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 530 KPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESEL 609
Cdd:cd05936 317 PPGEVGELWVRGPQVMKGYWNRPEETAEAF--VDG--WLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVL 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 610 KTCGIIENICVYGDPTKQY---TVALVVPnqnhleelaqKHGlgdksfeelcsspiiEKAILKEIAEHARKcKLQKYEVP 686
Cdd:cd05936 392 YEHPAVAEAAVVGVPDPYSgeaVKAFVVL----------KEG---------------ASLTEEEIIAFCRE-QLAGYKVP 445
|
....
gi 442622933 687 AAIT 690
Cdd:cd05936 446 RQVE 449
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
285-705 |
2.04e-42 |
|
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: 163.01 E-value: 2.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 285 PPKGDDIAIIMYTSGSTGTPKGVLLSHKNcIATM----KGFVDMVPiyPDDVLIGFLPLAHVFELVAESVCLMTGvPIGY 360
Cdd:cd17632 219 EPDDDPLALLIYTSGSTGTPKGAMYTERL-VATFwlkvSSIQDIRP--PASITLNFMPMSHIAGRISLYGTLARG-GTAY 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 361 STPL----TLIDtsskikrgckgDATVLKPTCMTSVPLILDRIskgindkvnsgsaFKKslfkflYQYKV-KWVQRGykt 435
Cdd:cd17632 295 FAAAsdmsTLFD-----------DLALVRPTELFLVPRVCDML-------------FQR------YQAELdRRSVAG--- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 436 plIDKLVFKKVAK------LMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETtsGATVMDyrdmtyGRTGGP 509
Cdd:cd17632 342 --ADAETLAERVKaelrerVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEA--GAVILD------GVIVRP 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 510 lTVCDIRLVNWEEGNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEdFFEEDGqrWFKTGDI-GEIQADGvLKIIDRK 588
Cdd:cd17632 412 -PVLDYKLVDVPELGYFRTDRPHPRGELLVKTDTLFPGYYKRPEVTAE-VFDEDG--FYRTGDVmAELGPDR-LVYVDRR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 589 KDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPNQNHLEelaqkhGLGDksfEELcsspiieKAIL 668
Cdd:cd17632 487 NNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALA------GEDT---ARL-------RAAL 550
|
410 420 430
....*....|....*....|....*....|....*...
gi 442622933 669 KE-IAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTA 705
Cdd:cd17632 551 AEsLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLSG 588
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
148-592 |
1.73e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 153.14 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQ---AMPIVTVYAT------LGDDGVAhcitete 218
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAgavVVPLNTRYTAdeaayiLARGDAK------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 219 vtTVITSHDLLPKFKTLLDKCPLVKTIIYIEDqlqkteTTGFKEGVKILPFNQVVKTGQDSKFEhVPPKGDDIAIIMYTS 298
Cdd:PRK07656 105 --ALFVLGLFLGVDYSATTRLPALEHVVICET------EEDDPHTEKMKTFTDFLAAGDPAERA-PEVDPDDVADILFTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 299 GSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFEL-VAESVCLMTGVPIgysTPLTLIDTSSKIKRGC 377
Cdd:PRK07656 176 GTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYkAGVNAPLMRGATI---LPLPVFDPDEVFRLIE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 378 KGDATVLK--PTcmtsvplildriskgindkvnsgsafkksLFKFLYQYkvkwvqrgyktpliDKLVFKKVAKLmggkvR 455
Cdd:PRK07656 253 TERITVLPgpPT-----------------------------MYNSLLQH--------------PDRSAEDLSSL-----R 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 456 IIMSGGAPLSADTHEQIKTCL-CLELIQGYGLTEtTSGATVM----DYRDMTYGRTGGPLTVCDIRLVNwEEGNYRVTNK 530
Cdd:PRK07656 285 LAVTGAASMPVALLERFESELgVDIVLTGYGLSE-ASGVTTFnrldDDRKTVAGTIGTAIAGVENKIVN-ELGEEVPVGE 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622933 531 PypqGEVLIGGECVSQGYYKLPGKTNEDfFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLV 592
Cdd:PRK07656 363 V---GELLVRGPNVMKGYYDDPEATAAA-IDADG--WLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
290-704 |
1.19e-38 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 148.98 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVC-LMTGVPIGYstpLTLID 368
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCpLFAGASVEF---LPKFD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 369 TSSKIKRGCKGDATVLkptcmTSVPLILDRISKGINDKVNSGSAFKKSLFKflyqykvkwvqrgyktplidklvfkkvak 448
Cdd:cd05941 167 PKEVAISRLMPSITVF-----MGVPTIYTRLLQYYEAHFTDPQFARAAAAE----------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 449 lmggKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTET---TSGATVMDYRDmtyGRTGGPLTVCDIRLVNWEEGNY 525
Cdd:cd05941 213 ----RLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIgmaLSNPLDGERRP---GTVGMPLPGVQARIVDEETGEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 526 RVTNKpypQGEVLIGGECVSQGYYKLPGKTNEDFfEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKV 605
Cdd:cd05941 286 LPRGE---VGEIQVRGPSVFKEYWNKPEATKEEF-TDDG--WFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEI 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 606 ESELKTCGIIENICVYGDPTKQY---TVALVVPNqnhleelAQKHGLgdkSFEELCsspiiekailkeiaEHARKcKLQK 682
Cdd:cd05941 360 ERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLR-------AGAAAL---SLEELK--------------EWAKQ-RLAP 414
|
410 420
....*....|....*....|..
gi 442622933 683 YEVPAAITLCKEVWSPDMGLVT 704
Cdd:cd05941 415 YKRPRRLILVDELPRNAMGKVN 436
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
142-726 |
2.73e-38 |
|
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: 150.97 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 142 GDYKWKTFT-----EAERTAAnfgRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITE 216
Cdd:cd05933 2 RGDKWHTLTykeyyEACRQAA---KAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 217 TEVTTVI-TSHDLLPKFKTLLDKCPLVKTIIYIEDQLQKTET-----TGFKEGVKILPFNQVvktgqDSKFEHVPPkgDD 290
Cdd:cd05933 79 SEANILVvENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPnlyswDEFMELGRSIPDEQL-----DAIISSQKP--NQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 291 IAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDV----LIGFLPLAHVfelVAESVCLMTGVPIGYSTPL-- 364
Cdd:cd05933 152 CCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHI---AAQILDIWLPIKVGGQVYFaq 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 365 ------TLIDTSSKIkrgckgdatvlKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKF-----LYQYKvKWVQRGY 433
Cdd:cd05933 229 pdalkgTLVKTLREV-----------RPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWakgvgLETNL-KLMGGES 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 434 KTP----LIDKLVFKKVAKLMG-GKVRIIMSGGAPLSADTHEQIKTcLCLELIQGYGLTETTSGATV---MDYRDMTYGR 505
Cdd:cd05933 297 PSPlfyrLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHTIsnpQAYRLLSCGK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 506 TggpLTVCDIRLVNWE-EGnyrvtnkpypQGEVLIGGECVSQGYYKLPGKTNEDfFEEDGqrWFKTGDIGEIQADGVLKI 584
Cdd:cd05933 376 A---LPGCKTKIHNPDaDG----------IGEICFWGRHVFMGYLNMEDKTEEA-IDEDG--WLHSGDLGKLDEDGFLYI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 585 IDRKKDLVKLQAGEYVSLGKVESELKT-CGIIENICVYGDPTKQYTVALVVPNQNHLE-------------ELAQKHGLG 650
Cdd:cd05933 440 TGRIKELIITAGGENVPPVPIEDAVKKeLPIISNAMLIGDKRKFLSMLLTLKCEVNPEtgepldelteeaiEFCRKLGSQ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 651 DKSFEELCSSP------IIEKAIlKEIAEHA--RKCKLQKYEVpaaitLCKEvWSPDMGLVTAAFKLKRKDIQDRYQHDI 722
Cdd:cd05933 520 ATRVSEIAGGKdpkvyeAIEEGI-KRVNKKAisNAQKIQKWVI-----LEKD-FSVPGGELGPTMKLKRPVVAKKYKDEI 592
|
....
gi 442622933 723 NRMY 726
Cdd:cd05933 593 DKLY 596
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
231-658 |
3.42e-36 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 146.99 E-value: 3.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 231 KFKTLLDKCPLVKTIIYIED---QLQKTETTGFKEGVKILPFNQVvktgqdSKFEHVPPKGDDIAIIMYTSGSTGTPKGV 307
Cdd:PRK08633 727 KNKGFDLELPENVKVIYLEDlkaKISKVDKLTALLAARLLPARLL------KRLYGPTFKPDDTATIIFSSGSEGEPKGV 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 308 LLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFEL-VAESVCLMTGVPIGYSTPLTLIDTSSKIKRgcKGDATVLkp 386
Cdd:PRK08633 801 MLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLtVTLWLPLLEGIKVVYHPDPTDALGIAKLVA--KHRATIL-- 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 387 tCMTSVplildriskgindkvnsgsafkkslfkFLYQYkvkwvqrgyktplidkLVFKKVAKLMGGKVRIIMSGGAPLSA 466
Cdd:PRK08633 877 -LGTPT---------------------------FLRLY----------------LRNKKLHPLMFASLRLVVAGAEKLKP 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 467 DTHEQIKTCLCLELIQGYGLTETTSGATVM--DYRDMTY--------GRTGGPLTVCDIRLVNWEegnyrvTNKPYPQGE 536
Cdd:PRK08633 913 EVADAFEEKFGIRILEGYGATETSPVASVNlpDVLAADFkrqtgskeGSVGMPLPGVAVRIVDPE------TFEELPPGE 986
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 537 ---VLIGGECVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSLGKVESELKTcg 613
Cdd:PRK08633 987 dglILIGGPQVMKGYLGDPEKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKI-GGEMVPLGAVEEELAK-- 1063
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 442622933 614 iienicVYGDPTKQYTVAlVVPNQNHLEELAQKHGLGDKSFEELC 658
Cdd:PRK08633 1064 ------ALGGEEVVFAVT-AVPDEKKGEKLVVLHTCGAEDVEELK 1101
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
284-593 |
6.52e-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: 142.37 E-value: 6.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVP--IYPDDVLIGFLPLAHVFELvaeSVCLMTGVPIG-- 359
Cdd:cd05904 153 VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGL---SSFALGLLRLGat 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 360 ------YSTPLTLidtsSKIKRgckgdatvLKPTCMTSVPLILDRISKGindkvnsgsafkkslfkflyqykvkwvqrgy 433
Cdd:cd05904 230 vvvmprFDLEELL----AAIER--------YKVTHLPVVPPIVLALVKS------------------------------- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 434 ktPLIDKLVFKKVaklmggkvRIIMSGGAPLSADTHEQIKTCLCL-ELIQGYGLTETTSGATVMDYRDMT---YGRTGGP 509
Cdd:cd05904 267 --PIVDKYDLSSL--------RQIMSGAAPLGKELIEAFRAKFPNvDLGQGYGMTESTGVVAMCFAPEKDrakYGSVGRL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 510 LTVCDIRLVNWEegnyrvTNKPYP---QGEVLIGGECVSQGYYKLPGKTNEDFfeeDGQRWFKTGDIGEIQADGVLKIID 586
Cdd:cd05904 337 VPNVEAKIVDPE------TGESLPpnqTGELWIRGPSIMKGYLNNPEATAATI---DKEGWLHTGDLCYIDEDGYLFIVD 407
|
....*..
gi 442622933 587 RKKDLVK 593
Cdd:cd05904 408 RLKELIK 414
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
204-649 |
1.47e-35 |
|
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: 140.93 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 204 TLGDDGVAHCITETEVTTVITSHDLLPKFKtlLDKCPLVKT---IIYIEDQLqktETTGFKEGVKILPFNQVVKTGQDSK 280
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQFIEKLK--LHHLFDVEYdarIVYLEDLR---AKISKADKCKAFLAGKFPPKWLLRI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 281 FEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELvaeSVCLMtgvpigy 360
Cdd:cd05909 139 FGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGL---TGCLW------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 361 sTPLTlidtsskikrgcKGDATVLKPTcmtsvPLILDRISKGINDKvnsGSAFKKSLFKFLYQYKVKWVQRGYKTplidk 440
Cdd:cd05909 209 -LPLL------------SGIKVVFHPN-----PLDYKKIPELIYDK---KATILLGTPTFLRGYARAAHPEDFSS----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 441 lvfkkvaklmggkVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATV----MDYRDMTYGRtggPLTVCDIR 516
Cdd:cd05909 263 -------------LRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVntpqSPNKEGTVGR---PLPGMEVK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 517 LVNWEegnyrvTNKPYPQGE---VLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVK 593
Cdd:cd05909 327 IVSVE------THEEVPIGEgglLLVRGPNVMLGYLNEPELTSFAF--GDG--WYDTGDIGKIDGEGFLTITGRLSRFAK 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622933 594 LqAGEYVSLGKVESEL-KTCGIIENICVYGDPTKQYTVALVV------PNQNHLEELAQKHGL 649
Cdd:cd05909 397 I-AGEMVSLEAIEDILsEILPEDNEVAVVSVPDGRKGEKIVLlttttdTDPSSLNDILKNAGI 458
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
286-712 |
3.00e-35 |
|
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: 138.63 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 286 PKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELvaeSVcLMTGVPigYSTPLT 365
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGL---SI-LMRSVI--YGMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 366 LIDtsskikrgcKGDAtvlkptcmtsvplilDRISKGIND-KVNSGSAFKKSLFKFLYQYkvkwvQRGYKTPLidklvfk 444
Cdd:cd05912 148 LVD---------KFDA---------------EQVLHLINSgKVTIISVVPTMLQRLLEIL-----GEGYPNNL------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 445 kvaklmggkvRIIMSGGAPLSADTHEQIKTcLCLELIQGYGLTETTSGATVMDYRDM--TYGRTGGPLTVCDIRLVNWEe 522
Cdd:cd05912 192 ----------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCSQIVTLSPEDAlnKIGSAGKPLFPVELKIEDDG- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 523 gnyrvtNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSL 602
Cdd:cd05912 260 ------QPPYEVGEILLKGPNVTKGYLNRPDATEESF--ENG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 603 GKVESELKTCGIIENICVYGDPTK---QYTVALVVpnqnhleelaqkhglgdksfeelCSSPIIEkailKEIAEHARKcK 679
Cdd:cd05912 329 AEIEEVLLSHPAIKEAGVVGIPDDkwgQVPVAFVV-----------------------SERPISE----EELIAYCSE-K 380
|
410 420 430
....*....|....*....|....*....|...
gi 442622933 680 LQKYEVPAAITLCKEVwsPDmglvTAAFKLKRK 712
Cdd:cd05912 381 LAKYKVPKKIYFVDEL--PR----TASGKLLRH 407
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
285-712 |
3.49e-35 |
|
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: 140.14 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 285 PPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAesVCLMTgvpigystpl 364
Cdd:cd05926 145 VPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVA--SLLST---------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 365 tlidtsskikRGCKGdATVLKPTCmtsvplildriskgindkvnSGSAFkkslFKFLYQYKVKWVQrgyKTPLIDKLVFK 444
Cdd:cd05926 213 ----------LAAGG-SVVLPPRF--------------------SASTF----WPDVRDYNATWYT---AVPTIHQILLN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 445 KVAKLMGG---KVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGAT-----VMDYRDMTYGRTGGPltvcDIR 516
Cdd:cd05926 255 RPEPNPESpppKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTsnplpPGPRKPGSVGKPVGV----EVR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 517 LVNwEEGNyrvTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFFEEDgqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQA 596
Cdd:cd05926 331 ILD-EDGE---ILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG---WFRTGDLGYLDADGYLFLTGRIKELIN-RG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 597 GEYVSLGKVESELKTCGIIENICVYGDPTKQY---TVALVVPNQNHleelaqkhglgdksfeelcsspiieKAILKEIAE 673
Cdd:cd05926 403 GEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVLREGA-------------------------SVTEEELRA 457
|
410 420 430
....*....|....*....|....*....|....*....
gi 442622933 674 HARKcKLQKYEVPaaitlcKEVWSPDMGLVTAAFKLKRK 712
Cdd:cd05926 458 FCRK-HLAAFKVP------KKVYFVDELPKTATGKIQRR 489
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
284-620 |
5.00e-34 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 135.09 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAH---VFELVAesvCLMTGvpigy 360
Cdd:TIGR01733 115 APSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFdasVEEIFG---ALLAG----- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 361 STPLTLIDTSSKIKRGCKGDAT-VLKPTCMTSVPLILDRISKGINDKVNSgsafkkslfkflyqykvkwvqrgyktplid 439
Cdd:TIGR01733 187 ATLVVPPEDEERDDAALLAALIaEHPVTVLNLTPSLLALLAAALPPALAS------------------------------ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 440 klvfkkvaklmggkVRIIMSGGAPLSADTHEQIK-TCLCLELIQGYGLTETTSGATVMDY--------RDMTYGRtggPL 510
Cdd:TIGR01733 237 --------------LRLVILGGEALTPALVDRWRaRGPGARLINLYGPTETTVWSTATLVdpddapreSPVPIGR---PL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 511 TVCDIRLVNwEEGNyrvtnkPYP---QGEVLIGGECVSQGYYKLPGKTNEDFFE-----EDGQRWFKTGDIGEIQADGVL 582
Cdd:TIGR01733 300 ANTRLYVLD-DDLR------PVPvgvVGELYIGGPGVARGYLNRPELTAERFVPdpfagGDGARLYRTGDLVRYLPDGNL 372
|
330 340 350
....*....|....*....|....*....|....*...
gi 442622933 583 KIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICV 620
Cdd:TIGR01733 373 EFLGRIDDQVKIR-GYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
266-717 |
7.95e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 133.97 E-value: 7.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 266 ILPFNQVVKT---GQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDD--VLIGFLPLA 340
Cdd:PRK05605 193 TVPWETLVDAaigGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGpeRVLAALPMF 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 341 HVFELvaeSVCLMTGVPIGystpltlidtsSKIkrgckgdatVLKPTcmTSVPLILDriskgindkvnsgsAFKKSLFKF 420
Cdd:PRK05605 273 HAYGL---TLCLTLAVSIG-----------GEL---------VLLPA--PDIDLILD--------------AMKKHPPTW 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 421 LYQYKvkwvqrgyktPLIDKLVfkKVAK-----LMGgkVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETT---SG 492
Cdd:PRK05605 314 LPGVP----------PLYEKIA--EAAEergvdLSG--VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 493 ATVMDYRDMTYgrTGGPLTVCDIRLVNWEegNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTnEDFFEEDgqrWFKTGD 572
Cdd:PRK05605 380 NPMSDDRRPGY--VGVPFPDTEVRIVDPE--DPDETMPDGEEGELLVRGPQVFKGYWNRPEET-AKSFLDG---WFRTGD 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 573 IGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALVVpnqnhLEELAqkhgl 649
Cdd:PRK05605 452 VVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREdgsEEVVAAVV-----LEPGA----- 520
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622933 650 gdksfeelcsspIIEKAILKeiaEHARKcKLQKYEVPAAITLCKEVWSPDMGlvtaafKLKRKDIQDR 717
Cdd:PRK05605 521 ------------ALDPEGLR---AYCRE-HLTRYKVPRRFYHVDELPRDQLG------KVRRREVREE 566
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
276-635 |
2.39e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 128.84 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 276 GQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFEL-VAESVCLMT 354
Cdd:PRK07514 143 AAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLfVATNVALLA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 355 GVPIGYstpLTLIDTSSKIKRgcKGDATVlkptcMTSVPLILDRIskgindkvnsgsafkkslfkflyqykvkwvqrgyk 434
Cdd:PRK07514 223 GASMIF---LPKFDPDAVLAL--MPRATV-----MMGVPTFYTRL----------------------------------- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 435 tpLIDKLVFKKVAKLMggkvRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTET---TS--------GATVmdyrdmty 503
Cdd:PRK07514 258 --LQEPRLTREAAAHM----RLFISGSAPLLAETHREFQERTGHAILERYGMTETnmnTSnpydgerrAGTV-------- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 504 grtGGPLTVCDIRLVNWEEGnyrvtnKPYPQGEvlIG-----GECVSQGYYKLPGKTNEDFfEEDGqrWFKTGDIGEIQA 578
Cdd:PRK07514 324 ---GFPLPGVSLRVTDPETG------AELPPGE--IGmievkGPNVFKGYWRMPEKTAEEF-RADG--FFITGDLGKIDE 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622933 579 DGVLKIIDRKKDLVkLQAGEYVSLGKVESELKTC-GIIENiCVYGDPTKQY---TVALVVP 635
Cdd:PRK07514 390 RGYVHIVGRGKDLI-ISGGYNVYPKEVEGEIDELpGVVES-AVIGVPHPDFgegVTAVVVP 448
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
289-624 |
1.49e-30 |
|
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: 125.28 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAEsvcLMTGVPIGystpltlid 368
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGS---LNTAVYVG--------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 369 tsskikrgckgdATVLkptcmtsvplildriSKGINDKVNSGSAFKKslfkflyqYKVK-WVqrGYKTPLIDKLVFKKVA 447
Cdd:cd05935 152 ------------GTYV---------------LMARWDRETALELIEK--------YKVTfWT--NIPTMLVDLLATPEFK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 448 KLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRV 527
Cdd:cd05935 195 TRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 528 TNKpypQGEVLIGGECVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSLGKVES 607
Cdd:cd05935 275 PNE---VGEIVVRGPQIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVEA 350
|
330
....*....|....*..
gi 442622933 608 ELKTCGIIENICVYGDP 624
Cdd:cd05935 351 KLYKHPAI*EVCVISVP 367
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
289-637 |
1.55e-30 |
|
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: 125.03 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIA-TMKGFVDMvPIYPDDVLIGFLPLAHVFELvaesvclmtGVPIGystPLTLI 367
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWnAVNALAAL-DLGPDDVLLVVAPLFHIGGL---------GVFTL---PTLLR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 DTSSKIKRGCKGDAtvlkptcmtsvplILDRISKGindKVNSGSAFKkSLFKFLYQykvkwvqrgykTPLIDKLVFKKVa 447
Cdd:cd17631 165 GGTVVILRKFDPET-------------VLDLIERH---RVTSFFLVP-TMIQALLQ-----------HPRFATTDLSSL- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 448 klmggkvRIIMSGGAPLSADTHEQIKTcLCLELIQGYGLTETTSGATVMDYRDM--TYGRTGGPLTVCDIRLVNwEEGNy 525
Cdd:cd17631 216 -------RAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGR- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 526 rvTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKV 605
Cdd:cd17631 286 --EVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF--RDG--WFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEV 358
|
330 340 350
....*....|....*....|....*....|....*
gi 442622933 606 ESELKTCGIIENICVYGDPTKQY---TVALVVPNQ 637
Cdd:cd17631 359 EDVLYEHPAVAEVAVIGVPDEKWgeaVVAVVVPRP 393
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
288-691 |
1.32e-29 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 122.56 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGvpigysTPLTLI 367
Cdd:TIGR01923 110 MDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEG------ATLRIV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 DtsskikrgckGDATVLkpTCMTsvplildriskgiNDKVNSGSAFKKSLFKFLYQykvkwvqRGYKTPLidklvfkkva 447
Cdd:TIGR01923 184 D----------KFNQLL--EMIA-------------NERVTHISLVPTQLNRLLDE-------GGHNENL---------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 448 klmggkvRIIMSGGAPLSAdthEQIKTCLC--LELIQGYGLTETTSGATVMDyRDMTYGRT--GGPLTVCDIRLvnweeg 523
Cdd:TIGR01923 222 -------RKILLGGSAIPA---PLIEEAQQygLPIYLSYGMTETCSQVTTAT-PEMLHARPdvGRPLAGREIKI------ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 524 nyRVTNKPyPQGEVLIGGECVSQGYYKlPGKTNEDFFEedgQRWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLG 603
Cdd:TIGR01923 285 --KVDNKE-GHGEIMVKGANLMKGYLY-QGELTPAFEQ---QGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 604 KVESELKTCGIIENICVYGDPTKQY---TVALVVPNQnhleelaqkhglgdksfeELCSSPIIekAILKEiaeharkcKL 680
Cdd:TIGR01923 357 EIETVLYQHPGIQEAVVVPKPDAEWgqvPVAYIVSES------------------DISQAKLI--AYLTE--------KL 408
|
410
....*....|.
gi 442622933 681 QKYEVPAAITL 691
Cdd:TIGR01923 409 AKYKVPIAFEK 419
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
265-592 |
1.90e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 123.72 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 265 KILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDD---VLIGFLPLAH 341
Cdd:PRK05677 183 QAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYH 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 342 VFELVAESVCLMtgvpigystpltLIdtsskikrgckGDATVLKPTcmtsvPLILDriskgindkvnsgsAFKKSLFKFL 421
Cdd:PRK05677 263 IYAFTFHCMAMM------------LI-----------GNHNILISN-----PRDLP--------------AMVKELGKWK 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 422 YQYKVkwvqrGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDM 501
Cdd:PRK05677 301 FSGFV-----GLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAI 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 502 TYGRTGGPLTVCDIRLVNwEEGNYRVTNKPypqGEVLIGGECVSQGYYKLPGKTNEdFFEEDGqrWFKTGDIGEIQADGV 581
Cdd:PRK05677 376 QVGTIGIPVPSTLCKVID-DDGNELPLGEV---GELCVKGPQVMKGYWQRPEATDE-ILDSDG--WLKTGDIALIQEDGY 448
|
330
....*....|.
