|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
3-478 |
0e+00 |
|
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: 895.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 3 KNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL---TDKHET 79
Cdd:cd05933 118 KEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLrpaTVGQES 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 80 VVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAF 159
Cdd:cd05933 198 VVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 160 VWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESS 239
Cdd:cd05933 278 SWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 240 GPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFL 319
Cdd:cd05933 358 GPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 320 YVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGDKLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLG 399
Cdd:cd05933 438 YITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDKRKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLG 517
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584663 400 SQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 478
Cdd:cd05933 518 SQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-478 |
3.67e-147 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 433.37 E-value: 3.67e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 1 MKKNNNLYSWDDFMELGRSI-PDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHET 79
Cdd:COG1022 148 LRDDPRLLSLDELLALGREVaDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP-GDR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 80 VVSYLPLSHIAAQMMDIWVpIKIGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAF 159
Cdd:COG1022 227 TLSFLPLAHVFERTVSYYA-LAAGATVAFAESPD---TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 160 VWARNIGFKVNSKKMLGKYNTP---VSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLS 236
Cdd:COG1022 303 RWALAVGRRYARARLAGKSPSLllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 237 ESSGPHTISNQNNYRLLSCGKILTGCKNMLfqqnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGL 316
Cdd:COG1022 382 ETSPVITVNRPGDNRIGTVGPPLPGVEVKI-----AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDED 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 317 GFLYVTGHIKEILITAGGENVPPIPVETLVkKKIPIISNAMLVGDKLKFLSMLLTlkcemnqmsgepldkLNFEAI-NFC 395
Cdd:COG1022 457 GFLRITGRKKDLIVTSGGKNVAPQPIENAL-KASPLIEQAVVVGDGRPFLAALIV---------------PDFEALgEWA 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 396 RGLGSQASTVTEIVkqQDPLVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQID 475
Cdd:COG1022 521 EENGLPYTSYAELA--QDPEVRALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIE 597
|
...
gi 574584663 476 HMY 478
Cdd:COG1022 598 ALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
33-466 |
8.64e-121 |
|
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: 360.76 E-value: 8.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 33 KANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTkDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQAD 112
Cdd:cd05907 85 DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALA-ERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 113 AlkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKnsAKSMGLKKKAFVWArnigfkvnskkMLGKyntpvsyrmaktlvf 192
Cdd:cd05907 164 E---TLLDDLSEVRPTVFLAVPRVWEKVYAAIKV--KAVPGLKRKLFDLA-----------VGGR--------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 193 skvktslgldhCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKnmlFQQNKD 272
Cdd:cd05907 213 -----------LRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVE---VRIADD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 273 GigEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPI 352
Cdd:cd05907 279 G--EILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 353 ISNAMLVGDKLKFLSMLLTLKCEMNQMSGEPldklnfeainfcrgLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEaM 432
Cdd:cd05907 356 ISQAVVIGDGRPFLVALIVPDPEALEAWAEE--------------HGIAYTDVAELAA--NPAVRAEIEAAVEAANAR-L 418
|
410 420 430
....*....|....*....|....*....|....
gi 574584663 433 NNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFV 466
Cdd:cd05907 419 SRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
6-478 |
1.49e-73 |
|
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: 241.74 E-value: 1.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 6 NLYSWDDFMELGRSIPdtqlEQVIESqKANQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGA--VTKDFKLTDKHETVVS 82
Cdd:cd05927 90 KVYSLEEFEKLGKKNK----VPPPPP-KPEDLATICYTSGTTGNPKGVMLTHGNIvSNVAGVfkILEILNKINPTDVYIS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 83 YLPLSHIAAQMMdIWVPIKIGALTYFAQADALKgtLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWA 162
Cdd:cd05927 165 YLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 163 RNigFKVNSKKMLGKYNTPVSYRmaktLVFSKVKTSLGLdHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGP 241
Cdd:cd05927 242 LN--YKLAELRSGVVRASPFWDK----LVFNKIKQALGG-NVRLMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 242 HTISNQNNYRLLSCGKILTGCKNML--------FQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL 313
Cdd:cd05927 315 ATLTLPGDTSVGHVGGPLPCAEVKLvdvpemnyDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEW 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 314 DGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDKLKflSMLLTLKCemnqmsgepldkLNFEAI- 392
Cdd:cd05927 395 LPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARS-PFVAQIFVYGDSLK--SFLVAIVV------------PDPDVLk 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 393 NFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEamNNAQRIE--KWVILEKD-FSIYGGELGPMMKLKRHFVAQK 469
Cdd:cd05927 460 EWAASKGGGTGSFEELCK--NPEVKKAILEDLVRLGKE--NGLKGFEqvKAIHLEPEpFSVENGLLTPTFKLKRPQLKKY 535
|
....*....
gi 574584663 470 YKKQIDHMY 478
Cdd:cd05927 536 YKKQIDEMY 544
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
38-396 |
4.77e-60 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 203.83 E-value: 4.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVtKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqaDALKGT 117
Cdd:cd05914 92 ALINYTSGTTGNSKGVMLTYRNIVSNVDGV-KEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 LVSTLKEVKPTVFIGVPQIW--EKIHEMVKKNsaksmglkkkafvwarnigfKVNSKKMLGKYNTPVSYRMAKTLVFSKV 195
Cdd:cd05914 169 KIIALAFAQVTPTLGVPVPLviEKIFKMDIIP--------------------KLTLKKFKFKLAKKINNRKIRKLAFKKV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 196 KTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQN-KDGI 274
Cdd:cd05914 229 HEAFG-GNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDpATGE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 275 GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVET-LVKKKIPII 353
Cdd:cd05914 308 GEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAkINNMPFVLE 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 574584663 354 SNAMLVGDKLKFLSML----LTLKCEMNQ-----MSGEPLDKLNFEAINFCR 396
Cdd:cd05914 388 SLVVVQEKKLVALAYIdpdfLDVKALKQRniidaIKWEVRDKVNQKVPNYKK 439
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
5-470 |
3.10e-57 |
|
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: 197.69 E-value: 3.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 5 NNLYSWDDFMELGrsipdtQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYL 84
Cdd:cd05932 113 NCQYQWDDLIAQH------PPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEE-NDRMLSYL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 85 PLSHIAAQMMDIWVPIKIGALTYFAQA-DalkgTLVSTLKEVKPTVFIGVPQIWEKIHEmvkknsaksmglkkkafvwar 163
Cdd:cd05932 186 PLAHVTERVFVEGGSLYGGVLVAFAESlD----TFVEDVQRARPTLFFSVPRLWTKFQQ--------------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 164 NIGFKVNSKKMlgkyNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHT 243
Cdd:cd05932 241 GVQDKIPQQKL----NLLLKIPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSH 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 244 ISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTG 323
Cdd:cd05932 317 LNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITG 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 324 HIKEILITAGGENVPPIPVEtlvkKKI---PIISNAMLVGDKLKFLSMLLtlkcemnQMSGEPldklNFEAINFCRGlGS 400
Cdd:cd05932 392 RVKDIFKTSKGKYVAPAPIE----NKLaehDRVEMVCVIGSGLPAPLALV-------VLSEEA----RLRADAFARA-EL 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 401 QASTvteivkqqdplvyKAIQQGINAvnqeAMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKY 470
Cdd:cd05932 456 EASL-------------RAHLARVNS----TLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
7-470 |
5.40e-57 |
|
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: 198.42 E-value: 5.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 7 LYSWDDFMELGRSI----PDtQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWIAGAVTKDFKLTDkhETVV 81
Cdd:cd17641 127 LISFEDVVALGRALdrrdPG-LYEREVAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNfLGHCAAYLAADPLGPG--DEYV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 82 SYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVW 161
Cdd:cd17641 204 SVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE---TMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFEL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 162 ARNIGFKVNSKKMLGK---YNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSES 238
Cdd:cd17641 281 GMKLGLRALDRGKRGRpvsLWLRLASWLADALLFRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTEL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 239 SGPHTISNQNNYRLLSCGKILTGCknmlfQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGF 318
Cdd:cd17641 361 AGAYTVHRDGDVDPDTVGVPFPGT-----EVRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGH 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 319 LYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDKLKFLSMLLTLKcemnqmsgepldklnFEAI-NFCRG 397
Cdd:cd17641 436 LVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEAVVLGAGRPYLTAFICID---------------YAIVgKWAEQ 499
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584663 398 LGSQASTVTEIVKQqdPLVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKY 470
Cdd:cd17641 500 RGIAFTTYTDLASR--PEVYELIRKEVEKVNAS-LPEAQRIRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
19-466 |
6.27e-53 |
|
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: 185.88 E-value: 6.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 19 SIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITW-IAGAVTKDFKLTDKHETVVSYLPLSHI---AAQMm 94
Cdd:cd17639 72 SLNETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAgIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 95 diwVPIKIGALTYFAQADAL--------KGTLVstlkEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarNIG 166
Cdd:cd17639 151 ---VCLYRGGTIGYGSPRTLtdkskrgcKGDLT----EFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLF----WTA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 167 FKVNSKKMLGKYNTPVsyrmAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISN 246
Cdd:cd17639 220 YQSKLKALKEGPGTPL----LDELVFKKVRAALG-GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 247 QNNYRLLSCGKILTGCKNML--------FQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGF 318
Cdd:cd17639 295 PGDLETGRVGPPLPCCEIKLvdweeggySTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 319 LYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGD--KLKFLSMLLTlkcemNQmsgEPLDKlnfeainFCR 396
Cdd:cd17639 375 LKIIDRKKDLVKLQNGEYIALEKLESIYRSN-PLVNNICVYADpdKSYPVAIVVP-----NE---KHLTK-------LAE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584663 397 GLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEAmnNAQRIE---KWVILEKDFSIYGGELGPMMKLKRHFV 466
Cdd:cd17639 439 KHGVINSEWEELCE--DKKLQKAVLKSLAETARAA--GLEKFEipqGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
37-360 |
1.83e-51 |
|
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: 180.78 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 37 CAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA----LTYFAQAD 112
Cdd:COG0318 102 TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP-GDVVLVALPLFHVFGLTVGLLAPLLAGAtlvlLPRFDPER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 113 ALKgtlvsTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntpvsYRMAKTLVF 192
Cdd:COG0318 181 VLE-----LIERERVTVLFGVPTML----------------------------------------------ARLLRHPEF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 193 SKVKTSlgldHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNY--RLLSCGKILTGCKNMLFqq 269
Cdd:COG0318 210 ARYDLS----SLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVNPEDPGerRPGSVGRPLPGVEVRIV-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 270 NKDG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 342
Cdd:COG0318 284 DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEV 361
|
330
....*....|....*...
gi 574584663 343 ETLVkKKIPIISNAMLVG 360
Cdd:COG0318 362 EEVL-AAHPGVAEAAVVG 378
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
17-332 |
1.21e-50 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 177.50 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 17 GRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNI----TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQ 92
Cdd:pfam00501 137 EEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGP-DDRVLSTLPLFHDFGL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 93 MMDIWVPIKIGA-LTYFAQADALKGT-LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkvn 170
Cdd:pfam00501 216 SLGLLGPLLAGAtVVLPPGFPALDPAaLLELIERYKVTVLYGVPTLLNML------------------------------ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 171 skkmlgkyntpVSYRMAKTLVFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNN 249
Cdd:pfam00501 266 -----------LEAGAPKRALLSSLRL---------VLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 250 YRLL---SCGKILTGCK------NMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLY 320
Cdd:pfam00501 326 EDLRslgSVGRPLPGTEvkivddETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLE 405
|
330
....*....|..
gi 574584663 321 VTGHIKEILITA 332
Cdd:pfam00501 406 IVGRKKDQIKLG 417
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
9-478 |
5.94e-50 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 180.68 E-value: 5.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 9 SWDDFMELGRSIPdtqleQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWIAGA-VTKDFKLTDKHetvVSYLPL 86
Cdd:PLN02736 200 TYSKLLAQGRSSP-----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNlIANVAGSsLSTKFYPSDVH---ISYLPL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 87 SHI---AAQMMDIWVPIKIGaltyFAQADALKgtLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwar 163
Cdd:PLN02736 272 AHIyerVNQIVMLHYGVAVG----FYQGDNLK--LMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLF---- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 164 NIGFkvNSKK---MLGKYNTPvsyrMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFflsLDIPIG----ELYGLS 236
Cdd:PLN02736 342 NAAY--NAKKqalENGKNPSP----MWDRLVFNKIKAKLG-GRVRFMSSGASPLSPDVMEF---LRICFGgrvlEGYGMT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 237 ESSGPHTISNQNNYrllSCGKI----------LTGCKNMLFqQNKDGI---GEICLWGRHIFMGYLESETETTEAIDDEG 303
Cdd:PLN02736 412 ETSCVISGMDEGDN---LSGHVgspnpacevkLVDVPEMNY-TSEDQPyprGEICVRGPIIFKGYYKDEVQTREVIDEDG 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 304 WLHSGDLGQ-LDGlGFLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAMLVGDKLKflSMLLTLkcemnqMSGE 382
Cdd:PLN02736 488 WLHTGDIGLwLPG-GRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFVYGDSLN--SSLVAV------VVVD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 383 PLDKLNFEAINfcrglGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKD-FSIYGGELGPMMKL 461
Cdd:PLN02736 558 PEVLKAWAASE-----GIKYEDLKQLCN--DPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEpFTVENGLLTPTFKV 630
|
490
....*....|....*..
gi 574584663 462 KRHFVAQKYKKQIDHMY 478
Cdd:PLN02736 631 KRPQAKAYFAKAISDMY 647
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
36-348 |
2.49e-48 |
|
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: 169.39 E-value: 2.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 36 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAaQMMDIWVPIKIGA----LTYFAQA 111
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE-GDVFLSTLPLFHIG-GLFGLLGALLAGGtvvlLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 112 DALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwARNIGFKvnskkmlgkyntpvsyrmakTLV 191
Cdd:cd04433 79 AALE-----LIEREKVTILLGVPTLLARL---------------------LKAPESA--------------------GYD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 192 FSKVKTslgldhchsFISGTAPLNQETAEFFLSL-DIPIGELYGLSESSGPHTISN--QNNYRLLSCGKILTGCKNMLFQ 268
Cdd:cd04433 113 LSSLRA---------LVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPpdDDARKPGSVGRPVPGVEVRIVD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 269 QNKD-----GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:cd04433 184 PDGGelppgEIGELVVRGPSVMKGYWNNP-EATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVE 261
|
....*
gi 574584663 344 TLVKK 348
Cdd:cd04433 262 AVLLG 266
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
38-466 |
4.77e-47 |
|
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: 169.08 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTkDFKLTDKHETVVSYLPLSHIAAQmmdiwvpikigALTYFAqadALKG- 116
Cdd:cd17640 91 ATIIYTSGTTGNPKGVMLTHANLLHQIRSLS-DIVPPQPGDRFLSILPIWHSYER-----------SAEYFI---FACGc 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 117 --------TLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIG-FKVNskkmlgkyntpvsyrma 187
Cdd:cd17640 156 sqaytsirTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGiFKFG----------------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 188 ktlvfskvktslgldhchsfISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF 267
Cdd:cd17640 219 --------------------ISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 268 QQNKDGI------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIP 341
Cdd:cd17640 279 DPEGNVVlppgekGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 342 VE-TLVKKkiPIISNAMLVGDKLKFLSMLLTlkcemnqmsgePldklNFEAINfcRGLGSQASTVTEIVKQ--QDPLVYK 418
Cdd:cd17640 359 IEeALMRS--PFIEQIMVVGQDQKRLGALIV-----------P----NFEELE--KWAKESGVKLANDRSQllASKKVLK 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 574584663 419 AIQQGINAV--NQEAMNNAQRIEKWVILEKDFsIYGGELGPMMKLKRHFV 466
Cdd:cd17640 420 LYKNEIKDEisNRPGFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRNVV 468
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
7-478 |
2.53e-42 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 159.21 E-value: 2.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 7 LYSWDDFMELGRSIPdtqlEQVIESQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAV---TKDFKLTDKHETV-VS 82
Cdd:PLN02430 197 TYSWIDFLHMGKENP----SETNPPKPLDICTIM-YTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQFEDKMTHDDVyLS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 83 YLPLSHIAAQMMDIWVPIKIGALTYF-AQADALKgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvw 161
Cdd:PLN02430 272 FLPLAHILDRMIEEYFFRKGASVGYYhGDLNALR----DDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIF-- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 162 arNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFF-LSLDIPIGELYGLSESSG 240
Cdd:PLN02430 346 --NALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEFLrVTSCAFVVQGYGLTETLG 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 241 PHTISNQNNYRLLSCGKILTGCKNMLFQQ---------NKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLG 311
Cdd:PLN02430 423 PTTLGFPDEMCMLGTVGAPAVYNELRLEEvpemgydplGEPPRGEICVRGKCLFSGYYKNPELTEEVMKD-GWFHTGDIG 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 312 QLDGLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDKLKflSMLLTLKCemnqmsgepldkLNF 389
Cdd:PLN02430 502 EILPNGVLKIIDRKKNLIKLSQGEYV---ALEYLenVYGQNPIVEDIWVYGDSFK--SMLVAVVV------------PNE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 390 EAINFCRGLGSQASTVTEIVKQqdPLVYKAIQQGINAVnqEAMNNAQRIE--KWVILE-KDFSIYGGELGPMMKLKRHFV 466
Cdd:PLN02430 565 ENTNKWAKDNGFTGSFEELCSL--PELKEHILSELKST--AEKNKLRGFEyiKGVILEtKPFDVERDLVTATLKKRRNNL 640
|
490
....*....|..
gi 574584663 467 AQKYKKQIDHMY 478
Cdd:PLN02430 641 LKYYQVEIDEMY 652
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
38-343 |
7.68e-39 |
|
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: 146.55 E-value: 7.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA----LTYFAQAD 112
Cdd:cd05936 128 AVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdLLEGDDVVLAALPLFHVFGLTVALLLPLALGAtivlIPRFRPIG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 113 ALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsaksMGLKKKAFVWarnigfkvnskkmlgkyntpvsyrmaktlvF 192
Cdd:cd05936 208 VLK-----EIRKHRVTIFPGVPTMYIAL-----------LNAPEFKKRD------------------------------F 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 193 SKVKTSlgldhchsfISGTAPLNQETAEFFLSL-DIPIGELYGLSESSgPHTISNQ--NNYRLLSCGKILTGCKNMLFqq 269
Cdd:cd05936 242 SSLRLC---------ISGGAPLPVEVAERFEELtGVPIVEGYGLTETS-PVVAVNPldGPRKPGSIGIPLPGTEVKIV-- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 270 NKDG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILItAGGENVPPIPV 342
Cdd:cd05936 310 DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREV 387
|
.
gi 574584663 343 E 343
Cdd:cd05936 388 E 388
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
6-478 |
1.43e-38 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 148.84 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 6 NLYSWDDFMELGRSipDTQLEQvieSQKANQCAVLiYTSGTTGIPKGVMLSHDNItwIAGAVTKD--FKLTDK----HET 79
Cdd:PLN02861 197 SCFSWEEFSLMGSL--DCELPP---KQKTDICTIM-YTSGTTGEPKGVILTNRAI--IAEVLSTDhlLKVTDRvateEDS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 80 VVSYLPLSHIAAQMMDIWVpIKIGALTYFAQADALkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAF 159
Cdd:PLN02861 269 YFSYLPLAHVYDQVIETYC-ISKGASIGFWQGDIR--YLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLF 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 160 VWARNigFKV-NSKKMLGKYNTpvSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIP-IGELYGLSE 237
Cdd:PLN02861 346 DFAYN--YKLgNLRKGLKQEEA--SPRLDR-LVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 238 SSGPHTISNQNNYRLL-SCGKILTGCKNMLFQQNKDGI--------GEICLWGRHIFMGYLESETETTEAIDDeGWLHSG 308
Cdd:PLN02861 420 SCGGCFTSIANVFSMVgTVGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTG 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 309 DLGQLDGLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDklKFLSMLLTLKCEMNQmSGEPLDK 386
Cdd:PLN02861 499 DIGEWQPNGAMKIIDRKKNIFKLSQGEYV---AVENLenTYSRCPLIASIWVYGN--SFESFLVAVVVPDRQ-ALEDWAA 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 387 LNFEAINF---CrglgsqastvteivkqQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKD-FSIYGGELGPMMKLK 462
Cdd:PLN02861 573 NNNKTGDFkslC----------------KNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLK 636
|
490
....*....|....*.
gi 574584663 463 RHFVAQKYKKQIDHMY 478
Cdd:PLN02861 637 RPQLLKYYKDCIDQLY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
7-478 |
2.40e-36 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 142.47 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 7 LYSWDDFMELGRSipdTQLEQVIEsQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-----LTDKhETVV 81
Cdd:PLN02614 200 IYAWDEFLKLGEG---KQYDLPIK-KKSDICTIM-YTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVK-DVYL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 82 SYLPLSHIAAQMMDIWVpIKIGALTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVW 161
Cdd:PLN02614 274 SYLPLAHIFDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDS 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 162 ARNIGFKvNSKKmlGKYNTPVSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLD-IPIGELYGLSESSG 240
Cdd:PLN02614 351 AFSYKFG-NMKK--GQSHVEASPLCDK-LVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCA 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 241 PHTISNQNNYRLLscGKILTGCKNM------LFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGD 309
Cdd:PLN02614 426 GTFVSLPDELDML--GTVGPPVPNVdirlesVPEMEYDALastprGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 310 LGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAMLVGDklKFLSMLLTLKCEMNQM----SGEPLD 385
Cdd:PLN02614 503 VGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGN--SFESFLVAIANPNQQIlerwAAENGV 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 386 KLNFEAInfCRGLGSQASTVTEIVKQQDPLVYKAIQQgINAVNQEAMNnaqriekwVILEKDFsiyggeLGPMMKLKRHF 465
Cdd:PLN02614 580 SGDYNAL--CQNEKAKEFILGELVKMAKEKKMKGFEI-IKAIHLDPVP--------FDMERDL------LTPTFKKKRPQ 642
|
490
....*....|...
gi 574584663 466 VAQKYKKQIDHMY 478
Cdd:PLN02614 643 LLKYYQSVIDEMY 655
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
7-345 |
4.10e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 141.65 E-value: 4.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 7 LYSWDDFMELGRSIPDTQLEQVIESqkANQCAVLIYTSGTTGIPKGVMLSHDNITwiAGAVTKDFKLTD------KHETV 80
Cdd:PTZ00216 238 LVAWTDVVAKGHSAGSHHPLNIPEN--NDDLALIMYTSGTTGDPKGVMHTHGSLT--AGILALEDRLNDligppeEDETY 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 81 VSYLPLSHIaaqmMDIWVP---IKIGALTYFAQADalkgTLVST-------LKEVKPTVFIGVPQIWEKIHEMVKKNSAK 150
Cdd:PTZ00216 314 CSYLPLAHI----MEFGVTnifLARGALIGFGSPR----TLTDTfarphgdLTEFRPVFLIGVPRIFDTIKKAVEAKLPP 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 151 SMGLKKKAFVWArnigFKVNSKKMLGKYNTPvsYRMAKtlVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIG 230
Cdd:PTZ00216 386 VGSLKRRVFDHA----YQSRLRALKEGKDTP--YWNEK--VFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVNVVFGMVI 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 231 ELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNK-------DGIGEICLWGRHIFMGYLESETETTEAIDDEG 303
Cdd:PTZ00216 457 QGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEykhtdtpEPRGEILLRGPFLFKGYYKQEELTREVLDEDG 536
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 574584663 304 WLHSGDLGQLDGLGFLYVTGHIKEILITAGGENvppIPVETL 345
Cdd:PTZ00216 537 WFHTGDVGSIAANGTLRIIGRVKALAKNCLGEY---IALEAL 575
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
10-343 |
1.23e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 138.78 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 10 WDDFMELGRSIPDTQLEQVIEsqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHI 89
Cdd:PRK06187 145 VGEYEELLAAASDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRD-DVYLVIVPMFHV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 90 AAqmmdiW----VPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEkihemvkknsaksmglkkkafvwarn 164
Cdd:PRK06187 221 HA-----WglpyLALMAGAkQVIPRRFDP--ENLLDLIETERVTFFFAVPTIWQ-------------------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 165 igfkvnskkMLGKYntPVSYRMAktlvFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSG--- 240
Cdd:PRK06187 268 ---------MLLKA--PRAYFVD----FSSLRL---------VIYGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvs 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 241 ----PHTISNQNNYRLlSCGKILTGCK------NMLFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGD 309
Cdd:PRK06187 324 vlppEDQLPGQWTKRR-SAGRPLPGVEarivddDGDELPPDGGeVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGD 401
|
330 340 350
....*....|....*....|....*....|....
gi 574584663 310 LGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK06187 402 VGYIDEDGYLYITDRIKDVIIS-GGENIYPRELE 434
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
32-345 |
2.49e-35 |
|
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: 137.34 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 32 QKANQCAVLIYTSGTTGIPKGVMLSHDNIT-WIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKiGALTY--- 107
Cdd:cd05911 143 DGKDDTAAILYSSGTTGLPKGVCLSHRNLIaNLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIimp 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 108 -FAQADALKgtlvsTLKEVKPTVFIGVPQIwekiheMVkknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSYRM 186
Cdd:cd05911 222 kFDSELFLD-----LIEKYKITFLYLVPPI------AA-----------------------------ALAKSPLLDKYDL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 187 AktlvfskvktSLgldhcHSFISGTAPLNQETAEFFLSLDIP--IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKN 264
Cdd:cd05911 262 S----------SL-----RVILSGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 265 MLF------QQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVP 338
Cdd:cd05911 327 KIVdddgkdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVA 405
|
....*..
gi 574584663 339 PIPVETL 345
Cdd:cd05911 406 PAELEAV 412
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
38-343 |
4.43e-34 |
|
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: 132.73 E-value: 4.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLSHIAAQMMDIWVPIKIGALTYFAQA-DAlkG 116
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVV-APLFHIGGLGVFTLPTLLRGGTVVILRKfDP--E 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 117 TLVSTLKEVKPTVFIGVPQIWEKihemvkknsaksmglkkkafvwarnigfkvnskkMLgkyNTPVsyrmAKTLVFSKVK 196
Cdd:cd17631 178 TVLDLIERHRVTSFFLVPTMIQA----------------------------------LL---QHPR----FATTDLSSLR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 197 TslgldhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTI--SNQNNYRLLSCGKILTGCKNMLFQQNKD-- 272
Cdd:cd17631 217 A---------VIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFlsPEDHRRKLGSAGRPVFFVEVRIVDPDGRev 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584663 273 ---GIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:cd17631 288 ppgEVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVE 359
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
3-479 |
2.20e-32 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 130.62 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 3 KNNNLYSWDDFMELGRSIP-DTQLEqviesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVV 81
Cdd:PLN02387 223 SNWTVSSFSEVEKLGKENPvDPDLP------SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 82 SYLPLSHI---AAQ--MMDIWVPIKIG-ALTYFAQADALK-GTL--VSTLkevKPTVFIGVPQIWEKIHEMVKKNSAKSM 152
Cdd:PLN02387 297 AYLPLAHIlelAAEsvMAAVGAAIGYGsPLTLTDTSNKIKkGTKgdASAL---KPTLMTAVPAILDRVRDGVRKKVDAKG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 153 GLKKKAF--VWARNIGFKVNS-------KKMLgkYNtpvsyrmakTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFF- 222
Cdd:PLN02387 374 GLAKKLFdiAYKRRLAAIEGSwfgawglEKLL--WD---------ALVFKKIRAVLG-GRIRFMLSGGAPLSGDTQRFIn 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 223 LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI---------GEICLWGRHIFMGYLESET 293
Cdd:PLN02387 442 ICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQE 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 294 ETTEA--IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDklKFLSML 369
Cdd:PLN02387 522 KTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVS-PYVDNIMVHAD--PFHSYC 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 370 LTLKCEMNQMSGEPLDKLNFEAINFCRgLGSQASTVTEivkqqdplvykaIQQGINAVNQEAmnnaqRIEKWVI------ 443
Cdd:PLN02387 599 VALVVPSQQALEKWAKKAGIDYSNFAE-LCEKEEAVKE------------VQQSLSKAAKAA-----RLEKFEIpakikl 660
|
490 500 510
....*....|....*....|....*....|....*.
gi 574584663 444 LEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH 479
Cdd:PLN02387 661 LPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
9-343 |
1.58e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 121.16 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 9 SWDDFMELGrsipdTQLEQVIEsQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSH 88
Cdd:PRK07656 146 TFTDFLAAG-----DPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEG-DRYLAANPFFH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 89 IAAQMMDIWVPIKIGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIwekihemvkknsaksmglkkkafvwarn 164
Cdd:PRK07656 219 VFGYKAGVNAPLMRGAtilpLPVFDPDEVFR-----LIETERITVLPGPPTM---------------------------- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 165 igfkvnskkmlgkYNTPVSYRMAKTLVFSkvktSLGLdhchsFISGTAPLNQETAEFFLS-LDIP-IGELYGLSESSGPH 242
Cdd:PRK07656 266 -------------YNSLLQHPDRSAEDLS----SLRL-----AVTGAASMPVALLERFESeLGVDiVLTGYGLSEASGVT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 243 TISNQNNYRLLSCGKILTGCKNM-------LFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLD 314
Cdd:PRK07656 324 TFNRLDDDRKTVAGTIGTAIAGVenkivneLGEEVPVGeVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLD 403
|
330 340
....*....|....*....|....*....
gi 574584663 315 GLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK07656 404 EEGYLYIVDRKKDMFIV-GGFNVYPAEVE 431
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
38-345 |
1.92e-26 |
|
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: 111.94 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVV-SYLPLSHIAAqmmdiwvpikigaLTYFAQAD-ALK 115
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFlCVLPMFHIYG-------------LSSFALGLlRLG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 116 GTLVStlkevkptvfigvpqiwekiheMVKKNSAKSMGLKKKafvwarnigFKVNSkkmlgkynTPVSYRMAKTLVFSKV 195
Cdd:cd05904 228 ATVVV----------------------MPRFDLEELLAAIER---------YKVTH--------LPVVPPIVLALVKSPI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 196 KTSLGLDHCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGP-HTISN--QNNYRLLSCGKILTGCKNMLFQQN 270
Cdd:cd05904 269 VDKYDLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvAMCFApeKDRAKYGSVGRLVPNVEAKIVDPE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 271 KDGI------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVET 344
Cdd:cd05904 349 TGESlppnqtGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKE-LIKYKGFQVAPAELEA 427
|
.
gi 574584663 345 L 345
Cdd:cd05904 428 L 428
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
15-360 |
2.53e-26 |
|
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: 110.84 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 15 ELGRSIPDTQLEQVI---ESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAA 91
Cdd:cd05941 66 PLNPSYPLAELEYVItdsEPSLVLDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT-EDDVLLHVLPLHHVHG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 92 QMMDIWVPIKIGA----LTYFaqaDAlkgTLVSTLKEVKP-TVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarnig 166
Cdd:cd05941 145 LVNALLCPLFAGAsvefLPKF---DP---KEVAISRLMPSiTVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 167 fkvnsKKMlgkyntpvsyRMaktlvfskvktslgldhchsFISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgpHTIS 245
Cdd:cd05941 212 -----ERL----------RL--------------------MVSGSAALPVPTLEEWEAITgHTLLERYGMTEIG--MALS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 246 N--QNNYRLLSCGKILTGCKNMLFQQN------KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG 317
Cdd:cd05941 255 NplDGERRPGTVGMPLPGVQARIVDEEtgeplpRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDG 334
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 574584663 318 FLYVTGHIKEILITAGGENVPPIPVETLVkKKIPIISNAMLVG 360
Cdd:cd05941 335 YYWILGRSSVDIIKSGGYKVSALEIERVL-LAHPGVSECAVIG 376
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
38-343 |
5.55e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 109.69 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqadalkgT 117
Cdd:cd05934 84 ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGED-DVYLTVLPLFHINAQAVSVLAALSVGA------------T 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 LVsTLKEVKPTVFIGVpqiwekihemVKKNSAksmglkkkafVWARNIGfkvnskKMLGK-YNTPVSYRMAktlvfskvk 196
Cdd:cd05934 151 LV-LLPRFSASRFWSD----------VRRYGA----------TVTNYLG------AMLSYlLAQPPSPDDR--------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 197 tslglDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF----QQNKD 272
Cdd:cd05934 195 -----AHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVdddgQELPA 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574584663 273 G-IGEICL-----WGrhIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 343
Cdd:cd05934 270 GePGELVIrglrgWG--FFKGYYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVE 342
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
39-360 |
6.52e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 110.33 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 39 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIaaqmmdiwvpikiGALTYFAQADALKGTL 118
Cdd:PRK06839 153 IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLT-MHDRSIVLLPLFHI-------------GGIGLFAFPTLFAGGV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 119 V------------STLKEVKPTVFIGVPQIWEKIHEMVKKnsaksmglkkkafvwarnigfkvnskkmlgkyntpvsyrm 186
Cdd:PRK06839 219 IivprkfeptkalSMIEKHKVTVVMGVPTIHQALINCSKF---------------------------------------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 187 aktlvfskVKTSLglDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYR--LLSCGKILTGCKN 264
Cdd:PRK06839 259 --------ETTNL--QSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDY 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 265 MLFQQNKD-----GIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPP 339
Cdd:PRK06839 329 ELIDENKNkvevgEVGELLIRGPNVMKEYWNRPDATEETIQD-GWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYP 406
|
330 340
....*....|....*....|.