gi 442622933 582 LKIIDRKKDLV 592
Cdd:PRK05677 449 MRIVDRKKDMI 459
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
288-637 |
1.94e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 121.87 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLA---HVFELVAesvCLMTG---VPIGYS 361
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSfdvSVWEIFG---ALLAGatlVVLPEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 362 T---PLTLIDTsskIKRGckgdatvlKPTCMTSVPlildriskgindkvnsgsafkkSLFKFLYQYkvkwvqrgyktpli 438
Cdd:cd05930 169 VrkdPEALADL---LAEE--------GITVLHLTP----------------------SLLRLLLQE-------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 439 dklvfkkVAKLMGGKVRIIMSGGAPLSADTHEQI-KTCLCLELIQGYGLTETTSGATVM--DYRDMTYGRT--GGPLTVC 513
Cdd:cd05930 202 -------LELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 514 DIRLVNwEEGNyrvtnkPYPQ---GEVLIGGECVSQGYYKLPGKTNEDFFE---EDGQRWFKTGDIGEIQADGVLKIIDR 587
Cdd:cd05930 275 RVYVLD-ENLR------PVPPgvpGELYIGGAGLARGYLNRPELTAERFVPnpfGPGERMYRTGDLVRWLPDGNLEFLGR 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 442622933 588 KKDLVKLqAGEYVSLGKVESELKTC-GIIENICV-YGDPTK-QYTVALVVPNQ 637
Cdd:cd05930 348 IDDQVKI-RGYRIELGEIEAALLAHpGVREAAVVaREDGDGeKRLVAYVVPDE 399
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
288-636 |
2.64e-29 |
|
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: 121.59 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELvaeSV-----CLMTGvpigyst 362
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFS--FDL---SVmdlypALASG------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 363 pltlidtsskikrgckgdATVlkptcmtsVPLILDRIskgindkvnsgsAFKKSLFKFLYQYKVK-WVQrgykTP-LIDK 440
Cdd:cd05945 164 ------------------ATL--------VPVPRDAT------------ADPKQLFRFLAEHGITvWVS----TPsFAAM 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 441 -LVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCL-ELIQGYGLTETTSGATVMDYRD---MTYGR--TGGPLTVC 513
Cdd:cd05945 202 cLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDaRIYNTYGPTEATVAVTYIEVTPevlDGYDRlpIGYAKPGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 514 DIRLVNwEEGnyrVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVK 593
Cdd:cd05945 282 KLVILD-EDG---RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVK 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 442622933 594 LQaGEYVSLGKVESELKTCGIIENICV---YGDPTKQYTVALVVPN 636
Cdd:cd05945 358 LN-GYRIELEEIEAALRQVPGVKEAVVvpkYKGEKVTELIAFVVPK 402
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
148-624 |
1.42e-27 |
|
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: 117.63 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHD 227
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 228 LLPKFKTLLDKCPLVKTIIY---IEDQLQKTETTGFKEGVKILPFNQvvktgqdSKFehVPP---KGDDIAIIMYTSGST 301
Cdd:cd17642 126 GLQKVLNVQKKLKIIKTIIIldsKEDYKGYQCLYTFITQNLPPGFNE-------YDF--KPPsfdRDEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 302 GTPKGVLLSHKNCIATMKGFVDmvPIY-----PDDVLIGFLPLAHVFElvaesvCLMTgvpIGYStpltlidtsskikrg 376
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSHARD--PIFgnqiiPDTAILTVIPFHHGFG------MFTT---LGYL--------------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 377 CKGDATVLKPTCMTSVPLildrisKGIND-KVNSgSAFKKSLFKFLYqykvkwvqrgyKTPLIDKLvfkKVAKLMggkvr 455
Cdd:cd17642 251 ICGFRVVLMYKFEEELFL------RSLQDyKVQS-ALLVPTLFAFFA-----------KSTLVDKY---DLSNLH----- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 456 IIMSGGAPLSADTHEQIKTCLCLELI-QGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTNKpypQ 534
Cdd:cd17642 305 EIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNE---R 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 535 GEVLIGGECVSQGYYKLPGKTNEdFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGI 614
Cdd:cd17642 382 GELCVKGPMIMKGYVNNPEATKA-LIDKDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYK-GYQVPPAELESILLQHPK 457
|
490
....*....|
gi 442622933 615 IENICVYGDP 624
Cdd:cd17642 458 IFDAGVAGIP 467
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
290-645 |
4.55e-27 |
|
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: 112.42 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHV---FELVAesvCLMTGvpigysTPLTL 366
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVgglAILVR---SLLAG------AELVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 367 IDTsskiKRGCKGDATVLKPTCMTSVPLILDRIskgindkvnsgsafkkslfkflyqykvkwvqrgyktpLIDKLVFKKV 446
Cdd:cd17630 72 LER----NQALAEDLAPPGVTHVSLVPTQLQRL-------------------------------------LDSGQGPAAL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 447 AKLmggkvRIIMSGGAPLSADTHEQIkTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNweegnyr 526
Cdd:cd17630 111 KSL-----RAVLLGGAPIPPELLERA-ADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 527 vtnkpypQGEVLIGGECVSQGYYKlpGKTNEDFFEEDgqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVE 606
Cdd:cd17630 178 -------DGEIWVGGASLAMGYLR--GQLVPEFNEDG---WFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE 244
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 442622933 607 SELKTCGIIENICVYGDPTKQY---TVALVVPNQNHL-EELAQ 645
Cdd:cd17630 245 AALAAHPAVRDAFVVGVPDEELgqrPVAVIVGRGPADpAELRA 287
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
267-592 |
5.73e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 116.07 E-value: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 267 LPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATM-KGFVDMVPIYPD---------DVLIGF 336
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMlQVRACLSQLGPDgqplmkegqEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 337 LPLAHVFELVAESVCLMTgvpigystpltlidtsskikrgcKGDATVLkptcmtsvplildriskgINDKVNSGsAFKKS 416
Cdd:PRK12492 265 LPLYHIYAFTANCMCMMV-----------------------SGNHNVL------------------ITNPRDIP-GFIKE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 417 LFKFLYQYKVkwvqrGYKT---PLIDKLVFKKvakLMGGKVRIIMSGGAPL---SADTHEQIKTClclELIQGYGLTETT 490
Cdd:PRK12492 303 LGKWRFSALL-----GLNTlfvALMDHPGFKD---LDFSALKLTNSGGTALvkaTAERWEQLTGC---TIVEGYGLTETS 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 491 SGATVMDYRDMT-YGRTGGPLTVCDIRLVNwEEGNYRVTNKpypQGEVLIGGECVSQGYYKLPGKTNEDFfeeDGQRWFK 569
Cdd:PRK12492 372 PVASTNPYGELArLGTVGIPVPGTALKVID-DDGNELPLGE---RGELCIKGPQVMKGYWQQPEATAEAL---DAEGWFK 444
|
330 340
....*....|....*....|...
gi 442622933 570 TGDIGEIQADGVLKIIDRKKDLV 592
Cdd:PRK12492 445 TGDIAVIDPDGFVRIVDRKKDLI 467
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
289-712 |
7.86e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 114.67 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAesvcLMTGVpIgYSTPLTLID 368
Cdd:PRK03640 141 DEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSI----LMRSV-I-YGMRVVLVE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 369 T--SSKIKRGCKGDatvlKPTCMTSVPLILDRIskgindkvnsgsafkkslfkflyqykvkwvqrgyktplidklvfkkV 446
Cdd:PRK03640 215 KfdAEKINKLLQTG----GVTIISVVSTMLQRL----------------------------------------------L 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 447 AKLMGG----KVRIIMSGGAPLSADTHEQiktclCLE----LIQGYGLTETTSGATVMDYRDM--TYGRTGGPLTVCDIR 516
Cdd:PRK03640 245 ERLGEGtypsSFRCMLLGGGPAPKPLLEQ-----CKEkgipVYQSYGMTETASQIVTLSPEDAltKLGSAGKPLFPCELK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 517 LVnwEEGNyrvTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQA 596
Cdd:PRK03640 320 IE--KDGV---VVPPFEEGEIVVKGPNVTKGYLNREDATRETF--QDG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISG 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 597 GEYVSLGKVESELKTCGIIENICVYGDPTKQY---TVALVVpnqnhleelaqkhglgdksfeelCSSPIIEkailKEIAE 673
Cdd:PRK03640 390 GENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWgqvPVAFVV-----------------------KSGEVTE----EELRH 442
|
410 420 430
....*....|....*....|....*....|....*....
gi 442622933 674 HARKcKLQKYEVPAAITLCKEVwsPDmglvTAAFKLKRK 712
Cdd:PRK03640 443 FCEE-KLAKYKVPKRFYFVEEL--PR----NASGKLLRH 474
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
151-592 |
2.41e-26 |
|
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: 113.92 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 151 EAERTAAnfgrGLRELGQKPRENIVIFAETRAEWMIAAHGCF-KQAMP-IVTVYAT--LGDDGVAHcitetevttvitsh 226
Cdd:cd05906 48 DARRLAA----GLRQLGLRPGDSVILQFDDNEDFIPAFWACVlAGFVPaPLTVPPTydEPNARLRK-------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 227 dlLPKFKTLLDKcPLVKTIIYIEDQLQKTETTGFKEGVKILPFNQVVKTGQDSkfeHVPPK-GDDIAIIMYTSGSTGTPK 305
Cdd:cd05906 110 --LRHIWQLLGS-PVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADH---DLPQSrPDDLALLMLTSGSTGFPK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 306 GVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESV------CLMTGVPIGY--STPLTLIDTSSKIKrgc 377
Cdd:cd05906 184 AVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLravylgCQQVHVPTEEilADPLRWLDLIDRYR--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 378 kgdATVlkpTCMTSVPLILdriskgINDKVNSGSAFKKSLfkflyqykvkwvqrgyktplidklvfkkvaklmgGKVRII 457
Cdd:cd05906 261 ---VTI---TWAPNFAFAL------LNDLLEEIEDGTWDL----------------------------------SSLRYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 458 MSGGAPLSADTHEQIktclcLELIQ-----------GYGLTETTSGATVmDYRDMTYGRT--------GGPLTVCDIRLV 518
Cdd:cd05906 295 VNAGEAVVAKTIRRL-----LRLLEpyglppdairpAFGMTETCSGVIY-SRSFPTYDHSqalefvslGRPIPGVSMRIV 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622933 519 nweegnyRVTNKPYPQGEV---LIGGECVSQGYYKLPgKTNEDFFEEDGqrWFKTGDIGEIQaDGVLKIIDRKKDLV 592
Cdd:cd05906 369 -------DDEGQLLPEGEVgrlQVRGPVVTKGYYNNP-EANAEAFTEDG--WFRTGDLGFLD-NGNLTITGRTKDTI 434
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
289-689 |
7.09e-26 |
|
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: 111.87 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLplAHVFEL-VAESVC-LMTGvpigystpltl 366
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFA--SYTFDVsILEIFTtLAAG----------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 367 idtsskikrGCkgdatvlkpTCMTSVpliLDRIskgiNDkvnsgsafkksLFKFLYQYKVKWVQRgykTPlidklvfkKV 446
Cdd:cd05918 173 ---------GC---------LCIPSE---EDRL----ND-----------LAGFINRLRVTWAFL---TP--------SV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 447 AKLMGGK----VRIIMSGGAPLsadTHEQIKT-CLCLELIQGYGLTETTSGATV-MDYRDMTYGRTGGPLTVCdIRLVNw 520
Cdd:cd05918 206 ARLLDPEdvpsLRTLVLGGEAL---TQSDVDTwADRVRLINAYGPAECTIAATVsPVVPSTDPRNIGRPLGAT-CWVVD- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 521 eEGNYrvtNKPYPQ---GEVLIGGECVSQGYYKLPGKTNEDFFE----------EDGQRWFKTGDIGEIQADGVLKIIDR 587
Cdd:cd05918 281 -PDNH---DRLVPIgavGELLIEGPILARGYLNDPEKTAAAFIEdpawlkqegsGRGRRLYRTGDLVRYNPDGSLEYVGR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 588 KKDLVKLQaGEYVSLGKVESELKTC-GIIENICVY-----GDPTKQYTVALVVPNQNHLEelaqkHGLGDKSFEELCSSP 661
Cdd:cd05918 357 KDTQVKIR-GQRVELGEIEHHLRQSlPGAKEVVVEvvkpkDGSSSPQLVAFVVLDGSSSG-----SGDGDSLFLEPSDEF 430
|
410 420
....*....|....*....|....*...
gi 442622933 662 iieKAILKEIAEHARKCkLQKYEVPAAI 689
Cdd:cd05918 431 ---RALVAELRSKLRQR-LPSYMVPSVF 454
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
263-647 |
1.24e-25 |
|
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: 113.80 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 263 GVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAH- 341
Cdd:COG1020 591 GVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFd 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 342 --VFELVAesvCLMTG---VPIGYSTPLTLIDTSSKIKRGckgdatvlKPTCMTSVPlildriskgindkvnsgsafkkS 416
Cdd:COG1020 671 asVWEIFG---ALLSGatlVLAPPEARRDPAALAELLARH--------RVTVLNLTP----------------------S 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 417 LFKflyqykvkwvqrgyktPLIDklvfkkVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLC-LELIQGYGLTETTSGATV 495
Cdd:COG1020 718 LLR----------------ALLD------AAPEALPSLRLVLVGGEALPPELVRRWRARLPgARLVNLYGPTETTVDSTY 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 496 MDYRD-------MTYGRtggPLTVCDIRLVNwEEGNyrvtnkPYPQ---GEVLIGGECVSQGYYKLPGKTNEDF----FE 561
Cdd:COG1020 776 YEVTPpdadggsVPIGR---PIANTRVYVLD-AHLQ------PVPVgvpGELYIGGAGLARGYLNRPELTAERFvadpFG 845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 562 EDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTC-GIIENI-CVYGD-PTKQYTVALVVPNQN 638
Cdd:COG1020 846 FPGARLYRTGDLARWLPDGNLEFLGRADDQVKIR-GFRIELGEIEAALLQHpGVREAVvVAREDaPGDKRLVAYVVPEAG 924
|
....*....
gi 442622933 639 HLEELAQKH 647
Cdd:COG1020 925 AAAAAALLR 933
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
148-689 |
1.41e-25 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 111.74 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAH-----------CITE 216
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADriedaeakvliTADG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 217 TEVTTVItsHDLLPKFKTLLDKCPLVKTIIYIEDQLQKTETTGFkegvkiLPFNQVVKtGQDSKFEHVPPKGDDIAIIMY 296
Cdd:COG0365 121 GLRGGKV--IDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGD------LDWDELLA-AASAEFEPEPTDADDPLFILY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 297 TSGSTGTPKGVLLSHK----NCIATMKGFVDMVpiyPDDVL-----IGFL---------PLAHvfelvAESVCLMTGVPI 358
Cdd:COG0365 192 TSGTTGKPKGVVHTHGgylvHAATTAKYVLDLK---PGDVFwctadIGWAtghsyivygPLLN-----GATVVLYEGRPD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 359 gYSTPLTLIDTSSKikrgckgdatvLKPTCMTSVPLILdriskgindkvnsgSAFKKSLFKFLYQYKVKwvqrgyktpli 438
Cdd:COG0365 264 -FPDPGRLWELIEK-----------YGVTVFFTAPTAI--------------RALMKAGDEPLKKYDLS----------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 439 dklvfkkvaklmggKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSG-ATVMDYRDMTYGRTGGPLTVCDIRL 517
Cdd:COG0365 307 --------------SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 518 VNwEEGNYRVTNKPypqGEVLIGGECVSQ--GYYKLPGKTNEDFFEE-DGqrWFKTGDIGEIQADGVLKIIDRKKDLVKL 594
Cdd:COG0365 373 VD-EDGNPVPPGEE---GELVIKGPWPGMfrGYWNDPERYRETYFGRfPG--WYRTGDGARRDEDGYFWILGRSDDVINV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 595 qAGEYVSLGKVESELKT-CGIIENICV-YGDPTK-QYTVALVVPNQNHL--EELAqkhglgdksfeelcsspiiekailK 669
Cdd:COG0365 447 -SGHRIGTAEIESALVShPAVAEAAVVgVPDEIRgQVVKAFVVLKPGVEpsDELA------------------------K 501
|
570 580
....*....|....*....|
gi 442622933 670 EIAEHARKcKLQKYEVPAAI 689
Cdd:COG0365 502 ELQAHVRE-ELGPYAYPREI 520
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
151-639 |
1.74e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 111.21 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 151 EAERTAANFGRglrELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLP 230
Cdd:PRK08314 44 EAERLAGYLQQ---ECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 231 KFKTLLDKCPLVKTII-----YIEDQ--------LQKTETTGFKEGVKILPFNQVVKTGqdskfeHVPPKG----DDIAI 293
Cdd:PRK08314 121 KVAPAVGNLRLRHVIVaqysdYLPAEpeiavpawLRAEPPLQALAPGGVVAWKEALAAG------LAPPPHtagpDDLAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 294 IMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVfelvaesvclmTGVPIGYSTPLTLidtsski 373
Cdd:PRK08314 195 LPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHV-----------TGMVHSMNAPIYA------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 374 krgckGDATVLKPtcmtsvplILDR------ISKgindkvnsgsafkkslfkflyqYKVK-WVQrgYKTPLIDKLVFKKV 446
Cdd:PRK08314 257 -----GATVVLMP--------RWDReaaarlIER----------------------YRVThWTN--IPTMVVDFLASPGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 447 AKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSgATVMDYRDmtygRT-----GGPLTVCDIRLVNWE 521
Cdd:PRK08314 300 AERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMA-QTHSNPPD----RPklqclGIPTFGVDARVIDPE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 522 egnyrvTNKPYPQGEV---LIGGECVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGE 598
Cdd:PRK08314 375 ------TLEELPPGEVgeiVVHGPQVFKGYWNRPEATAEAFIEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGF 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 442622933 599 YVSLGKVESELKTCGIIENICVYG--DPTKQYTV-ALVVPNQNH 639
Cdd:PRK08314 448 KVWPAEVENLLYKHPAIQEACVIAtpDPRRGETVkAVVVLRPEA 491
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
227-592 |
7.31e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 110.04 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 227 DLLPKFKTLLDKCPLVKTIIYIEDQLQKTETTGF-------KEGVKILPFNQVVKTGQDSK-FEHVPPKGDDIAIIMYTS 298
Cdd:PRK07529 143 DIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLavplirrKAHARILDFDAELARQPGDRlFSGRPIGPDDVAAYFHTG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 299 GSTGTPKGVLLSHKN------CIATMKGFVdmvpiyPDDVLIGFLPLAHVFELVAesVCLMT---------GVPIGYSTP 363
Cdd:PRK07529 223 GTTGMPKLAQHTHGNevanawLGALLLGLG------PGDTVFCGLPLFHVNALLV--TGLAPlargahvvlATPQGYRGP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 lTLIDTSSKIKRGCKgdatvlkPTCMTSVPLILDRISKGINDKVNSGSafkkslfkflyqykvkwvqrgyktplidklvf 443
Cdd:PRK07529 295 -GVIANFWKIVERYR-------INFLSGVPTVYAALLQVPVDGHDISS-------------------------------- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 444 kkvaklmggkVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATvMDYRD--MTYGRTGGPLTVCDIRLVNWE 521
Cdd:PRK07529 335 ----------LRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSS-VNPPDgeRRIGSVGLRLPYQRVRVVILD 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622933 522 E-GNYRVTNKPYPQGEVLIGGECVSQGYykLPGKTNEDFFEEDgqRWFKTGDIGEIQADGVLKIIDRKKDLV 592
Cdd:PRK07529 404 DaGRYLRDCAVDEVGVLCIAGPNVFSGY--LEAAHNKGLWLED--GWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
280-624 |
8.00e-25 |
|
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: 108.24 E-value: 8.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 280 KFEHVPpKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHvfelvaesvclMTGVPIG 359
Cdd:cd05903 85 QFDPAA-MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAH-----------QTGFVYG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 360 YSTPLTLidtsskikrgckGDATVLKPTCMTSVPLILDRiskgiNDKVNSGSAfkkslfkflyqykvkwvqrgyKTPLID 439
Cdd:cd05903 153 FTLPLLL------------GAPVVLQDIWDPDKALALMR-----EHGVTFMMG---------------------ATPFLT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 440 KLVfkKVAKLMGGKV---RIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVM-DYRDMTYGRTGG-PLTVCD 514
Cdd:cd05903 195 DLL--NAVEEAGEPLsrlRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSItPAPEDRRLYTDGrPLPGVE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 515 IRLVNweegNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkL 594
Cdd:cd05903 273 IKVVD----DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA--PEG--WFRTGDLARLDEDGYLRITGRSKDII-I 343
|
330 340 350
....*....|....*....|....*....|
gi 442622933 595 QAGEYVSLGKVESELKTCGIIENICVYGDP 624
Cdd:cd05903 344 RGGENIPVLEVEDLLLGHPGVIEAAVVALP 373
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
288-712 |
9.89e-25 |
|
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: 107.84 E-value: 9.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSH----KNCIATMKGFvdmvPIYPDDVLIGFLPLAhvFELVAEsvCLMTgvpigystP 363
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHgplaAHCQATAERY----GLTPGDRELQFASFN--FDGAHE--QLLP--------P 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LTlidtsskikrgcKGDATVLKPTCMTSVPLILDRISKgiNDKVNSGSAFKKSLFKFLyQYKVKWVQRGYktplidklvf 443
Cdd:cd17649 157 LI------------CGACVVLRPDELWASADELAEMVR--ELGVTVLDLPPAYLQQLA-EEADRTGDGRP---------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 444 kkvaklmgGKVRIIMSGGAPLSADTHEQIKTCLCLeLIQGYGLTETTSGATVMDYR--------DMTYGRTGGPLTVC-- 513
Cdd:cd17649 212 --------PSLRLYIFGGEALSPELLRRWLKAPVR-LFNAYGPTEATVTPLVWKCEagaaragaSMPIGRPLGGRSAYil 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 514 DIRLvnweegnyrvtnKPYPQ---GEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQADGVLKIID 586
Cdd:cd17649 283 DADL------------NPVPVgvtGELYIGGEGLARGYLGRPELTAERFvpdpFGAPGSRLYRTGDLARWRDDGVIEYLG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 587 RKKDLVKLQaGEYVSLGKVESELKTCGIIENICVYGDPTKQYT--VALVVPNQnhleelaqkhglgdksfeelcssPIIE 664
Cdd:cd17649 351 RVDHQVKIR-GFRIELGEIEAALLEHPGVREAAVVALDGAGGKqlVAYVVLRA-----------------------AAAQ 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 442622933 665 KAILKEIAEHARKcKLQKYEVPAAItlckeVWSPDMGLvTAAFKLKRK 712
Cdd:cd17649 407 PELRAQLRTALRA-SLPDYMVPAHL-----VFLARLPL-TPNGKLDRK 447
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
269-716 |
4.08e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 107.27 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 269 FNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPD-----DVLIGFLPLAHVF 343
Cdd:PRK08751 188 FREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYHIF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 344 ELVAESVCLMT--GVPIGYSTPltlidtsskikRGCKGDATVLKPTCMTSVplildrisKGINdkvnsgsafkkSLFKFL 421
Cdd:PRK08751 268 ALTANGLVFMKigGCNHLISNP-----------RDMPGFVKELKKTRFTAF--------TGVN-----------TLFNGL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 422 YQykvkwvqrgykTPLIDKLVFKKVaklmggkvRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATV--MDYR 499
Cdd:PRK08751 318 LN-----------TPGFDQIDFSSL--------KMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACInpLTLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 500 DMTyGRTGGPLTVCDIRLVNwEEGNYRVTNKpypQGEVLIGGECVSQGYYKLPGKTNEDFfeeDGQRWFKTGDIGEIQAD 579
Cdd:PRK08751 379 EYN-GSIGLPIPSTDACIKD-DAGTVLAIGE---IGELCIKGPQVMKGYWKRPEETAKVM---DADGWLHTGDIARMDEQ 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 580 GVLKIIDRKKDLVkLQAGEYVSLGKVESELKTC-GIIEnicvygdptkqytVALVvpnqnhleelaqkhGLGDKSFEELC 658
Cdd:PRK08751 451 GFVYIVDRKKDMI-LVSGFNVYPNEIEDVIAMMpGVLE-------------VAAV--------------GVPDEKSGEIV 502
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622933 659 SSPIIEK---AILKEIAEHARkCKLQKYEVPAAITLCKEVWSPDMGlvtaafKLKRKDIQD 716
Cdd:PRK08751 503 KVVIVKKdpaLTAEDVKAHAR-ANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
283-637 |
1.87e-23 |
|
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: 104.59 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 283 HVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGfVDMVPIYPDDVLIGFLPL---AHVFELVaesVCLMTG---V 356
Cdd:cd12117 130 AVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN-TNYVTLGPDDRVLQTSPLafdASTFEIW---GALLNGarlV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 357 PIGYSTPLTLIDTSSKIKRGckgDATVLkptCMTSvplildriskgindkvnsgsafkkSLFKFLYQykvkwvqrgyktp 436
Cdd:cd12117 206 LAPKGTLLDPDALGALIAEE---GVTVL---WLTA------------------------ALFNQLAD------------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 437 lidklvfkKVAKLMGGkVRIIMSGGAPLSAdthEQIKTCL--C--LELIQGYGLTETTSGAT--VMDYRDMTYGRT--GG 508
Cdd:cd12117 243 --------EDPECFAG-LRELLTGGEVVSP---PHVRRVLaaCpgLRLVNGYGPTENTTFTTshVVTELDEVAGSIpiGR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 509 PLTVCDIRLVNweegnyrVTNKPYPQ---GEVLIGGECVSQGYYKLPGKTNEDFFE---EDGQRWFKTGDIGEIQADGVL 582
Cdd:cd12117 311 PIANTRVYVLD-------EDGRPVPPgvpGELYVGGDGLALGYLNRPALTAERFVAdpfGPGERLYRTGDLARWLPDGRL 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622933 583 KIIDRKKDLVKLQaGEYVSLGKVESELKTC-GIIENICVY--GDPTKQYTVALVVPNQ 637
Cdd:cd12117 384 EFLGRIDDQVKIR-GFRIELGEIEAALRAHpGVREAVVVVreDAGGDKRLVAYVVAEG 440
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
288-638 |
6.87e-23 |
|
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: 102.39 E-value: 6.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGF-------------LPLAHVFELVAesvclmt 354
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFhsyafdfsvweiwGALLHGGRLVV------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 355 gVPigYSTPLTLIDTSSKIkrgCKGDATVLKPTcmtsvPlildriskgindkvnsgSAFkkslfkflYQYkVKWVQRGYK 434
Cdd:cd17643 165 -VP--YEVARSPEDFARLL---RDEGVTVLNQT-----P-----------------SAF--------YQL-VEAADRDGR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 435 TPLidklvfkkvaklmggKVRIIMSGGAPLSADT---HEQIKTCLCLELIQGYGLTETTSGATV--MDyRDMTYGRT--- 506
Cdd:cd17643 208 DPL---------------ALRYVIFGGEALEAAMlrpWAGRFGLDRPQLVNMYGITETTVHVTFrpLD-AADLPAAAasp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 507 -GGPLTVCDIRLVNwEEGNyrvtnkPYP---QGEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQA 578
Cdd:cd17643 272 iGRPLPGLRVYVLD-ADGR------PVPpgvVGELYVSGAGVARGYLGRPELTAERFvanpFGGPGSRMYRTGDLARRLP 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622933 579 DGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICV---YGDPTKQYTVALVVPNQN 638
Cdd:cd17643 345 DGELEYLGRADEQVKIR-GFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDG 406
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
268-616 |
7.89e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 103.18 E-value: 7.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 268 PFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATM-KGFVDMVPIY----PDDVLIGF--LPLA 340
Cdd:PRK07059 183 RFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlQMEAWLQPAFekkpRPDQLNFVcaLPLY 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 341 HVFELvaeSVCLMTGVPIGYSTplTLIDTSSKIKrgckGDATVLKPTCMTSVPlildriskGINdkvnsgsafkkSLFKF 420
Cdd:PRK07059 263 HIFAL---TVCGLLGMRTGGRN--ILIPNPRDIP----GFIKELKKYQVHIFP--------AVN-----------TLYNA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 421 LYQykvkwvqrgykTPLIDKLVFKKVAKLMGGKvriiMSGGAPLSADTHEQIKTclclELIQGYGLTETTSGATV--MDY 498
Cdd:PRK07059 315 LLN-----------NPDFDKLDFSKLIVANGGG----MAVQRPVAERWLEMTGC----PITEGYGLSETSPVATCnpVDA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 499 RDMTyGRTGGPL--TVCDIRLvnwEEGNYRVTNKPypqGEVLIGGECVSQGYYKLPGKTNEDFFEeDGqrWFKTGDIGEI 576
Cdd:PRK07059 376 TEFS-GTIGLPLpsTEVSIRD---DDGNDLPLGEP---GEICIRGPQVMAGYWNRPDETAKVMTA-DG--FFRTGDVGVM 445
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 442622933 577 QADGVLKIIDRKKDLVkLQAGEYVSLGKVESELKTC-GIIE 616
Cdd:PRK07059 446 DERGYTKIVDRKKDMI-LVSGFNVYPNEIEEVVASHpGVLE 485
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
148-643 |
8.44e-23 |
|
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: 102.41 E-value: 8.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQA---MPIVTVYAT------LGDDGVahcitete 218
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGgayLPIDPDYPEeriqyiLEDSGA-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 219 vttvitshdllpkfKTLLDKCPLVKTIIYIEDQLQKTETTGFKEGVKILpfnqvvktgqdskfeHVPPKGDDIAIIMYTS 298
Cdd:cd17655 96 --------------DILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENL---------------EPVSKSDDLAYVIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 299 GSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELVAESVclmtgvpigySTPLTLidtsskikrgck 378
Cdd:cd17655 147 GSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASIS--FDASVTEI----------FASLLS------------ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 379 GDATVLKPtcmtsvplildriskgiNDKVNSGSAfkksLFKFLYQYKVKWVQrgyKTPLIDKLVfKKVAKLMGGKVRIIM 458
Cdd:cd17655 203 GNTLYIVR-----------------KETVLDGQA----LTQYIRQNRITIID---LTPAHLKLL-DAADDSEGLSLKHLI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 459 SGGAPLSADTHEQIKTCLCL--ELIQGYGLTETTSGATVMDYRDMTYGRT----GGPLtvcdirlvnweeGNYRV----- 527
Cdd:cd17655 258 VGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDASIYQYEPETDQQVsvpiGKPL------------GNTRIyildq 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 528 TNKPYP---QGEVLIGGECVSQGYYKLPGKTNEDFFE---EDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVS 601
Cdd:cd17655 326 YGRPQPvgvAGELYIGGEGVARGYLNRPELTAEKFVDdpfVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR-GYRIE 404
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 442622933 602 LGKVESELKTcgiIENIcvygdptkQYTVALVVPNQNHLEEL 643
Cdd:cd17655 405 LGEIEARLLQ---HPDI--------KEAVVIARKDEQGQNYL 435
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
148-695 |
1.46e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 102.27 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFK-QAMPI-----------VTVYATLGDDGVAHcit 215
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKaRAVPVnvnyryvedelRYLLDDSDAVALVY--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 216 etevttvitSHDLLPKFKTLLDKCPLVKTIIYIEDQLQKTETTGfkeGVkilPFNQVVKTGqDSKFEHVPPKGDDIaIIM 295
Cdd:PRK07798 107 ---------EREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPG---AV---DYEDALAAG-SPERDFGERSPDDL-YLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 296 YTSGSTGTPKGVLLSHknciatmkgfvdmvpiypDDvligflplahVFELVAESVCLMTGVPIgySTPLTLidtsskIKR 375
Cdd:PRK07798 170 YTGGTTGMPKGVMWRQ------------------ED----------IFRVLLGGRDFATGEPI--EDEEEL------AKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 376 GCKGDATVLKPTCmtsvPLI-------------------------------LDRISKginDKVNS----GSAFKKslfkf 420
Cdd:PRK07798 214 AAAGPGMRRFPAP----PLMhgagqwaafaalfsgqtvvllpdvrfdadevWRTIER---EKVNVitivGDAMAR----- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 421 lyqykvkwvqrgyktPLIDKLVFKKVAKLMGgkVRIIMSGGAPLSADTHEQIKTCLC-LELIQGYGLTETTSGATVMDYR 499
Cdd:PRK07798 282 ---------------PLLDALEARGPYDLSS--LFAIASGGALFSPSVKEALLELLPnVVLTDSIGSSETGFGGSGTVAK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 500 DMTygRTGGPLTVCDIRLVNWEEGNYRVTNKPYPQGEVLIGGEcVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQAD 579
Cdd:PRK07798 345 GAV--HTGGPRFTIGPRTVVLDEDGNPVEPGSGEIGWIARRGH-IPLGYYKDPEKTAETFPTIDGVRYAIPGDRARVEAD 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 580 GVLKIIDRkKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALVVPNQNHLEELAqkhglgdksfee 656
Cdd:PRK07798 422 GTITLLGR-GSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDErwgQEVVAVVQLREGARPDLA------------ 488
|
570 580 590
....*....|....*....|....*....|....*....
gi 442622933 657 lcsspiiekailkEIAEHARKcKLQKYEVPAAITLCKEV 695
Cdd:PRK07798 489 -------------ELRAHCRS-SLAGYKVPRAIWFVDEV 513
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
283-636 |
2.00e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 101.22 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 283 HVPPKGDD--IAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVaesVCLMTGVPIGY 360
Cdd:PRK07787 120 HRYPEPDPdaPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLV---LGVLGPLRIGN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 361 STPLTLIDTSSKIKRGCKGDATVLkptcmTSVPLILDRISkginDKVNSGSAFKKSlfkflyqykvkwvqrgyktplidk 440
Cdd:PRK07787 197 RFVHTGRPTPEAYAQALSEGGTLY-----FGVPTVWSRIA----ADPEAARALRGA------------------------ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 441 lvfkkvaklmggkvRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTET---TSGATVMDYRDmtyGRTGGPLTVCDIRL 517
Cdd:PRK07787 244 --------------RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETlitLSTRADGERRP---GWVGLPLAGVETRL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 518 VNwEEGNyRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDfFEEDGqrWFKTGDIGEIQADGVLKIIDRKK-DLVKlqA 596
Cdd:PRK07787 307 VD-EDGG-PVPHDGETVGELQVRGPTLFDGYLNRPDATAAA-FTADG--WFRTGDVAVVDPDGMHRIVGREStDLIK--S 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 442622933 597 GEY-VSLGKVESELKTCGIIENICVYGDPTK---QYTVALVVPN 636
Cdd:PRK07787 380 GGYrIGAGEIETALLGHPGVREAAVVGVPDDdlgQRIVAYVVGA 423
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
227-601 |
2.18e-22 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 101.55 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 227 DLLPKFKTLLDKCPLVKTIIYIEDQLQKTETTGfkegVKILPFNQVVktGQDSKFEHVPP-KGDDIAIIMYTSGSTGTPK 305
Cdd:cd12119 106 DFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAG----VGVLAYEELL--AAESPEYDWPDfDENTAAAICYTSGTTGNPK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 306 GVLLSHKNCI--ATMKGFVDMVPIYPDDVLIGFLPLAHVfelvaesvcLMTGVPigYSTPltlidtsskikrgckgdatv 383
Cdd:cd12119 180 GVVYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPMFHV---------NAWGLP--YAAA-------------------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 384 lkptcMTSVPLILdriskgindkvnSGSAFK-KSLFKFLYQYKVKWVQrGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGA 462
Cdd:cd12119 229 -----MVGAKLVL------------PGPYLDpASLAELIEREGVTFAA-GVPTVWQGLLDHLEANGRDLSSLRRVVIGGS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 463 PLSADTHEQIKTcLCLELIQGYGLTETTSGATV---------------MDYRDMTyGRtggPLTVCDIRLVNwEEGNyRV 527
Cdd:cd12119 291 AVPRSLIEAFEE-RGVRVIHAWGMTETSPLGTVarppsehsnlsedeqLALRAKQ-GR---PVPGVELRIVD-DDGR-EL 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622933 528 TNKPYPQGEVLIGGECVSQGYYKLPGKTneDFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVS 601
Cdd:cd12119 364 PWDGKAVGELQVRGPWVTKSYYKNDEES--EALTEDG--WLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWIS 432
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
284-643 |
2.24e-22 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 101.75 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVfelvaesvclmTGVPIGYSTP 363
Cdd:PRK06087 182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHA-----------TGFLHGVTAP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LTLidtsskikrgckGDATVLKptcmtsvplildriskginDKVNSGSAFKkslfkFLYQYKVKWVQRGykTPLI-DKLV 442
Cdd:PRK06087 251 FLI------------GARSVLL-------------------DIFTPDACLA-----LLEQQRCTCMLGA--TPFIyDLLN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 443 FKKVAKLMGGKVRIIMSGGAPLSADTHEQ-----IKTCLCleliqgYGLTETTSGATVM--DYRDMTYGRTGGPLTVCDI 515
Cdd:PRK06087 293 LLEKQPADLSALRFFLCGGTTIPKKVAREcqqrgIKLLSV------YGSTESSPHAVVNldDPLSRFMHTDGYAAAGVEI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 516 RLVNweegNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEdFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQ 595
Cdd:PRK06087 367 KVVD----EARKTLPPGCEGEEASRGPNVFMGYLDEPELTAR-ALDEEG--WYYSGDLCRMDEAGYIKITGRKKDII-VR 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 442622933 596 AGEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALVVPNQNH----LEEL 643
Cdd:PRK06087 439 GGENISSREVEDILLQHPKIHDACVVAMPDErlgERSCAYVVLKAPHhsltLEEV 493
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
148-592 |
3.05e-22 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 101.16 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGqKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYAtlgDDGVAHcitetevttvitshd 227
Cdd:cd05931 26 TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP---PTPGRH--------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 228 lLPKFKTLLDKC--PLVKTIIYIEDQLQKTETTGFKEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPK 305
Cdd:cd05931 87 -AERLAAILADAgpRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 306 GVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVaesvcLMTGVPIGYSTPLTLIDTSSKIKRgckgdatvlk 385
Cdd:cd05931 166 GVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLI-----GGLLTPLYSGGPSVLMSPAAFLRR---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 386 ptcmtsvPLI-LDRISKgiNDKVNSGSAfkkslfKFLYQYKVKWVQRGYKTPLiDkLvfkkvaklmgGKVRIIMSGGAPL 464
Cdd:cd05931 231 -------PLRwLRLISR--YRATISAAP------NFAYDLCVRRVRDEDLEGL-D-L----------SSWRVALNGAEPV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 465 SADT--------------HEQIKTClcleliqgYGLTETT---------SGATVMDYRDMTYGRT--------------- 506
Cdd:cd05931 284 RPATlrrfaeafapfgfrPEAFRPS--------YGLAEATlfvsggppgTGPVVLRVDRDALAGRavavaaddpaarelv 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 507 --GGPLTVCDIRLVNWEegnyrvTNKPYPQ---GEVLIGGECVSQGYYKLPGKTNEDFFEEDGQ---RWFKTGDIGEIqA 578
Cdd:cd05931 356 scGRPLPDQEVRIVDPE------TGRELPDgevGEIWVRGPSVASGYWGRPEATAETFGALAATdegGWLRTGDLGFL-H 428
|
490
....*....|....
gi 442622933 579 DGVLKIIDRKKDLV 592
Cdd:cd05931 429 DGELYITGRLKDLI 442
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
288-592 |
7.48e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 97.94 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELV---------AESVCLMTgvPI 358
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVvtlltplasGAHVVLAG--PA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 359 GYSTPlTLIDTSSK-IKRgckgdatvLKPTCMTSVPLILDRI-SKGINDKVNSgsafkkslfkflyqykvkwvqrgyktp 436
Cdd:cd05944 79 GYRNP-GLFDNFWKlVER--------YRITSLSTVPTVYAALlQVPVNADISS--------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 437 lidklvfkkvaklmggkVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVmDYRD--MTYGRTGGPLTVCD 514
Cdd:cd05944 123 -----------------LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAV-NPPDgpKRPGSVGLRLPYAR 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622933 515 IRLVNWE-EGNYRVTNKPYPQGEVLIGGECVSQGYykLPGKTNEDFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLV 592
Cdd:cd05944 185 VRIKVLDgVGRLLRDCAPDEVGEICVAGPGVFGGY--LYTEGNKNAFVADG--WLNTGDLGRLDADGYLFITGRAKDLI 259
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
148-637 |
1.38e-21 |
|
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: 98.98 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQ-AMPIVTVYATLGDDgVAHCITETEVTTVITSH 226
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAgIVPVPVNTLLTPDD-YAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 227 DLLPKFKTLLDK-CPLVKTIIYIEdqlqktettGFKEGVKILPFNQVVKTGQDSkFEHVPPKGDDIAIIMYTSGSTGTPK 305
Cdd:cd05959 110 ELAPVLAAALTKsEHTLVVLIVSG---------GAGPEAGALLLAELVAAEAEQ-LKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 306 GVLLSHKNCIATMKGFV-DMVPIYPDDVLIGFLPLAHVFEL---------VAESVCLMTGVPigysTPLTLIDTsskIKR 375
Cdd:cd05959 180 GVVHLHADIYWTAELYArNVLGIREDDVCFSAAKLFFAYGLgnsltfplsVGATTVLMPERP----TPAAVFKR---IRR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 376 GckgdatvlKPTCMTSVPLILDRISKGINdkvnsgsafkkslfkflyqykvkWVQRGYKTplidklvfkkvaklmggkVR 455
Cdd:cd05959 253 Y--------RPTVFFGVPTLYAAMLAAPN-----------------------LPSRDLSS------------------LR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 456 IIMSGGAPLSADTHEQIKTCLCLELIQGYGLTET----TSGATvmdyRDMTYGRTGGPLTVCDIRLVNwEEGNYRVTNKP 531
Cdd:cd05959 284 LCVSAGEALPAEVGERWKARFGLDILDGIGSTEMlhifLSNRP----GRVRYGTTGKPVPGYEVELRD-EDGGDVADGEP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 532 ypqGEVLIGGECVSQGYYKLPGKTNEDFFEEdgqrWFKTGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSLGKVESELKT 611
Cdd:cd05959 359 ---GELYVRGPSSATMYWNNRDKTRDTFQGE----WTRTGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFEVESALVQ 430
|
490 500 510
....*....|....*....|....*....|.
gi 442622933 612 CGIIENICVYG--DP---TKqyTVALVVPNQ 637
Cdd:cd05959 431 HPAVLEAAVVGveDEdglTK--PKAFVVLRP 459
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
159-642 |
2.02e-21 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 98.70 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 159 FGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPKFKTLLDK 238
Cdd:TIGR03098 38 LASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 239 CPLVKTIIYIEDQLQKTETtgfKEGVKILPFNQVVKTG-QDSKFEHVPpkgDDIAIIMYTSGSTGTPKGVLLSHKNCIAT 317
Cdd:TIGR03098 118 CHDLRTLIIVGDPAHASEG---HPGEEPASWPKLLALGdADPPHPVID---SDMAAILYTSGSTGRPKGVVLSHRNLVAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 318 MKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTG---VPIGYSTPLTLIDTSSKikrgckgdatvLKPTCMTSVPL 394
Cdd:TIGR03098 192 AQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGatvVLHDYLLPRDVLKALEK-----------HGITGLAAVPP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 395 IldriskgindkvnsgsafkkslfkflyqykvkWVQrgyktplIDKLVFKKVAklmGGKVRIIMSGGAPLSADTHEQIKT 474
Cdd:TIGR03098 261 L--------------------------------WAQ-------LAQLDWPESA---APSLRYLTNSGGAMPRATLSRLRS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 475 CLCL-ELIQGYGLTE----TTSGATVMDYRDMTYGRTggpLTVCDIRLVNwEEGNYRVTNKPypqGEVLIGGECVSQGYY 549
Cdd:TIGR03098 299 FLPNaRLFLMYGLTEafrsTYLPPEEVDRRPDSIGKA---IPNAEVLVLR-EDGSECAPGEE---GELVHRGALVAMGYW 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 550 KLPGKTNEDFFEEDGQR----------WfkTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKVESELKTCGIIENIC 619
Cdd:TIGR03098 372 NDPEKTAERFRPLPPFPgelhlpelavW--SGDTVRRDEEGFLYFVGRRDEMIK-TSGYRVSPTEVEEVAYATGLVAEAV 448
|
490 500
....*....|....*....|....*
gi 442622933 620 VYG--DPTKQYTVALVVPNQNHLEE 642
Cdd:TIGR03098 449 AFGvpDPTLGQAIVLVVTPPGGEEL 473
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
283-635 |
3.98e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 97.36 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 283 HVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLA---HVFELVaesvclmtgvpig 359
Cdd:cd12116 120 RTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAfdiSLLELL------------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 360 ysTPLtlidtsskikrgCKGDATVLKPTCMTSVPLIL-DRI-SKGINdkvnsgsafkkslfkflyqykvkWVQrgyKTPL 437
Cdd:cd12116 187 --LPL------------LAGARVVIAPRETQRDPEALaRLIeAHSIT-----------------------VMQ---ATPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 438 IDKLVFKKvaklmGGKVR---IIMSGGAPLSADTHEQiktcLCL---ELIQGYGLTETTSGATVMDYRDMTYGRT-GGPL 510
Cdd:cd12116 227 TWRMLLDA-----GWQGRaglTALCGGEALPPDLAAR----LLSrvgSLWNLYGPTETTIWSTAARVTAAAGPIPiGRPL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 511 T-----VCDIRLvnweegnyrvtnKPYPQG---EVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQA 578
Cdd:cd12116 298 AntqvyVLDAAL------------RPVPPGvpgELYIGGDGVAQGYLGRPALTAERFvpdpFAGPGSRLYRTGDLVRRRA 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622933 579 DGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICV--YGDPTKQYTVALVVP 635
Cdd:cd12116 366 DGRLEYLGRADGQVKIR-GHRIELGEIEAALAAHPGVAQAAVvvREDGGDRRLVAYVVL 423
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
288-720 |
7.39e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.88 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAesVCLMTGVPIGystpLTLI 367
Cdd:PRK05852 175 RPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIA--ALLATLASGG----AVLL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 DTSSKIK-RGCKGDATVLKPTCMTSVPLIldriskgindkvnsgsafkkslFKFLYQyKVKWVQRGYKTPlidklvfkkv 446
Cdd:PRK05852 249 PARGRFSaHTFWDDIKAVGATWYTAVPTI----------------------HQILLE-RAATEPSGRKPA---------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 447 aklmggKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGA--TVMDYRDMTY---------GRTGGPltvcDI 515
Cdd:PRK05852 296 ------ALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVttTQIEGIGQTEnpvvstglvGRSTGA----QI 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 516 RLVNWEEGNYrvtnKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQ 595
Cdd:PRK05852 366 RIVGSDGLPL----PAGAVGEVWLRGTTVVRGYLGDPTITAANF--TDG--WLRTGDLGSLSAAGDLSIRGRIKELIN-R 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 596 AGEYVSLGKVESELKTC-GIIENIcVYGDPTKQY--TV-ALVVPNQNhleelaqkhglgdksfeelcSSPIIEkailkEI 671
Cdd:PRK05852 437 GGEKISPERVEGVLASHpNVMEAA-VFGVPDQLYgeAVaAVIVPRES--------------------APPTAE-----EL 490
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 442622933 672 AEHARKcKLQKYEVPAAITLCKEVwsPDmglvTAAFKLKRKDIQDRYQH 720
Cdd:PRK05852 491 VQFCRE-RLAAFEIPASFQEASGL--PH----TAKGSLDRRAVAEQFGH 532
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
268-637 |
1.71e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 96.06 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 268 PFNQVVKtgQDSKFEHVPP-KGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPI---YP--DDVLIGFLPLAH 341
Cdd:PLN02574 178 KFYELIK--EDFDFVPKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASqyeYPgsDNVYLAALPMFH 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 342 VFELVaesvCLMTGvpigystpltLIDTSSKIKRGCKGDAtvlkptcmtsvplildriskgiNDKVNSGSAFKKSLFKFL 421
Cdd:PLN02574 256 IYGLS----LFVVG----------LLSLGSTIVVMRRFDA----------------------SDMVKVIDRFKVTHFPVV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 422 yqykvkwvqrgykTPLIDKLVfkKVAKLMGGKV----RIIMSGGAPLSADTHEQ-IKTCLCLELIQGYGLTETTSGAT-- 494
Cdd:PLN02574 300 -------------PPILMALT--KKAKGVCGEVlkslKQVSCGAAPLSGKFIQDfVQTLPHVDFIQGYGMTESTAVGTrg 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 495 VMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRvtnKPYPQGEVLIGGECVSQGYYKLPgKTNEDFFEEDGqrWFKTGDIG 574
Cdd:PLN02574 365 FNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLL---PPGNCGELWIQGPGVMKGYLNNP-KATQSTIDKDG--WLRTGDIA 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622933 575 EIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALVVPNQ 637
Cdd:PLN02574 439 YFDEDGYLYIVDRLKEIIKYK-GFQIAPADLEAVLISHPEIIDAAVTAVPDKecgEIPVAFVVRRQ 503
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
284-635 |
1.77e-20 |
|
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: 95.42 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAH---VFELVAesvCLMTGVPIGY 360
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFdlsVYDIFG---ALSAGATLVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 361 STPLTLIDTSSKIKRGCKGDATVLkptcmTSVPLILDRISkginDKVNSGSAFKKSLfkflyqykvkwvqRGyktplidk 440
Cdd:cd12114 198 PDEARRRDPAHWAELIERHGVTLW-----NSVPALLEMLL----DVLEAAQALLPSL-------------RL-------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 441 lvfkkvaklmggkvrIIMSG---GAPLSADTHEQIKTClclELIQGYGLTETTSGATV-------MDYRDMTYGRtggPL 510
Cdd:cd12114 248 ---------------VLLSGdwiPLDLPARLRALAPDA---RLISLGGATEASIWSIYhpidevpPDWRSIPYGR---PL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 511 TvcdirlvnweeGN-YRVTN---KPYPQ---GEVLIGGECVSQGYYKLPGKTNEDFFE-EDGQRWFKTGDIGEIQADGVL 582
Cdd:cd12114 307 A-----------NQrYRVLDprgRDCPDwvpGELWIGGRGVALGYLGDPELTAARFVThPDGERLYRTGDLGRYRPDGTL 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 442622933 583 KIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICV--YGDPTKQYTVALVVP 635
Cdd:cd12114 376 EFLGRRDGQVKVR-GYRIELGEIEAALQAHPGVARAVVvvLGDPGGKRLAAFVVP 429
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
237-645 |
1.94e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 95.87 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 237 DKCPLVKTIIYIEDQLQKTE-TTGFKEGVKILPFNQVVKTgQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCI 315
Cdd:PRK06710 154 DFLPFPKNLLYPFVQKKQSNlVVKVSESETIHLWNSVEKE-VNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 316 A-TMKGFVDMVP-IYPDDVLIGFLPLAHVFELVA-ESVCLMTGVPIgystpltlidtsskikrgckgdatVLKPTcmTSV 392
Cdd:PRK06710 233 SnTLMGVQWLYNcKEGEEVVLGVLPFFHVYGMTAvMNLSIMQGYKM------------------------VLIPK--FDM 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 393 PLILDRISKgindkvnsgsaFKKSLFKflyqykvkwvqrGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQI 472
Cdd:PRK06710 287 KMVFEAIKK-----------HKVTLFP------------GAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKF 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 473 KTCLCLELIQGYGLTETTSGA-TVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNyrvTNKPYPQGEVLIGGECVSQGYYKL 551
Cdd:PRK06710 344 ETVTGGKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSLETGE---ALPPGEIGEIVVKGPQIMKGYWNK 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 552 PGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESELKTCGIIENICVYG--DPTKQYT 629
Cdd:PRK06710 421 PEETAAVL--QDG--WLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYEHEKVQEVVTIGvpDPYRGET 495
|
410 420
....*....|....*....|
gi 442622933 630 V-ALVVPNQNHL---EELAQ 645
Cdd:PRK06710 496 VkAFVVLKEGTEcseEELNQ 515
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
284-717 |
4.59e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.18 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELVAEsvclmtgvpiGYSTP 363
Cdd:PRK12316 4689 VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFS--FDGSHE----------GLYHP 4756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LtlidtsskikrgCKGDATVLKPTcmtsvplildriskGINDKvnsgsafkKSLFKFLYQYKVKWVQrgYKTPLIDKLVF 443
Cdd:PRK12316 4757 L------------INGASVVIRDD--------------SLWDP--------ERLYAEIHEHRVTVLV--FPPVYLQQLAE 4800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 444 KKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCL-CLELIQGYGLTETTSGATVMDYRDMT-----YGRTGGPLTVCDIRL 517
Cdd:PRK12316 4801 HAERDGEPPSLRVYCFGGEAVAQASYDLAWRALkPVYLFNGYGPTETTVTVLLWKARDGDacgaaYMPIGTPLGNRSGYV 4880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 518 VNWEEGnyrvtnkPYP---QGEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQADGVLKIIDRKKD 590
Cdd:PRK12316 4881 LDGQLN-------PLPvgvAGELYLGGEGVARGYLERPALTAERFvpdpFGAPGGRLYRTGDLARYRADGVIDYLGRVDH 4953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 591 LVKLQaGEYVSLGKVESELKTCGIIENICVYGD--PTKQYTVALVVPNQNHLEElaqkhglgdksfeelcsSPIIEKAIL 668
Cdd:PRK12316 4954 QVKIR-GFRIELGEIEARLREHPAVREAVVIAQegAVGKQLVGYVVPQDPALAD-----------------ADEAQAELR 5015
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622933 669 KEIAEHARKCkLQKYEVPAAITLC-------------KEVWSPDMGLVTAAFKLKRKDIQDR 717
Cdd:PRK12316 5016 DELKAALRER-LPEYMVPAHLVFLarmpltpngkldrKALPQPDASLLQQAYVAPRSELEQQ 5076
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
284-695 |
6.51e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 93.27 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELvaeSVcLMTGVPIGYStp 363
Cdd:cd05922 112 HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGL---SV-LNTHLLRGAT-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 lTLIDTSSKIKRGCKGDATVLKPTCMTSVPlildriskgindkvnsgsafkkSLFKFLyqykvkwvqrgyktpliDKLVF 443
Cdd:cd05922 186 -LVLTNDGVLDDAFWEDLREHGATGLAGVP----------------------STYAML-----------------TRLGF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 444 KKvAKLmgGKVRIIMSGGAPLSADTHEQIKtclclELIQG------YGLTETTsgatvmdyRDMTY----------GRTG 507
Cdd:cd05922 226 DP-AKL--PSLRYLTQAGGRLPQETIARLR-----ELLPGaqvyvmYGQTEAT--------RRMTYlpperilekpGSIG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 508 GPLTVCDIRLVNwEEGNyrvtnkPYPQGEVligGECVSQGYYKLPGKTNEDFFEEDGQRW---FKTGDIGEIQADGVLKI 584
Cdd:cd05922 290 LAIPGGEFEILD-DDGT------PTPPGEP---GEIVHRGPNVMKGYWNDPPYRRKEGRGggvLHTGDLARRDEDGFLFI 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 585 IDRKKDLVKLqAGEYVSLGKVESELKTCGIIENICVYGDP-TKQYTVALVVpnqnhleelaqkhglgdksfeeLCSSPII 663
Cdd:cd05922 360 VGRRDRMIKL-FGNRISPTEIEAAARSIGLIIEAAAVGLPdPLGEKLALFV----------------------TAPDKID 416
|
410 420 430
....*....|....*....|....*....|..
gi 442622933 664 EKAILKEIAEharkcKLQKYEVPAAITLCKEV 695
Cdd:cd05922 417 PKDVLRSLAE-----RLPPYKVPATVRVVDEL 443
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-624 |
8.16e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 92.74 E-value: 8.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHvfeLVAESVCLMTGVPIGYStpLTLIDT 369
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFH---INAQAVSVLAALSVGAT--LVLLPR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 370 SSKikRGCKGDATVLKPTCMTSVPLILdriskgindkvnsgsafkkslfKFLYqykvkwvqrgyKTPlidklvfkKVAKL 449
Cdd:cd05934 157 FSA--SRFWSDVRRYGATVTNYLGAML----------------------SYLL-----------AQP--------PSPDD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 450 MGGKVRIIMSGGAPlsADTHEQIKTCLCLELIQGYGLTET---TSGATVMDYRDMTYGRtGGPLtvCDIRLVNWEegnyr 526
Cdd:cd05934 194 RAHRLRAAYGAPNP--PELHEEFEERFGVRLLEGYGMTETivgVIGPRDEPRRPGSIGR-PAPG--YEVRIVDDD----- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 527 vtNKPYPQGEVligGECV---------SQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAG 597
Cdd:cd05934 264 --GQELPAGEP---GELVirglrgwgfFKGYYNMPEATAEAM--RNG--WFHTGDLGYRDADGFFYFVDRKKDMIR-RRG 333
|
330 340
....*....|....*....|....*..
gi 442622933 598 EYVSLGKVESELKTCGIIENICVYGDP 624
Cdd:cd05934 334 ENISSAEVERAILRHPAVREAAVVAVP 360
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
289-628 |
9.71e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 91.19 E-value: 9.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCI--ATMKGfvDMVPIYPDDVLIGFLPLAHVFELVAESV-CLMTGvpigystplt 365
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIG--ERLGLTEQDRLCIPVPLFHCFGSVLGVLaCLTHG---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 366 lidtsskikrgckgdATVLKPTCMTSVPLILDRISKgindkvnsgsaFKKSlfkFLYqykvkwvqrGYKTPLIDKLVFKK 445
Cdd:cd05917 70 ---------------ATMVFPSPSFDPLAVLEAIEK-----------EKCT---ALH---------GVPTMFIAELEHPD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 446 VAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQ-GYGLTETTSGAT---VMDYRDMTYGRTGGPLTVCDIRLVNwE 521
Cdd:cd05917 112 FDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTiAYGMTETSPVSTqtrTDDSIEKRVNTVGRIMPHTEAKIVD-P 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 522 EGnyRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEdffEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVS 601
Cdd:cd05917 191 EG--GIVPPVGVPGELCIRGYSVMKGYWNDPEKTAE---AIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIY 264
|
330 340
....*....|....*....|....*..