gi 574584663 340 IPVETLVkKKIPIISNAMLVG 360
Cdd:PRK06839 407 LEVEQVI-NKLSDVYEVAVVG 426
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
5-346 |
3.46e-25 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 108.81 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 5 NNLYSWDDFMELGR--SIPDTQLEqviesqkANQCAVLIYTSGTTGIPKGVMLSHDNIT--------WIAGAVtkdfKLT 74
Cdd:PRK08751 183 NGAIRFREALALGRkhSMPTLQIE-------PDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqqahqWLAGTG----KLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 75 DKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksmgl 154
Cdd:PRK08751 252 EGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGL-------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 155 kkkafvwarnigfkvnskkmlgkYNTPvsyrMAKTLVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGELY 233
Cdd:PRK08751 318 -----------------------LNTP----GFDQIDFSSLKMTLG---------GGMAVQRSVAERWKQVTgLTLVEAY 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 234 GLSESS-----GPHTISNQNNYRLL------SCGKILTGCKNMLFQqnkdgIGEICLWGRHIFMGYLESETETTEAIDDE 302
Cdd:PRK08751 362 GLTETSpaaciNPLTLKEYNGSIGLpipstdACIKDDAGTVLAIGE-----IGELCIKGPQVMKGYWKRPEETAKVMDAD 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 574584663 303 GWLHSGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETLV 346
Cdd:PRK08751 437 GWLHTGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVI 479
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
38-343 |
4.45e-24 |
|
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: 104.70 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVsYLPLSHIAAQMM----------DIWVPIKIGALTY 107
Cdd:cd05926 152 ALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLV-VMPLFHVHGLVAsllstlaaggSVVLPPRFSASTF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 108 FAQadalkgtlvstLKEVKPTVFIGVPQIwekiHEMVKKNSAKSmglkkkafvwarnigfkvnskkmlgKYNTPVSYRma 187
Cdd:cd05926 231 WPD-----------VRDYNATWYTAVPTI----HQILLNRPEPN-------------------------PESPPPKLR-- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 188 ktlvfskvktslgldhchsFI-SGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTiSNQ---NNYRLLSCGKIlTGC 262
Cdd:cd05926 269 -------------------FIrSCSASLPPAVLEALeATFGAPVLEAYGMTEAAHQMT-SNPlppGPRKPGSVGKP-VGV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 263 KNMLFQQN----KDG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENV 337
Cdd:cd05926 328 EVRILDEDgeilPPGvVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKEL-INRGGEKI 406
|
....*.
gi 574584663 338 PPIPVE 343
Cdd:cd05926 407 SPLEVD 412
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
16-360 |
8.23e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 104.44 E-value: 8.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 16 LGRSIPDTQLEQVIESQK---------ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPL 86
Cdd:PRK06087 159 LAPATSSLSLSQIIADYEplttaitthGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT-WQDVFMMPAPL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 87 SHIAAQMMDIWVPIKIGALTYFAQadalkgtlvstlkEVKPTVFIGVpqiwekihemvkknsaksmgLKKKAFVWarnig 166
Cdd:PRK06087 238 GHATGFLHGVTAPFLIGARSVLLD-------------IFTPDACLAL--------------------LEQQRCTC----- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 167 fkvnskkMLGKynTPVSYRMAKTLVFSKVK-TSLGLdhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTIS 245
Cdd:PRK06087 280 -------MLGA--TPFIYDLLNLLEKQPADlSALRF-----FLCGGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 246 NQNN---YRLLSCGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG 317
Cdd:PRK06087 345 NLDDplsRFMHTDGYAAAGVEIKVVDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAG 424
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 574584663 318 FLYVTGHIKEILITaGGENVPPIPVETLVKKKiPIISNAMLVG 360
Cdd:PRK06087 425 YIKITGRKKDIIVR-GGENISSREVEDILLQH-PKIHDACVVA 465
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
38-360 |
8.39e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 104.31 E-value: 8.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNI--------TWIAGavtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYF 108
Cdd:PRK05605 222 ALILYTSGTTGKPKGAQLTHRNLfanaaqgkAWVPG-------LGDGPERVLAALPMFHAYGLTLCLTLAVSIGGeLVLL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 109 AQADAlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKnsaksmglkkkafvwaRNIGFKvnskkmlgkyntpvSYRMAk 188
Cdd:PRK05605 295 PAPDI--DLILDAMKKHPPTWLPGVPPLYEKIAEAAEE----------------RGVDLS--------------GVRNA- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 189 tlvfskvktslgldhchsfISGTAPLNQETAEFFLSLdipIG----ELYGLSESSgPHTISN--QNNYRLLSCG------ 256
Cdd:PRK05605 342 -------------------FSGAMALPVSTVELWEKL---TGgllvEGYGLTETS-PIIVGNpmSDDRRPGYVGvpfpdt 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 257 KILTGCKNMLFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGE 335
Cdd:PRK05605 399 EVRIVDPEDPDETMPDGeEGELLVRGPQVFKGYWNRPEETAKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGF 476
|
330 340
....*....|....*....|....*
gi 574584663 336 NVPPIPVETlVKKKIPIISNAMLVG 360
Cdd:PRK05605 477 NVYPAEVEE-VLREHPGVEDAAVVG 500
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
38-360 |
1.20e-23 |
|
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: 102.81 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAqmmdiwVPIKIGALTYfaqadALKGT 117
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED-DNWLCALPLFHISG------LSILMRSVIY-----GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 LVSTLKEvkptvfigvpqiwEKIHEMVKKNSAKSMGLKKKAFVWarnigfkvnskkMLGKYNTPVSYRMAKTLVfskvkt 197
Cdd:cd05912 148 LVDKFDA-------------EQVLHLINSGKVTIISVVPTMLQR------------LLEILGEGYPNNLRCILL------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 198 slgldhchsfisGTAPLNQETAEFFLSLDIPIGELYGLSE-SSGPHTISNQNNY-RLLSCGKILTGCKNMLFQ--QNKDG 273
Cdd:cd05912 197 ------------GGGPAPKPLLEQCKEKGIPVYQSYGMTEtCSQIVTLSPEDALnKIGSAGKPLFPVELKIEDdgQPPYE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 274 IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 353
Cdd:cd05912 265 VGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEEVL-LSHPAI 341
|
....*..
gi 574584663 354 SNAMLVG 360
Cdd:cd05912 342 KEAGVVG 348
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
7-343 |
3.49e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 102.54 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 7 LYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPL 86
Cdd:PRK12583 173 FLAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTE-HDRLCVPVPL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 87 SHIAAQMMDIWVPIKIGA-LTYFAQA-DALkGTLvSTLKEVKPTVFIGVPQIWekIHEMvkknsaksmglkkkafvwarn 164
Cdd:PRK12583 252 YHCFGMVLANLGCMTVGAcLVYPNEAfDPL-ATL-QAVEEERCTALYGVPTMF--IAEL--------------------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 165 igfkvnSKKMLGKYNtpvsyrmaktlvFSKVKTSlgldhchsfISGTAPLNQET-----AEFFLSlDIPIGelYGLSESS 239
Cdd:PRK12583 307 ------DHPQRGNFD------------LSSLRTG---------IMAGAPCPIEVmrrvmDEMHMA-EVQIA--YGMTETS 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 240 GPHTISNQNN---YRLLSCGKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLG 311
Cdd:PRK12583 357 PVSLQTTAADdleRRVETVGRTQPHLEVKVVDPDgatvpRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLA 436
|
330 340 350
....*....|....*....|....*....|..
gi 574584663 312 QLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK12583 437 TMDEQGYVRIVGRSKDMIIR-GGENIYPREIE 467
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
38-343 |
9.94e-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: 96.40 E-value: 9.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIA--GAVTKDFKLTDkheTVVSYLPLSHIAAQMMDIWVPIKIGALTYFA-----Q 110
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAwmLALNSLFDPDD---VLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 111 ADALKGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkAFVWARNIGFKVNSkkmlgkyntpvsYRMAktl 190
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVY--------------------AALLQVPVNADISS------------LRFA--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 191 vfskvktslgldhchsfISGTAPLNQET-AEFFLSLDIPIGELYGLSESSGPHTISNQNN-YRLLSCG----------KI 258
Cdd:cd05944 127 -----------------MSGAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGlrlpyarvriKV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 259 LTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVP 338
Cdd:cd05944 190 LDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVAD-GWLNTGDLGRLDADGYLFITGRAKD-LIIRGGHNID 267
|
....*
gi 574584663 339 PIPVE 343
Cdd:cd05944 268 PALIE 272
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
40-360 |
3.56e-21 |
|
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: 94.10 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 40 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT-DKHETVVSylPLSHIAAQMMDIWVPIKIGAlTYFAQA--DALKg 116
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTeDDRYLIIN--PFFHTFGYKAGIVACLLTGA-TVVPVAvfDVDA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 117 tLVSTLKEVKPTVFIGVPQIWEKI--HEMVKKnsaksmglkkkafvwarnigFKVNSKK--MLGKYNTPVSY--RMAKTL 190
Cdd:cd17638 81 -ILEAIERERITVLPGPPTLFQSLldHPGRKK--------------------FDLSSLRaaVTGAATVPVELvrRMRSEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 191 VFSKVKTSLGLDHChsfisGTAPLNQEtaefflsldipigelyglseSSGPHTISNqnnyrllSCGKILTGcknmlFQQN 270
Cdd:cd17638 140 GFETVLTAYGLTEA-----GVATMCRP--------------------GDDAETVAT-------TCGRACPG-----FEVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 271 KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILItAGGENVPPIPVETLVkKKI 350
Cdd:cd17638 183 IADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-AEH 260
|
330
....*....|
gi 574584663 351 PIISNAMLVG 360
Cdd:cd17638 261 PGVAQVAVIG 270
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
8-343 |
3.66e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 96.42 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 8 YSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT----WIAGAVtkdfKLTDKhETVVSY 83
Cdd:PRK08315 172 LNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILnngyFIGEAM----KLTEE-DRLCIP 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 84 LPLSHIAAQMMDIWVPIKIGA-LTYFAQA-DALKgTLVSTLKEvKPTVFIGVPQ--IWEKIHEMVKKnsaksmglkkkaf 159
Cdd:PRK08315 247 VPLYHCFGMVLGNLACVTHGAtMVYPGEGfDPLA-TLAAVEEE-RCTALYGVPTmfIAELDHPDFAR------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 160 vwarnigFKVNSKK---MLGKyNTPVSyrmaktlVFSKVKTSLGLDhchsfisgtaplnqetaefflslDIPIGelYGLS 236
Cdd:PRK08315 312 -------FDLSSLRtgiMAGS-PCPIE-------VMKRVIDKMHMS-----------------------EVTIA--YGMT 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 237 ESSGPHTISNQNN---YRLLSCGKIL-----------TGCKNMLFQQnkdgiGEICLWGRHIFMGYLESETETTEAIDDE 302
Cdd:PRK08315 352 ETSPVSTQTRTDDpleKRVTTVGRALphlevkivdpeTGETVPRGEQ-----GELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 574584663 303 GWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIE 466
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
38-360 |
5.01e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 93.55 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLSHIAAQMMdIWVPIKIGALTYFAQADALkgt 117
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLS-LPLYHVGGLAI-LVRSLLAGAELVLLERNQA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 LVSTLKEVKPTVFIGVP-QIWekiheMVKKNSAKSMGLKkkafvwarniGFKVnskkmlgkyntpvsyrmaktlVFSkvk 196
Cdd:cd17630 78 LAEDLAPPGVTHVSLVPtQLQ-----RLLDSGQGPAALK----------SLRA---------------------VLL--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 197 tslgldhchsfisGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGE 276
Cdd:cd17630 119 -------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----GE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 277 ICLWGRHIFMGYLESETEttEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNA 356
Cdd:cd17630 181 IWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAAL-AAHPAVRDA 256
|
....
gi 574584663 357 MLVG 360
Cdd:cd17630 257 FVVG 260
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
12-343 |
5.78e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 90.01 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 12 DFMELGRSIPDTQLEQViESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT---WIAGAVTKDfkltDKHETVVSYLPLSH 88
Cdd:PRK07529 191 DFDAELARQPGDRLFSG-RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVanaWLGALLLGL----GPGDTVFCGLPLFH 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 89 IAAQMMDIWVPIKIGALTYFAQADALKG-TLVSTLKEV----KPTVFIGVPqiwekihemvkknSAKSMGLKKKafVWAR 163
Cdd:PRK07529 266 VNALLVTGLAPLARGAHVVLATPQGYRGpGVIANFWKIveryRINFLSGVP-------------TVYAALLQVP--VDGH 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 164 NIgfkvnskkmlgkyntpvsyrmaktlvfSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPH 242
Cdd:PRK07529 331 DI---------------------------SSLRY---------ALCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVS 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 243 TIsnqnNY-----RLLSCG--------KILTGCKNMLFQQN--KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHS 307
Cdd:PRK07529 375 SV----NPpdgerRIGSVGlrlpyqrvRVVILDDAGRYLRDcaVDEVGVLCIAGPNVFSGYLEAAHNKGLWLED-GWLNT 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 574584663 308 GDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 343
Cdd:PRK07529 450 GDLGRIDADGYFWLTGRAKD-LIIRGGHNIDPAAIE 484
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
33-360 |
9.96e-19 |
|
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: 88.74 E-value: 9.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 33 KANQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDKHET-VVSYLPLSHiAAQMMDIWVPIKIGA----LT 106
Cdd:cd17642 182 RDEQVALIMNSSGSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPDTaILTVIPFHH-GFGMFTTLGYLICGFrvvlMY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 107 YFAQAdalkgTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkAFVwarnigfkvNSKKMLGKYNtpvsyrm 186
Cdd:cd17642 261 KFEEE-----LFLRSLQDYKVQSALLVPTLF--------------------AFF---------AKSTLVDKYD------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 187 aktlvfskvktslgLDHCHSFISGTAPLNQETAEFFLS-LDIP-IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKN 264
Cdd:cd17642 300 --------------LSNLHEIASGGAPLSKEVGEAVAKrFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 265 MLFQQNKDGI------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVP 338
Cdd:cd17642 366 KVVDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVP 444
|
330 340
....*....|....*....|..
gi 574584663 339 PIPVETLVKKKiPIISNAMLVG 360
Cdd:cd17642 445 PAELESILLQH-PKIFDAGVAG 465
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
42-360 |
1.16e-18 |
|
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: 86.95 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 42 YTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYlPLSHIAAQMMDIWVPIKIGALTYFAQA--DALkgTLV 119
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPV-PLFHCFGSVLGVLACLTHGATMVFPSPsfDPL--AVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 120 STLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkVNSKKMLgKYNtpvsyrmaktlvFSKVKTSl 199
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAE----------------------------LEHPDFD-KFD------------LSSLRTG- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 200 gldhchsfISGTAPLNQETAEFFLSL----DIPIGelYGLSESSGPHTISNQNN---YRLLSCGKIL----------TGC 262
Cdd:cd05917 124 --------IMAGAPCPPELMKRVIEVmnmkDVTIA--YGMTETSPVSTQTRTDDsieKRVNTVGRIMphteakivdpEGG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 263 KNMLFQQnkdgIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 342
Cdd:cd05917 194 IVPPVGV----PGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPREI 268
|
330
....*....|....*...
gi 574584663 343 ETLVKKKiPIISNAMLVG 360
Cdd:cd05917 269 EEFLHTH-PKVSDVQVVG 285
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
32-354 |
1.18e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 88.31 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 32 QKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSH----IAAQMmdiwVPIKIGALTY 107
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK-DRILSWMPLTHdmglIAFHL----APLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 108 FAqadalkgtlvstlkevkPT-VFIGVPQIW-EKIHEmvkknsaksmglKKKAFVWARNIGFKVnskkMLGKYNTPVSYr 185
Cdd:cd05908 178 LM-----------------PTrLFIRRPILWlKKASE------------HKATIVSSPNFGYKY----FLKTLKPEKAN- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 186 maktlvfskvktSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESS--------GPHTI------ 244
Cdd:cd05908 224 ------------DWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrnailPVYGLAEASvgaslpkaQSPFKtitlgr 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 245 --------------SNQNNYRLLSCGKILTGCK-NMLFQQNK---DG-IGEICLWGRHIFMGYLESETETTEAIDDEGWL 305
Cdd:cd05908 292 rhvthgepepevdkKDSECLTFVEVGKPIDETDiRICDEDNKilpDGyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 574584663 306 HSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVETLVKKKIPIIS 354
Cdd:cd05908 372 KTGDLGFIRN-GRLVITGREKDIIFV-NGQNVYPHDIERIAEELEGVEL 418
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
36-360 |
1.56e-17 |
|
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: 84.74 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 36 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQA-DAL 114
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG-DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwDPD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 115 KGtlVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKkaFVWArnigfkvnskkmlGKYNTPVSYRMAKTLVFSK 194
Cdd:cd05903 173 KA--LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT--FVCG-------------GATVPRSLARRAAELLGAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 195 VKTSLGLDHCHSFISGTAPLNQETAEF-----FLSLDIPIGELYGLSESSGPhtisnqnnyrllscgkiltgcknmlfqq 269
Cdd:cd05903 236 VCSAYGSTECPGAVTSITPAPEDRRLYtdgrpLPGVEIKVVDDTGATLAPGV---------------------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 270 nkdgIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKK 349
Cdd:cd05903 288 ----EGELLSRGPSVFLGYLDRP-DLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLL-LG 360
|
330
....*....|.
gi 574584663 350 IPIISNAMLVG 360
Cdd:cd05903 361 HPGVIEAAVVA 371
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
39-360 |
1.66e-17 |
|
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: 83.47 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 39 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVpIKIGA----LTYFAQADAL 114
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTE-ADVYLNMLPLFHIAGLNLALAT-FHAGGanvvMEKFDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 115 KgtlvsTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKsmglkkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvFSK 194
Cdd:cd17637 82 E-----LIEEEKVTLMGSFPPILSNLLDAAEKSGVD-----------------------------------------LSS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 195 VKTSLGLDhchsfisgtAPlnqETAEFFLSL-DIPIGELYGLSESSGPHTISNQNNyRLLSCGKILTGCKNMLFQQNKDG 273
Cdd:cd17637 116 LRHVLGLD---------AP---ETIQRFEETtGATFWSLYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDDNDRP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 274 I-----GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHI--KEiLITAGGENVPPIPVETlV 346
Cdd:cd17637 183 VpagetGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKE-LIKPGGENVYPAEVEK-V 259
|
330
....*....|....
gi 574584663 347 KKKIPIISNAMLVG 360
Cdd:cd17637 260 ILEHPAIAEVCVIG 273
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
32-364 |
1.81e-17 |
|
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: 84.69 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 32 QKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqA 111
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPE-DVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-P 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 112 DALKG-TLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLKKKAfvwarnigfkvnskkmlGKYNTPvSYRMAktl 190
Cdd:cd05909 222 NPLDYkKIPELIYDKKATILLGTPTFL--------------RGYARAA-----------------HPEDFS-SLRLV--- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 191 vfskvktslgldhchsfISGTAPLNQETAEFFLSL-DIPIGELYGLSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQ 268
Cdd:cd05909 267 -----------------VAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTPQSPNKEGTvGRPLPGMEVKIVS 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 269 ---QNKDGIGE---ICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPV 342
Cdd:cd05909 330 vetHEEVPIGEgglLLVRGPNVMLGYLNEPELTSFAFGD-GWYDTGDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAI 407
|
330 340
....*....|....*....|....
gi 574584663 343 ETLVKKKIPIISN--AMLVGDKLK 364
Cdd:cd05909 408 EDILSEILPEDNEvaVVSVPDGRK 431
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
35-346 |
3.11e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 84.31 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 35 NQCAVLIYTSGTTGIPKGVMLSHDN--------ITWIagavtkdFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALT 106
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNlvsntlmgVQWL-------YNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 107 YFAQADALKgTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkafvwarnigfkvnskkmLGKYNTPvsyrM 186
Cdd:PRK06710 279 VLIPKFDMK-MVFEAIKKHKVTLFPGAPTIY-------------------------------------IALLNSP----L 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 187 AKTLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSldIPIGEL---YGLSESSgPHTISN----------------Q 247
Cdd:PRK06710 317 LKEYDISSIRAC---------ISGSAPLPVEVQEKFET--VTGGKLvegYGLTESS-PVTHSNflwekrvpgsigvpwpD 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 248 NNYRLLS--CGKILTGCKnmlfqqnkdgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHI 325
Cdd:PRK06710 385 TEAMIMSleTGEALPPGE----------IGEIVVKGPQIMKGYWNKPEETAAVLQD-GWLHTGDVGYMDEDGFFYVKDRK 453
|
330 340
....*....|....*....|.
gi 574584663 326 KEiLITAGGENVPPIPVETLV 346
Cdd:PRK06710 454 KD-MIVASGFNVYPREVEEVL 473
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
38-339 |
3.77e-17 |
|
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: 83.83 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQadalkgt 117
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDP-GDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 lvstlkevkPTVFIGVPQIWekiHEMVKKNSAKSMGlkkkafvwARNIGF-----KVNSKKM----LGKYNT------PV 182
Cdd:cd05931 224 ---------PAAFLRRPLRW---LRLISRYRATISA--------APNFAYdlcvrRVRDEDLegldLSSWRValngaePV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 183 SyrmAKTL-VFSKVKTSLGLD-HCHS----------FISGTAPLNQETAEFFLSLdipigELYGLSESSGPHTisnQNNY 250
Cdd:cd05931 284 R---PATLrRFAEAFAPFGFRpEAFRpsyglaeatlFVSGGPPGTGPVVLRVDRD-----ALAGRAVAVAADD---PAAR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 251 RLLSCGKILTGcknMLF--------QQNKDG-IGEICLWGRHIFMGYL--ESETETT----EAIDDEGWLHSGDLGQLDG 315
Cdd:cd05931 353 ELVSCGRPLPD---QEVrivdpetgRELPDGeVGEIWVRGPSVASGYWgrPEATAETfgalAATDEGGWLRTGDLGFLHD 429
|
330 340
....*....|....*....|....
gi 574584663 316 lGFLYVTGHIKEILITAgGENVPP 339
Cdd:cd05931 430 -GELYITGRLKDLIIVR-GRNHYP 451
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
38-346 |
5.68e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 83.56 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNI-------TWIAGAVtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaq 110
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMlanleqaKAAYGPL-----LHPGKELVVTALPLYHIFALTVNCLLFIELGG------ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 111 adalKGTLVSTLKEvkptvfigvpqiwekIHEMVKKnsaksmgLKKKAFVWARNigfkVNSkkmlgKYNTPVSYRMAKTL 190
Cdd:PRK08974 278 ----QNLLITNPRD---------------IPGFVKE-------LKKYPFTAITG----VNT-----LFNALLNNEEFQEL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 191 VFSKVKTSLGldhchsfisGTAPLNQETAEFFLSL-DIPIGELYGLSESS-----GPHTISNQNNyrllSCG-------- 256
Cdd:PRK08974 323 DFSSLKLSVG---------GGMAVQQAVAERWVKLtGQYLLEGYGLTECSplvsvNPYDLDYYSG----SIGlpvpstei 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 257 KILTGCKNMLFQqnkDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGEN 336
Cdd:PRK08974 390 KLVDDDGNEVPP---GEPGELWVKGPQVMLGYWQRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDM-ILVSGFN 464
|
330
....*....|
gi 574584663 337 VPPIPVETLV 346
Cdd:PRK08974 465 VYPNEIEDVV 474
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
38-343 |
6.12e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 83.11 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhetvVSYL---PLSHIAAQMMdiwVP--IKIGALTYFAQAD 112
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPAD----PRFLmctPLSHAGGAFF---LPtlLRGGTVIVLAKFD 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 113 AlkGTLVSTLKEVKPTVFIGVP-QIWEKI-HEMVKKNSAKSMGLkkkafvwarnigfkvnskkmlgkyntpVSYrmaktl 190
Cdd:PRK06188 244 P--AEVLRAIEEQRITATFLVPtMIYALLdHPDLRTRDLSSLET---------------------------VYY------ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 191 vfskvktslgldhchsfisGTAPLN----QETAEFFLsldiPI-GELYGLSESsgPHTIS--------NQNNYRLLSCGK 257
Cdd:PRK06188 289 -------------------GASPMSpvrlAEAIERFG----PIfAQYYGQTEA--PMVITylrkrdhdPDDPKRLTSCGR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 258 ILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITa 332
Cdd:PRK06188 344 PTPGLRVALLDEDgrevaQGEVGEICVRGPLVMDGYWNRPEETAEAFRD-GWLHTGDVAREDEDGFYYIVDRKKDMIVT- 421
|
330
....*....|.
gi 574584663 333 GGENVPPIPVE 343
Cdd:PRK06188 422 GGFNVFPREVE 432
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
40-362 |
7.27e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 83.11 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 40 LIYTSGTTGIPKGVMLSHDN-ITWIAGAVTKD-----FKLTDkheTVVSYLPLSHIaaqmmdiwvpikigaltYfaqadA 113
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHKGlVTSVAQQVDGEnpnlyFHSDD---VILCVLPMFHI-----------------Y-----S 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 114 LKGTLVSTLKeVKPTVFIgvpqiwekiheMVKKNSAKSMGLKKKafvwarnigFKVNskkmLGKYNTPVSYRMAKtlvfS 193
Cdd:PLN02246 239 LNSVLLCGLR-VGAAILI-----------MPKFEIGALLELIQR---------HKVT----IAPFVPPIVLAIAK----S 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 194 KVKTSLGLDHCHSFISGTAPLNQETAEFFLSlDIP---IGELYGLSESsGPhtisnqnnyrLL----------------S 254
Cdd:PLN02246 290 PVVEKYDLSSIRMVLSGAAPLGKELEDAFRA-KLPnavLGQGYGMTEA-GP----------VLamclafakepfpvksgS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 255 CG--------KIL---TGCKnmlFQQNKDGigEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTG 323
Cdd:PLN02246 358 CGtvvrnaelKIVdpeTGAS---LPRNQPG--EICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVD 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 574584663 324 HIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVGDK 362
Cdd:PLN02246 433 RLKEL-IKYKGFQVAPAELEALLISH-PSIADAAVVPMK 469
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
38-333 |
7.98e-17 |
|
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: 82.49 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKGT 117
Cdd:cd05922 120 ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI-TADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaKSMGLKKKAFVWARnigfkvnskkmlgkYNTPVSYRMAKTLVfskvkt 197
Cdd:cd05922 198 FWEDLREHGATGLAGVPSTYAML---------TRLGFDPAKLPSLR--------------YLTQAGGRLPQETI------ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 198 slgldhchsfisgtaplnQETAEFFLSLDIPIgeLYGLSESSG------PHTISNqnnyRLLSCGKILTGCKnmLFQQNK 271
Cdd:cd05922 249 ------------------ARLRELLPGAQVYV--MYGQTEATRrmtylpPERILE----KPGSIGLAIPGGE--FEILDD 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584663 272 DG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAG 333
Cdd:cd05922 303 DGtptppgePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFG 371
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
33-346 |
1.91e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 81.73 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 33 KANQCAVLIYTSGTTGIPKGVMLSHDNItwIAGAV-TKDF---KLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYF 108
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNL--VANMLqCRALmgsNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNIL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 109 AQADALKGTLVSTLKEVKPTVFIGVPQIwekihemvkknsaksmglkkkaFV-WARNIGFKvnskkmlgkyntpvsyrma 187
Cdd:PRK05677 283 ISNPRDLPAMVKELGKWKFSGFVGLNTL----------------------FVaLCNNEAFR------------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 188 kTLVFSKVKTSLgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGLSESSGPHTISNQNNYRLLSCGKIL--TGCKN 264
Cdd:PRK05677 322 -KLDFSALKLTL---------SGGMALQLATAERWKEVTgCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVpsTLCKV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 265 MlfqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGeNV 337
Cdd:PRK05677 392 I----DDDGnelplgeVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NV 466
|
....*....
gi 574584663 338 PPIPVETLV 346
Cdd:PRK05677 467 YPNELEDVL 475
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
9-343 |
2.44e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 81.52 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 9 SWDDFMELGRSIPDTQLEQVIESqkaNQCAVLIYTSGTTGIPKGVMLSHDNITW------IAGAVTKDfkltdkhETVVS 82
Cdd:PRK08316 148 GWLDFADWAEAGSVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHRALIAeyvsciVAGDMSAD-------DIPLH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 83 YLPLSHiAAQMMDIWVP-IKIGALTYFAQADALkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLkkkafvw 161
Cdd:PRK08316 218 ALPLYH-CAQLDVFLGPyLYVGATNVILDAPDP-ELILRTIEAERITSFFAPPTVW--------------ISL------- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 162 ARNIGFKVNSKKMLGK--YNT-----PVSYRMAKTLvfskvkTSLGLDHChsfisgtaplnqetaefflsldipigelYG 234
Cdd:PRK08316 275 LRHPDFDTRDLSSLRKgyYGAsimpvEVLKELRERL------PGLRFYNC----------------------------YG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 235 LSESSGPHTISNQNNY--RLLSCGKiltgckNMLFQQNK----DG-------IGEICLWGRHIFMGYLESETETTEAIDD 301
Cdd:PRK08316 321 QTEIAPLATVLGPEEHlrRPGSAGR------PVLNVETRvvddDGndvapgeVGEIVHRSPQLMLGYWDDPEKTAEAFRG 394
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 574584663 302 eGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK08316 395 -GWFHSGDLGVMDEEGYITVVDRKKDMIKT-GGENVASREVE 434
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3-346 |
2.50e-16 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 81.56 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 3 KNNNLYSWDDFMELGRSIPDTQLEQVIesQKANQCAvLIYTSGTTGIPKGVMLSHDNItwIAGAVTKDFKLTDK---HET 79
Cdd:PLN02330 155 KIEGAVNWKELLEAADRAGDTSDNEEI--LQTDLCA-LPFSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEmigQVV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 80 VVSYLPLSHIAAqmmdiwvpikigaltyfaqadaLKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVkknsaksmglkkkaf 159
Cdd:PLN02330 230 TLGLIPFFHIYG----------------------ITGICCATLRNKGKVVVMSRFELRTFLNALI--------------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 160 vwARNIGFkvnskkmlgkynTPVSYRMAKTLVFSKVKTSLGLDHC--HSFISGTAPLNQETAEFFLSL--DIPIGELYGL 235
Cdd:PLN02330 273 --TQEVSF------------APIVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 236 SESS-------GP---HTISNQNnyrllSCGKILTGCKNMLFQQN------KDGIGEICLWGRHIFMGYLESETETTEAI 299
Cdd:PLN02330 339 TEHScitlthgDPekgHGIAKKN-----SVGFILPNLEVKFIDPDtgrslpKNTPGELCVRSQCVMQGYYNNKEETDRTI 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 574584663 300 DDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLV 346
Cdd:PLN02330 414 DEDGWLHTGDIGYIDDDGDIFIVDRIKE-LIKYKGFQVAPAELEAIL 459
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
38-346 |
4.45e-16 |
|
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: 80.79 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALkgt 117
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ-DVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEI--- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 lvstLKEvkPTVFIgvpqiwekihEMVKKNSAksmglkkkAFVWARNigFkvnskkMLGKYNTPVSYRMAKTLVFSKVKt 197
Cdd:cd05906 246 ----LAD--PLRWL----------DLIDRYRV--------TITWAPN--F------AFALLNDLLEEIEDGTWDLSSLR- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 198 slgldhchSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-------SSGPHTISNQNNYRLLSCGKILTGCK 263
Cdd:cd05906 293 --------YLVNAGEAVVAKTIRRLLRLLEPYGlppdairPAFGMTEtcsgviySRSFPTYDHSQALEFVSLGRPIPGVS 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 264 NMLFQQNKDG-----IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEILITaGGENVP 338
Cdd:cd05906 365 MRIVDDEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIV-NGVNYY 442
|
....*...
gi 574584663 339 PIPVETLV 346
Cdd:cd05906 443 SHEIEAAV 450
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-360 |
1.09e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 79.24 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI---AAQMMDIWVPIKIGALTYFaqaDAl 114
Cdd:PRK03640 144 ATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTE-DDCWLAAVPIFHIsglSILMRSVIYGMRVVLVEKF---DA- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 115 kgtlvstlkevkptvfigvpqiwEKIHEMVKKNSAKSMGlkkkafvwarnigfkvnskkmlgkyntpVSYRMAKTLVfsk 194
Cdd:PRK03640 219 -----------------------EKINKLLQTGGVTIIS----------------------------VVSTMLQRLL--- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 195 vkTSLGLDHCHS----FISGTAPLNQETAEFFLSLDIPIGELYGLSESSG------PHTISNqnnyRLLSCGKILTGC-- 262
Cdd:PRK03640 245 --ERLGEGTYPSsfrcMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASqivtlsPEDALT----KLGSAGKPLFPCel 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 263 ---KNMLFQQNKDgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPP 339
Cdd:PRK03640 319 kieKDGVVVPPFE-EGEIVVKGPNVTKGYLNREDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYP 395
|
330 340
....*....|....*....|.