gi 442622933 602 LGKVESELKTCGIIENICVYGDPTKQY 628
Cdd:cd05917 265 PREIEEFLHTHPKVSDVQVVGVPDERY 291
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
142-639 |
1.08e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 93.07 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 142 GDYKWkTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTT 221
Cdd:PRK08316 33 GDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 222 VITSHDLLPKFKTLLDKCPLVKTIIyiEDQLQKTETTGfkegvKILPFNQVVKTGQDSKFEhVPPKGDDIAIIMYTSGST 301
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLIL--SLVLGGREAPG-----GWLDFADWAEAGSVAEPD-VELADDDLAQILYTSGTE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 302 GTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELvaeSVCLMTGVPIGYSTplTLIDtsskikrgckgda 381
Cdd:PRK08316 184 SLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQL---DVFLGPYLYVGATN--VILD------------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 382 tvlKPTcmtsVPLILDRISKginDKVNSgsafkkslfkfLYQYKVKWVqrgyktPLIDKLVFKKvAKLmgGKVRIIMSGG 461
Cdd:PRK08316 246 ---APD----PELILRTIEA---ERITS-----------FFAPPTVWI------SLLRHPDFDT-RDL--SSLRKGYYGA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 462 APLSADTHEQIKTCL-CLELIQGYGLTETTSGATVM--DYRDMTYGRTGGPLTVCDIRLVNwEEGNyrvtnkPYPQGEVl 538
Cdd:PRK08316 296 SIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLgpEEHLRRPGSAGRPVLNVETRVVD-DDGN------DVAPGEV- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 539 igGECVSQ------GYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKVESELKTC 612
Cdd:PRK08316 368 --GEIVHRspqlmlGYWDDPEKTAEAF--RGG--WFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVASREVEEALYTH 440
|
490 500 510
....*....|....*....|....*....|
gi 442622933 613 GIIENICVYGDPTKQY---TVALVVPNQNH 639
Cdd:PRK08316 441 PAVAEVAVIGLPDPKWieaVTAVVVPKAGA 470
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
289-715 |
2.23e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 92.55 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGvpiGYSTPLTLID 368
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVG---ACHVLLPKFD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 369 TSSKIKrgckgdatVLKP---TCMTSVPLIL-DRIS---KGINDKVNSGsafkkslfkflyqykvkwvqrgyktplidkl 441
Cdd:PLN02860 249 AKAALQ--------AIKQhnvTSMITVPAMMaDLISltrKSMTWKVFPS------------------------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 442 vfkkvaklmggkVRIIMSGGAPLSAD-THEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTygrtggpLTVCDIRLVNW 520
Cdd:PLN02860 290 ------------VRKILNGGGSLSSRlLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPT-------LESPKQTLQTV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 521 EEGNYRVTN--------KPYPQGEVLIG-------------GECVSQGYYKLPGKTNEDFfEEDGqrWFKTGDIGEIQAD 579
Cdd:PLN02860 351 NQTKSSSVHqpqgvcvgKPAPHVELKIGldessrvgriltrGPHVMLGYWGQNSETASVL-SNDG--WLDTGDIGWIDKA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 580 GVLKIIDRKKDLVKlQAGEYVSLGKVESEL-KTCGIIENIcVYGDPTKQYT---VALVVPNQN----HLEELAQKHGLgd 651
Cdd:PLN02860 428 GNLWLIGRSNDRIK-TGGENVYPEEVEAVLsQHPGVASVV-VVGVPDSRLTemvVACVRLRDGwiwsDNEKENAKKNL-- 503
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622933 652 ksfeELCSSpiiekaILKeiaEHARKCKLQKYEVPAAITLCKEVWSpdmglVTAAFKLKRKDIQ 715
Cdd:PLN02860 504 ----TLSSE------TLR---HHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
269-592 |
3.23e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 92.04 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 269 FNQVVKTGQdsKFEHVPP--KGDDIAIIMYTSGSTGTPKGVLLSHKNCIATM---KGFVDMVPIYPDDVLIGFLPLAHVF 343
Cdd:PRK08974 186 FRSALHKGR--RMQYVKPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqaKAAYGPLLHPGKELVVTALPLYHIF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 344 ELVAEsvCLMTgVPIGySTPLtLIDTSSKIkrgckgDATV--LKP---TCMTSVPLILdriskgiNDKVNSgSAFKKSLF 418
Cdd:PRK08974 264 ALTVN--CLLF-IELG-GQNL-LITNPRDI------PGFVkeLKKypfTAITGVNTLF-------NALLNN-EEFQELDF 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 419 KFLyqykvkwvqrgyktplidklvfkkvaklmggkvRIIMSGGAPLS---ADTHEQIKTClclELIQGYGLTETTSGATV 495
Cdd:PRK08974 325 SSL---------------------------------KLSVGGGMAVQqavAERWVKLTGQ---YLLEGYGLTECSPLVSV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 496 MDYRDMTY-GRTGGPLTVCDIRLVNwEEGNYRVTNKPypqGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIG 574
Cdd:PRK08974 369 NPYDLDYYsGSIGLPVPSTEIKLVD-DDGNEVPPGEP---GELWVKGPQVMLGYWQRPEATDEVI--KDG--WLATGDIA 440
|
330
....*....|....*...
gi 442622933 575 EIQADGVLKIIDRKKDLV 592
Cdd:PRK08974 441 VMDEEGFLRIVDRKKDMI 458
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
277-710 |
3.63e-19 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 90.98 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 277 QDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGF-VDMVPIYPDDVLIG--------------FLPLAh 341
Cdd:cd05919 79 RDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSsakmffgyglgnslWFPLA- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 342 vfelVAESVCLMTGVPigysTPLTLIDTSSKikrgckgdatvLKPTCMTSVPLILDRIskgINDKVNSGSAFKKslfkfl 421
Cdd:cd05919 158 ----VGASAVLNPGWP----TAERVLATLAR-----------FRPTVLYGVPTFYANL---LDSCAGSPDALRS------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 422 yqykvkwvqrgyktplidklvfkkvaklmggkVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETtsGATVMDYR-- 499
Cdd:cd05919 210 --------------------------------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEV--GHIFLSNRpg 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 500 DMTYGRTGGPLTVCDIRLVNwEEGNyrvTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFFEEdgqrWFKTGDIGEIQAD 579
Cdd:cd05919 256 AWRLGSTGRPVPGYEIRLVD-EEGH---TIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG----WYRTGDKFCRDAD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 580 GVLKIIDRKKDLVKLqAGEYVSLGKVESelktcgiieniCVYGDPTKQYTVALVVPNQNHLEELaqkhglgdKSFEELCS 659
Cdd:cd05919 328 GWYTHAGRADDMLKV-GGQWVSPVEVES-----------LIIQHPAVAEAAVVAVPESTGLSRL--------TAFVVLKS 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 442622933 660 SPIIEKAILKEIAEHARKcKLQKYEVPAAITLCKEVWSPDMGLVtAAFKLK 710
Cdd:cd05919 388 PAAPQESLARDIHRHLLE-RLSAHKVPRRIAFVDELPRTATGKL-QRFKLR 436
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
290-631 |
3.70e-19 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 89.25 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGvpiGYSTPLTLIDT 369
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAG---GANVVMEKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 370 SSKIKRGCKGDATVlkptcMTSVPLILDRISkginDKVNSGSAFKKSLfkflyqykvkwvqrgyktplidklvfkkvakl 449
Cdd:cd17637 78 AEALELIEEEKVTL-----MGSFPPILSNLL----DAAEKSGVDLSSL-------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 450 mggkvRIIMSGGAPlsaDTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTyGRTGGPLTVCDIRLVNwEEGNyrvtn 529
Cdd:cd17637 117 -----RHVLGLDAP---ETIQRFEETTGATFWSLYGQTETSGLVTLSPYRERP-GSAGRPGPLVRVRIVD-DNDR----- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 530 kPYPQ---GEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRK--KDLVKlQAGEYVSLGK 604
Cdd:cd17637 182 -PVPAgetGEIVVRGPLVFQGYWNLPELTAYTF--RNG--WHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAE 255
|
330 340
....*....|....*....|....*..
gi 442622933 605 VESELKTCGIIENICVYGDPTKQYTVA 631
Cdd:cd17637 256 VEKVILEHPAIAEVCVIGVPDPKWGEG 282
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
244-695 |
7.52e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 91.57 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 244 TIIYIEDqLQKTETTGFKEGVKILPFNQVVKTGQdskfehvpPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVD 323
Cdd:PRK06814 757 RIIYLED-VRAQIGLADKIKGLLAGRFPLVYFCN--------RDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAA 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 324 MVPIYPDDVLIGFLPLAHVFELVAESVC-LMTGVPIG-YSTPL------TLI-DTsskikrgckgDATVLKPTcmtsvpl 394
Cdd:PRK06814 828 RIDFSPEDKVFNALPVFHSFGLTGGLVLpLLSGVKVFlYPSPLhyriipELIyDT----------NATILFGT------- 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 395 ildriskginDKVNSGSAFKKSLFKFLyqykvkwvqrgyktplidklvfkkvaklmggKVRIIMSGGAPLSADTHEQIKT 474
Cdd:PRK06814 891 ----------DTFLNGYARYAHPYDFR-------------------------------SLRYVFAGAEKVKEETRQTWME 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 475 CLCLELIQGYGLTETT---SGATVMDYRDMTYGRTggpLTVCDIRLV---NWEEGnyrvtnkpypqGEVLIGGECVSQGY 548
Cdd:PRK06814 930 KFGIRILEGYGVTETApviALNTPMHNKAGTVGRL---LPGIEYRLEpvpGIDEG-----------GRLFVRGPNVMLGY 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 549 YKL--PGktnedFFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSLGKVESelktcgIIENIcvygDPTK 626
Cdd:PRK06814 996 LRAenPG-----VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKI-AGEMISLAAVEE------LAAEL----WPDA 1059
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622933 627 QyTVALVVPNQNHLEELAQkhglgdksfeeLCSSPIIEKAilkEIAEHARKCKLQKYEVPAAITLCKEV 695
Cdd:PRK06814 1060 L-HAAVSIPDARKGERIIL-----------LTTASDATRA---AFLAHAKAAGASELMVPAEIITIDEI 1113
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
282-636 |
1.10e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 89.95 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 282 EHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHV--FELVAESVCLMTGVpig 359
Cdd:PRK06145 142 PQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVgaFDLPGIAVLWVGGT--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 360 ystpltlidtsSKIKRGCKGDATVL-----KPTCMTSVPLILDRI-SKGINDKVNSGSafkkslfkflyqykVKW-VQRG 432
Cdd:PRK06145 219 -----------LRIHREFDPEAVLAaierhRLTCAWMAPVMLSRVlTVPDRDRFDLDS--------------LAWcIGGG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 433 YKTPLIDKLVFKKVakLMGGKvriimsggaplsadtheqiktclcleLIQGYGLTETTSGATVMDY-RDM-TYGRTGGPL 510
Cdd:PRK06145 274 EKTPESRIRDFTRV--FTRAR--------------------------YIDAYGLTETCSGDTLMEAgREIeKIGSTGRAL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 511 TVCDIRLVNwEEGNYRVTNKpypQGEVLIGGECVSQGYYKLPGKTNEDFFEEdgqrWFKTGDIGEIQADGVLKIIDRKKD 590
Cdd:PRK06145 326 AHVEIRIAD-GAGRWLPPNM---KGEICMRGPKVTKGYWKDPEKTAEAFYGD----WFRSGDVGYLDEEGFLYLTDRKKD 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 442622933 591 LVkLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQY---TVALVVPN 636
Cdd:PRK06145 398 MI-ISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWgerITAVVVLN 445
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
263-637 |
3.73e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.84 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 263 GVKILPFNQVVKTGQDSKFEHVPPK--GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLA 340
Cdd:PRK12467 628 GLRSLCLDEPADLLCGYSGHNPEVAldPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFA 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 341 HVFELVAESVCLMTGVPIGYSTPLTLIDTSSKIKRGCKGDATVLKptcmtSVPlildriskgindkvnsgsafkkSLFKF 420
Cdd:PRK12467 708 FDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLK-----IVP----------------------SHLQA 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 421 LYQYKVKWVQRGYKTPLIdklvfkkvaklmggkvriimsGGAPLSADTHEQIKTC-LCLELIQGYGLTETTSGATVMDY- 498
Cdd:PRK12467 761 LLQASRVALPRPQRALVC---------------------GGEALQVDLLARVRALgPGARLINHYGPTETTVGVSTYELs 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 499 ---RDMTYGRTGGPLTvcdirlvnwEEGNYRVTN--KPYP---QGEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQR 566
Cdd:PRK12467 820 deeRDFGNVPIGQPLA---------NLGLYILDHylNPVPvgvVGELYIGGAGLARGYHRRPALTAERFvpdpFGADGGR 890
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622933 567 WFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIEN---ICVYGDPTKQYtVALVVPNQ 637
Cdd:PRK12467 891 LYRTGDLARYRADGVIEYLGRMDHQVKIR-GFRIELGEIEARLLAQPGVREavvLAQPGDAGLQL-VAYLVPAA 962
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
284-695 |
5.38e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 87.61 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHV--FELVAESVCLMTGVPI--G 359
Cdd:PRK06839 144 VEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIggIGLFAFPTLFAGGVIIvpR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 360 YSTP---LTLIDTSskikrgckgdatvlKPTCMTSVPLILDRISKGINdkvnsgsafkkslfkflyqykvkwvqrgYKTP 436
Cdd:PRK06839 224 KFEPtkaLSMIEKH--------------KVTVVMGVPTIHQALINCSK----------------------------FETT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 437 LIDKlvfkkvaklmggkVRIIMSGGAPLSADTHEQIKTcLCLELIQGYGLTETTSGATVMDYRDMTY--GRTGGPLTVCD 514
Cdd:PRK06839 262 NLQS-------------VRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSPTVFMLSEEDARRkvGSIGKPVLFCD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 515 IRLVNWEEGNYrvtnKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkL 594
Cdd:PRK06839 328 YELIDENKNKV----EVGEVGELLIRGPNVMKEYWNRPDATEETI--QDG--WLCTGDLARVDEDGFVYIVGRKKEMI-I 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 595 QAGEYVSLGKVESELKTCGIIENICVYGDPTKQY---TVALVVPNQnhleelaqkhglgdksfeelcSSPIIEkailKEI 671
Cdd:PRK06839 399 SGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWgeiPIAFIVKKS---------------------SSVLIE----KDV 453
|
410 420
....*....|....*....|....
gi 442622933 672 AEHARKcKLQKYEVPAAITLCKEV 695
Cdd:PRK06839 454 IEHCRL-FLAKYKIPKEIVFLKEL 476
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
286-639 |
6.29e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 87.80 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 286 PKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHvfelvaesvclMTGVPIGYSTPLT 365
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAH-----------QTGFMYGLMMPVM 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 366 LidtsskikrgckGDATVLKPTCmtSVPLILDRI-SKGINDKVNSgsafkkslfkflyqykvkwvqrgykTPLIDKLVfk 444
Cdd:PRK13295 263 L------------GATAVLQDIW--DPARAAELIrTEGVTFTMAS-------------------------TPFLTDLT-- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 445 KVAKLMGGKV---RIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTET--TSGATVMDYRDMTYGRTGGPLTVCDIRLVN 519
Cdd:PRK13295 302 RAVKESGRPVsslRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENgaVTLTKLDDPDERASTTDGCPLPGVEVRVVD 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 520 weegnyrVTNKPYPQGE---VLIGGECVSQGYYKLPGKTNEDFfeeDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQA 596
Cdd:PRK13295 382 -------ADGAPLPAGQigrLQVRGCSNFGGYLKRPQLNGTDA---DG--WFDTGDLARIDADGYIRISGRSKDVI-IRG 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 442622933 597 GEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALVVPNQNH 639
Cdd:PRK13295 449 GENIPVVEIEALLYRHPAIAQVAIVAYPDErlgERACAFVVPRPGQ 494
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
277-635 |
7.62e-18 |
|
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: 86.99 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 277 QDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDmvpIYPDDVLIGFLPLA------HVFELVAEsv 350
Cdd:cd12115 93 EDAQARLVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAA---AFSAEELAGVLASTsicfdlSVFELFGP-- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 351 cLMTG---VPIgySTPLTLIDTSSKikrgckGDATVLkptcmTSVPlildriskgindkvnsgSAFKkSLFKflyqykvk 427
Cdd:cd12115 168 -LATGgkvVLA--DNVLALPDLPAA------AEVTLI-----NTVP-----------------SAAA-ELLR-------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 428 wvqrgyktplIDKLVfkkvaklmgGKVRIIMSGGAPLSADTHEQIKTCLCLELIQG-YGLTETTSGATVM-----DYRDM 501
Cdd:cd12115 208 ----------HDALP---------ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNlYGPSEDTTYSTVApvppgASGEV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 502 TYGRTGGPLTVcdirLVNWEEGNyrvtnkPYPQ---GEVLIGGECVSQGYYKLPGKTNEDFF---EEDGQRWFKTGDIGE 575
Cdd:cd12115 269 SIGRPLANTQA----YVLDRALQ------PVPLgvpGELYIGGAGVARGYLGRPGLTAERFLpdpFGPGARLYRTGDLVR 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622933 576 IQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICV--YGD-PTKQYTVALVVP 635
Cdd:cd12115 339 WRPDGLLEFLGRADNQVKVR-GFRIELGEIEAALRSIPGVREAVVvaIGDaAGERRLVAYIVA 400
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
269-609 |
1.11e-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: 86.58 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 269 FNQVVKTGqDSKFEHVPPKGDDIAIIM-YTSGSTGTPKGVLLSHK----NCIATMKGF-VDMVPIYpddvlIGFLPLAH- 341
Cdd:cd12118 113 YEDLLAEG-DPDFEWIPPADEWDPIALnYTSGTTGRPKGVVYHHRgaylNALANILEWeMKQHPVY-----LWTLPMFHc 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 342 --------VFELVAESVCLMTgvpIGYSTPLTLIDTsskikrgckgdatvLKPTCMTSVPLILDRIskgindkVNSGSAF 413
Cdd:cd12118 187 ngwcfpwtVAAVGGTNVCLRK---VDAKAIYDLIEK--------------HKVTHFCGAPTVLNML-------ANAPPSD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 414 KKSLfkflyqykvkwvqrgyktplidklvfkkvaklmGGKVRIiMSGGAPLSADTHEQIKTcLCLELIQGYGLTETTSGA 493
Cdd:cd12118 243 ARPL---------------------------------PHRVHV-MTAGAPPPAAVLAKMEE-LGFDVTHVYGLTETYGPA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 494 TV-----------MDYRDMTYGRTG------GPLTVCDirlvnweegnyRVTNKPYPQ-----GEVLIGGECVSQGYYKL 551
Cdd:cd12118 288 TVcawkpewdelpTEERARLKARQGvryvglEEVDVLD-----------PETMKPVPRdgktiGEIVFRGNIVMKGYLKN 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622933 552 PGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESEL 609
Cdd:cd12118 357 PEATAEAF--RGG--WFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVL 409
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
289-592 |
1.12e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 86.77 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVA-ESVCLMTGVpigystPLTLI 367
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAfHLAPLIAGM------NQYLM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 DTSSKIKRgckgdatvlkPTcmtsvpLILDRISKginDKVNSGSAfkkslFKFLYQYkvkwvqrgyktpLIDKLVFKKVA 447
Cdd:cd05908 180 PTRLFIRR----------PI------LWLKKASE---HKATIVSS-----PNFGYKY------------FLKTLKPEKAN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 448 KLMGGKVRIIMSGGAPLSAD-THEQIKTCLCLELIQG-----YGLTETTSGATV-----------MDYRDMTYGR----- 505
Cdd:cd05908 224 DWDLSSIRMILNGAEPIDYElCHEFLDHMSKYGLKRNailpvYGLAEASVGASLpkaqspfktitLGRRHVTHGEpepev 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 506 ------------TGGPLTVCDIRLVNWEegnyrvtNKPYPQ---GEVLIGGECVSQGYYKLPGKTNEdFFEEDGqrWFKT 570
Cdd:cd05908 304 dkkdsecltfveVGKPIDETDIRICDED-------NKILPDgyiGHIQIRGKNVTPGYYNNPEATAK-VFTDDG--WLKT 373
|
330 340
....*....|....*....|..
gi 442622933 571 GDIGEIQaDGVLKIIDRKKDLV 592
Cdd:cd05908 374 GDLGFIR-NGRLVITGREKDII 394
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
284-645 |
1.88e-17 |
|
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: 85.79 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLA---HVFELVaesVCLMTG----- 355
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSfdvSVWELF---WPLVAGarlvv 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 356 -VPIGYSTPLTLIDTsskIKRGCkgdatVlkpTCMTSVPLILDriskgindkvnsgsAFkkslfkflyqykVKWVQRGYK 434
Cdd:cd17646 210 aRPGGHRDPAYLAAL---IREHG-----V---TTCHFVPSMLR--------------VF------------LAEPAAGSC 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 435 TPLidklvfkkvaklmggkvRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRT---GGPLT 511
Cdd:cd17646 253 ASL-----------------RRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpiGRPVP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 512 VCDIRLVNwEEGNyrvtnkPYPQ---GEVLIGGECVSQGYYKLPGKTNEDF----FeEDGQRWFKTGDIGEIQADGVLKI 584
Cdd:cd17646 316 NTRLYVLD-DALR------PVPVgvpGELYLGGVQLARGYLGRPALTAERFvpdpF-GPGSRMYRTGDLARWRPDGALEF 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622933 585 IDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVY---GDPTKQYTVALVVPNQNHLEELAQ 645
Cdd:cd17646 388 LGRSDDQVKIR-GFRVEPGEIEAALAAHPAVTHAVVVaraAPAGAARLVGYVVPAAGAAGPDTA 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
262-712 |
3.61e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.75 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 262 EGVKILPFNQV--VKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPL 339
Cdd:PRK12467 1689 DGLRSLVLDQEddWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSF 1768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 340 A---HVFELVAEsvcLMTGVPIGYSTPLTLIDTSSKIKRGCKGDATVLKptcmtsvplildriskgindkvnsgsaFKKS 416
Cdd:PRK12467 1769 AfdvSVWELFWP---LINGARLVIAPPGAHRDPEQLIQLIERQQVTTLH---------------------------FVPS 1818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 417 LFKFLYQykvkwVQRGYKTPLidklvfkkvaklmggKVRIIMSGGAPLSADTHEQIKTCL-CLELIQGYGLTETTSGAT- 494
Cdd:PRK12467 1819 MLQQLLQ-----MDEQVEHPL---------------SLRRVVCGGEALEVEALRPWLERLpDTGLFNLYGPTETAVDVTh 1878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 495 -VMDYRDMTyGRTGGPLTVCDIRLvnweeGNYRVTNKPYPQ-----GEVLIGGECVSQGYYKLPGKTNEDF----FEEDG 564
Cdd:PRK12467 1879 wTCRRKDLE-GRDSVPIGQPIANL-----STYILDASLNPVpigvaGELYLGGVGLARGYLNRPALTAERFvadpFGTVG 1952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 565 QRWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVY---GDPTKQYtVALVVPNqnhle 641
Cdd:PRK12467 1953 SRLYRTGDLARYRADGVIEYLGRIDHQVKIR-GFRIELGEIEARLREQGGVREAVVIaqdGANGKQL-VAYVVPT----- 2025
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622933 642 elaqkhglgDKSFEELCSSPIIEKAILKEiaehARKCKLQKYEVPAAITLCKEVwsPdmglVTAAFKLKRK 712
Cdd:PRK12467 2026 ---------DPGLVDDDEAQVALRAILKN----HLKASLPEYMVPAHLVFLARM--P----LTPNGKLDRK 2077
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
277-645 |
4.23e-17 |
|
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: 84.79 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 277 QDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELVAESVCLmtgv 356
Cdd:cd17644 94 EDAQISVLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIA--FDVAAEEIYV---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 357 pigystplTLidtsskikrgCKGDATVLKPTCM-TSVPLILDRISKgindkvnsgsaFKKSLFKFLYQYKVKWVQRGYKT 435
Cdd:cd17644 168 --------TL----------LSGATLVLRPEEMrSSLEDFVQYIQQ-----------WQLTVLSLPPAYWHLLVLELLLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 436 --PLIDKLvfkkvaklmggkvRIIMSGGAPLSADTHEQIKTCLC--LELIQGYGLTETTSGATVMDYRDMTYGRT----- 506
Cdd:cd17644 219 tiDLPSSL-------------RLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNItsvpi 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 507 GGPLT-----VCDIRLvnweegnyrvtnKPYP---QGEVLIGGECVSQGYYKLPGKTNEDF----FEE-DGQRWFKTGDI 573
Cdd:cd17644 286 GRPIAntqvyILDENL------------QPVPvgvPGELHIGGVGLARGYLNRPELTAEKFishpFNSsESERLYKTGDL 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622933 574 GEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVYG--DPTKQ-YTVALVVP---NQNHLEELAQ 645
Cdd:cd17644 354 ARYLPDGNIEYLGRIDNQVKIR-GFRIELGEIEAVLSQHNDVKTAVVIVreDQPGNkRLVAYIVPhyeESPSTVELRQ 430
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
146-609 |
5.18e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 84.81 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 146 WKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCF---KQAMPIVTVY--ATLgddgvAHCITETEVT 220
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAwlgAIAVPINTALrgPQL-----EHILRNSGAR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 221 TVITSHDLLPKFKTLLDK-CPLVKTIIYIEDQLQKTETtgfkeGVKILPFNQVvktgqDSKFEHVPPKGDDIAIIMYTSG 299
Cdd:PRK06155 121 LLVVEAALLAALEAADPGdLPLPAVWLLDAPASVSVPA-----GWSTAPLPPL-----DAPAPAAAVQPGDTAAILYTSG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 300 STGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGvpigystpltlidtsskikrgckg 379
Cdd:PRK06155 191 TTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAG------------------------ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 380 dAT-VLKPtcmtsvplildRISkgindkvnsGSAFKKSLFKflYQYKVKWVQrGYKTPLIDKLvfKKVAKLMGGKVRIIM 458
Cdd:PRK06155 247 -ATyVLEP-----------RFS---------ASGFWPAVRR--HGATVTYLL-GAMVSILLSQ--PARESDRAHRVRVAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 459 SGGAPlsADTHEQIKTCLCLELIQGYGLTETTS--GATVMDYRDMTYGRTGGPLTvcdIRLVNwEEGNyrvtnkPYPQGE 536
Cdd:PRK06155 301 GPGVP--AALHAAFRERFGVDLLDGYGSTETNFviAVTHGSQRPGSMGRLAPGFE---ARVVD-EHDQ------ELPDGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 537 VligGECV---------SQGYYKLPGKTNEDFfeedGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVES 607
Cdd:PRK06155 369 P---GELLlradepfafATGYFGMPEKTVEAW----RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRR-GENISSFEVEQ 440
|
..