gi 574584663 340 IPVETlVKKKIPIISNAMLVG 360
Cdd:PRK03640 396 AEIEE-VLLSHPGVAEAGVVG 415
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
38-310 |
1.15e-15 |
|
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: 79.42 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDfkLTDKHETVVSYLPLSHIAAQMmdiwvpIKIGALT-----YFAQ 110
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLVAtfWLKVSSIQD--IRPPASITLNFMPMSHIAGRI------SLYGTLArggtaYFAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 111 ADALKgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVsyrmaktl 190
Cdd:cd17632 298 ASDMS-TLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLAAV-------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 191 vfskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELYGLSEsSGPHTISNQ------NNYRLLSC---GKILT 260
Cdd:cd17632 369 ------------------CGSAPLSAEMKAFMESlLDLDLHDGYGSTE-AGAVILDGVivrppvLDYKLVDVpelGYFRT 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 574584663 261 gcknmlfqQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 310
Cdd:cd17632 430 --------DRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
38-343 |
1.31e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 79.27 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqaDALKGT 117
Cdd:PRK07768 155 ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGA-------ELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 lvstlkevkPTVFIGVPQIWekihemvkknsAKSMGLKKKAFVWARNIGFKVNSKKmLGKYNTPVSYRMaktlvfSKVKT 197
Cdd:PRK07768 228 ---------PMDFLRDPLLW-----------AELISKYRGTMTAAPNFAYALLARR-LRRQAKPGAFDL------SSLRF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 198 SLgldhchsfiSGTAPLNQETAEFFLSLDIPIG-------ELYGLSESSGPHTIS------------------------- 245
Cdd:PRK07768 281 AL---------NGAEPIDPADVEDLLDAGARFGlrpeailPAYGMAEATLAVSFSpcgaglvvdevdadllaalrravpa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 246 -NQNNYRLLSCGKILTGCKNMLFQQNKD-----GIGEICLWGRHIFMGYLESETeTTEAIDDEGWLHSGDLGQLDGLGFL 319
Cdd:PRK07768 352 tKGNTRRLATLGPPLPGLEVRVVDEDGQvlpprGVGVIELRGESVTPGYLTMDG-FIPAQDADGWLDTGDLGYLTEEGEV 430
|
330 340
....*....|....*....|....
gi 574584663 320 YVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK07768 431 VVCGRVKDVIIM-AGRNIYPTDIE 453
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
38-346 |
4.25e-15 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 76.15 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKgT 117
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK-S 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 LVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLkkkafvwaRNIGFkvnskkmlgkyntpvsyrmaktlvfskvkt 197
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSL--------RLIGY------------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 198 slgldhchsfiSGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLL-SCGKILTGCK-----NMLFQQNK 271
Cdd:cd17635 125 -----------GGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEInAVGRPYPGVDvylaaTDGIAGPS 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574584663 272 DGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLV 346
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLGERREDGFLFITGRSSES-INCGGVKIAPDEVERIA 266
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
21-360 |
4.94e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 77.53 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 21 PDTQLEQVIESQKANQC-----AVLI-YTSGTTGIPKGVMLSHDNIT-------WIAGAVTKDFKLtdkHETvvsylPLS 87
Cdd:PLN02860 152 TEMLKQRALGTTELDYAwapddAVLIcFTSGTTGRPKGVTISHSALIvqslakiAIVGYGEDDVYL---HTA-----PLC 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 88 HIA------AQMMdiwvpikIGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIHEMvkknSAKSMGLKKK 157
Cdd:PLN02860 224 HIGglssalAMLM-------VGAchvlLPKFDAKAALQ-----AIKQHNVTSMITVPAMMADLISL----TRKSMTWKVF 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 158 AFVwarnigfkvnsKKML-GKYNTPVSYRMAKTLVF--SKVKTSLGL-DHCHSFIsgtaplnqetaefFLSLDIPIGELY 233
Cdd:PLN02860 288 PSV-----------RKILnGGGSLSSRLLPDAKKLFpnAKLFSAYGMtEACSSLT-------------FMTLHDPTLESP 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 234 GLSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQ 312
Cdd:PLN02860 344 KQTLQTVNQTKSSSVHQPQGVCvGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGW 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 574584663 313 LDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG 360
Cdd:PLN02860 424 IDKAGNLWLIGRSNDR-IKTGGENVYPEEVEAVLSQH-PGVASVVVVG 469
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
40-360 |
1.05e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 76.08 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 40 LIYTSGTTGIPKGVMLSHDNITW------IAGAVTKDFKLTdkhetVVSylPLSHIAA-QMMDIWVPIKIGALTYFAQAD 112
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWksidhvIALGLTASERLL-----VVG--PLYHVGAfDLPGIAVLWVGGTLRIHREFD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 113 AlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSaksmgLKKKAFVWArnIGfkvnskkmlGKYNTPVSYRMAKTLVF 192
Cdd:PRK06145 227 P--EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDR-----FDLDSLAWC--IG---------GGEKTPESRIRDFTRVF 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 193 SKVKtslgldhchsFISGtaplnqetaefflsldipigelYGLSESSGPHTISNQNNY--RLLSCGK--------ILTGC 262
Cdd:PRK06145 289 TRAR----------YIDA----------------------YGLTETCSGDTLMEAGREieKIGSTGRalahveirIADGA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 263 KNMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 342
Cdd:PRK06145 337 GRWLPPNMK---GEICMRGPKVTKGYWKDPEKTAEAFYG-DWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEV 411
|
330
....*....|....*...
gi 574584663 343 ETLVkKKIPIISNAMLVG 360
Cdd:PRK06145 412 ERVI-YELPEVAEAAVIG 428
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
38-343 |
1.27e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 76.08 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVsYLPLSH----IAAQMMDIwvpIKIGALTYFAQADA 113
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVA-VMPLYHghglIAALLATL---ASGGAVLLPARGRF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 114 LKGTLVSTLKEVKPTVFIGVPqiweKIHEMvkknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSYRMAKTLVFS 193
Cdd:PRK05852 255 SAHTFWDDIKAVGATWYTAVP----TIHQI------------------------------LLERAATEPSGRKPAALRFI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 194 KvktslgldhchsfiSGTAPLNQETAEF----FLSldiPIGELYGLSE---------------------SSGPHTISNQN 248
Cdd:PRK05852 301 R--------------SCSAPLTAETAQAlqteFAA---PVVCAFGMTEathqvtttqiegigqtenpvvSTGLVGRSTGA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 249 NYRLL-SCGKILTgcknmlfqqnKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKE 327
Cdd:PRK05852 364 QIRIVgSDGLPLP----------AGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKE 432
|
330
....*....|....*.
gi 574584663 328 iLITAGGENVPPIPVE 343
Cdd:PRK05852 433 -LINRGGEKISPERVE 447
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1-343 |
1.36e-14 |
|
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: 75.74 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 1 MKKNNNLYSWDDFmeLGRSIPDTQLEQVIEsqkaNQCAVLIYTSGTTGIPKGVMLSHDNITWIA-GAVTKDFKLTDKHET 79
Cdd:cd12119 135 EPAGVGVLAYEEL--LAAESPEYDWPDFDE----NTAAAICYTSGTTGNPKGVVYSHRSLVLHAmAALLTDGLGLSESDV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 80 VVSYLPLSHIAAqmmdiW-VPIK---IGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLK 155
Cdd:cd12119 209 VLPVVPMFHVNA-----WgLPYAaamVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 156 KkafvwarnigfkvnskkmlgkyntpvsyrmaktlvfskvktslgldhchsFISGTAPLNQETAEFFLSLDIPIGELYGL 235
Cdd:cd12119 284 R--------------------------------------------------VVIGGSAVPRSLIEAFEERGVRVIHAWGM 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 236 SESSGPHTIS------------NQNNYRllscgkILTGCKNMLFQ---QNKDG---------IGEICLWGRHIFMGYLES 291
Cdd:cd12119 314 TETSPLGTVArppsehsnlsedEQLALR------AKQGRPVPGVElriVDDDGrelpwdgkaVGELQVRGPWVTKSYYKN 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 574584663 292 EtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 343
Cdd:cd12119 388 D-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSVELE 437
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
38-455 |
1.85e-14 |
|
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: 75.55 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDF-KLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFaqaDALK- 115
Cdd:cd05921 168 AKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYpFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYI---DDGKp 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 116 -----GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmgLKKKAFvwarnigfkvnsKKMlgkyntpvsyrmaktl 190
Cdd:cd05921 245 mpggfEETLRNLREISPTVYFNVPAGWEMLVAALEKDEA----LRRRFF------------KRL---------------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 191 vfskvktslgldhcHSFISGTAPLNQETAEfflSLD----------IPIGELYGLSESSGPHTISNQNNYRLLSCGKILT 260
Cdd:cd05921 293 --------------KLMFYAGAGLSQDVWD---RLQalavatvgerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 261 GCKNMLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL----DGLGFLYVTGHIKEILITAGGEN 336
Cdd:cd05921 356 GTELKLVPS--GGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTW 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 337 VPPIPVET-LVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGL-GSQASTVTEIVKQqdP 414
Cdd:cd05921 434 VSVGPLRArAVAACAPLVHDAVVAGEDRAEVGALV------------------FPDLLACRRLvGLQEASDAEVLRH--A 493
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 574584663 415 LVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 455
Cdd:cd05921 494 KVRAAFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEI 534
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
39-360 |
3.05e-14 |
|
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: 74.64 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 39 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtdKHETVvsYL---PLSHiAAQMMDIWVPIKIGaltyfaqadalk 115
Cdd:cd12118 137 ALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEM--KQHPV--YLwtlPMFH-CNGWCFPWTVAAVG------------ 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 116 GTLVsTLKEVKPtvfigvPQIWEKIHE----------MVKKNSAKSMGLKKKAFVWARNIgfkvnskkMLGKYNTPVSyr 185
Cdd:cd12118 200 GTNV-CLRKVDA------KAIYDLIEKhkvthfcgapTVLNMLANAPPSDARPLPHRVHV--------MTAGAPPPAA-- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 186 maktlVFSKVkTSLGLDHCHSfisgtaplnqetaefflsldipigelYGLSESSGPHTI----------SNQNNYRLlsc 255
Cdd:cd12118 263 -----VLAKM-EELGFDVTHV--------------------------YGLTETYGPATVcawkpewdelPTEERARL--- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 256 gKILTGCKNMLFQQ------------NKDG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYV 321
Cdd:cd12118 308 -KARQGVRYVGLEEvdvldpetmkpvPRDGktIGEIVFRGNIVMKGYLKNPEATAEAFRG-GWFHSGDLAVIHPDGYIEI 385
|
330 340 350
....*....|....*....|....*....|....*....
gi 574584663 322 TGHIKEILITaGGENVPPIPVETlVKKKIPIISNAMLVG 360
Cdd:cd12118 386 KDRSKDIIIS-GGENISSVEVEG-VLYKHPAVLEAAVVA 422
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
38-360 |
4.24e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 74.46 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNitwiAGAVTKDFKLTDKHETVVSYL---PLSHIaaqmmdiwvpikIGALTYFAQADAL 114
Cdd:PRK09088 138 SLILFTSGTSGQPKGVMLSERN----LQQTAHNFGVLGRVDAHSSFLcdaPMFHI------------IGLITSVRPVLAV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 115 KGT-LVSTLKEVKPTV------------FIGVPQIWEKIHemvkknsaksmglkkkafvwaRNIGFKVNSkkmlgkyntp 181
Cdd:PRK09088 202 GGSiLVSNGFEPKRTLgrlgdpalgithYFCVPQMAQAFR---------------------AQPGFDAAA---------- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 182 vsyrmaktlvfskvktslgLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSE-------SSGPHTISNqnnyRLLS 254
Cdd:PRK09088 251 -------------------LRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEagtvfgmSVDCDVIRA----KAGA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 255 CGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIL 329
Cdd:PRK09088 308 AGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF 387
|
330 340 350
....*....|....*....|....*....|.
gi 574584663 330 ITaGGENVPPIPVETLVKKKiPIISNAMLVG 360
Cdd:PRK09088 388 IS-GGENVYPAEIEAVLADH-PGIRECAVVG 416
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
233-360 |
4.62e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.31 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 233 YGLSESSG-----P---HTISNQNNYRLLSCGKILTGcknMLFQ-QNKDG-------IGEICLWGRHIFMGYLESETETT 296
Cdd:PRK07470 312 FGLGEVTGnitvlPpalHDAEDGPDARIGTCGFERTG---MEVQiQDDEGrelppgeTGEICVIGPAVFAGYYNNPEANA 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574584663 297 EAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVEtlvkKKI---PIISNAMLVG 360
Cdd:PRK07470 389 KAFRD-GWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIE----EKLlthPAVSEVAVLG 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
19-325 |
6.74e-14 |
|
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: 73.44 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 19 SIPDTQLEQVIESQKA-------NQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVtKDFKLTDkHETVVSYLPLSHIA 90
Cdd:cd05945 74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDNLvSFTNWML-SDFPLGP-GDVFLNQAPFSFDL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 91 AqMMDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIWEkihemvkknsaksMGLKKKAFvwarnigfk 168
Cdd:cd05945 152 S-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAA-------------MCLLSPTF--------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 169 vNSKKMlgkyntpvsyrmaKTLVfskvktslgldhcHSFISGTaPLNQETAEFFLSL--DIPIGELYGLSESSGP---HT 243
Cdd:cd05945 209 -TPESL-------------PSLR-------------HFLFCGE-VLPHKTARALQQRfpDARIYNTYGPTEATVAvtyIE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 244 ISNQ--NNYRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLG 311
Cdd:cd05945 261 VTPEvlDGYDRLPIGYAKPGAKLVIL--DEDGrpvppgeKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLV 338
|
330
....*....|....
gi 574584663 312 QLDGLGFLYVTGHI 325
Cdd:cd05945 339 RLEADGLLFYRGRL 352
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
20-360 |
7.04e-14 |
|
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: 73.26 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 20 IPDTQLEQVIESQKAnqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSylplshiAAQMM----- 94
Cdd:cd05919 78 ARDCEARLVVTSADD--IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFS-------SAKMFfgygl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 95 --DIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWekihemvkKNSAKSMGLKKKAFVWARnigfkvnsk 172
Cdd:cd05919 149 gnSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFY--------ANLLDSCAGSPDALRSLR--------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 173 kmlgkyntpvsyrmaktlvfskvktslgldHChsfISGTAPLNQETAEFFLS-LDIPIGELYGLSESSgpHT-ISNQ-NN 249
Cdd:cd05919 212 ------------------------------LC---VSAGEALPRGLGERWMEhFGGPILDGIGATEVG--HIfLSNRpGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 250 YRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESeTETTEAIDDEGWLHSGDLGQLDGLGFLYVT 322
Cdd:cd05919 257 WRLGSTGRPVPGYEIRLV--DEEGhtippgeEGDLLVRGPSAAVGYWNN-PEKSRATFNGGWYRTGDKFCRDADGWYTHA 333
|
330 340 350
....*....|....*....|....*....|....*...
gi 574584663 323 GHIKEILITaGGENVPPIPVETLVkKKIPIISNAMLVG 360
Cdd:cd05919 334 GRADDMLKV-GGQWVSPVEVESLI-IQHPAVAEAAVVA 369
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
42-360 |
3.29e-13 |
|
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: 70.51 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 42 YTSGTTGIPKGVMLSHDniTWIAGAVT--KDFKLtDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGtlV 119
Cdd:cd17633 7 FTSGTTGLPKAYYRSER--SWIESFVCneDLFNI-SGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSW--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 120 STLKEVKPTVFIGVPQiwekiheMVKknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSyrmaktlvfsKVKtsl 199
Cdd:cd17633 82 RKINQYNATVIYLVPT-------MLQ----------------------------ALARTLEPES----------KIK--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 200 gldhchSFISGTAPLNQETAEFF--LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEI 277
Cdd:cd17633 114 ------SIFSSGQKLFESTKKKLknIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 278 CLWGRHIFMGYLESEtetteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNAM 357
Cdd:cd17633 188 FVKSEMVFSGYVRGG-----FSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVL-KAIPGIEEAI 260
|
...
gi 574584663 358 LVG 360
Cdd:cd17633 261 VVG 263
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
15-360 |
3.68e-13 |
|
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: 70.97 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 15 ELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMM 94
Cdd:cd05935 64 ELEYILNDSGAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS-DVILACLPLFHVTGFVG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 95 DIWVPIKIGAlTYFAQADALKGTLVSTLKEVKPTVfigvpqiWEKIHEMVKKNSAkSMGLKKKAFvwarnigfkvNSKKM 174
Cdd:cd05935 143 SLNTAVYVGG-TYVLMARWDRETALELIEKYKVTF-------WTNIPTMLVDLLA-TPEFKTRDL----------SSLKV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 175 LGKYNTPVSYRMAKtlvfsKVKTSLGLDHChsfisgtaplnqetaefflsldipigELYGLSESSgPHTISNQNNYRLLS 254
Cdd:cd05935 204 LTGGGAPMPPAVAE-----KLLKLTGLRFV--------------------------EGYGLTETM-SQTHTNPPLRPKLQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 255 CGKILTGCKNMLFQQNKDGI-------GEICLWGRHIFMGYLESETETTEA-IDDEG--WLHSGDLGQLDGLGFLYVTGH 324
Cdd:cd05935 252 CLGIP*FGVDARVIDIETGRelppnevGEIVVRGPQIFKGYWNRPEETEESfIEIKGrrFFRTGDLGYMDEEGYFFFVDR 331
|
330 340 350
....*....|....*....|....*....|....*.
gi 574584663 325 IKEiLITAGGENVPPIPVETLVKKKiPIISNAMLVG 360
Cdd:cd05935 332 VKR-MINVSGFKVWPAEVEAKLYKH-PAI*EVCVIS 365
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
38-360 |
4.21e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 71.39 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK---------LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGaltyf 108
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIAPLPLYHIYAFTANCMCMMVSG----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 109 aqadalkgtlvstlkevKPTVFIGVPQiweKIHEMVKKnsaksmgLKKKAFvwarnigfkvnsKKMLGkYNTPVSYRMA- 187
Cdd:PRK12492 285 -----------------NHNVLITNPR---DIPGFIKE-------LGKWRF------------SALLG-LNTLFVALMDh 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 188 ---KTLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgphTISNQNNY----RLLSCGKIL 259
Cdd:PRK12492 325 pgfKDLDFSALKLT---------NSGGTALVKATAERWEQLTgCTIVEGYGLTETS---PVASTNPYgelaRLGTVGIPV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 260 TGCKNMLFqqNKDGI-------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 332
Cdd:PRK12492 393 PGTALKVI--DDDGNelplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
|
330 340
....*....|....*....|....*...
gi 574584663 333 GGeNVPPIPVETLVKKKiPIISNAMLVG 360
Cdd:PRK12492 471 GF-NVYPNEIEDVVMAH-PKVANCAAIG 496
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
29-475 |
1.87e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 69.75 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 29 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTK-DFKLTDKHETVVSYLPLSHI-------AAQMMDIWVPI 100
Cdd:PTZ00342 298 IQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKhSIFKKYNPKTHLSYLPISHIyerviayLSFMLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 101 KIGALTYFAqadalkgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKK---KAFVWARNIGFKVNSKKMLGK 177
Cdd:PTZ00342 378 WSKDINYFS----------KDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRflvKKILSLRKSNNNGGFSKFLEG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 178 YnTPVSYRMAktlvfSKVKTSLGLdhchsFISGTAPLNQETA-EFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCG 256
Cdd:PTZ00342 448 I-THISSKIK-----DKVNPNLEV-----ILNGGGKLSPKIAeELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIG 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 257 KILtgCKNMLFQ-------QNKDGI--GEICLWGRHIFMGY-LESETeTTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK 326
Cdd:PTZ00342 517 GPI--SPNTKYKvrtwetyKATDTLpkGELLIKSDSIFSGYfLEKEQ-TKNAFTEDGYFKTGDIVQINKNGSLTFLDRSK 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 327 EILITAGGENvppIPVETL--VKKKIPIISNAMLVGDK-----LKFLSM--LLTLKC----EMNQMSG----EPLDKLNF 389
Cdd:PTZ00342 594 GLVKLSQGEY---IETDMLnnLYSQISFINFCVVYGDDsmdgpLAIISVdkYLLFKClkddNMLESTGinekNYLEKLTD 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 390 EAINfcrglgsqASTVTEIVKQQDPLVYKaiQQGINAVNqeAMNNAQRIEK-WvilekDFSIYggeLGPMMKLKRHFVAQ 468
Cdd:PTZ00342 671 ETIN--------NNIYVDYVKGKMLEVYK--KTNLNRYN--IINDIYLTSKvW-----DTNNY---LTPTFKVKRFYVFK 730
|
....*..
gi 574584663 469 KYKKQID 475
Cdd:PTZ00342 731 DYAFFID 737
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
38-360 |
2.14e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 69.04 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAA-----QMMDIWVPIKIGALTYFaqaD 112
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGigsmlPGLLLGAPTVIYPLGAF---D 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 113 AlkGTLVSTLKEVKPTVFIGVPQIWEKIhemVKKNSAKSMGLKKKAFVWarnigfkvnskkmlgkyntpvsyrmaktlvf 192
Cdd:PRK07786 254 P--GQLLDVLEAEKVTGIFLVPAQWQAV---CAEQQARPRDLALRVLSW------------------------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 193 skvktslgldhchsfisGTAP----LNQETAEFFLslDIPIGELYGLSESSgPHT--ISNQNNYRLL-SCGKILTGCKNM 265
Cdd:PRK07786 298 -----------------GAAPasdtLLRQMAATFP--EAQILAAFGQTEMS-PVTcmLLGEDAIRKLgSVGKVIPTVAAR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 266 LFQQNKDG-----IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPI 340
Cdd:PRK07786 358 VVDENMNDvpvgeVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCA 435
|
330 340
....*....|....*....|
gi 574584663 341 PVETLVKKKiPIISNAMLVG 360
Cdd:PRK07786 436 EVENVLASH-PDIVEVAVIG 454
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
34-360 |
2.16e-12 |
|
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: 68.52 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMLSHdnitwiagavtkdfkltdkhetvvSYlPLSHIAAqmMDIWVPIKIGALtYFAQADA 113
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTH------------------------SY-PLGHIPT--AAYWLGLRPDDI-HWNIADP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 114 --LKGTLvSTLKEVkptVFIGVPQIwekIHEMVKKNSAKSMGLKKKafvwarnigFKVNSKkmlgkYNTPVSYRM-AKTL 190
Cdd:cd05972 132 gwAKGAW-SSFFGP---WLLGATVF---VYEGPRFDAERILELLER---------YGVTSF-----CGPPTAYRMlIKQD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 191 VFSKVKTSLgldhcHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSEssgphTISNQNNYRLL-----SCGKILTGCKN 264
Cdd:cd05972 191 LSSYKFSHL-----RLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTE-----TGLTVGNFPDMpvkpgSMGRPTPGYDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 265 MLFQQNKDGI-----GEICL-WGRH-IFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENV 337
Cdd:cd05972 261 AIIDDDGRELppgeeGDIAIkLPPPgLFLGYVGDPEKTEASIRG-DYYLTGDRAYRDEDGYFWFVGRADDI-IKSSGYRI 338
|
330 340
....*....|....*....|....
gi 574584663 338 PPIPVE-TLVKKkiPIISNAMLVG 360
Cdd:cd05972 339 GPFEVEsALLEH--PAVAEAAVVG 360
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
29-351 |
3.66e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 68.80 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 29 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHiaaqmmdiwvpikigaltyf 108
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNL-RNDDVILSSLPFFH-------------------- 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 109 aqADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMgLKKKAF--VWARNIgfKVNsKKMLGkyntpvSYRM 186
Cdd:PRK08633 835 --SFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATIL-LGTPTFlrLYLRNK--KLH-PLMFA------SLRL 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 187 AktlvfskvktslgldhchsfISGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQNnyRLLSCGKILTGCKN- 264
Cdd:PRK08633 903 V--------------------VAGAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVNLPD--VLAADFKRQTGSKEg 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 265 ----------------MLFQQNKDGI-GEICLWGRHIFMGYLESETETTEAI---DDEGWLHSGDLGQLDGLGFLYVTGH 324
Cdd:PRK08633 961 svgmplpgvavrivdpETFEELPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
330 340 350
....*....|....*....|....*....|
gi 574584663 325 IK---EIlitaGGENVPPIPVETLVKKKIP 351
Cdd:PRK08633 1041 YSrfaKI----GGEMVPLGAVEEELAKALG 1066
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
13-346 |
3.72e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 68.36 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 13 FMELGRSIPDTqLEQVieSQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPL------ 86
Cdd:PRK07514 137 LLEAAAAAPDD-FETV--PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPD-DVLIHALPIfhthgl 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 87 ---SHIA----AQMmdIWVPiKIGA---LTYFAQAdalkgtlvstlkevkpTVFIGVPQIWEKI--HEMVKKNSAKSMGL 154
Cdd:PRK07514 213 fvaTNVAllagASM--IFLP-KFDPdavLALMPRA----------------TVMMGVPTFYTRLlqEPRLTREAAAHMRL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 155 kkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvfskvktslgldhchsFISGTAPLNQET-AEFFLSLDIPIGELY 233
Cdd:PRK07514 274 ----------------------------------------------------FISGSAPLLAEThREFQERTGHAILERY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 234 GLSEssgphTISNQNN-Y------------------RLLSC--GKILTgcknmlfqqnKDGIGEICLWGRHIFMGYLESE 292
Cdd:PRK07514 302 GMTE-----TNMNTSNpYdgerragtvgfplpgvslRVTDPetGAELP----------PGEIGMIEVKGPNVFKGYWRMP 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 574584663 293 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 346
Cdd:PRK07514 367 EKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEGEI 419
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
38-334 |
6.18e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 67.32 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIG---------ALTYF 108
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD-DVLVHGLPLFHVHGLVLGVLGPLRIGnrfvhtgrpTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 109 AQADALKGTLvstlkevkptvFIGVPQIWEKIHEmvKKNSAKSMglkkkafvwarnigfkvnskkmlgkyntpvsyRMAK 188
Cdd:PRK07787 210 AQALSEGGTL-----------YFGVPTVWSRIAA--DPEAARAL--------------------------------RGAR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 189 TLVfskvktslgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGLSES--------SGPHtisnqnnyRLLSCGKIL 259
Cdd:PRK07787 245 LLV-----------------SGSAALPVPVFDRLAALTgHRPVERYGMTETlitlstraDGER--------RPGWVGLPL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 260 TGCKNMLFQQN-----KDG--IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 332
Cdd:PRK07787 300 AGVETRLVDEDggpvpHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKS 379
|
..
gi 574584663 333 GG 334
Cdd:PRK07787 380 GG 381
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
21-152 |
1.77e-11 |
|
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: 66.01 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 21 PDTQLEQVIESQKA-------NQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAqM 93
Cdd:cd05930 72 PAERLAYILEDSGAklvltdpDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLT-PGDRVLQFTSFSFDVS-V 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574584663 94 MDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSM 152
Cdd:cd05930 150 WEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL 210
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
38-360 |
2.47e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 65.83 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADALkg 116
Cdd:PRK06178 212 AALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGAtLVLLARWDAV-- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 117 TLVSTLKEVKPTVFIG-VPQIWEKI-HEMVKKNSAKSmgLKKK---AFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTlv 191
Cdd:PRK06178 290 AFMAAVERYRVTRTVMlVDNAVELMdHPRFAEYDLSS--LRQVrvvSFVKKLNPDYRQRWRALTGSVLAEAAWGMTET-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 192 fskvktslgldH-CHSFISG--TAPLNQETAEFFLSLDIPIGELYGLSESSGphtisnqnnyRLLSCGkiltgcknmlfq 268
Cdd:PRK06178 366 -----------HtCDTFTAGfqDDDFDLLSQPVFVGLPVPGTEFKICDFETG----------ELLPLG------------ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 269 qnkdGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAgGENVPPIPVETLVKK 348
Cdd:PRK06178 413 ----AEGEIVVRTPSLLKGYWNKPEATAEALRD-GWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQ 486
|
330
....*....|..
gi 574584663 349 KiPIISNAMLVG 360
Cdd:PRK06178 487 H-PAVLGSAVVG 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
38-346 |
3.36e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 65.43 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNI--------TWIAGAVTKdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALtyfa 109
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWLQPAFEK--KPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGR---- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 110 qadalkgtlvstlkevkpTVFIGVPQiweKIHEMVKKnsaksmgLKKKAFvwarNIGFKVNSkkmlgKYNTPVSYRMAKT 189
Cdd:PRK07059 281 ------------------NILIPNPR---DIPGFIKE-------LKKYQV----HIFPAVNT-----LYNALLNNPDFDK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 190 LVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGELYGLSESSgPHTISNQNNyrllscGKILTGCKNM--- 265
Cdd:PRK07059 324 LDFSKLIVANG---------GGMAVQRPVAERWLEMTgCPITEGYGLSETS-PVATCNPVD------ATEFSGTIGLplp 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 266 ---LFQQNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGE 335
Cdd:PRK07059 388 steVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKD-MILVSGF 466
|
330
....*....|.