gi 442622933 608 EL 609
Cdd:PRK06155 441 VL 442
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
271-609 |
6.50e-17 |
|
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: 83.90 E-value: 6.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 271 QVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELVAESV 350
Cdd:cd17653 87 QAILRTSGATLLLTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIA--FDACIGEI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 351 --CLMTGVPIGYSTPLtliDTSSKIKRGCkgDATVLKPTCMTSVPLildriskgindkvnsgsafkkslfkflyqykvkw 428
Cdd:cd17653 165 fsTLCNGGTLVLADPS---DPFAHVARTV--DALMSTPSILSTLSP---------------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 429 vqRGYKTplidklvfkkvaklmggkVRIIMSGGAPLSADTHEQIKTCLCLelIQGYGLTETTSGATVMDYRDMTYGRTGG 508
Cdd:cd17653 206 --QDFPN------------------LKTIFLGGEAVPPSLLDRWSPGRRL--YNAYGPTECTISSTMTELLPGQPVTIGK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 509 PLTVCDIRLVnwEEGNYRVtnkPYPQ-GEVLIGGECVSQGYYKLPGKTNEDFFE---EDGQRWFKTGDIGEIQADGVLKI 584
Cdd:cd17653 264 PIPNSTCYIL--DADLQPV---PEGVvGEICISGVQVARGYLGNPALTASKFVPdpfWPGSRMYRTGDYGRWTEDGGLEF 338
|
330 340
....*....|....*....|....*
gi 442622933 585 IDRKKDLVKLQaGEYVSLGKVESEL 609
Cdd:cd17653 339 LGREDNQVKVR-GFRINLEEIEEVV 362
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
134-727 |
7.94e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 84.71 E-value: 7.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 134 RVF-KKYNLGDYKWK--TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTV---YATLgd 207
Cdd:PRK12582 65 RPWlAQREPGHGQWRkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLM-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 208 dgvahcitetevttvitSHDLLpKFKTLLDkcpLVK-TIIYIED-----------QLQKTE---TTGFKEGVKILPFNQV 272
Cdd:PRK12582 143 -----------------SHDHA-KLKHLFD---LVKpRVVFAQSgapfaralaalDLLDVTvvhVTGPGEGIASIAFADL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 273 VKT----GQDSKFEHVPPkgDDIAIIMYTSGSTGTPKGVLLSHKN-C--IATMKGFVDMVPIYPDDVLIGFLPLAHVFEL 345
Cdd:PRK12582 202 AATpptaAVAAAIAAITP--DTVAKYLFTSGSTGMPKAVINTQRMmCanIAMQEQLRPREPDPPPPVSLDWMPWNHTMGG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 346 VAesvcLMTGVPIGYST-------PLT-LIDTSSKIKRGCKgdatvlkPTCMTSVPLILDRISKGI-NDKvnsgsAFKKS 416
Cdd:PRK12582 280 NA----NFNGLLWGGGTlyiddgkPLPgMFEETIRNLREIS-------PTVYGNVPAGYAMLAEAMeKDD-----ALRRS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 417 LFKflyqykvkwvqrgyktplidklvfkkvaklmggKVRIIMSGGAPLSADTHEQIK------TCLCLELIQGYGLTETt 490
Cdd:PRK12582 344 FFK---------------------------------NLRLMAYGGATLSDDLYERMQalavrtTGHRIPFYTGYGATET- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 491 SGATVMDYRDMT-YGRTGGPLTVCDIRLVnweegnyrvtnkpyPQG---EVLIGGECVSQGYYKLPGKTnEDFFEEDGqr 566
Cdd:PRK12582 390 APTTTGTHWDTErVGLIGLPLPGVELKLA--------------PVGdkyEVRVKGPNVTPGYHKDPELT-AAAFDEEG-- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 567 WFKTGDIGEI--QADGVLKII--DRKKDLVKLQAGEYVSLGKVESE-LKTC-GIIENICVYGDpTKQYTVALVVPNQNHL 640
Cdd:PRK12582 453 FYRLGDAARFvdPDDPEKGLIfdGRVAEDFKLSTGTWVSVGTLRPDaVAACsPVIHDAVVAGQ-DRAFIGLLAWPNPAAC 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 641 EELAQKHglgDKSFEELCSSPIIeKAILKE-IAEHARKCKLQKYEVpAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQ 719
Cdd:PRK12582 532 RQLAGDP---DAAPEDVVKHPAV-LAILREgLSAHNAEAGGSSSRI-ARALLMTEPPSIDAGEITDKGYINQRAVLERRA 606
|
....*...
gi 442622933 720 HDINRMYA 727
Cdd:PRK12582 607 ALVERLYA 614
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
270-635 |
9.87e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.39 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 270 NQVVKTGQDSKFEHVPPK---GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELV 346
Cdd:PRK12316 3174 VLDLDRGDENYAEANPAIrtmPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS--FDVF 3251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 347 AESVclmtgvpigySTPLTlidtsskikrgcKGDATVLKPTCMTSVPlildrisKGINDKVNSGSAFkkslfkflyqykv 426
Cdd:PRK12316 3252 VEEL----------FWPLM------------SGARVVLAGPEDWRDP-------ALLVELINSEGVD------------- 3289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 427 kwVQRGYKTPLIDKLVFKKVAKLMGgkVRIIMSGGAPLSADTheQIKTCLCLELIQGYGLTETTSGATVMDYRDMT--YG 504
Cdd:PRK12316 3290 --VLHAYPSMLQAFLEEEDAHRCTS--LKRIVCGGEALPADL--QQQVFAGLPLYNLYGPTEATITVTHWQCVEEGkdAV 3363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 505 RTGGPLTVCDIRLVNweegnyrVTNKPYPQG---EVLIGGECVSQGYYKLPGKTNEDFFEE---DGQRWFKTGDIGEIQA 578
Cdd:PRK12316 3364 PIGRPIANRACYILD-------GSLEPVPVGalgELYLGGEGLARGYHNRPGLTAERFVPDpfvPGERLYRTGDLARYRA 3436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622933 579 DGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVYGDPTKQyTVALVVP 635
Cdd:PRK12316 3437 DGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVP 3491
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
148-635 |
1.41e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.62 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQA---MPIVTVYAT------LGDDGVAhcitete 218
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGgayVPLDPNYPAerlaymLEDSGAA------- 2102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 219 vttvitshdLLPKFKTLLDKCPLvktiiyiedqlqktettgfKEGVKILPFNQVVKTgQDSKFEHVPPK--GDDIAIIMY 296
Cdd:PRK12316 2103 ---------LLLTQRHLLERLPL-------------------PAGVARLPLDRDAEW-ADYPDTAPAVQlaGENLAYVIY 2153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 297 TSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELVAEsvclmtgvpiGYSTPLtlidtsskikrg 376
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFS--FDGAHE----------QWFHPL------------ 2209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 377 CKGDATVLKPTCMTSVPLILDRISK-GIndkvnSGSAFKKSlfkFLYQYkVKWVQRGYKTPlidklvfkkvaklmggKVR 455
Cdd:PRK12316 2210 LNGARVLIRDDELWDPEQLYDEMERhGV-----TILDFPPV---YLQQL-AEHAERDGRPP----------------AVR 2264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 456 IIMSGGAPLSADTHEQIKTCLCLE-LIQGYGLTETTSGATVMDYR-----DMTYGRTGGPLT-----VCDIRLvnweegn 524
Cdd:PRK12316 2265 VYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRpqdpcGAAYVPIGRALGnrrayILDADL------- 2337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 525 yrvtnKPYPQ---GEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQaG 597
Cdd:PRK12316 2338 -----NLLAPgmaGELYLGGEGLARGYLNRPGLTAERFvpdpFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIR-G 2411
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 442622933 598 EYVSLGKVESELKTC-GIIENICVYGD-PTKQYTVALVVP 635
Cdd:PRK12316 2412 FRIELGEIEARLQAHpAVREAVVVAQDgASGKQLVAYVVP 2451
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
289-634 |
1.64e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 83.33 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELvaeSVC----LMTGVPIGYS-TP 363
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGF---NSCtlfpLLSGVPVVFAyNP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LT------LIDTSskikrgckgdatvlKPTCMTSVPLILDRISKGINDK----------VNSGSAFKKSLFKflyqykvk 427
Cdd:PRK06334 260 LYpkkiveMIDEA--------------KVTFLGSTPVFFDYILKTAKKQesclpslrfvVIGGDAFKDSLYQ-------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 428 wvqrgyktplidklvfkkvaklmggkvriimsggaplsadthEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGR-T 506
Cdd:PRK06334 318 ------------------------------------------EALKTFPHIQLRQGYGTTECSPVITINTVNSPKHEScV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 507 GGPLTVCDIRLVNWEegnyrvTNKPYPQGE---VLIGGECVSQGYykLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLK 583
Cdd:PRK06334 356 GMPIRGMDVLIVSEE------TKVPVSSGEtglVLTRGTSLFSGY--LGEDFGQGFVELGGETWYVTGDLGYVDRHGELF 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442622933 584 IIDRKKDLVKLqAGEYVSLGKVESELktcgiIENicvYGDPTKQYTVALVV 634
Cdd:PRK06334 428 LKGRLSRFVKI-GAEMVSLEALESIL-----MEG---FGQNAADHAGPLVV 469
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
144-642 |
2.05e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 82.90 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 144 YKWKTFTEAERTAAnfgRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTV----------YAtLGDDGVaHC 213
Cdd:PRK12583 46 YTWRQLADAVDRLA---RGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNInpayraseleYA-LGQSGV-RW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 214 ITETEVTTVITSH----DLLPKFKT------LLDKCPLVKTIIYiedqLQKTETTGFKEGVKILPFNQVVkTGQDSKFEH 283
Cdd:PRK12583 121 VICADAFKTSDYHamlqELLPGLAEgqpgalACERLPELRGVVS----LAPAPPPGFLAWHELQARGETV-SREALAERQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELV-AESVCLMTG----VPI 358
Cdd:PRK12583 196 ASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVlANLGCMTVGaclvYPN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 359 GYSTPLTLIDTSSKIKrgCkgdatvlkpTCMTSVPlildriskgindkvnsgsafkkslfkflyqykvkwvqrgykTPLI 438
Cdd:PRK12583 276 EAFDPLATLQAVEEER--C---------TALYGVP-----------------------------------------TMFI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 439 DKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQ-IKTCLCLELIQGYGLTET------TSGATVMDYRDMTYGRTGGPLT 511
Cdd:PRK12583 304 AELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRvMDEMHMAEVQIAYGMTETspvslqTTAADDLERRVETVGRTQPHLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 512 VcdiRLVNwEEGNyrvTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfEEDGqrWFKTGDIGEIQADGVLKIIDRKKDL 591
Cdd:PRK12583 384 V---KVVD-PDGA---TVPRGEIGELCTRGYSVMKGYWNNPEATAESI-DEDG--WMHTGDLATMDEQGYVRIVGRSKDM 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622933 592 VkLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQY---TVALVV--PNQNHLEE 642
Cdd:PRK12583 454 I-IRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYgeeIVAWVRlhPGHAASEE 508
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
290-591 |
2.55e-16 |
|
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: 80.62 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESV-CLMTGVPIgysTPLTLID 368
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVaCLLTGATV---VPVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 369 TSSKIKRGCKGDATVL--KPTCMTSvplILDRiskgindkvnsgsafkkslfkflyqykvkwvqrgyktPLIDKLvfkKV 446
Cdd:cd17638 78 VDAILEAIERERITVLpgPPTLFQS---LLDH-------------------------------------PGRKKF---DL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 447 AKLmggkvRIIMSGGAPLSADTHEQIKTCLCLELI-QGYGLTETTSgATVMDYRD--MTYGRTGG-PLTVCDIRLVNwee 522
Cdd:cd17638 115 SSL-----RAAVTGAATVPVELVRRMRSELGFETVlTAYGLTEAGV-ATMCRPGDdaETVATTCGrACPGFEVRIAD--- 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622933 523 gnyrvtnkpypQGEVLIGGECVSQGYYKLPGKTNEDFfEEDGqrWFKTGDIGEIQADGVLKIIDRKKDL 591
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAEAI-DADG--WLHTGDVGELDERGYLRITDRLKDM 240
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
205-646 |
2.66e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.91 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 205 LGDDGVAHCITETEVTTVITSHDLLPKFKTLLDKCPLVKTIIYIEDQLQKTETTGFKEGVKILPFNQVVKtGQDSKFEHV 284
Cdd:PRK05620 98 LMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVYDWP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 285 PPKGDDIAIIMYTSGSTGTPKGVLLSHKN--------------CIATMKGFVDMVPIYpdDVLIGFLPLAhvfelvaesv 350
Cdd:PRK05620 177 ELDETTAAAICYSTGTTGAPKGVVYSHRSlylqslslrttdslAVTHGESFLCCVPIY--HVLSWGVPLA---------- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 351 CLMTGvpigysTPLTLIDTSSkikrgckgDATVLKPTCMTSVPlildRISKGIndkvnsgsafkkslfkflyqyKVKWVQ 430
Cdd:PRK05620 245 AFMSG------TPLVFPGPDL--------SAPTLAKIIATAMP----RVAHGV---------------------PTLWIQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 431 RgyktplidkLV--FKKVAKLMggKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETT------------SGATVM 496
Cdd:PRK05620 286 L---------MVhyLKNPPERM--SLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSpvgtvarppsgvSGEARW 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 497 DYRdMTYGRTGGPLtvcDIRLVNweEGNYRVTNKpYPQGEVLIGGECVSQGYYKLPGKTN---------------EDFFE 561
Cdd:PRK05620 355 AYR-VSQGRFPASL---EYRIVN--DGQVMESTD-RNEGEIQVRGNWVTASYYHSPTEEGggaastfrgedvedaNDRFT 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 562 EDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKVESELKTCGIIENICVYGDPTKQY-----TVALVVPN 636
Cdd:PRK05620 428 ADG--WLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWgerplAVTVLAPG 504
|
490
....*....|
gi 442622933 637 QNHLEELAQK 646
Cdd:PRK05620 505 IEPTRETAER 514
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
289-711 |
4.25e-16 |
|
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: 81.37 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGF-VDMVPIYPDDVLIGFLPLAHVFELvaesvclmTGVPIgysTPLTLi 367
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGL--------GGVLL---FPFGV- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 dtsskikrgckGDATVLKPTcmTSVPLILDRISKgindkvnsgsaFKKSLFkflyqykvkwvqrgYKTPLIDK--LVFKK 445
Cdd:cd05958 165 -----------GASGVLLEE--ATPDLLLSAIAR-----------YKPTVL--------------FTAPTAYRamLAHPD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 446 VAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNwEEGNy 525
Cdd:cd05958 207 AAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGN- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 526 rvtnkPYPQGEV---LIGGEcvsQGYYKLPGKTNEDFFEEDgqrWFKTGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSL 602
Cdd:cd05958 285 -----PVPDGTIgrlAVRGP---TGCRYLADKRQRTYVQGG---WNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 603 GKVESELKTCGIIENICVYGDPTKQytvALVVPnqnhleelaqkhglgdKSFEELCSSPIIEKAILKEIAEHArKCKLQK 682
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDES---RGVVV----------------KAFVVLRPGVIPGPVLARELQDHA-KAHIAP 412
|
410 420
....*....|....*....|....*....
gi 442622933 683 YEVPAAITLCKEVwsPDmglvTAAFKLKR 711
Cdd:cd05958 413 YKYPRAIEFVTEL--PR----TATGKLQR 435
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
289-691 |
7.23e-16 |
|
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: 80.76 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPL---AHVFELVAE-----SVCLMTGVPIGY 360
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPsfdASVWELLMAllagaTLVLAPAEELLP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 361 STPLTLIDTSSKIkrgckgDATVLKPTCMTSVPlildriskgindkvnsgsafkkslfkflyqykvkwvqrgyktplidk 440
Cdd:cd17652 173 GEPLADLLREHRI------THVTLPPAALAALP----------------------------------------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 441 lvfkkVAKLMGGkvRIIMSGGAPLSADTHEQIKTCLCLelIQGYGLTETTSGATVMD-YRDMTYGRTGGPLT-----VCD 514
Cdd:cd17652 200 -----PDDLPDL--RTLVVAGEACPAELVDRWAPGRRM--INAYGPTETTVCATMAGpLPGGGVPPIGRPVPgtrvyVLD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 515 IRLvnweegnyrvtnKPYP---QGEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQADGVLKIIDR 587
Cdd:cd17652 271 ARL------------RPVPpgvPGELYIAGAGLARGYLNRPGLTAERFvadpFGAPGSRMYRTGDLARWRADGQLEFLGR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 588 KKDLVKLQaGEYVSLGKVESELKTC-GIIEnicvygdptkqytvALVVpnqnhleelAQKHGLGDKSFEELCSSPIIEKA 666
Cdd:cd17652 339 ADDQVKIR-GFRIELGEVEAALTEHpGVAE--------------AVVV---------VRDDRPGDKRLVAYVVPAPGAAP 394
|
410 420
....*....|....*....|....*
gi 442622933 667 ILKEIAEHARKcKLQKYEVPAAITL 691
Cdd:cd17652 395 TAAELRAHLAE-RLPGYMVPAAFVV 418
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
290-641 |
7.89e-16 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 81.18 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGfvDMVPIYPDDV----LIGFLPLAHVFELVAesVCLMTGVPIGYSTPLT 365
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCS--SLFSVGPEMIgqvvTLGLIPFFHIYGITG--ICCATLRNKGKVVVMS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 366 LIDTSSKIkrgckgDATVLKPTCMTSV--PLILDRIskgindkvnsgsafkkslfkflyqykvkwvqrgyKTPLIDKLVF 443
Cdd:PLN02330 261 RFELRTFL------NALITQEVSFAPIvpPIILNLV----------------------------------KNPIVEEFDL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 444 KKVaklmggKVRIIMSGGAPLSADTHEQIKTCL-CLELIQGYGLTETTsgATVMDYRDMTYGR-------TGGPLTVCDI 515
Cdd:PLN02330 301 SKL------KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsVGFILPNLEV 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 516 RLVNWEEGNYRVTNKPypqGEVLIGGECVSQGYYKLPGKTNEDFfeeDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQ 595
Cdd:PLN02330 373 KFIDPDTGRSLPKNTP---GELCVRSQCVMQGYYNNKEETDRTI---DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYK 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 442622933 596 aGEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALVVPNQNHLE 641
Cdd:PLN02330 447 -GFQVAPAELEAILLTHPSVEDAAVVPLPDEeagEIPAACVVINPKAKE 494
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
262-674 |
1.25e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 80.32 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 262 EGVKILPFNQVvktgQDSKFEHVPP------KGDDIAIIMYTSGSTGTPKGVLLSHKNCIAtmkgFVD-MVPiypddvli 334
Cdd:PRK04813 114 LGIPVITLDEL----KDIFATGNPYdfdhavKGDDNYYIIFTSGTTGKPKGVQISHDNLVS----FTNwMLE-------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 335 gflplahVFELVAESVCLmTGVPigYSTPLTLIDtsskikrgckgdatvLKPTCMTSVPLILdrISKGINDKvnsgsaFK 414
Cdd:PRK04813 178 -------DFALPEGPQFL-NQAP--YSFDLSVMD---------------LYPTLASGGTLVA--LPKDMTAN------FK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 415 KsLFKFLYQYKVK-WVQrgykTP-LIDklvfkkvaklmggkvriiMSGGAP-LSADTHEQIKTCL-CLE----------- 479
Cdd:PRK04813 225 Q-LFETLPQLPINvWVS----TPsFAD------------------MCLLDPsFNEEHLPNLTHFLfCGEelphktakkll 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 480 -------LIQGYGLTETTSGAT-------VMDYRD---MTYGRTGGPLTVCDIRLVNWEEGNyrvtnkpypQGEVLIGGE 542
Cdd:PRK04813 282 erfpsatIYNTYGPTEATVAVTsieitdeMLDQYKrlpIGYAKPDSPLLIIDEEGTKLPDGE---------QGEIVISGP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 543 CVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQaDGVLKIIDRKKDLVKLqAGEYVSLGKVESELKTCGIIENICV-- 620
Cdd:PRK04813 353 SVSKGYLNNPEKTAEAFFTFDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKL-NGYRIELEEIEQNLRQSSYVESAVVvp 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 442622933 621 -YGDPTKQYTVALVVPNQNHLEELAQkhglgdksfeelcsspiIEKAILKEIAEH 674
Cdd:PRK04813 431 yNKDHKVQYLIAYVVPKEEDFEREFE-----------------LTKAIKKELKER 468
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
141-716 |
1.91e-15 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 79.40 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 141 LGDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHcitetevt 220
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEY-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 221 tvitshdllpkfktlldkcplvktiiyiedQLQKTETTGFkegvkilpfnqvvktgqdskfehVPPKGDDIAIIMYTSGS 300
Cdd:cd05971 73 ------------------------------RLSNSGASAL-----------------------VTDGSDDPALIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 301 TGTPKGVLLSHKnciatmkgfvdmvpiypddVLIGFLP-LAHVFELVAESVCLMTGvPIGYSTPLTLIDtsskikrgckg 379
Cdd:cd05971 100 TGPPKGALHAHR-------------------VLLGHLPgVQFPFNLFPRDGDLYWT-PADWAWIGGLLD----------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 380 datVLKPTCMTSVPLILDRISKgindkvnsgsaFK-KSLFKFLYQYKVKWVqrgYKTPLIDKLV--FKKVAKLMGGKVRI 456
Cdd:cd05971 149 ---VLLPSLYFGVPVLAHRMTK-----------FDpKAALDLMSRYGVTTA---FLPPTALKMMrqQGEQLKHAQVKLRA 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 457 IMSGGAPLSADTHEQIKTCLCLELIQGYGLTE----TTSGATVMDYRDmtyGRTGGPLTVCDIRLVNwEEGNyrvtnkPY 532
Cdd:cd05971 212 IATGGESLGEELLGWAREQFGVEVNEFYGQTEcnlvIGNCSALFPIKP---GSMGKPIPGHRVAIVD-DNGT------PL 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 533 PQGEVliGGECVSQ-------GYYKLPGKTnEDFFEEDgqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKV 605
Cdd:cd05971 282 PPGEV--GEIAVELpdpvaflGYWNNPSAT-EKKMAGD---WLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEI 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 606 ESELKTCGIIENICVYG--DPTKQYTV-ALVVPNQNHLEelaqkhglgdksfeelcsspiiEKAILKEIAEHArKCKLQK 682
Cdd:cd05971 355 EECLLKHPAVLMAAVVGipDPIRGEIVkAFVVLNPGETP----------------------SDALAREIQELV-KTRLAA 411
|
570 580 590
....*....|....*....|....*....|....
gi 442622933 683 YEVPaaitlcKEVWSPDMGLVTAAFKLKRKDIQD 716
Cdd:cd05971 412 HEYP------REIEFVNELPRTATGKIRRRELRA 439
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
289-647 |
2.93e-15 |
|
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: 78.66 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNciatmkgFVDMVPIYPDDVLIGFLPLAHV------FELVAESVC--LMTGVPIGY 360
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRN-------VAHAAHAWRREYELDSFPVRLLqmasfsFDVFAGDFArsLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 361 STPLTLIDTSSKIKRGCKGDATVlkptcMTSVPlildriskgindkvnsgsAFKKSLFKFLYQykvkwvqRGYKTPLIDK 440
Cdd:cd17650 166 CPDEVKLDPAALYDLILKSRITL-----MESTP------------------ALIRPVMAYVYR-------NGLDLSAMRL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 441 LV----------FKKVAKLMGGKVRIIMSggaplsadtheqiktclcleliqgYGLTETTSGATVMDYRDMTYGRT---- 506
Cdd:cd17650 216 LIvgsdgckaqdFKTLAARFGQGMRIINS------------------------YGVTEATIDSTYYEEGRDPLGDSanvp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 507 -GGPLTVCDIRLVNweegnyrVTNKPYP---QGEVLIGGECVSQGYYKLPGKTNEDFFE---EDGQRWFKTGDIGEIQAD 579
Cdd:cd17650 272 iGRPLPNTAMYVLD-------ERLQPQPvgvAGELYIGGAGVARGYLNRPELTAERFVEnpfAPGERMYRTGDLARWRAD 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622933 580 GVLKIIDRKKDLVKLQaGEYVSLGKVESEL-KTCGIIENICVYGDPTKQ------YTVALVVPNQNHLEELAQKH 647
Cdd:cd17650 345 GNVELLGRVDHQVKIR-GFRIELGEIESQLaRHPAIDEAVVAVREDKGGearlcaYVVAAATLNTAELRAFLAKE 418
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
282-628 |
3.63e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 78.70 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 282 EHVPPkgDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVA--ESVCLMTG---V 356
Cdd:PRK09088 130 PSIPP--ERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITsvRPVLAVGGsilV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 357 PIGYSTPLTLidtsskikrGCKGDATvLKPTCMTSVPLILDRISKgindkvnsgsafkkslfkflyqykvkwvQRGYKTP 436
Cdd:PRK09088 208 SNGFEPKRTL---------GRLGDPA-LGITHYFCVPQMAQAFRA----------------------------QPGFDAA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 437 LIDKLVfkkvaklmggkvrIIMSGGAPLSAdthEQIKTCLC--LELIQGYGLTE--TTSGATV-MDYRDMTYGRTGGPLT 511
Cdd:PRK09088 250 ALRHLT-------------ALFTGGAPHAA---EDILGWLDdgIPMVDGFGMSEagTVFGMSVdCDVIRAKAGAAGIPTP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 512 VCDIRLVNwEEGNYRVTNKPypqGEVLIGGECVSQGYYKLPGKTNEDFfeeDGQRWFKTGDIGEIQADGVLKIIDRKKDL 591
Cdd:PRK09088 314 TVQTRVVD-DQGNDCPAGVP---GELLLRGPNLSPGYWRRPQATARAF---TGDGWFRTGDIARRDADGFFWVVDRKKDM 386
|
330 340 350
....*....|....*....|....*....|....*..
gi 442622933 592 VkLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQY 628
Cdd:PRK09088 387 F-ISGGENVYPAEIEAVLADHPGIRECAVVGMADAQW 422
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
288-636 |
3.73e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.21 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELVAESVClmtgvpigysTPLtli 367
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFS--FDGAQERFL----------WTL--- 3300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 dtsskikrgCKGDATVLKPTCMTSvPlilDRISKGINDKVNSGSAFKKSLFKFLYQykvkwvqrgyktplidklvFKKVA 447
Cdd:PRK12467 3301 ---------ICGGCLVVRDNDLWD-P---EELWQAIHAHRISIACFPPAYLQQFAE-------------------DAGGA 3348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 448 KlmGGKVRIIMSGGAPLSADTHEQIKTCLC-LELIQGYGLTETTSGATVMD-----YRDMTYGRTGGPLTVCDIRLVnwe 521
Cdd:PRK12467 3349 D--CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLWKcggdaVCEAPYAPIGRPVAGRSIYVL--- 3423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 522 EGNYrvtnKPYPQG---EVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKL 594
Cdd:PRK12467 3424 DGQL----NPVPVGvagELYIGGVGLARGYHQRPSLTAERFvadpFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKI 3499
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 442622933 595 QaGEYVSLGKVESELKTCGIIENICVYGDPTKQYT--VALVVPN 636
Cdd:PRK12467 3500 R-GFRIELGEIEARLLQHPSVREAVVLARDGAGGKqlVAYVVPA 3542
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
289-593 |
4.28e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 78.87 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVD-MVP---IYPDDVLIGFLPLAHVFELvaESVcLMTGVPIGystpl 364
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPnlyFHSDDVILCVLPMFHIYSL--NSV-LLCGLRVG----- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 365 tlidtsskikrgckgdATVlkptcmtsvpLILDRISKGindkvnsgsafkkSLFKFLYQYKVKWVqrgyktPLIDKLVFK 444
Cdd:PLN02246 251 ----------------AAI----------LIMPKFEIG-------------ALLELIQRHKVTIA------PFVPPIVLA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 445 -----KVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELI-QGYGLTEttSGATVmdyrDMTYGRTGGPLTV----C- 513
Cdd:PLN02246 286 iakspVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE--AGPVL----AMCLAFAKEPFPVksgsCg 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 514 ------DIRLVNWEEGNYRVTNKPypqGEVLIGGECVSQGYYKLPGKTnEDFFEEDGqrWFKTGDIGEIQADGVLKIIDR 587
Cdd:PLN02246 360 tvvrnaELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDPEAT-ANTIDKDG--WLHTGDIGYIDDDDELFIVDR 433
|
....*.