gi 574584663 336 NVPPIPVETLV 346
Cdd:PRK07059 467 NVYPNEIEEVV 477
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
13-362 |
4.38e-11 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 64.86 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 13 FMELGRSIPDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTK----DFKLTDKHETVVSYLPLSH 88
Cdd:PLN02574 179 FYELIKEDFDFVPKPVIKQDDV---AAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEYPGSDNVYLAALPMFH 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 89 IAAQMMDIWVPIKIG-ALTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLKKKAfvwarnigf 167
Cdd:PLN02574 256 IYGLSLFVVGLLSLGsTIVVMRRFDA--SDMVKVIDRFKVTHFPVVPPIL--------------MALTKKA--------- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 168 kvnskkmlgkynTPVSYRMAKTLVfskvktslgldhchSFISGTAPLNQETAEFFLS----LDIPIGelYGLSESS--GP 241
Cdd:PLN02574 311 ------------KGVCGEVLKSLK--------------QVSCGAAPLSGKFIQDFVQtlphVDFIQG--YGMTESTavGT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 242 HTISNQNNYRLLSCG--------KIL---TGCknMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 310
Cdd:PLN02574 363 RGFNTEKLSKYSSVGllapnmqaKVVdwsTGC--LLPPGNC---GELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDI 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 574584663 311 GQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKIPIISNAML-VGDK 362
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEI-IKYKGFQIAPADLEAVLISHPEIIDAAVTaVPDK 489
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
12-402 |
8.22e-11 |
|
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: 63.68 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 12 DFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDFKLTDKHETVVSylPlSHI 89
Cdd:cd05969 66 DRLENSEAKVLITTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIfyYFTGKYVLDLHPDDIYWCTAD--P-GWV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 90 AAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVfigvpqiwekihemvkknsaksmglkkkafvWarnigfkv 169
Cdd:cd05969 143 TGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTV-------------------------------W-------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 170 nskkmlgkYNTPVSYRMAKTLVFSKVKtSLGLDHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESsGPHTISNQ- 247
Cdd:cd05969 184 --------YTAPTAIRMLMKEGDELAR-KYDLSSLRFIHSVGEPLNPEAIRWGMEvFGVPIHDTWWQTET-GSIMIANYp 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 248 -NNYRLLSCGKILTGCKNMLFQQNKDGI-----GEICL---WGRhIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGF 318
Cdd:cd05969 254 cMPIKPGSMGKPLPGVKAAVVDENGNELppgtkGILALkpgWPS-MFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 319 LYVTGHIKEILITAgGENVPPIPVETLVKKKiPIISNAMLVG--DKLK--FLSMLLTLKcemnqmSG-EPLDKLNFEAIN 393
Cdd:cd05969 332 FWFVGRADDIIKTS-GHRVGPFEVESALMEH-PAVAEAGVIGkpDPLRgeIIKAFISLK------EGfEPSDELKEEIIN 403
|
410
....*....|
gi 574584663 394 FCR-GLGSQA 402
Cdd:cd05969 404 FVRqKLGAHV 413
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
6-360 |
1.11e-10 |
|
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: 63.65 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 6 NLYSWDDFMELGRSIPdtqLEQVIESQkanqCAVLIYTSGTTGIPKGVMLSHDNItwIAGA--VTKDFKLTDKhETVVSY 83
Cdd:TIGR03098 141 EPASWPKLLALGDADP---PHPVIDSD----MAAILYTSGSTGRPKGVVLSHRNL--VAGAqsVATYLENRPD-DRLLAV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 84 LPLSHIAA--QMMDIWVpikIGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkk 157
Cdd:TIGR03098 211 LPLSFDYGfnQLTTAFY---VGAtvvlHDYLLPRDVLK-----ALEKHGITGLAAVPPLWAQLAQLDWPESA-------- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 158 afvwARNIGFKVNSKKmlgkyntpvsyRMAKTLVfSKVKTSLGLdhchsfisgtaplnqetAEFFLsldipigeLYGLSE 237
Cdd:TIGR03098 275 ----APSLRYLTNSGG-----------AMPRATL-SRLRSFLPN-----------------ARLFL--------MYGLTE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 238 SSGPHTISNQN-NYRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEAI------DDEG 303
Cdd:TIGR03098 314 AFRSTYLPPEEvDRRPDSIGKAIPNAEVLVL--REDGsecapgeEGELVHRGALVAMGYWNDPEKTAERFrplppfPGEL 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574584663 304 WLH-----SGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETlVKKKIPIISNAMLVG 360
Cdd:TIGR03098 392 HLPelavwSGDTVRRDEEGFLYFVGR-RDEMIKTSGYRVSPTEVEE-VAYATGLVAEAVAFG 451
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
38-353 |
2.18e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.84 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSH----DNITWIAGAVtkdfKLTDKHETVVSYLPLSHIAAQMMdIWVPikigaltyfaqadA 113
Cdd:PRK12476 196 SHLQYTSGSTRPPVGVEITHravgTNLVQMILSI----DLLDRNTHGVSWLPLYHDMGLSM-IGFP-------------A 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 114 LKG---TLVStlkevkPTVFIGVPQIWekIHEMVKKNSAKSM--GLKKKAFVWARNIGFKVN------SKKMLGKYNTPV 182
Cdd:PRK12476 258 VYGghsTLMS------PTAFVRRPQRW--IKALSEGSRTGRVvtAAPNFAYEWAAQRGLPAEgddidlSNVVLIIGSEPV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 183 SyrMAKTLVFSK-----------VKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTISNqnnyr 251
Cdd:PRK12476 330 S--IDAVTTFNKafapyglprtaFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADA-PNAVAH----- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 252 lLSCGKIL-----------TGCknmlfqQNKDG-IGEICLWGRHIFMGYLE--SETETT----------------EAIDD 301
Cdd:PRK12476 402 -VSCGQVArsqwavivdpdTGA------ELPDGeVGEIWLHGDNIGRGYWGrpEETERTfgaklqsrlaegshadGAADD 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 574584663 302 EGWLHSGDLG-QLDGLgfLYVTGHIKEiLITAGGENVPPIPVETLVKKKIPII 353
Cdd:PRK12476 475 GTWLRTGDLGvYLDGE--LYITGRIAD-LIVIDGRNHYPQDIEATVAEASPMV 524
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
38-455 |
2.21e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.97 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-LTDKHETVVSYLPLSHIaaqmmdiwvpikIGALTYFAQADALKG 116
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfLAEEPPVLVDWLPWNHT------------FGGNHNLGIVLYNGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 117 TL---------------VSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkkafvwarnigfkvnskkmlgkyntp 181
Cdd:PRK08180 280 TLyiddgkptpggfdetLRNLREISPTVYFNVPKGWEMLVPALERDAA-------------------------------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 182 vsyrMAKTLvFSKVKtslgldhchSFISGTAPLNQETAEfflSLD----------IPIGELYGLSESSGPHTISNQNNYR 251
Cdd:PRK08180 328 ----LRRRF-FSRLK---------LLFYAGAALSQDVWD---RLDrvaeatcgerIRMMTGLGMTETAPSATFTTGPLSR 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 252 LLSCGKILTGCKNMLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL-D----GLGFLYvTGHIK 326
Cdd:PRK08180 391 AGNIGLPAPGCEVKLVPV--GGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDpadpERGLMF-DGRIA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 327 EILITAGGE--NVPPIPVEtLVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGLGSQAST 404
Cdd:PRK08180 468 EDFKLSSGTwvSVGPLRAR-AVSAGAPLVQDVVITGHDRDEIGLLV------------------FPNLDACRRLAGLLAD 528
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 574584663 405 VTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 455
Cdd:PRK08180 529 ASLAEVLAHPAVRAAFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEI 579
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
274-360 |
4.54e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 61.61 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 274 IGEICLWGRHIFMGYLESETETteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKiPII 353
Cdd:PRK13295 392 IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEIEALLYRH-PAI 467
|
....*..
gi 574584663 354 SNAMLVG 360
Cdd:PRK13295 468 AQVAIVA 474
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
274-360 |
2.78e-09 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 59.31 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 274 IGEICLWG---RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKi 350
Cdd:PRK08008 366 IGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR-RCNMIKRGGENVSCVELENIIATH- 443
|
90
....*....|
gi 574584663 351 PIISNAMLVG 360
Cdd:PRK08008 444 PKIQDIVVVG 453
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
272-343 |
2.98e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 59.19 E-value: 2.98e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584663 272 DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK08162 384 DGetIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVE 455
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
22-333 |
5.21e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 58.42 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 22 DTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFkLTDKHE------TVVSYLPLSHIAAQMMD 95
Cdd:PRK05850 147 DSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY-FGDTGGvpppdtTVVSWLPFYHDMGLVLG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 96 IWVPIKIGALTYfaqadalkgtLVStlkevkPTVFIGVPQIWekIHeMVKKNSAksmglkkkAFVWARNIGFKVNSKK-- 173
Cdd:PRK05850 226 VCAPILGGCPAV----------LTS------PVAFLQRPARW--MQ-LLASNPH--------AFSAAPNFAFELAVRKts 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 174 ---MLGkyntpvsyrmaktlvfskvktsLGLDHCHSFISGTAPLNQET--------AEFFLSlDIPIGELYGLSE----- 237
Cdd:PRK05850 279 dddMAG----------------------LDLGGVLGIISGSERVHPATlkrfadrfAPFNLR-ETAIRPSYGLAEatvyv 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 238 -----SSGPHTIS---------------NQNNYRLLSCG-------KILTGCKNMlfqQNKDG-IGEICLWGRHIFMGYL 289
Cdd:PRK05850 336 atrepGQPPESVRfdyeklsaghakrceTGGGTPLVSYGsprsptvRIVDPDTCI---ECPAGtVGEIWVHGDNVAAGYW 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 574584663 290 E--SETETT--EAIDD------EG-WLHSGDLGQLDGlGFLYVTGHIKEILITAG 333
Cdd:PRK05850 413 QkpEETERTfgATLVDpspgtpEGpWLRTGDLGFISE-GELFIVGRIKDLLIVDG 466
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
233-358 |
7.35e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 58.11 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 233 YGLSESSGP------------------HTISNQNNYRLLSCGKILTGCKNMLFQQNKDG--IGEICLWGRHIFMGYLESE 292
Cdd:PLN03102 331 YGLTEATGPvlfcewqdewnrlpenqqMELKARQGVSILGLADVDVKNKETQESVPRDGktMGEIVIKGSSIMKGYLKNP 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574584663 293 TETTEAIDdEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKIPIISNAML 358
Cdd:PLN03102 411 KATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVENVLYKYPKVLETAVV 474
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
38-138 |
2.48e-08 |
|
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: 56.12 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDkhETVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKG 116
Cdd:TIGR01733 123 AYVIYTSGSTGRPKGVVVTHRSLvNLLAWLARRYGLDPD--DRVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERD 199
|
90 100
....*....|....*....|....*
gi 574584663 117 TLVST---LKEVKPTVFIGVPQIWE 138
Cdd:TIGR01733 200 DAALLaalIAEHPVTVLNLTPSLLA 224
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
38-346 |
4.67e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 55.74 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTK-DFKLTDKhetVVSYLPLSHiaaqmmdiwvpiKIGaLTyfaqadalK 115
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLlANRAQVAARiDFSPEDK---VFNALPVFH------------SFG-LT--------G 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 116 GTLVSTLKEVkPTVFIGVPQIWEKIHEMVkknsaksmglkkkafvwarnigFKVNSKKMLG---------KYNTPVSYRM 186
Cdd:PRK06814 852 GLVLPLLSGV-KVFLYPSPLHYRIIPELI----------------------YDTNATILFGtdtflngyaRYAHPYDFRS 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 187 AKtLVFskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNM 265
Cdd:PRK06814 909 LR-YVF----------------AGAEKVKEETRQTWMEkFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYR 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 266 LfqQNKDGI---GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK---EIlitaGGENVPP 339
Cdd:PRK06814 972 L--EPVPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKrfaKI----AGEMISL 1045
|
....*..
gi 574584663 340 IPVETLV 346
Cdd:PRK06814 1046 AAVEELA 1052
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
229-360 |
5.67e-08 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 55.08 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 229 IGELYGLSESSGPHTISNQNnyrLL----SCGKILTGCKNMLfqqNKDG-------IGEICLWGRHIFMgYLESETETTE 297
Cdd:cd05929 272 IWEYYGGTEGQGLTIINGEE---WLthpgSVGRAVLGKVHIL---DEDGnevppgeIGEVYFANGPGFE-YTNDPEKTAA 344
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584663 298 AIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKiPIISNAMLVG 360
Cdd:cd05929 345 ARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAH-PKVLDAAVVG 405
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
193-346 |
6.70e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 54.85 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 193 SKVKTSLGLDH-CHSFISGTAPlnqeTAEFFLSLDIP---IGELYGLSESSGPHTISN----------QNNYRLLSCGKI 258
Cdd:PLN02479 301 PKSETILPLPRvVHVMTAGAAP----PPSVLFAMSEKgfrVTHTYGLSETYGPSTVCAwkpewdslppEEQARLNARQGV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 259 ----LTGCKNMLFQQNK----DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEI 328
Cdd:PLN02479 377 ryigLEGLDVVDTKTMKpvpaDGktMGEIVMRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDI 455
|
170
....*....|....*...
gi 574584663 329 LITaGGENVPPIPVETLV 346
Cdd:PLN02479 456 IIS-GGENISSLEVENVV 472
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
38-338 |
9.37e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 54.35 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHIAAQMMdIWVPIKIGAltYFaqadalkgT 117
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEG-QEGDRGVSWLPFFHDMGLIT-VLLPALLGH--YI--------T 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 LVStlkevkPTVFIGVPQIWekIHEMVKKNsaksmGLKKKAFVWARNIGFKVNSKKMLGKYNTPvsyrmaktlvfskvkt 197
Cdd:PRK07769 251 FMS------PAAFVRRPGRW--IRELARKP-----GGTGGTFSAAPNFAFEHAAARGLPKDGEP---------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 198 SLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-----SSGPHTISNQ---------NNYRLL--- 253
Cdd:PRK07769 302 PLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGlpptaikPSYGMAEatlfvSTTPMDEEPTviyvdrdelNAGRFVevp 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 254 ----------SCGKIL-----------TGcknmlfQQNKDG-IGEICLWGRHIFMGYLESETETTE-------------- 297
Cdd:PRK07769 382 adapnavaqvSAGKVGvsewavivdpeTA------SELPDGqIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlsesh 455
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 574584663 298 ---AIDDEGWLHSGDLGQ-LDglGFLYVTGHIKEILITAGGENVP 338
Cdd:PRK07769 456 aegAPDDALWVRTGDYGVyFD--GELYITGRVKDLVIIDGRNHYP 498
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
38-138 |
1.05e-07 |
|
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: 54.86 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKGT 117
Cdd:COG1020 620 AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGP-GDRVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEARRDP 697
|
90 100
....*....|....*....|...
gi 574584663 118 --LVSTLKEVKPTVFIGVPQIWE 138
Cdd:COG1020 698 aaLAELLARHRVTVLNLTPSLLR 720
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
36-360 |
1.51e-07 |
|
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: 53.67 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 36 QCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDKHETVVSYLPLSHIaaqmmdiwvpikIGALTYFAQADAL 114
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAeSRVLFMSTQAGLRHGRHNVVLGLMPLYHV------------IGFFAVLVAALAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 115 KGTLVsTLKEVKPtvfigvpqiwekihemvkknsaksmglkKKAFVWarnigfkVNSKKMLGKYNTPVSYrmaKTLVFSK 194
Cdd:cd05923 219 DGTYV-VVEEFDP----------------------------ADALKL-------IEQERVTSLFATPTHL---DALAAAA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 195 VKTSLGLDHCHSFISGTAPLNQ---ETAEFFLSldIPIGELYGLSESSgpHTISNQN-------------NYRLLSCGki 258
Cdd:cd05923 260 EFAGLKLSSLRHVTFAGATMPDavlERVNQHLP--GEKVNIYGTTEAM--NSLYMRDartgtemrpgffsEVRIVRIG-- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 259 ltGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVP 338
Cdd:cd05923 334 --GSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQD-GWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIH 409
|
330 340
....*....|....*....|..
gi 574584663 339 PIPVETLVKKKiPIISNAMLVG 360
Cdd:cd05923 410 PSEIERVLSRH-PGVTEVVVIG 430
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-353 |
1.58e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 33 KANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL-TDKHETVVSYLPLSHiaaqmmDIWVpikIGALtyfaqa 111
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdLNPDDVIVSWLPLYH------DMGL---IGGL------ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 112 dalkgtlvstlkeVKPtVFIGVPQIwekihemvkknsaksmgLKKKAFVWARnigfKVNSKKMLGKYNTPVS------YR 185
Cdd:PRK05691 229 -------------LQP-IFSGVPCV-----------------LMSPAYFLER----PLRWLEAISEYGGTISggpdfaYR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 186 MAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESS----------GPHTIS--- 245
Cdd:PRK05691 274 LCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGfdpdsffASYGLAEATlfvsggrrgqGIPALElda 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 246 ---NQNNYR------LLSCGK------ILTGCKNMLFQQNKDGIGEICLWGRHIFMGYL---ESETETTEAIDDEGWLHS 307
Cdd:PRK05691 354 ealARNRAEpgtgsvLMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWrnpEASAKTFVEHDGRTWLRT 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 574584663 308 GDLGQLDGlGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIPII 353
Cdd:PRK05691 434 GDLGFLRD-GELFVTGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
273-346 |
2.27e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.09 E-value: 2.27e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584663 273 GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEiLITAGGENVPPIPVETLV 346
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKD-LIIINGRNIWPQDIEWIA 480
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
38-335 |
2.39e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 53.25 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNItWIAGA---VTKDFKLTDKhETVVSYLPLSHIAAqmmdiW-VPIKI---GALTYFAQ 110
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSL-YLQSLslrTTDSLAVTHG-ESFLCCVPIYHVLS-----WgVPLAAfmsGTPLVFPG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 111 ADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLkKKAFV------------WARNIGFKVNSkkmlgky 178
Cdd:PRK05620 257 PDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSL-QEIYVggsavppilikaWEERYGVDVVH------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 179 ntpvSYRMAKTLVFSKVKtslgldHCHSFISGTAPLNqetaefflsldipigelYGLSESSGPHTIsnqnNYRLLSCGKI 258
Cdd:PRK05620 329 ----VWGMTETSPVGTVA------RPPSGVSGEARWA-----------------YRVSQGRFPASL----EYRIVNDGQV 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 259 LTGcknmlfqqNKDGIGEICLWGRHIFMGYLESETETT---------EAIDDE-------GWLHSGDLGQLDGLGFLYVT 322
Cdd:PRK05620 378 MES--------TDRNEGEIQVRGNWVTASYYHSPTEEGggaastfrgEDVEDAndrftadGWLRTGDVGSVTRDGFLTIH 449
|
330
....*....|...
gi 574584663 323 GHIKEIlITAGGE 335
Cdd:PRK05620 450 DRARDV-IRSGGE 461
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
40-360 |
2.59e-07 |
|
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: 52.38 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 40 LIYTSGTTGIPKGVMLSHDNI-------TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDiwvpikiGALTYFAQAD 112
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmlmggADFGTGEFTPSEDAH-KAAAAAAGTVMFPAPPLMH-------GTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 113 ALKGTLVstlkeVKPTVFIGVPQIWEKIHEMvkknsaksmglkkkafvwarnigfKVNSKKMLGKyntpvsyRMAKTLV- 191
Cdd:cd05924 80 LLGGQTV-----VLPDDRFDPEEVWRTIEKH------------------------KVTSMTIVGD-------AMARPLId 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 192 -FSKVKTsLGLDHCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGPHTISNQNN------YRLLSCGKILTGC 262
Cdd:cd05924 124 aLRDAGP-YDLSSLFAISSGGALLSPEVKQGLLELvpNITLVDAFGSSETGFTGSGHSAGSgpetgpFTRANPDTVVLDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 263 KNMLFQQNKDGIGEICLWGrHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPP 339
Cdd:cd05924 203 DGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR-GSVCINTGGEKVFP 280
|
330 340
....*....|....*....|.