gi 442622933 588 KKDLVK 593
Cdd:PLN02246 434 LKELIK 439
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
289-609 |
4.85e-15 |
|
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: 78.15 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLI--------------GFLPLAHvfelvaesvclmt 354
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWniadpgwakgawssFFGPWLL------------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 355 GVP-IGYstpltlidtsskikRGCKGDATVlkptcmtsvplILDRISK-GINDKVNSGSAFKKslfkflyqykvkWVQrg 432
Cdd:cd05972 148 GATvFVY--------------EGPRFDAER-----------ILELLERyGVTSFCGPPTAYRM------------LIK-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 433 yktPLIDKLVFKKVaklmggkvRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETtsGATVMDYRDMTY--GRTGGPL 510
Cdd:cd05972 189 ---QDLSSYKFSHL--------RLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTET--GLTVGNFPDMPVkpGSMGRPT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 511 TVCDIRLVNwEEGNyrvTNKPYPQGE--VLIGGECVSQGYYKLPGKTnEDFFEEDgqrWFKTGDIGEIQADGVLKIIDRK 588
Cdd:cd05972 256 PGYDVAIID-DDGR---ELPPGEEGDiaIKLPPPGLFLGYVGDPEKT-EASIRGD---YYLTGDRAYRDEDGYFWFVGRA 327
|
330 340
....*....|....*....|.
gi 442622933 589 KDLVKlQAGEYVSLGKVESEL 609
Cdd:cd05972 328 DDIIK-SSGYRIGPFEVESAL 347
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
284-645 |
4.87e-15 |
|
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: 78.54 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHknciATMKGFVDMvpiypddvligflpLAHVFELVAESVCLMTgVPIGYstp 363
Cdd:cd17651 131 PALDADDLAYVIYTSGSTGRPKGVVMPH----RSLANLVAW--------------QARASSLGPGARTLQF-AGLGF--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 ltlidtsskikrgckgDATVLK--PTCMTSVPLILdriskgINDKVNSGSAfkkSLFKFLYQYKVkwvQRGY-KTPLIDK 440
Cdd:cd17651 189 ----------------DVSVQEifSTLCAGATLVL------PPEEVRTDPP---ALAAWLDEQRI---SRVFlPTVALRA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 441 LV-FKKVAKLMGGKVRIIMSGGAPLS--ADTHEQIKTCLCLELIQGYGLTETTS-GATVMDYRDMTYGRT---GGPLTVC 513
Cdd:cd17651 241 LAeHGRPLGVRLAALRYLLTGGEQLVltEDLREFCAGLPGLRLHNHYGPTETHVvTALSLPGDPAAWPAPppiGRPIDNT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 514 DIRLVNwEEGnyrvtnKPYP---QGEVLIGGECVSQGYYKLPGKTNEDFFEED---GQRWFKTGDIGEIQADGVLKIIDR 587
Cdd:cd17651 321 RVYVLD-AAL------RPVPpgvPGELYIGGAGLARGYLNRPELTAERFVPDPfvpGARMYRTGDLARWLPDGELEFLGR 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622933 588 KKDLVKLQaGEYVSLGKVESELKTCGIIENICVYG---DPTKQYTVALVVPNQNH---LEELAQ 645
Cdd:cd17651 394 ADDQVKIR-GFRIELGEIEAALARHPGVREAVVLAredRPGEKRLVAYVVGDPEApvdAAELRA 456
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
288-635 |
9.89e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.85 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLA---HVFELVaesVCLMTGVPIGYSTPL 364
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSfdvSVWEFF---WPLMSGARLVVAAPG 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 365 TLIDTSSKIKRGCKGDATVLKptcmtSVPLILDriskgindkvnsgsAFkkslfkflyqykvkwvqrgyktplidkLVFK 444
Cdd:PRK12316 731 DHRDPAKLVELINREGVDTLH-----FVPSMLQ--------------AF---------------------------LQDE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 445 KVAKLMggKVRIIMSGGAPLSADTHEQIKTCLCL-ELIQGYGLTETTSGATVMDYRDMTyGRT---GGPLTVCDIRLVnw 520
Cdd:PRK12316 765 DVASCT--SLRRIVCSGEALPADAQEQVFAKLPQaGLYNLYGPTEAAIDVTHWTCVEEG-GDSvpiGRPIANLACYIL-- 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 521 eEGNYrvtnKPYPQ---GEVLIGGECVSQGYYKLPGKTNEDFFEE---DGQRWFKTGDIGEIQADGVLKIIDRKKDLVKL 594
Cdd:PRK12316 840 -DANL----EPVPVgvlGELYLAGRGLARGYHGRPGLTAERFVPSpfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 914
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 442622933 595 QaGEYVSLGKVESELKTCGIIENICVYGDPTKQYtVALVVP 635
Cdd:PRK12316 915 R-GLRIELGEIEARLLEHPWVREAAVLAVDGKQL-VGYVVL 953
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
284-606 |
1.12e-14 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.83 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFelvaesvclmtGVPIGYSTP 363
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSF-----------GLTVGLFTP 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LtlidtsskikrgCKGDATVLKPTCM--TSVP-LILDRiskgiNDKVNSG-SAFKKSLFKFLYQYKVkwvqrgyktplid 439
Cdd:PRK08043 429 L------------LTGAEVFLYPSPLhyRIVPeLVYDR-----NCTVLFGtSTFLGNYARFANPYDF------------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 440 klvfkkvaklmgGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATV---MDYRDMTYGRTggpLTVCDIR 516
Cdd:PRK08043 479 ------------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSInvpMAAKPGTVGRI---LPGMDAR 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 517 LVN---WEEGnyrvtnkpypqGEVLIGGECVSQGYYKL--------PGKTNEDFFEEDGqrWFKTGDIGEIQADGVLKII 585
Cdd:PRK08043 544 LLSvpgIEQG-----------GRLQLKGPNIMNGYLRVekpgvlevPTAENARGEMERG--WYDTGDIVRFDEQGFVQIQ 610
|
330 340
....*....|....*....|.
gi 442622933 586 DRKKDLVKLqAGEYVSLGKVE 606
Cdd:PRK08043 611 GRAKRFAKI-AGEMVSLEMVE 630
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
290-592 |
1.34e-14 |
|
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: 75.76 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMV-PIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLID 368
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 369 TSSKIKRGCKGDATVLKPTCMTSVPLILdriskgindkvnsgsafkKSLFKFLYQykvkwvqrgyktplidklvfkkvak 448
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSEL------------------KSANATVPS------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 449 lmggkVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSgATVMDYRD--MTYGRTGGPLTVCDIRLVNweegNYR 526
Cdd:cd17635 119 -----LRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGT-ALCLPTDDdsIEINAVGRPYPGVDVYLAA----TDG 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622933 527 VTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFFEEdgqrWFKTGDIGEIQADGVLKIIDRKKDLV 592
Cdd:cd17635 189 IAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG----WVNTGDLGERREDGFLFITGRSSESI 250
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
270-645 |
1.55e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 77.12 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 270 NQVVKTGQDSKFEHVPpkGDDIAIIMYTSGSTGTPKGVLLSHKN-------CIATMKGFVdmvpiyPDDVliGFL--PLA 340
Cdd:PRK07786 157 DLLAEAGPAHAPVDIP--NDSPALIMYTSGTTGRPKGAVLTHANltgqamtCLRTNGADI------NSDV--GFVgvPLF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 341 HVFELVAESVCLMTGVPigystpltlidtsskikrgckgdaTVLKPTCMTSVPLILDRISKginDKVNsgsafkkSLFKF 420
Cdd:PRK07786 227 HIAGIGSMLPGLLLGAP------------------------TVIYPLGAFDPGQLLDVLEA---EKVT-------GIFLV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 421 LYQYK-VKWVQRGYKTPLidklvfkkvaklmggKVRIIMSGGAPLSADTHEQIKTCLCLELI-QGYGLTETTSGATVMDY 498
Cdd:PRK07786 273 PAQWQaVCAEQQARPRDL---------------ALRVLSWGAAPASDTLLRQMAATFPEAQIlAAFGQTEMSPVTCMLLG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 499 RDM--TYGRTGGPLTVCDIRLVNwEEGNyrvtnkPYPQGEVligGECV------SQGYYKLPGKTNEDFfeeDGQrWFKT 570
Cdd:PRK07786 338 EDAirKLGSVGKVIPTVAARVVD-ENMN------DVPVGEV---GEIVyraptlMSGYWNNPEATAEAF---AGG-WFHS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 571 GDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYT---VALVVPNQN----HLEEL 643
Cdd:PRK07786 404 GDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGevpVAVAAVRNDdaalTLEDL 482
|
..
gi 442622933 644 AQ 645
Cdd:PRK07786 483 AE 484
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
286-662 |
6.08e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 73.96 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 286 PKGDDIAIImYTSGSTGTPKGVLLSHKNCIATMKGFVDMV-PIYPDDVLIGflplahvfeLVAESVCLMTGVPI-----G 359
Cdd:cd05924 1 RSADDLYIL-YTGGTTGMPKGVMWRQEDIFRMLMGGADFGtGEFTPSEDAH---------KAAAAAAGTVMFPApplmhG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 360 YSTPLTLIDTSskikrgckGDATVLKPTCMTSVPLILDRISKginDKVNS----GSAFKKslfkflyqykvkwvqrgykt 435
Cdd:cd05924 71 TGSWTAFGGLL--------GGQTVVLPDDRFDPEEVWRTIEK---HKVTSmtivGDAMAR-------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 436 PLIDKLVFKKVAKLMGgkVRIIMSGGAPLSadthEQIKTCLC-----LELIQGYGLTETTSGATVMDyRDMtyGRTGGPL 510
Cdd:cd05924 120 PLIDALRDAGPYDLSS--LFAISSGGALLS----PEVKQGLLelvpnITLVDAFGSSETGFTGSGHS-AGS--GPETGPF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 511 TVCDIRLVNWEEGNYRVTnkPYPQGEVLIG--GEcVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLKIIDRK 588
Cdd:cd05924 191 TRANPDTVVLDDDGRVVP--PGSGGVGWIArrGH-IPLGYYGDEAKTAETFPEVDGVRYAVPGDRATVEADGTVTLLGRG 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622933 589 KDLVKlQAGEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALVvpnqnhleELAQKHGLGDKSFEELCSSPI 662
Cdd:cd05924 268 SVCIN-TGGEKVFPEEVEEALKSHPAVYDVLVVGRPDErwgQEVVAVV--------QLREGAGVDLEELREHCRTRI 335
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
287-592 |
6.09e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 76.36 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 287 KGDDIAIIMYTSGSTGTPKGVLLSHKNCIAT----MKGFvdMVPIYPDDVLIGFLPLAHVFELVAEsvcLMTgvPIGYST 362
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANeqliRHGF--GIDLNPDDVIVSWLPLYHDMGLIGG---LLQ--PIFSGV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 363 PLTLIDTSSKIKRgckgdatvlkptcmtsvPL-ILDRISKgINDKVNSGSafkkslfKFLYQYKVKWVQRGyktplidkl 441
Cdd:PRK05691 237 PCVLMSPAYFLER-----------------PLrWLEAISE-YGGTISGGP-------DFAYRLCSERVSES--------- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 442 vfkKVAKLMGGKVRIIMSGGAPLSADT----HEQIKTCLCLE--LIQGYGLTETT---------SGATVMDYRDMTYGR- 505
Cdd:PRK05691 283 ---ALERLDLSRWRVAYSGSEPIRQDSlerfAEKFAACGFDPdsFFASYGLAEATlfvsggrrgQGIPALELDAEALARn 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 506 -----TGGPLTVC-------DIRLVNWEEGNYRVTNKpypQGEVLIGGECVSQGYYKLPGKTNEDFFEEDGQRWFKTGDI 573
Cdd:PRK05691 360 raepgTGSVLMSCgrsqpghAVLIVDPQSLEVLGDNR---VGEIWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDL 436
|
330
....*....|....*....
gi 442622933 574 GEIQaDGVLKIIDRKKDLV 592
Cdd:PRK05691 437 GFLR-DGELFVTGRLKDML 454
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
290-642 |
1.82e-13 |
|
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: 73.20 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHK---NCIATMKGFVDMvpIYPDDVLIGFLPlAHVFELVAESVCLmtgvpigystplTL 366
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGsvvNLRTSLSERYFG--RDNGDEAVLFFS-NYVFDFFVEQMTL------------AL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 367 IDtsskikrgckGDATVLKPTCMTSVPlilDRISKGIND-KVNSGSAfkkslfkflyqykvkwvqrgykTP-LIDKLVFK 444
Cdd:cd17648 160 LN----------GQKLVVPPDEMRFDP---DRFYAYINReKVTYLSG----------------------TPsVLQQYDLA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 445 KVAKLmggkvRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYR-----DMTYGRTggpltvcdIRLVN 519
Cdd:cd17648 205 RLPHL-----KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPgdqrfDKSLGRP--------VRNTK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 520 WEEGNYRVtnKPYP---QGEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQ-------RWFKTGDIGEIQADGVLKII 585
Cdd:cd17648 272 CYVLNDAM--KRVPvgaVGELYLGGDGVARGYLNRPELTAERFlpnpFQTEQErargrnaRLYKTGDLVRWLPSGELEYL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622933 586 DRKKDLVKLQaGEYVSLGKVESELKTC-GIIENICVYGD-------PTKQYTVALVVPNQNHLEE 642
Cdd:cd17648 350 GRNDFQVKIR-GQRIEPGEVEAALASYpGVRECAVVAKEdasqaqsRIQKYLVGYYLPEPGHVPE 413
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
286-645 |
4.64e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 71.23 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 286 PKGDDIAIIMYTSGSTGTPKGVLLSHKNCIAT-------MKGfvdmvpiyPDDVLIGfLPLAHVfelvAESVCLMTGVPI 358
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTASadathdrLGG--------PGQWLLA-LPAHHI----AGLQVLVRSVIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 359 GYstpltlidtsskikrgckgdatvlkptcmtsVPLILDrISKG--INDKVNSGSAFKKSlfkflyqykvkwvqRGYKTp 436
Cdd:PRK07824 99 GS-------------------------------EPVELD-VSAGfdPTALPRAVAELGGG--------------RRYTS- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 437 lidkLVFKKVAKLMGGKVRI--------IMSGGAPLSADTHEQIKTcLCLELIQGYGLTETtSGATVMDyrdmtygrtGG 508
Cdd:PRK07824 132 ----LVPMQLAKALDDPAATaalaeldaVLVGGGPAPAPVLDAAAA-AGINVVRTYGMSET-SGGCVYD---------GV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 509 PLTVCDIRLVNweegnyrvtnkpypqGEVLIGGECVSQGYYKLPgktNEDFFEEDGqrWFKTGDIGEIQaDGVLKIIDRK 588
Cdd:PRK07824 197 PLDGVRVRVED---------------GRIALGGPTLAKGYRNPV---DPDPFAEPG--WFRTDDLGALD-DGVLTVLGRA 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 589 KDLVKlQAGEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALVVPNQNHLEELAQ 645
Cdd:PRK07824 256 DDAIS-TGGLTVLPQVVEAALATHPAVADCAVFGLPDDrlgQRVVAAVVGDGGPAPTLEA 314
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
134-727 |
4.82e-13 |
|
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: 72.46 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 134 RVFKKYNLGDYKWKTFT--EAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFK---QAMPIVTVYATLGDD 208
Cdd:cd05921 11 RTWLAEREGNGGWRRVTyaEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYagvPAAPVSPAYSLMSQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 209 --GVAHCITETEVTTVITSHDllPKFKTLLDKC-PLVKTIIYIEDQLQKTETTGFKEGVKILPFNQVvktgqDSKFEHVP 285
Cdd:cd05921 91 laKLKHLFELLKPGLVFAQDA--APFARALAAIfPLGTPLVVSRNAVAGRGAISFAELAATPPTAAV-----DAAFAAVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 286 PkgDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDD--VLIGFLPLAHVFelvaesvclmtGVPIGYStp 363
Cdd:cd05921 164 P--DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTF-----------GGNHNFN-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LTLIDTSS-KIKRG---CKGDATVLK------PTCMTSVPlildrisKGINDKVNS---GSAFKKSLFKflyqykvkwvq 430
Cdd:cd05921 229 LVLYNGGTlYIDDGkpmPGGFEETLRnlreisPTVYFNVP-------AGWEMLVAAlekDEALRRRFFK----------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 431 rgyktplidklvfkkvaklmggKVRIIMSGGAPLSADTHEQI-----KTC-LCLELIQGYGLTETTSGATVMDYRDMTYG 504
Cdd:cd05921 291 ----------------------RLKLMFYAGAGLSQDVWDRLqalavATVgERIPMMAGLGATETAPTATFTHWPTERSG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 505 RTGGPLTVCDIRLVnweegnyrvtnkpyPQG---EVLIGGECVSQGYYKLPGKTNEdFFEEDGqrWFKTGDIGEIqADGV 581
Cdd:cd05921 349 LIGLPAPGTELKLV--------------PSGgkyEVRVKGPNVTPGYWRQPELTAQ-AFDEEG--FYCLGDAAKL-ADPD 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 582 lkiiDRKKDLV---------KLQAGEYVSLG--KVESELKTCGIIENICVYGdPTKQYTVALVVPNQNHLEELAqkhGLG 650
Cdd:cd05921 411 ----DPAKGLVfdgrvaedfKLASGTWVSVGplRARAVAACAPLVHDAVVAG-EDRAEVGALVFPDLLACRRLV---GLQ 482
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622933 651 DKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVpAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQHDINRMYA 727
Cdd:cd05921 483 EASDAEVLRHAKVRAAFRDRLAALNGEATGSSSRI-ARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYA 558
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
276-599 |
5.40e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 72.24 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 276 GQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDV-LIGFlPLAHVFelvaeSVCL-M 353
Cdd:PRK09274 161 GAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIdLPTF-PLFALF-----GPALgM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 354 TGV--PIGYSTPLT-----LIDTsskIKR-GCkgdatvlkpTCMTSVPLILDRISkgindkvnsgsafkkslfkflyQYK 425
Cdd:PRK09274 235 TSVipDMDPTRPATvdpakLFAA---IERyGV---------TNLFGSPALLERLG----------------------RYG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 426 vkwVQRGYKTPlidklvfkkvaklmggKVRIIMSGGAPLSADTHEQIKTCL--CLELIQGYGLTET------TSGATVMD 497
Cdd:PRK09274 281 ---EANGIKLP----------------SLRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpissiESREILFA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 498 YRDMTygRTGG------PLTVCDIRLVnweegnyRVTNKPYPQ------------GEVLIGGECVSQGYYKLPGKTNED- 558
Cdd:PRK09274 342 TRAAT--DNGAgicvgrPVDGVEVRII-------AISDAPIPEwddalrlatgeiGEIVVAGPMVTRSYYNRPEATRLAk 412
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 442622933 559 FFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEY 599
Cdd:PRK09274 413 IPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
289-592 |
6.68e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 71.95 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPD-DVLIGFLPLAHVFELVAE-SVCLMTGVPIGYSTPLT- 365
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFlTVPMYFGAELVKVTPMDf 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 366 LIDTSSKIKRGCKGDATvlkptcMTSVPlildriskgindkvnsgsafkkslfKFLYQYKVKWVQRGYKTPLIDKlvfkk 445
Cdd:PRK07768 232 LRDPLLWAELISKYRGT------MTAAP-------------------------NFAYALLARRLRRQAKPGAFDL----- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 446 vaklmgGKVRIIMSGGAPLSADTHEQiktcLCLE----------LIQGYGLTETTSGAT--------VMDYRD------- 500
Cdd:PRK07768 276 ------SSLRFALNGAEPIDPADVED----LLDAgarfglrpeaILPAYGMAEATLAVSfspcgaglVVDEVDadllaal 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 501 -----MTYGRT------GGPLTVCDIRLVNwEEGNYRVTNKpypQGEVLIGGECVSQGYyklpgkTNEDFFEE--DGQRW 567
Cdd:PRK07768 346 rravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRG---VGVIELRGESVTPGY------LTMDGFIPaqDADGW 415
|
330 340
....*....|....*....|....*
gi 442622933 568 FKTGDIGEIQADGVLKIIDRKKDLV 592
Cdd:PRK07768 416 LDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
148-624 |
9.37e-13 |
|
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: 70.99 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGvahcitetevttvitshd 227
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEA------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 228 llpkfktlldkcplvktiiyIEDQLQKTETtgfkegvkilpfnQVVKTGQdSKFEHVPPKgdDIAIIMYTSGSTGTPKGV 307
Cdd:cd05969 64 --------------------IRDRLENSEA-------------KVLITTE-ELYERTDPE--DPTLLHYTSGTTGTPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 308 LLSHKnciatmkgfvDMVPIYpddvligfLPLAHVFELVAESVCLMTGVPiGYSTpltlidtsskikrgckGDATVLKPT 387
Cdd:cd05969 108 LHVHD----------AMIFYY--------FTGKYVLDLHPDDIYWCTADP-GWVT----------------GTVYGIWAP 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 388 CMTSVPLILDriskgindkvnSGSAFKKSLFKFLYQYKVK-WvqrgYKTPLIDKLVFKK----VAKLMGGKVRIIMSGGA 462
Cdd:cd05969 153 WLNGVTNVVY-----------EGRFDAESWYGIIERVKVTvW----YTAPTAIRMLMKEgdelARKYDLSSLRFIHSVGE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 463 PLSADTHEQIKTCLCLELIQGYGLTETTSGAtVMDY--RDMTYGRTGGPLTVCDIRLVNwEEGNyrvTNKPYPQGEVLI- 539
Cdd:cd05969 218 PLNPEAIRWGMEVFGVPIHDTWWQTETGSIM-IANYpcMPIKPGSMGKPLPGVKAAVVD-ENGN---ELPPGTKGILALk 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 540 -GGECVSQGYYKLPGKTNEDFFeeDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSLGKVESELKTCGIIENI 618
Cdd:cd05969 293 pGWPSMFRGIWNDEERYKNSFI--DG--WYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPAVAEA 367
|
....*.
gi 442622933 619 CVYGDP 624
Cdd:cd05969 368 GVIGKP 373
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
291-620 |
1.85e-12 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 70.19 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 291 IAIIMYTSGSTGTPKGVLLSHKnCIAT-MKGFVDMVPIYPDDVLIGFLPL------AHVFELVAESVCLMTGVPIGYSTP 363
Cdd:cd17654 120 LAYVIHTSGTTGTPKIVAVPHK-CILPnIQHFRSLFNITSEDILFLTSPLtfdpsvVEIFLSLSSGATLLIVPTSVKVLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LTLIDTSSKIKRgckgdATVLKPTcmtsvPLILDRI-SKGINDKVNSGSafkKSLfkflyqykvkwvqrgyktplidklv 442
Cdd:cd17654 199 SKLADILFKRHR-----ITVLQAT-----PTLFRRFgSQSIKSTVLSAT---SSL------------------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 443 fkkvaklmggkvRIIMSGGAPLSADT------HEQIKTclclELIQGYGLTETTSGATVMDYRDMTYGRTGG-PL--TVC 513
Cdd:cd17654 241 ------------RVLALGGEPFPSLVilsswrGKGNRT----RIFNIYGITEVSCWALAYKVPEEDSPVQLGsPLlgTVI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 514 DIRLVNWEEGnyrvtnkpypQGEVLIGGE---CVSQGYYKLPGKTnedffeedgqrWFKTGDIGEIQaDGVLKIIDRKKD 590
Cdd:cd17654 305 EVRDQNGSEG----------TGQVFLGGLnrvCILDDEVTVPKGT-----------MRATGDFVTVK-DGELFFLGRKDS 362
|
330 340 350
....*....|....*....|....*....|
gi 442622933 591 LVKlQAGEYVSLGKVESELKTCGIIENICV 620
Cdd:cd17654 363 QIK-RRGKRINLDLIQQVIESCLGVESCAV 391
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
294-637 |
2.68e-12 |
|
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: 68.59 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 294 IMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIgystpltLIDTSSKI 373
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTF-------IGQRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 374 KRGCKGDATvLKPTCMTSVPLILDRISKgINDKVNsgsafkkslfkflyqykvkwvqrgyktplidklvfkkvaklmggK 453
Cdd:cd17633 78 KSWIRKINQ-YNATVIYLVPTMLQALAR-TLEPES--------------------------------------------K 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 454 VRIIMSGGAPLSADTHEQIKTCLC-LELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNyrvtnkpy 532
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLKNIFPkANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE-------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 533 pQGEVLIGGECVSQGYyklpgkTNEDFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESELKTC 612
Cdd:cd17633 184 -IGKIFVKSEMVFSGY------VRGGFSNPDG--WMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAI 253
|
330 340
....*....|....*....|....*...
gi 442622933 613 GIIENICVYGDPTK---QYTVALVVPNQ 637
Cdd:cd17633 254 PGIEEAIVVGIPDArfgEIAVALYSGDK 281
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
229-601 |
3.03e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.78 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 229 LPKFKTLLDKCPLVKTIIYIEDQLQKTETTgFKEGVKilpFNQVVKtGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVL 308
Cdd:PRK06018 122 VPILEKIADKLPSVERYVVLTDAAHMPQTT-LKNAVA---YEEWIA-EADGDFAWKTFDENTAAGMCYTSGTTGDPKGVL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 309 LSHKNCI--ATMKGFVDMVPIYPDDVLIGFLPLAHvfelvAESVclmtgvPIGYSTPLTlidTSSKIKRGCKGDATvlkp 386
Cdd:PRK06018 197 YSHRSNVlhALMANNGDALGTSAADTMLPVVPLFH-----ANSW------GIAFSAPSM---GTKLVMPGAKLDGA---- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 387 tcmtSVPLILDriskgiNDKVnSGSAFKKSLFKFLYQYKVKwvqRGYKTPLIDKLVfkkvaklMGGkvriimsggaplSA 466
Cdd:PRK06018 259 ----SVYELLD------TEKV-TFTAGVPTVWLMLLQYMEK---EGLKLPHLKMVV-------CGG------------SA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 467 DTHEQIKTCL--CLELIQGYGLTET----TSGATVMDYRDMTY----------GRTggPLTVcDIRLVNwEEGNyRVTNK 530
Cdd:PRK06018 306 MPRSMIKAFEdmGVEVRHAWGMTEMsplgTLAALKPPFSKLPGdarldvlqkqGYP--PFGV-EMKITD-DAGK-ELPWD 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622933 531 PYPQGEVLIGGECVSQGYYKLPGKtnedFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVS 601
Cdd:PRK06018 381 GKTFGRLKVRGPAVAAAYYRVDGE----ILDDDG--FFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWIS 444
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
455-637 |
3.05e-12 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 69.25 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 455 RIIMSGGAP-----LSADTHEQIKTCLCleliqgYGLTETTSGATVMDYRDMTYGR--TGGPLTvcdirlvnweegNYRV 527
Cdd:PRK07445 233 RTILLGGAPawpslLEQARQLQLRLAPT------YGMTETASQIATLKPDDFLAGNnsSGQVLP------------HAQI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 528 TNKPYPQGEVLIGGECVSQGYYklPgktneDFFeeDGQRWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVES 607
Cdd:PRK07445 295 TIPANQTGNITIQAQSLALGYY--P-----QIL--DSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEA 364
|
170 180 190
....*....|....*....|....*....|...
gi 442622933 608 ELKTCGIIENICVYGDPTKQY---TVALVVPNQ 637
Cdd:PRK07445 365 AILATGLVQDVCVLGLPDPHWgevVTAIYVPKD 397
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
296-609 |
3.47e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 69.66 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 296 YTSGSTGTPKGVLLSHKNC-IATMKGFVDM-VPIYPddVLIGFLPLAHvfelvaesvClmTGVPIGYSTpltlidtsski 373
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGAyLSTLSAIIGWeMGTCP--VYLWTLPMFH---------C--NGWTFTWGT----------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 374 krGCKGDATVlkptCMTSVplILDRISKGINDKVNSGSAFKKSLFKFLYQykvkwvqrGYKTPLIDKlvfkkvaklmGGK 453
Cdd:PLN03102 249 --AARGGTSV----CMRHV--TAPEIYKNIEMHNVTHMCCVPTVFNILLK--------GNSLDLSPR----------SGP 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 454 VRIiMSGGAPLSADTHEQIKTcLCLELIQGYGLTETTSGATVMDYRD----------MTYGRTGG--PLTVCDIRLVNWE 521
Cdd:PLN03102 303 VHV-LTGGSPPPAALVKKVQR-LGFQVMHAYGLTEATGPVLFCEWQDewnrlpenqqMELKARQGvsILGLADVDVKNKE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 522 egnyrvTNKPYPQ-----GEVLIGGECVSQGYYKLPGKTNEDFfeedGQRWFKTGDIGEIQADGVLKIIDRKKDLVkLQA 596
Cdd:PLN03102 381 ------TQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAF----KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISG 449
|
330
....*....|...
gi 442622933 597 GEYVSLGKVESEL 609
Cdd:PLN03102 450 GENISSVEVENVL 462
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
229-606 |
3.54e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 69.35 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 229 LPKFKTLLDKCPLVKTIIYIEDQLQKTETTgfkegVKILPFNQVVkTGQDSKFEHvPPKGDDIAIIM-YTSGSTGTPKGV 307
Cdd:PRK07008 122 LPLVDALAPQCPNVKGWVAMTDAAHLPAGS-----TPLLCYETLV-GAQDGDYDW-PRFDENQASSLcYTSGTTGNPKGA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 308 LLSHKNCI--ATMKGFVDMVPIYPDDVLIGFLPLAHVFELvaesvclmtGVPigYSTPLTlidtsskikrGCKgdatvlk 385
Cdd:PRK07008 195 LYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHVNAW---------GLP--YSAPLT----------GAK------- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 386 ptcmtsvpLILdriskgindkvnSGSAFK-KSLFKFLYQYKVKWVQrGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGAPL 464
Cdd:PRK07008 247 --------LVL------------PGPDLDgKSLYELIEAERVTFSA-GVPTVWLGLLNHMREAGLRFSTLRRTVIGGSAC 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 465 SADTHEQIKTCLCLELIQGYGLTETTSGATV-----------MDYRDMTYGRTGGPLTVCDIRLVNwEEGnyrvtnKPYP 533
Cdd:PRK07008 306 PPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLcklkwkhsqlpLDEQRKLLEKQGRVIYGVDMKIVG-DDG------RELP 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622933 534 -----QGEVLIGGECVSQGYYKlpgktNEDFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKVE 606
Cdd:PRK07008 379 wdgkaFGDLQVRGPWVIDRYFR-----GDASPLVDG--WFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
290-622 |
5.83e-12 |
|
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: 68.53 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAH-VFELVAESVCLMTGVpigystplTLId 368
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHsTALIVGWSACLASGA--------TLV- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 369 tsskIKRgcKGDATVLKPTCM----TSVPLIldriskgindkvnsgsafkKSLFKFLYQYKVKWVQRGYKtplidklvfk 444
Cdd:cd05940 153 ----IRK--KFSASNFWDDIRkyqaTIFQYI-------------------GELCRYLLNQPPKPTERKHK---------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 445 kvaklmggkVRIIMSGGapLSADTHEQIKTCLCLELI-QGYGLTETTSGATVMDYRDMTYGRTGGPLT-VCDIRLVNWEE 522
Cdd:cd05940 198 ---------VRMIFGNG--LRPDIWEEFKERFGVPRIaEFYAATEGNSGFINFFGKPGAIGRNPSLLRkVAPLALVKYDL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 523 GNYRVTN------KPYPQGEVligGECVS--------QGYYKlPGKTNE----DFFEeDGQRWFKTGDIGEIQADGVLKI 584
Cdd:cd05940 267 ESGEPIRdaegrcIKVPRGEP---GLLISrinplepfDGYTD-PAATEKkilrDVFK-KGDAWFNTGDLMRLDGEGFWYF 341
|
330 340 350
....*....|....*....|....*....|....*...
gi 442622933 585 IDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVYG 622
Cdd:cd05940 342 VDRLGDTFRWK-GENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
290-689 |
7.13e-12 |
|
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: 68.51 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 290 DIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESV--CLMTGvpigystpltli 367
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACPGVlgTLLAG------------ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 dtsskikrGCkgdaTVL--KPTCMTSVPLIlDRiskginDKVNSgSAFKKSLFKFlyqykvkWVQRGYKTPLIDklvfkk 445
Cdd:cd05920 208 --------GR----VVLapDPSPDAAFPLI-ER------EGVTV-TALVPALVSL-------WLDAAASRRADL------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 446 vaklmgGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGG-PLTVCD-IRLVNwEEG 523
Cdd:cd05920 255 ------SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGrPMSPDDeIRVVD-EEG 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 524 NyrvtnkPYPQGEV---LIGGECVSQGYYKLPgKTNEDFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYV 600
Cdd:cd05920 328 N------PVPPGEEgelLTRGPYTIRGYYRAP-EHNARAFTPDG--FYRTGDLVRRTPDGYLVVEGRIKDQIN-RGGEKI 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 601 SLGKVESELKTcgiienicvygDPTKQYTVALVVPNQNhleelaqkhgLGDKSfeelCSSPIIEKAILK--EIAEHARKC 678
Cdd:cd05920 398 AAEEVENLLLR-----------HPAVHDAAVVAMPDEL----------LGERS----CAFVVLRDPPPSaaQLRRFLRER 452
|
410
....*....|.
gi 442622933 679 KLQKYEVPAAI 689
Cdd:cd05920 453 GLAAYKLPDRI 463
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
148-637 |
1.21e-11 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 67.50 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHcitetevttvitshd 227
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 228 llpkfkTLLDK-CPLVKTIIYIEDQLQKTETTgfkegvkILPFNQVVKTGQDSKFEHVPpKGDDIAIIMYTSGSTGTPKG 306
Cdd:cd17656 80 ------IMLDSgVRVVLTQRHLKSKLSFNKST-------ILLEDPSISQEDTSNIDYIN-NSDDLLYIIYTSGTTGKPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 307 VLLSHKNCIATMK-GFVDMVPIYPDDVLigflplahVFELVAESVCLMTGVpigySTPL---TLIDTSSKIKRgckgdat 382
Cdd:cd17656 146 VQLEHKNMVNLLHfEREKTNINFSDKVL--------QFATCSFDVCYQEIF----STLLsggTLYIIREETKR------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 383 vlkptcmtSVPLILDRISKGINDKVNSGSAFKKSLFKflyqykvkwvQRGYKTPLidklvFKKVAKLMGGKVRIIMSGga 462
Cdd:cd17656 207 --------DVEQLFDLVKRHNIEVVFLPVAFLKFIFS----------EREFINRF-----PTCVKHIITAGEQLVITN-- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 463 PLSADTHEqiKTClclELIQGYGLTETTsgaTVMDYR------DMTYGRTGGPLTVCDIRLVNWEEgnyrvtnKPYPQG- 535
Cdd:cd17656 262 EFKEMLHE--HNV---HLHNHYGPSETH---VVTTYTinpeaeIPELPPIGKPISNTWIYILDQEQ-------QLQPQGi 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 536 --EVLIGGECVSQGYYKLPGKTNEDFFE---EDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELK 610
Cdd:cd17656 327 vgELYISGASVARGYLNRQELTAEKFFPdpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR-GYRIELGEIEAQLL 405
|
490 500 510
....*....|....*....|....*....|
gi 442622933 611 TCGIIEN--ICVYGDPTKQ-YTVALVVPNQ 637
Cdd:cd17656 406 NHPGVSEavVLDKADDKGEkYLCAYFVMEQ 435
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
278-609 |
1.36e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 67.66 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 278 DSKFEHVPPKGDDIAIIM-YTSGSTGTPKGVLLSHK----NCIATMKGFvDMvPIYPddVLIGFLPLAH----------- 341
Cdd:PRK08162 170 DPDFAWTLPADEWDAIALnYTSGTTGNPKGVVYHHRgaylNALSNILAW-GM-PKHP--VYLWTLPMFHcngwcfpwtva 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 342 ----------------VFELVAE-SVCLMTGVPIGYSTpltLIDTSSKIKRGckgdatvlkptcmtsvplildriskgIN 404
Cdd:PRK08162 246 aragtnvclrkvdpklIFDLIREhGVTHYCGAPIVLSA---LINAPAEWRAG--------------------------ID 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 405 DKVNSgsafkkslfkflyqykvkwvqrgyktplidklvfkkvaklmggkvriiMSGGAPLSADTHEQIKTcLCLELIQGY 484
Cdd:PRK08162 297 HPVHA------------------------------------------------MVAGAAPPAAVIAKMEE-IGFDLTHVY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 485 GLTETTSGATV-----------MDYRDMTYGRTGGP------LTVCDirlvnweegnyRVTNKPYP-----QGEVLIGGE 542
Cdd:PRK08162 328 GLTETYGPATVcawqpewdalpLDERAQLKARQGVRyplqegVTVLD-----------PDTMQPVPadgetIGEIMFRGN 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622933 543 CVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESEL 609
Cdd:PRK08162 397 IVMKGYLKNPKATEEAF--AGG--WFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVL 458
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
280-592 |
4.11e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 66.16 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 280 KFEHVPPK----GDDIAIIMYTSGSTGTPKGVLLSHKnCIATMkgfvdMVPIYPDdvligflplahvFELVAESVCLMTg 355
Cdd:PRK06188 155 KFGPAPLVaaalPPDIAGLAYTGGTTGKPKGVMGTHR-SIATM-----AQIQLAE------------WEWPADPRFLMC- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 356 VPIGYSTPLTLIDTsskIKRGckGDATVLKPTCMTSVpliLDRISKginDKVNsgsafkkslFKFLYQYKVkwvqrgYKt 435
Cdd:PRK06188 216 TPLSHAGGAFFLPT---LLRG--GTVIVLAKFDPAEV---LRAIEE---QRIT---------ATFLVPTMI------YA- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 436 pLID--KLVFKKVAKLmggkvRIIMSGGAPLS----ADTHEQIKTCLclelIQGYGLTETTSGATVMDYRDM------TY 503
Cdd:PRK06188 269 -LLDhpDLRTRDLSSL-----ETVYYGASPMSpvrlAEAIERFGPIF----AQYYGQTEAPMVITYLRKRDHdpddpkRL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 504 GRTGGPLTVCDIRLVNwEEGNyrvtnkPYPQGEVligGE-CVS-----QGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQ 577
Cdd:PRK06188 339 TSCGRPTPGLRVALLD-EDGR------EVAQGEV---GEiCVRgplvmDGYWNRPEETAEAF--RDG--WLHTGDVARED 404
|
330
....*....|....*
gi 442622933 578 ADGVLKIIDRKKDLV 592
Cdd:PRK06188 405 EDGFYYIVDRKKDMI 419
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
282-636 |
4.72e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 65.86 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 282 EHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIatMKGFVD--MVPIYPDDVLIGFLPLAHV-FELVAESVCLMTGvpi 358
Cdd:PRK08008 166 YAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSawQCALRDDDVYLTVMPAFHIdCQCTAAMAAFSAG--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 359 gySTpLTLIDTSSK---IKRGCKGDATVLKptCMtsvPLILdriskgindkvnsgsafkKSLfkfLYQYKVKWvQRGYKt 435
Cdd:PRK08008 241 --AT-FVLLEKYSArafWGQVCKYRATITE--CI---PMMI------------------RTL---MVQPPSAN-DRQHC- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 436 pLIDKLVFkkvaklmggkvriimsggAPLSADTHEQIKTCLCLELIQGYGLTETTSGA---TVMDYRDM-TYGRTGgplt 511
Cdd:PRK08008 290 -LREVMFY------------------LNLSDQEKDAFEERFGVRLLTSYGMTETIVGIigdRPGDKRRWpSIGRPG---- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 512 vcdirlVNWEEGNYRVTNKPYPQGEVligGE-CVS--------QGYYKLPGKTnEDFFEEDGqrWFKTGDIGEIQADGVL 582
Cdd:PRK08008 347 ------FCYEAEIRDDHNRPLPAGEI---GEiCIKgvpgktifKEYYLDPKAT-AKVLEADG--WLHTGDTGYVDEEGFF 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622933 583 KIIDRKKDLVKlQAGEYVSLGKVESELKTCGIIENICVYG--DPTKQYTV-ALVVPN 636
Cdd:PRK08008 415 YFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIVVVGikDSIRDEAIkAFVVLN 470
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
262-679 |
2.54e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 63.74 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 262 EGVKILPFNQVVKT----GQDSKFEHVPPkgDDIAIIMYTSGSTGTPKGVLLSHKN-CI------ATMKGFVDMVPiypd 330
Cdd:PRK08180 180 PGRAATPFAALLATpptaAVDAAHAAVGP--DTIAKFLFTSGSTGLPKAVINTHRMlCAnqqmlaQTFPFLAEEPP---- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 331 dVLIGFLPLAHVFelvaesvclmtgvpiGYSTPLTL---------ID----TSSKIkrgckgDATV--LK---PTCMTSV 392
Cdd:PRK08180 254 -VLVDWLPWNHTF---------------GGNHNLGIvlynggtlyIDdgkpTPGGF------DETLrnLReisPTVYFNV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 393 PlildrisKG---INDKVNSGSAFKKSLFkflyqykvkwvqrgyktplidklvfkkvaklmgGKVRIIMSGGAPLSADTH 469
Cdd:PRK08180 312 P-------KGwemLVPALERDAALRRRFF---------------------------------SRLKLLFYAGAALSQDVW 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 470 EQIKTC---LCLELIQ---GYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVnweegnyrvtnkpyPQG---EVLIG 540
Cdd:PRK08180 352 DRLDRVaeaTCGERIRmmtGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLV--------------PVGgklEVRVK 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 541 GECVSQGYYKLPGKTNEdFFEEDGqrWFKTGDIGE----------IQADGvlkiidRKKDLVKLQAGEYVSLG----KVE 606
Cdd:PRK08180 418 GPNVTPGYWRAPELTAE-AFDEEG--YYRSGDAVRfvdpadpergLMFDG------RIAEDFKLSSGTWVSVGplraRAV 488
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622933 607 SELKtcGIIENICVYGdPTKQYTVALVVPNQNHLEELAqkhGLG-DKSFEELCSSPIIEKAILKEIAEHARKCK 679
Cdd:PRK08180 489 SAGA--PLVQDVVITG-HDRDEIGLLVFPNLDACRRLA---GLLaDASLAEVLAHPAVRAAFRERLARLNAQAT 556
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
263-597 |
3.45e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.25 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 263 GVKILPFNQVVKTGQDSKFEHVPPKGddIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPD-DVLIGFLPLAH 341
Cdd:PRK05851 128 SVTVHDLATAAHTNRSASLTPPDSGG--PAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 342 VFELVAESVCLMTGVPigystpltlidtsskikrgckgdaTVLKPTcmtsvplildriskgindkvnsgSAFKKSLFKFL 421
Cdd:PRK05851 206 DMGLAFLLTAALAGAP------------------------LWLAPT-----------------------TAFSASPFRWL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 422 yqykvKWVQRGYKT----P-----LIDKLVfKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCL------ELIQGYGL 486
Cdd:PRK05851 239 -----SWLSDSRATltaaPnfaynLIGKYA-RRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPfgfdagAAAPSYGL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 487 TETTSGATV--------MDYRDM-------TYGRTGGPLTVCDIRLvnwEEGNYRVTNKPYPQGEVLIGGECVSQGYykl 551
Cdd:PRK05851 313 AESTCAVTVpvpgiglrVDEVTTddgsgarRHAVLGNPIPGMEVRI---SPGDGAAGVAGREIGEIEIRGASMMSGY--- 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 442622933 552 pgkTNEDFFEEDGqrWFKTGDIGEIQADGvLKIIDRKKDLVKLqAG 597
Cdd:PRK05851 387 ---LGQAPIDPDD--WFPTGDLGYLVDGG-LVVCGRAKELITV-AG 425
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
285-639 |
3.91e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 63.14 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 285 PPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDM-VPIYPDDVLIGFLPLahvFELVAESVCLMtgVPIGYSTP 363
Cdd:PRK06178 205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVaVVGGEDSVFLSFLPE---FWIAGENFGLL--FPLFSGAT 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LTLIdtsskikrgCKGDATvlkpTCMTSVPlildriskgiNDKVNSGSAFKKSLFKFL-----YQYKVKWVQRGYKTPLI 438
Cdd:PRK06178 280 LVLL---------ARWDAV----AFMAAVE----------RYRVTRTVMLVDNAVELMdhprfAEYDLSSLRQVRVVSFV 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 439 DKL---VFKKVAKLMGGkvriIMSGGAplsadtheqiktclcleliqgYGLTET------TSGATVMDYrDMTYGRT--G 507
Cdd:PRK06178 337 KKLnpdYRQRWRALTGS----VLAEAA---------------------WGMTEThtcdtfTAGFQDDDF-DLLSQPVfvG 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 508 GPLTVCDIRLVNWEEGnyrvtnKPYP---QGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKI 584
Cdd:PRK06178 391 LPVPGTEFKICDFETG------ELLPlgaEGEIVVRTPSLLKGYWNKPEATAEAL--RDG--WLHTGDIGKIDEQGFLHY 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622933 585 IDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVYG--DPTK-QYTVALVVPNQNH 639
Cdd:PRK06178 461 LGRRKEMLKVN-GMSVFPSEVEALLGQHPAVLGSAVVGrpDPDKgQVPVAFVQLKPGA 517
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
289-635 |
4.41e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 62.75 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 289 DDIAIIMYTSGSTGTPKGVLLSHknciATMkGFV------DMVP-IYPDDVLIGFLPLAHvfelvaesvclmtGVPIGYs 361
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTH----GQM-AFVitnhlaDLMPgTTEQDASLVVAPLSH-------------GAGIHQ- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 362 tpltLIDTSskikrgcKGDATVLKPTcmtsvplildriskginDKVNSGSAFKkslfkFLYQYKVKWVqrgYKTPLIDKL 441
Cdd:PRK07470 224 ----LCQVA-------RGAATVLLPS-----------------ERFDPAEVWA-----LVERHRVTNL---FTVPTILKM 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 442 VFK--KVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVM-----DYRDMT--------YGRT 506
Cdd:PRK07470 268 LVEhpAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLppalhDAEDGPdarigtcgFERT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 507 GGPLTVCDirlvnwEEGNyrvTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIID 586
Cdd:PRK07470 348 GMEVQIQD------DEGR---ELPPGETGEICVIGPAVFAGYYNNPEANAKAF--RDG--WFRTGDLGHLDARGFLYITG 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622933 587 RKKDLvklqageYVSLG------KVESELKTCGIIENICVYG--DPT-KQYTVALVVP 635
Cdd:PRK07470 415 RASDM-------YISGGsnvyprEIEEKLLTHPAVSEVAVLGvpDPVwGEVGVAVCVA 465
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
227-592 |
9.53e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 61.75 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 227 DLLPKFKTL------LDKCPLVKTIIYIEDQlqktETTGFkegvkiLPFNQVVKTGQDSKFEHVPP-----KGDDIAIIM 295
Cdd:PRK08315 136 ELAPELATCepgqlqSARLPELRRVIFLGDE----KHPGM------LNFDELLALGRAVDDAELAArqatlDPDDPINIQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 296 YTSGSTGTPKGVLLSHKNCI-------ATMKgfvdmvpIYPDDVLIGFLPLAHVFELV-AESVCLMTG---VPIGYS-TP 363
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILnngyfigEAMK-------LTEEDRLCIPVPLYHCFGMVlGNLACVTHGatmVYPGEGfDP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 364 LTLIDTSSKIKrgCkgdaTVLK--PT---CMTSVPLI----LDRISKGINdkvnSGSafkkslfkflyqykvkwvqrgyk 434
Cdd:PRK08315 279 LATLAAVEEER--C----TALYgvPTmfiAELDHPDFarfdLSSLRTGIM----AGS----------------------- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 435 TPLIDklVFKKVAKLMGgkvriiMSggaplsadtheqiktclclELIQGYGLTETTSGatvmdyrdMTYGRTGGPL---- 510
Cdd:PRK08315 326 PCPIE--VMKRVIDKMH------MS-------------------EVTIAYGMTETSPV--------STQTRTDDPLekrv 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 511 -TV------CDIRLVNWEEGNyrvTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFfeeDGQRWFKTGDIGEIQADGVLK 583
Cdd:PRK08315 371 tTVgralphLEVKIVDPETGE---TVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI---DADGWMHTGDLAVMDEEGYVN 444
|
....*....
gi 442622933 584 IIDRKKDLV 592
Cdd:PRK08315 445 IVGRIKDMI 453
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
286-592 |
1.28e-09 |
|
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: 60.94 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 286 PKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFelvaesvclmtGVPIGYSTPLT 365
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALGLTSVIP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 366 LIDtsskikrgckgdatvlkPTCmtsvplildriskgindkvnSGSAFKKSLFKFLYQYKVKWVqrgYKTPLIDKLVFKK 445
Cdd:cd05910 151 DMD-----------------PTR--------------------PARADPQKLVGAIRQYGVSIV---FGSPALLERVARY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 446 VAK--LMGGKVRIIMSGGAPLSADTHEQIKTCLC--LELIQGYGLTETTSGATVMDyRDMTYGRT-----------GGPL 510
Cdd:cd05910 191 CAQhgITLPSLRRVLSAGAPVPIALAARLRKMLSdeAEILTPYGATEALPVSSIGS-RELLATTTaatsggagtcvGRPI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 511 TVCDIRLVNWEEGNYRVTNK-----PYPQGEVLIGGECVSQGYYKLPGKTN-EDFFEEDGQRWFKTGDIGEIQADGVLKI 584
Cdd:cd05910 270 PGVRVRIIEIDDEPIAEWDDtlelpRGEIGEITVTGPTVTPTYVNRPVATAlAKIDDNSEGFWHRMGDLGYLDDEGRLWF 349
|
....*...
gi 442622933 585 IDRKKDLV 592
Cdd:cd05910 350 CGRKAHRV 357
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
292-691 |
2.23e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 292 AIIMYTSGSTGTPKGVLLSH----KNCIATMKGFvDMvpiYPDDVLIGFLPLAhvFELVAESVClmtgvpigysTPLTli 367
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHgeiaMHCQAVIERF-GM---RADDCELHFYSIN--FDAASERLL----------VPLL-- 2397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 368 dtsskikrgCkGDATVLKPTCMTSVplilDRISKGINDKVNSGSAFKKSLFKFLYQYKVKwvqRGYKTPlidklvfkkva 447
Cdd:PRK05691 2398 ---------C-GARVVLRAQGQWGA----EEICQLIREQQVSILGFTPSYGSQLAQWLAG---QGEQLP----------- 2449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 448 klmggkVRIIMSGGAPLSADTHEQIKTCLCLELI-QGYGLTETTsgatVM------------DYRDMTYGRTGGPLT--V 512
Cdd:PRK05691 2450 ------VRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTETV----VMplaclapeqleeGAASVPIGRVVGARVayI 2519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 513 CDIRLVnweegnyrvtnkPYPQG---EVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQADGVLKII 585
Cdd:PRK05691 2520 LDADLA------------LVPQGatgELYVGGAGLAQGYHDRPGLTAERFvadpFAADGGRLYRTGDLVRLRADGLVEYV 2587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 586 DRKKDLVKLQaGEYVSLGKVESELKTCGIIENICV--YGDPTKQYTVALVVPNQNHLEELAQkhglgdksfeelcsspii 663
Cdd:PRK05691 2588 GRIDHQVKIR-GFRIELGEIESRLLEHPAVREAVVlaLDTPSGKQLAGYLVSAVAGQDDEAQ------------------ 2648
|
410 420
....*....|....*....|....*...
gi 442622933 664 ekAILKEIAEHARKCKLQKYEVPAAITL 691
Cdd:PRK05691 2649 --AALREALKAHLKQQLPDYMVPAHLIL 2674
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
126-355 |
3.39e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 59.89 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 126 EDEVQQNG-RVFKKYNLGDYkwkTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFK----QAMpIVT 200
Cdd:PRK08279 44 EEAAARHPdRPALLFEDQSI---SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKlgavVAL-LNT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 201 vyaTLGDDGVAHCITETEVTTVITSHDLLPKFKTLLDkCPLVKTIIYIEDQLQKTETTGFKEGVKIL----PFNQVVKtg 276
Cdd:PRK08279 120 ---QQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARA-DLARPPRLWVAGGDTLDDPEGYEDLAAAAagapTTNPASR-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 277 qdskfEHVPpkGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAH-VFELVAESVCLMTG 355
Cdd:PRK08279 194 -----SGVT--AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHnTGGTVAWSSVLAAG 266
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
288-715 |
4.66e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 59.50 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAH-VFELVAESVCLMTGvpigystpltl 366
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHnTGGTVAWSSVLAAG----------- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 367 idtsskikrgckgdATvlkptcmtsvpLILDRiskgindKVnSGSAF-------KKSLF-------KFLYQYKVKWVQRG 432
Cdd:PRK08279 267 --------------AT-----------LALRR-------KF-SASRFwddvrryRATAFqyigelcRYLLNQPPKPTDRD 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 433 YKtplidklvfkkvaklmggkVRIIMsgGAPLSADTHEQIKTCLCLELI-QGYGLTETTSGATVMDYRDMTYGRTGGPLT 511
Cdd:PRK08279 314 HR-------------------LRLMI--GNGLRPDIWDEFQQRFGIPRIlEFYAASEGNVGFINVFNFDGTVGRVPLWLA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 512 VcDIRLVNW----------EEGNYRVTNKpypqGEVligGECVSQ--------GYYKlPGKTNE----DFFEeDGQRWFK 569
Cdd:PRK08279 373 H-PYAIVKYdvdtgepvrdADGRCIKVKP----GEV---GLLIGRitdrgpfdGYTD-PEASEKkilrDVFK-KGDAWFN 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 570 TGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVYGdptkqytVAlvVPNQNHLEELAQKHGL 649
Cdd:PRK08279 443 TGDLMRDDGFGHAQFVDRLGDTFRWK-GENVATTEVENALSGFPGVEEAVVYG-------VE--VPGTDGRAGMAAIVLA 512
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622933 650 GDKSFEelcsspiiekaiLKEIAEHARKCkLQKYEVPAAITLCKEVwspDMglvTAAFKLKRKDIQ 715
Cdd:PRK08279 513 DGAEFD------------LAALAAHLYER-LPAYAVPLFVRLVPEL---ET---TGTFKYRKVDLR 559
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
245-628 |
5.94e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 59.09 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 245 IIYIEDQLQKTETTGFKEGVKILPFNQVVKTGqDSKFEHVPPKGDDIAIIM-YTSGSTGTPKGVLLSHKNCIaTMKGFVD 323
Cdd:PLN02479 151 LIVIGDPTCDPKSLQYALGKGAIEYEKFLETG-DPEFAWKPPADEWQSIALgYTSGTTASPKGVVLHHRGAY-LMALSNA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 324 MVPIYPDD-VLIGFLPLAHvfelvAESVCLMTGVPIGYSTPLTLIDTSSKIKRGCKGDATVlkpTCMTSVPLILDRIskg 402
Cdd:PLN02479 229 LIWGMNEGaVYLWTLPMFH-----CNGWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGV---THFCAAPVVLNTI--- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 403 indkVNSGSAfkkslfkflyqykvkwvQRGYKTPLIdklvfkkvaklmggkVRIIMSGGAP----LSADTHEQIKtclcl 478
Cdd:PLN02479 298 ----VNAPKS-----------------ETILPLPRV---------------VHVMTAGAAPppsvLFAMSEKGFR----- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 479 eLIQGYGLTETTSGATV-----------MDYRDMTYGRTGgpltvcdIRLVNWEEGNY--RVTNKPYPQ-----GEVLIG 540
Cdd:PLN02479 337 -VTHTYGLSETYGPSTVcawkpewdslpPEEQARLNARQG-------VRYIGLEGLDVvdTKTMKPVPAdgktmGEIVMR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 541 GECVSQGYYKLPgKTNEDFFEEDgqrWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESELKTCGIIENICV 620
Cdd:PLN02479 409 GNMVMKGYLKNP-KANEEAFANG---WFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLEVENVVYTHPAVLEASV 483
|
....*...
gi 442622933 621 YGDPTKQY 628
Cdd:PLN02479 484 VARPDERW 491
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
263-651 |
8.42e-09 |
|
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: 58.67 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 263 GVKILPFNQVVKTGQDSKF----EHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNC------IATMKGFvdmvpIYPD-D 331
Cdd:cd05923 120 GVRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAesrvlfMSTQAGL-----RHGRhN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 332 VLIGFLPLAHV---FELVAESVCL-MTGVPIGYSTP---LTLIDTsskikrgckgdatvLKPTCMTSVPLILDRISKGIn 404
Cdd:cd05923 195 VVLGLMPLYHVigfFAVLVAALALdGTYVVVEEFDPadaLKLIEQ--------------ERVTSLFATPTHLDALAAAA- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 405 dkvnsgsafkkslfkflyqykvkwVQRGYKTPLIDKLVFkkvaklmggkvriimsGGAPLSADTHEQIKTCLCLELIQGY 484
Cdd:cd05923 260 ------------------------EFAGLKLSSLRHVTF----------------AGATMPDAVLERVNQHLPGEKVNIY 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 485 GLTETTSgATVMdyRDMTYGRTGGPLTVCDIRLVnweegnyRVTNKP---YPQGE-----VLIGGECVSQGYYKLPGKTN 556
Cdd:cd05923 300 GTTEAMN-SLYM--RDARTGTEMRPGFFSEVRIV-------RIGGSPdeaLANGEegeliVAAAADAAFTGYLNQPEATA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 557 EDFFEedgqRWFKTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVESELKTCGIIENICVYGDPTK---QYTVALV 633
Cdd:cd05923 370 KKLQD----GWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGVADErwgQSVTACV 444
|
410 420
....*....|....*....|...
gi 442622933 634 VPNQ-----NHLEELAQKHGLGD 651
Cdd:cd05923 445 VPREgtlsaDELDQFCRASELAD 467
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
277-635 |
8.99e-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: 58.33 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 277 QDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDD---VLIGFLPLAHVFELvaesvclM 353
Cdd:cd17645 92 ADSSAKILLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADkslVYASFSFDASAWEI-------F 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 354 TGVPIGYStpLTLIDTSSKikrgckgdatvlkptcmtsvpLILDRISKGINDKVNSGSafkkslfkFLyqykvkwvqrgy 433
Cdd:cd17645 165 PHLTAGAA--LHVVPSERR---------------------LDLDALNDYFNQEGITIS--------FL------------ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 434 KTPLIDKLVfkkvaKLMGGKVRIIMSGGAPLSADTHEQIKtclcleLIQGYGLTETTSGATVMDYrDMTYGRTGGPLTVC 513
Cdd:cd17645 202 PTGAAEQFM-----QLDNQSLRVLLTGGDKLKKIERKGYK------LVNNYGPTENTVVATSFEI-DKPYANIPIGKPID 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 514 DIRLVNWEEGNyrvtnKPYPQG---EVLIGGECVSQGYYKLPGKTNEDFFEE---DGQRWFKTGDIGEIQADGVLKIIDR 587
Cdd:cd17645 270 NTRVYILDEAL-----QLQPIGvagELCIAGEGLARGYLNRPELTAEKFIVHpfvPGERMYRTGDLAKFLPDGNIEFLGR 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 442622933 588 KKDLVKLQaGEYVSLGKVESELKTCGIIENICVY------GDPtkqYTVALVVP 635
Cdd:cd17645 345 LDQQVKIR-GYRIEPGEIEPFLMNHPLIELAAVLakedadGRK---YLVAYVTA 394
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
288-609 |
1.11e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.03 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 288 GDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAhvFELvaeSV--CLMtgvpigystPLT 365
Cdd:PRK05691 1272 GDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIS--FDV---SVweCFW---------PLI 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 366 lidtsskikRGCKgdatvlkptcmtsvpLILdrisKGINDKVNSgsafkkslfkflyQYKVKWVQRGYKT------PLID 439
Cdd:PRK05691 1338 ---------TGCR---------------LVL----AGPGEHRDP-------------QRIAELVQQYGVTtlhfvpPLLQ 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 440 KLVFKKVAKLMGgKVRIIMSGGAPLSADTHEQIKTCL-CLELIQGYGLTETTSGATVMDYR--DMTYGRTGGPL--TVCD 514
Cdd:PRK05691 1377 LFIDEPLAAACT-SLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHWQCQaeDGERSPIGRPLgnVLCR 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 515 IRlvnweEGNYRVTNKPYPqGEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQADGVLKIIDRKKD 590
Cdd:PRK05691 1456 VL-----DAELNLLPPGVA-GELCIGGAGLARGYLGRPALTAERFvpdpLGEDGARLYRTGDRARWNADGALEYLGRLDQ 1529
|
330
....*....|....*....
gi 442622933 591 LVKLQaGEYVSLGKVESEL 609
Cdd:PRK05691 1530 QVKLR-GFRVEPEEIQARL 1547
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
483-639 |
1.07e-07 |
|
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: 54.23 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 483 GYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNwEEGNyrvtnkPYPQGEVligGECVSQGYYKLPGKTNEDffEE 562
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGR------EVPDGEV---GEIVARGPTVMAGYWNRP--EV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 563 DGQR----WFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKVESELKTCGIIENICVYG--DPT-KQYTVALVVP 635
Cdd:cd17636 210 NARRtrggWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVERCLRQHPAVADAAVIGvpDPRwAQSVKAIVVL 288
|
....
gi 442622933 636 NQNH 639
Cdd:cd17636 289 KPGA 292
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
453-717 |
2.43e-07 |
|
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: 54.04 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 453 KVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEegnyrvtNKPY 532
Cdd:cd05970 302 SLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDRE-------GRSC 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 533 PQGEvliGGECVSQ-----------GYYKLPGKTNEDFFeeDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVS 601
Cdd:cd05970 375 EAGE---EGEIVIRtskgkpvglfgGYYKDAEKTAEVWH--DG--YYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIG 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 602 LGKVESELKTCGIIENICVYG--DPTK-QYTVALVVPNQNHleelaqkhglgdKSFEELcsspiiekaiLKEIAEHARKC 678
Cdd:cd05970 447 PFEVESALIQHPAVLECAVTGvpDPIRgQVVKATIVLAKGY------------EPSEEL----------KKELQDHVKKV 504
|
250 260 270
....*....|....*....|....*....|....*....
gi 442622933 679 KlQKYEVPAAITLCKEVwsPDmglvTAAFKLKRKDIQDR 717
Cdd:cd05970 505 T-APYKYPRIVEFVDEL--PK----TISGKIRRVEIRER 536
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
294-633 |
5.39e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 52.78 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 294 IMYTSGSTGTPKGVllshKNCIAT---MKGFVDMVpiypddvligflplAHVFELVAESVCLMTGvPIGYSTPltlidTS 370
Cdd:PRK12406 157 MIYTSGTTGHPKGV----RRAAPTpeqAAAAEQMR--------------ALIYGLKPGIRALLTG-PLYHSAP-----NA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 371 SKIKRGCKGDATVLKP----------------TCMTSVPLILDRISKgINDKVnsgsafkkslfkflyqykvkwvQRGYK 434
Cdd:PRK12406 213 YGLRAGRLGGVLVLQPrfdpeellqlierhriTHMHMVPTMFIRLLK-LPEEV----------------------RAKYD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 435 TplidklvfkkvaklmgGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTET--TSGATVMDYRDMTyGRTGGPLTV 512
Cdd:PRK12406 270 V----------------SSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESgaVTFATSEDALSHP-GTVGKAAPG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 513 CDIRLVNwEEGnyrvtnKPYPQGEVligGECVSQ-------GYYKLPGKTNEdfFEEDGqrWFKTGDIGEIQADGVLKII 585
Cdd:PRK12406 333 AELRFVD-EDG------RPLPQGEI---GEIYSRiagnpdfTYHNKPEKRAE--IDRGG--FITSGDVGYLDADGYLFLC 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 442622933 586 DRKKDLVkLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALV 633
Cdd:PRK12406 399 DRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALM 445
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
455-609 |
7.98e-07 |
|
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: 52.46 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 455 RIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTEttsGATVM----DYRDMTYGRTGGPLTVCD-IRLVNwEEGNyrvtn 529
Cdd:COG1021 303 RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GLVNYtrldDPEEVILTTQGRPISPDDeVRIVD-EDGN----- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 530 kPYPQGEV---LIGGECVSQGYYKLPGKtNEDFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlQAGEYVSLGKVE 606
Cdd:COG1021 374 -PVPPGEVgelLTRGPYTIRGYYRAPEH-NARAFTPDG--FYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVE 448
|
...
gi 442622933 607 SEL 609
Cdd:COG1021 449 NLL 451
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
148-332 |
1.37e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 51.43 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAmPIVT-VYATLGDDGVAHCITETEVTTVITSH 226
Cdd:PRK04319 75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNG-AIVGpLFEAFMEEAVRDRLEDSEAKVLITTP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 227 DLLPKFKtlLDKCPLVKTIIYIEDQLqktettgfKEGVKILPFNQVVKTGQDSkFEHVPPKGDDIAIIMYTSGSTGTPKG 306
Cdd:PRK04319 154 ALLERKP--ADDLPSLKHVLLVGEDV--------EEGPGTLDFNALMEQASDE-FDIEWTDREDGAILHYTSGSTGKPKG 222
|
170 180
....*....|....*....|....*....
gi 442622933 307 VLLSHKNCI---ATMKGFVDMvpiYPDDV 332
Cdd:PRK04319 223 VLHVHNAMLqhyQTGKYVLDL---HEDDV 248
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
281-592 |
2.15e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.90 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 281 FEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKnciATMKGFVDMvpIYPDDVL------IGFLPLAHVFELvaesvcLMT 354
Cdd:PRK12476 185 FVPVELDTDDVSHLQYTSGSTRPPVGVEITHR---AVGTNLVQM--ILSIDLLdrnthgVSWLPLYHDMGL------SMI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 355 GVPIGYSTPLTLIDTSSKIKRgckgdatvlkptcmtsvPLildRISKGINDKVNSGSAFKKSLfKFLYQYKvkwVQRGYK 434
Cdd:PRK12476 254 GFPAVYGGHSTLMSPTAFVRR-----------------PQ---RWIKALSEGSRTGRVVTAAP-NFAYEWA---AQRGLP 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 435 TPLiDKLVFKKVAklmggkvriIMSGGAPLSADTHEQIKTCLC------LELIQGYGLTETT-----------SGATVMD 497
Cdd:PRK12476 310 AEG-DDIDLSNVV---------LIIGSEPVSIDAVTTFNKAFApyglprTAFKPSYGIAEATlfvatiapdaePSVVYLD 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 498 YRDMTYGRT-----GGPLTVCDIRLVNWEEGNYRVTNKPYPQ--------GEVLIGGECVSQGYYKLPGKTNEDFFE--- 561
Cdd:PRK12476 380 REQLGAGRAvrvaaDAPNAVAHVSCGQVARSQWAVIVDPDTGaelpdgevGEIWLHGDNIGRGYWGRPEETERTFGAklq 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 442622933 562 ------------EDGQRWFKTGDIGeIQADGVLKIIDRKKDLV 592
Cdd:PRK12476 460 srlaegshadgaADDGTWLRTGDLG-VYLDGELYITGRIADLI 501
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
284-365 |
2.24e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.10 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIAT----MKGFV---DMVPiYPDDVLIGFLPLAHvfelvaeSVCLMTGV 356
Cdd:PRK05850 155 RPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANfeqlMSDYFgdtGGVP-PPDTTVVSWLPFYH-------DMGLVLGV 226
|
90
....*....|...
gi 442622933 357 --PI--GYSTPLT 365
Cdd:PRK05850 227 caPIlgGCPAVLT 239
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
285-354 |
4.46e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 50.00 E-value: 4.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622933 285 PPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFV-DMVPIYPDDVLIGFLPLAHVFELVAesvCLMT 354
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIShDGLKVRPGDRCVSWLPFYHDMGLVG---FLLT 239
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
236-332 |
1.60e-05 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) 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 widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 48.33 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 236 LDKCPLVKTIIYiedqLQKTET-TGFKEGVKIlPFNQVVKtGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKN- 313
Cdd:cd05966 183 LEKCPSVEKVLV----VKRTGGeVPMTEGRDL-WWHDLMA-KQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGy 256
|
90 100
....*....|....*....|..
gi 442622933 314 ---CIATMKGFVDmvpIYPDDV 332
Cdd:cd05966 257 llyAATTFKYVFD---YHPDDI 275
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
535-712 |
1.88e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.63 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 535 GEVLIGGECVSQGYYKLPGKTNEDF----FEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELK 610
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFvphpFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIR-GYRIELGEIEARLH 4145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 611 TCGIIEN--ICVYGDPTKQYTVALVVPNQNhleelAQKHGlgdksfeelcsspiiekAILKEIAEHARKCkLQKYEVPAA 688
Cdd:PRK05691 4146 EQAEVREaaVAVQEGVNGKHLVGYLVPHQT-----VLAQG-----------------ALLERIKQRLRAE-LPDYMVPLH 4202
|
170 180
....*....|....*....|....
gi 442622933 689 ItlckeVWSPDMGLvTAAFKLKRK 712
Cdd:PRK05691 4203 W-----LWLDRLPL-NANGKLDRK 4220
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
483-587 |
2.00e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 47.56 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 483 GYGLTETTSgaTVMDYR-DMTYGrTGGPLTVCDIRLVNweegnyrvtnkpypqGEVLIGGECVSQGYYKlPGKTNeDFFE 561
Cdd:PRK09029 270 GYGLTEMAS--TVCAKRaDGLAG-VGSPLPGREVKLVD---------------GEIWLRGASLALGYWR-QGQLV-PLVN 329
|
90 100
....*....|....*....|....*.
gi 442622933 562 EDGqrWFKTGDIGEIQaDGVLKIIDR 587
Cdd:PRK09029 330 DEG--WFATRDRGEWQ-NGELTILGR 352
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
148-592 |
4.43e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 46.82 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 148 TFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHD 227
Cdd:PRK08276 13 TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 228 LLPKFKTLLDKCPLVKTIIYIEDQlqktETTGFkegvkiLPFNQVVKTGQDSKFEHVPPkGDDIAiimYTSGSTGTPKGV 307
Cdd:PRK08276 93 LADTAAELAAELPAGVPLLLVVAG----PVPGF------RSYEEALAAQPDTPIADETA-GADML---YSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 308 LlshknciatmkgfVDMVPIYPDDVLIGFL-PLAHVFELVAESVCLMTGvPIGYSTPLTLIDTSSKIkrgckGDATVL-- 384
Cdd:PRK08276 159 K-------------RPLPGLDPDEAPGMMLaLLGFGMYGGPDSVYLSPA-PLYHTAPLRFGMSALAL-----GGTVVVme 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 385 --------------KPTCMTSVPLILDRISKgINDKVNSGsafkkslfkflyqYKVKwvqrgyktplidklvfkkvaklm 450
Cdd:PRK08276 220 kfdaeealalieryRVTHSQLVPTMFVRMLK-LPEEVRAR-------------YDVS----------------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 451 ggKVRIIMSGGAPLSADTHEQIktclcLE-----LIQGYGLTEtTSGATVMDYRDM-----TYGRT-GGPLTVCDirlvn 519
Cdd:PRK08276 263 --SLRVAIHAAAPCPVEVKRAM-----IDwwgpiIHEYYASSE-GGGVTVITSEDWlahpgSVGKAvLGEVRILD----- 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622933 520 wEEGNyrvtnkPYPQGEvlIGGECVSQG-----YYKLPGKTNEdffEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLV 592
Cdd:PRK08276 330 -EDGN------ELPPGE--IGTVYFEMDgypfeYHNDPEKTAA---ARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI 395
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
257-367 |
4.64e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 46.65 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 257 TTGFKEGV----KILPFNQ--------VVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDM 324
Cdd:PRK07769 136 TTDSAEGVrkffRARPAKErprviavdAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDA 215
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 442622933 325 VPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLI 367
Cdd:PRK07769 216 LEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFV 258
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
284-635 |
9.99e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 45.81 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 284 VPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLA---HVFE----LVAESvCLMTGV 356
Cdd:PRK10252 593 QLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSfdvSVWEffwpFIAGA-KLVMAE 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 357 PIGYSTPLTLIDTsskIKRgckgdatvLKPTCMTSVPLILdriskgindkvnsgSAFKKSLfkflyqykvkwvqrgykTP 436
Cdd:PRK10252 672 PEAHRDPLAMQQF---FAE--------YGVTTTHFVPSML--------------AAFVASL-----------------TP 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 437 lidKLVFKKVAKLMggkvRIIMSGGApLSADTHEQIKTCLCLELIQGYGLTEttsgATVmdyrDMTYGRTGGPltvcDIR 516
Cdd:PRK10252 710 ---EGARQSCASLR----QVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTE----AAV----DVSWYPAFGE----ELA 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 517 LVN----------WEEGNYRVTNKPYPQ-----GEVLIGGECVSQGYYKLPGKTNEDFFEE---DGQRWFKTGDIGEIQA 578
Cdd:PRK10252 770 AVRgssvpigypvWNTGLRILDARMRPVppgvaGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERMYRTGDVARWLD 849
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622933 579 DGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENI----CVY------GDPTKQYtVALVVP 635
Cdd:PRK10252 850 DGAVEYLGRSDDQLKIR-GQRIELGEIDRAMQALPDVEQAvthaCVInqaaatGGDARQL-VGYLVS 914
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
239-341 |
1.09e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 45.44 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 239 CPLVKTiiyieDQLQKTETTGFKEGVKIL-----PFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKN 313
Cdd:PRK07867 102 CQLVLT-----ESAHAELLDGLDPGVRVInvdspAWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRK 176
|
90 100
....*....|....*....|....*...
gi 442622933 314 CIATMKGFVDMVPIYPDDVLIGFLPLAH 341
Cdd:PRK07867 177 VASAGVMLAQRFGLGPDDVCYVSMPLFH 204
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
453-609 |
1.35e-04 |
|
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: 44.87 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 453 KVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTvcdirlvnweegNYRVT---- 528
Cdd:cd05974 201 KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLP------------GYRVAlldp 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 529 -NKPYPQGEV-LIGGEC----VSQGYYKLPGKTNEDFfeEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKlqAGEY-VS 601
Cdd:cd05974 269 dGAPATEGEVaLDLGDTrpvgLMKGYAGDPDKTAHAM--RGG--YYRTGDIAMRDEDGYLTYVGRADDVFK--SSDYrIS 342
|
....*...
gi 442622933 602 LGKVESEL 609
Cdd:cd05974 343 PFELESVL 350
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
225-609 |
1.71e-04 |
|
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: 44.76 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 225 SHDLLPKFKTLLDKCPLVKTIIYIEDQLqktettgfKEGvkILPFNQVVKTGQDskfEH--VPPKGDDIAIIMYTSGSTG 302
Cdd:cd05928 121 SDELAPEVDSVASECPSLKTKLLVSEKS--------RDG--WLNFKELLNEAST---EHhcVETGSQEPMAIYFTSGTTG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 303 TPKgvLLSHKNCIATMKGFVD---MVPIYPDDVL-----IGFLPLA--HVFELVAESVCLMTGVPIGYStPLTLIDTSSK 372
Cdd:cd05928 188 SPK--MAEHSHSSLGLGLKVNgryWLDLTASDIMwntsdTGWIKSAwsSLFEPWIQGACVFVHHLPRFD-PLVILKTLSS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 373 IkrgckgdatvlkP-TCMTSVPlildriskgindkvnsgSAFKKSLFKFLYQYKVKWVQRGYktplidklvfkkvaklmg 451
Cdd:cd05928 265 Y------------PiTTFCGAP-----------------TVYRMLVQQDLSSYKFPSLQHCV------------------ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 452 gkvriimSGGAPLSADTHEQIKTCLCLELIQGYGLTETtsGATVMDYRDMTY--GRTGGPLTVCDIRLVNwEEGNYRVTN 529
Cdd:cd05928 298 -------TGGEPLNPEVLEKWKAQTGLDIYEGYGQTET--GLICANFKGMKIkpGSMGKASPPYDVQIID-DNGNVLPPG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 530 KpypQGEVLIGGE-----CVSQGYYKLPGKTNEDffeEDGQRWFkTGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGK 604
Cdd:cd05928 368 T---EGDIGIRVKpirpfGLFSGYVDNPEKTAAT---IRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFE 439
|
....*
gi 442622933 605 VESEL 609
Cdd:cd05928 440 VESAL 444
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
277-636 |
2.52e-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: 44.49 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 277 QDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLlsHKNCIATMKGFVDMVPIY---PDDVLIGFLPLAHVFE--------- 344
Cdd:cd17634 220 ASPEHQPEAMNAEDPLFILYTSGTTGKPKGVL--HTTGGYLVYAATTMKYVFdygPGDIYWCTADVGWVTGhsyllygpl 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 345 LVAESVCLMTGVPIGySTPLTLIDTSSKikrgckgdatvlkptcmtsvplildrisKGINDKVNSGSAFKKslfkfLYQY 424
Cdd:cd17634 298 ACGATTLLYEGVPNW-PTPARMWQVVDK----------------------------HGVNILYTAPTAIRA-----LMAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 425 KVKWVQRGYKTPLidklvfkkvaklmggkvRIIMSGGAPLSADTHEQIKTCLCLE---LIQGYGLTEtTSGATVMDYRDM 501
Cdd:cd17634 344 GDDAIEGTDRSSL-----------------RILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTE-TGGFMITPLPGA 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 502 TYGRTGGPL--------TVCDirlvnwEEGNyrvTNKPYPQGEVLIGGecvsqgyyKLPGKT-----NEDFFEEDGQRWF 568
Cdd:cd17634 406 IELKAGSATrpvfgvqpAVVD------NEGH---PQPGGTEGNLVITD--------PWPGQTrtlfgDHERFEQTYFSTF 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622933 569 K----TGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSLGKVESELKTCGIIENICVYG--DPTK-QYTVALVVPN 636
Cdd:cd17634 469 KgmyfSGDGARRDEDGYYWITGRSDDVINV-AGHRLGTAEIESVLVAHPKVAEAAVVGipHAIKgQAPYAYVVLN 542
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
269-606 |
2.75e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 44.15 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 269 FNQVVKTGQDSKFEhVPPKGDDIaIIMyTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAE 348
Cdd:PRK07788 190 LDDLIAGSSTAPLP-KPPKPGGI-VIL-TSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 349 SVCLMTGVpigystplTLIdtsskIKRgcKGDA-TVL------KPTCMTSVPLILDRIskgindkvnsgsafkkslfkfl 421
Cdd:PRK07788 267 TLAMALGS--------TVV-----LRR--RFDPeATLediakhKATALVVVPVMLSRI---------------------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 422 yqykvkwvqrgyktplIDkLVFKKVAKLMGGKVRIIMSGGAPLSAD----THEQIKTCLCleliQGYGLTEtTSGATVMD 497
Cdd:PRK07788 310 ----------------LD-LGPEVLAKYDTSSLKIIFVSGSALSPElatrALEAFGPVLY----NLYGSTE-VAFATIAT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 498 YRDM-----TYGRtggPLTVCDIRLVNwEEGNyrvtnkPYPQGEV---LIGGECVSQGYYKLPGKTnedffEEDGqrWFK 569
Cdd:PRK07788 368 PEDLaeapgTVGR---PPKGVTVKILD-ENGN------EVPRGVVgriFVGNGFPFEGYTDGRDKQ-----IIDG--LLS 430
|
330 340 350
....*....|....*....|....*....|....*..
gi 442622933 570 TGDIGEIQADGVLKIIDRKKDLVkLQAGEYVSLGKVE 606
Cdd:PRK07788 431 SGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVE 466
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
546-716 |
6.82e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 42.80 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 546 QGYYKLPGKTN----EDFFEEdGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQaGEYVSLGKVESELKTCGIIENICVY 621
Cdd:cd05937 315 QGYLHNEDATEsklvRDVFRK-GDIYFRTGDLLRQDADGRWYFLDRLGDTFRWK-SENVSTTEVADVLGAHPDIAEANVY 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 622 GdptkqytvaLVVPNQN--------HLEElaqkhglgdksfeelcSSPIIEKAILKEIAEHARKcKLQKYEVPAAITLCK 693
Cdd:cd05937 393 G---------VKVPGHDgragcaaiTLEE----------------SSAVPTEFTKSLLASLARK-NLPSYAVPLFLRLTE 446
|
170 180
....*....|....*....|...
gi 442622933 694 EVWSpdmglvTAAFKLKRKDIQD 716
Cdd:cd05937 447 EVAT------TDNHKQQKGVLRD 463
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
236-332 |
7.25e-04 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 43.00 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 236 LDKCPL-VKTIIYiedqLQKT--ETTGFKEGvKILPFNQVVKtGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVL---- 308
Cdd:TIGR02188 187 LEKCPVsVEHVLV----VRRTgnPVVPWVEG-RDVWWHDLMA-KASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLhttg 260
|
90 100
....*....|....*....|....*.
gi 442622933 309 --LSHknCIATMKGFVDmvpIYPDDV 332
Cdd:TIGR02188 261 gyLLY--AAMTMKYVFD---IKDGDI 281
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
534-635 |
9.57e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 42.42 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 534 QGEVLIGGECVSQGYYKLPGKTnEDFFEEDGqrWFKTGDIGEIQADGVLKIIDRKKDLVKLqAGEYVSLGKVESELKTCG 613
Cdd:PRK06164 377 SGEIEIRAPSLMRGYLDNPDAT-ARALTDDG--YFRTGDLGYTRGDGQFVYQTRMGDSLRL-GGFLVNPAEIEHALEALP 452
|
90 100
....*....|....*....|....
gi 442622933 614 IIENICVYGDPTKQYT--VALVVP 635
Cdd:PRK06164 453 GVAAAQVVGATRDGKTvpVAFVIP 476
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
283-342 |
1.41e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 41.89 E-value: 1.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 283 HVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIAtMKGFVDMVPIYPDDVLIGFLPLAHV 342
Cdd:cd05938 138 RAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLCGVTADDVIYITLPLYHS 196
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
226-311 |
1.51e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.70 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 226 HDLLPKFKTLLDKCPLVKTIIYIeDQLQKTETtgFKEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPK 305
Cdd:PRK03584 203 FDRRAKVAELRAALPSLEHVVVV-PYLGPAAA--AAALPGALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPK 279
|
90
....*....|...
gi 442622933 306 -------GVLLSH 311
Cdd:PRK03584 280 civhghgGILLEH 292
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
294-308 |
4.11e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 40.51 E-value: 4.11e-03
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
226-312 |
5.44e-03 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 39.95 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622933 226 HDLLPKFKTLLDKCPLVKTIIYIEDqLQKTETTGFKEGVKILPFNQVVKTGQDSK--FEHVPPkgDDIAIIMYTSGSTGT 303
Cdd:cd05943 187 HDVREKVAELVKGLPSLLAVVVVPY-TVAAGQPDLSKIAKALTLEDFLATGAAGEleFEPLPF--DHPLYILYSSGTTGL 263
|
90
....*....|....*.
gi 442622933 304 PK-------GVLLSHK 312
Cdd:cd05943 264 PKcivhgagGTLLQHL 279
|
|
| |