gi 574584663 340 IPVETLVKKKiPIISNAMLVG 360
Cdd:cd05924 281 EEVEEALKSH-PAVYDVLVVG 300
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
23-344 |
2.61e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.85 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 23 TQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHiaaqmmDIwvpiki 102
Cdd:PRK05851 140 TNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYH------DM------ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 103 gALTyFAQADALKGTlvsTLKEVKPTVFIGVPQIWekihemvkknsAKSMGLKKKAFVWARNIGFKvnskkMLGKYNTPV 182
Cdd:PRK05851 208 -GLA-FLLTAALAGA---PLWLAPTTAFSASPFRW-----------LSWLSDSRATLTAAPNFAYN-----LIGKYARRV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 183 SYRMAKTLVFSkvktslgldhchsfISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESSGPHTIS---------- 245
Cdd:PRK05851 267 SDVDLGALRVA--------------LNGGEPVDCDGFERFATAMAPFGfdagaaaPSYGLAESTCAVTVPvpgiglrvde 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 246 -----NQNNYRLLSCGKILTG------CKNMLFQQNKDGIGEICLWGRHIFMGYLESETetteaIDDEGWLHSGDLGQLd 314
Cdd:PRK05851 333 vttddGSGARRHAVLGNPIPGmevrisPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL- 406
|
330 340 350
....*....|....*....|....*....|
gi 574584663 315 GLGFLYVTGHIKEiLITAGGENVPPIPVET 344
Cdd:PRK05851 407 VDGGLVVCGRAKE-LITVAGRNIFPTEIER 435
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
271-360 |
3.56e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 52.47 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 271 KDGIGEICLWGRHIFMGYLeSETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKI 350
Cdd:PRK07638 330 KGEIGTVYVKSPQFFMGYI-IGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEH 406
|
90
....*....|
gi 574584663 351 PIISNAMLVG 360
Cdd:PRK07638 407 PAVDEIVVIG 416
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
41-346 |
3.57e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 52.62 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 41 IYTSGTTGIPKGVMLSHDNI-TWIAGAVTK-DFKltdKHETVVsylplshIAAQMMDIWvpikigALTYFAQADALKGTL 118
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEPSPlAPLAGLLSRvPFR---AGETTL-------LPAPMFHAT------GWAHLTLAMALGSTV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 119 V--------STLKEV---KPTVFIGVPQIwekIHEMVKKnsaksmglkkkafvwarnigfkvnSKKMLGKYNTPvSYRMA 187
Cdd:PRK07788 277 VlrrrfdpeATLEDIakhKATALVVVPVM---LSRILDL------------------------GPEVLAKYDTS-SLKII 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 188 ktlvfskvktslgldhchsFISG---TAPLNQETAEFFlsldipiGE----LYGLSESSGPhTISNQNNYRL--LSCGKI 258
Cdd:PRK07788 329 -------------------FVSGsalSPELATRALEAF-------GPvlynLYGSTEVAFA-TIATPEDLAEapGTVGRP 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 259 LTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYleSETETTEAIDdeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAG 333
Cdd:PRK07788 382 PKGVTVKILDENGNEVprgvvGRIFVGNGFPFEGY--TDGRDKQIID--GLLSSGDVGYFDEDGLLFVDGRDDD-MIVSG 456
|
330
....*....|...
gi 574584663 334 GENVPPIPVETLV 346
Cdd:PRK07788 457 GENVFPAEVEDLL 469
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
34-104 |
5.60e-07 |
|
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: 51.82 E-value: 5.60e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVtkDFKLTDKHETVVSYLPLSHIAAqMMDIWVPIKIGA 104
Cdd:cd12117 135 PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT--NYVTLGPDDRVLQTSPLAFDAS-TFEIWGALLNGA 202
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
29-346 |
5.66e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.13 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 29 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYF 108
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKED-DVMMSFLPPFHAYGFNSCTLFPLLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 109 AQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKkkaFVWARNIGFKvnskkmlgkyntpvsyrmak 188
Cdd:PRK06334 256 AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLR---FVVIGGDAFK-------------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 189 tlvfskvktslgldhcHSfisgtapLNQETAEFFLSLDIPIGelYGLSESSGPHTISNQNNYRLLSC-GKILTGCKNMLF 267
Cdd:PRK06334 313 ----------------DS-------LYQEALKTFPHIQLRQG--YGTTECSPVITINTVNSPKHESCvGMPIRGMDVLIV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 268 QQ------NKDGIGEICLWGRHIFMGYL-ESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPI 340
Cdd:PRK06334 368 SEetkvpvSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSR-FVKIGAEMVSLE 446
|
....*.
gi 574584663 341 PVETLV 346
Cdd:PRK06334 447 ALESIL 452
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
35-360 |
5.84e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 52.06 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 35 NQCAVLIYTSGTTGIPKGVMLSH-DNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPiKIGALTYFAQADA 113
Cdd:PRK06018 177 NTAAGMCYTSGTTGDPKGVLYSHrSNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVMPGAKL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 114 LKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAfvwarnIGFKVNSKKMLG---KYNTPV--SYRMAK 188
Cdd:PRK06018 256 DGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVV------CGGSAMPRSMIKafeDMGVEVrhAWGMTE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 189 TlvfSKVKTSLGLDHCHSFISGTAPLN----QETAEFFLSLDipigelyglsessgphtISNQNNYRLLSCGKILtgckn 264
Cdd:PRK06018 330 M---SPLGTLAALKPPFSKLPGDARLDvlqkQGYPPFGVEMK-----------------ITDDAGKELPWDGKTF----- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 265 mlfqqnkdgiGEICLWGRHIFMGYLESETETteaIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVET 344
Cdd:PRK06018 385 ----------GRLKVRGPAVAAAYYRVDGEI---LDDDGFFDTGDVATIDAYGYMRITDRSKDV-IKSGGEWISSIDLEN 450
|
330
....*....|....*.
gi 574584663 345 LVKKKiPIISNAMLVG 360
Cdd:PRK06018 451 LAVGH-PKVAEAAVIG 465
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
19-343 |
6.90e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 51.63 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 19 SIPDTQLEQVIESQKA---------NQCAVLIYTSGTTGIPKGVMLSHDNITWIA-GAVTKDFKLTDKHETVVSYLPLSH 88
Cdd:PRK07008 151 STPLLCYETLVGAQDGdydwprfdeNQASSLCYTSGTTGNPKGALYSHRSTVLHAyGAALPDAMGLSARDAVLPVVPMFH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 89 IAAQMMDIWVPIkIGALTYFAqADALKGTLVSTLKEVKPTVF-IGVPQIWEKIHEMVKKNSAKSMGLKkkafvwarnigf 167
Cdd:PRK07008 231 VNAWGLPYSAPL-TGAKLVLP-GPDLDGKSLYELIEAERVTFsAGVPTVWLGLLNHMREAGLRFSTLR------------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 168 kvnsKKMLGKYNTPVSyrMAKTLvfskvKTSLGLDHCHSF-ISGTAPLNQETAEFFLSLDIPIGELYGLSESSGpHTIsn 246
Cdd:PRK07008 297 ----RTVIGGSACPPA--MIRTF-----EDEYGVEVIHAWgMTEMSPLGTLCKLKWKHSQLPLDEQRKLLEKQG-RVI-- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 247 qnnyrllsCG---KILTGCKNMLfqqNKDGI--GEICLWGRHIFMGYLESETETTeaidDEGWLHSGDLGQLDGLGFLYV 321
Cdd:PRK07008 363 --------YGvdmKIVGDDGREL---PWDGKafGDLQVRGPWVIDRYFRGDASPL----VDGWFPTGDVATIDADGFMQI 427
|
330 340
....*....|....*....|..
gi 574584663 322 TGHIKEIlITAGGENVPPIPVE 343
Cdd:PRK07008 428 TDRSKDV-IKSGGEWISSIDIE 448
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
38-360 |
6.98e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 51.50 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNItwIAGAVTKDFKLTDKHETVV-SYLPLSHIAAQMMDIWVPIKIGA-LTYFAQAD-AL 114
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTV--MANAVGSVLWSNSTPESVVlAVLPLFHVTGMVHSMNAPIYAGAtVVLMPRWDrEA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 115 KGTLVSTLkevKPTVfigvpqiWEKIHEMVkknsaksmglkkkafvwarnIGFKVNSKkmLGKYNtpvsyrmaktlvFSK 194
Cdd:PRK08314 271 AARLIERY---RVTH-------WTNIPTMV--------------------VDFLASPG--LAERD------------LSS 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 195 VKTSLGldhchsfisGTAPLNQETAEFFLSL-DIPIGELYGLSESSGPhTISNQNNYRLLSCGKILTgcknmlfqQNKDG 273
Cdd:PRK08314 307 LRYIGG---------GGAAMPEAVAERLKELtGLDYVEGYGLTETMAQ-THSNPPDRPKLQCLGIPT--------FGVDA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 274 ---------------IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGE 335
Cdd:PRK08314 369 rvidpetleelppgeVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKR-MINASGF 447
|
330 340
....*....|....*....|....*
gi 574584663 336 NVPPIPVETLVKKKiPIISNAMLVG 360
Cdd:PRK08314 448 KVWPAEVENLLYKH-PAIQEACVIA 471
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
225-346 |
7.65e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 51.53 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 225 LDIPIGELYGLSESSG------PHTISNQNNyrllSCGKILTGCKNMLFQQNkdgIGEICLWGRHIFMGYLEsetettEA 298
Cdd:PRK07445 253 LQLRLAPTYGMTETASqiatlkPDDFLAGNN----SSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QI 319
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 574584663 299 IDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 346
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
38-343 |
9.54e-07 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 51.30 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMdiwvpikigaltyFAQADALKGT 117
Cdd:PRK06155 183 AAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGAD-DVLYTTLPLFHTNALNA-------------FFQALLAGAT 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 118 LVSTlkevkptvfigvpqiwekihemvKKNSAKSMglkkkafvWARnigfkvnskkmLGKYNTPVSY---RMAKTLVFSK 194
Cdd:PRK06155 249 YVLE-----------------------PRFSASGF--------WPA-----------VRRHGATVTYllgAMVSILLSQP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 195 VKTSlglDHCHSFISGTAP--LNQETAEFFLSLDIPIGELYGLSESSGP--HTISNQnnyRLLSCGKILTGCKNMLFQQN 270
Cdd:PRK06155 287 ARES---DRAHRVRVALGPgvPAALHAAFRERFGVDLLDGYGSTETNFViaVTHGSQ---RPGSMGRLAPGFEARVVDEH 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 271 KDGI-----GEICLWGR--HIFM-GYLESETETTEAIDDEgWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPV 342
Cdd:PRK06155 361 DQELpdgepGELLLRADepFAFAtGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIKDA-IRRRGENISSFEV 438
|
.
gi 574584663 343 E 343
Cdd:PRK06155 439 E 439
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
17-134 |
1.08e-06 |
|
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: 50.79 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 17 GRSIPDTQLEQVIesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLShIAAQMMDI 96
Cdd:cd17655 122 IYHEESENLEPVS---KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQ-GEHLRVALFASIS-FDASVTEI 196
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 574584663 97 WVPIKIGA-LTYFAQADALKG-TLVSTLKEVKPTVFIGVP 134
Cdd:cd17655 197 FASLLSGNtLYIVRKETVLDGqALTQYIRQNRITIIDLTP 236
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
34-360 |
1.40e-06 |
|
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: 50.51 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMlsHdnitwiagavtkdfkltdKHETVVSYLPLSHIAAQMMDiwvpiKIGALtYFAQAD- 112
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGAL--H------------------AHRVLLGHLPGVQFPFNLFP-----RDGDL-YWTPADw 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 113 ALKGTLVSTLKevkPTVFIGVPQIwekIHEMVKKNSAKSMglkkkafvwarnigfkvnskKMLGKYN------TPVSYRM 186
Cdd:cd05971 141 AWIGGLLDVLL---PSLYFGVPVL---AHRMTKFDPKAAL--------------------DLMSRYGvttaflPPTALKM 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 187 AKtlvFSKVKTSLGLDHCHSFISGTAPLNQE-TAEFFLSLDIPIGELYGLSESSgpHTISNQNNY---RLLSCGKILTGC 262
Cdd:cd05971 195 MR---QQGEQLKHAQVKLRAIATGGESLGEElLGWAREQFGVEVNEFYGQTECN--LVIGNCSALfpiKPGSMGKPIPGH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 263 KNMLFQQN-----KDGIGEICLW--GRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGE 335
Cdd:cd05971 270 RVAIVDDNgtplpPGEVGEIAVElpDPVAFLGYWNNP-SATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV-ITSSGY 347
|
330 340
....*....|....*....|....*
gi 574584663 336 NVPPIPVETLVKKKiPIISNAMLVG 360
Cdd:cd05971 348 RIGPAEIEECLLKH-PAVLMAAVVG 371
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
267-343 |
1.56e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 50.53 E-value: 1.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584663 267 FQQNKDG-IGEICLWGRHIFMGYLESETETTEaiddEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 343
Cdd:PRK13382 383 FREVPTGeVGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFVVGRDDE-MIVSGGENVYPIEVE 455
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
38-343 |
1.90e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 49.66 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVtkdfkltdkHETV------VSYLPLSHIAAqmMDIWVPikigaltyfaqa 111
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADAT---------HDRLggpgqwLLALPAHHIAG--LQVLVR------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 112 dalkgtlvSTLKEVKPTVfIGVpqiwekihemvkknsakSMGLKKKAFVWArnigfkVNSKKMLGKYNTPVSYRMAKTLV 191
Cdd:PRK07824 95 --------SVIAGSEPVE-LDV-----------------SAGFDPTALPRA------VAELGGGRRYTSLVPMQLAKALD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 192 FSKVKTSL-GLDhchSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGphtisnqnnyrllSC---GKILTGCKNMLf 267
Cdd:PRK07824 143 DPAATAALaELD---AVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSG-------------GCvydGVPLDGVRVRV- 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574584663 268 qqnkdGIGEICLWGRHIFMGYleSETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEIlITAGGENVPPIPVE 343
Cdd:PRK07824 206 -----EDGRIALGGPTLAKGY--RNPVDPDPFAEPGWFRTDDLGALDD-GVLTVLGRADDA-ISTGGLTVLPQVVE 272
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
27-75 |
2.04e-06 |
|
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: 50.23 E-value: 2.04e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 574584663 27 QVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 75
Cdd:cd05918 98 KVVLTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTS 146
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
274-360 |
2.38e-06 |
|
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: 50.02 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 274 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 353
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVENLL-LRHPAV 412
|
....*..
gi 574584663 354 SNAMLVG 360
Cdd:cd05920 413 HDAAVVA 419
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
274-360 |
2.47e-06 |
|
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: 49.76 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 274 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPII 353
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-QINRGGEKIAAEEVENLLLAH-PAV 457
|
....*..
gi 574584663 354 SNAMLVG 360
Cdd:COG1021 458 HDAAVVA 464
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
15-360 |
2.78e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 49.77 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 15 ELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQM- 93
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALg 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 94 MDIWVPikigALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEmvkknsaksmglkkkafvWARNIGFKVNSKK 173
Cdd:cd05910 145 LTSVIP----DMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVAR------------------YCAQHGITLPSLR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 174 MLGKYNTPVsyRMAKTLVFSK-------VKTSLGLDHC--------HSFISGTAPLNQETAEFFLSLDIPIGELYGLSES 238
Cdd:cd05910 203 RVLSAGAPV--PIALAARLRKmlsdeaeILTPYGATEAlpvssigsRELLATTTAATSGGAGTCVGRPIPGVRVRIIEID 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 239 SGPhtISNQNNYRLLSCGkiltgcknmlfqqnkdGIGEICLWGRHIFMGYLESETETTEA-IDDEG---WLHSGDLGQLD 314
Cdd:cd05910 281 DEP--IAEWDDTLELPRG----------------EIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLD 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 574584663 315 GLGFLYVTGHIKEILITAGGeNVPPIPVETlVKKKIPIISNAMLVG 360
Cdd:cd05910 343 DEGRLWFCGRKAHRVITTGG-TLYTEPVER-VFNTHPGVRRSALVG 386
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
38-74 |
2.82e-06 |
|
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: 49.56 E-value: 2.82e-06
10 20 30
....*....|....*....|....*....|....*..
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 74
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG 132
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
13-455 |
3.12e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 49.66 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 13 FMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSH----DNITWIAGavTKDFKLTDKHETVVSYLPLSH 88
Cdd:PRK12582 198 FADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQrmmcANIAMQEQ--LRPREPDPPPPVSLDWMPWNH 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 89 IAAQMMdIWVPIKIGALTYFAQAD----ALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmgLKKKAFvwaRN 164
Cdd:PRK12582 276 TMGGNA-NFNGLLWGGGTLYIDDGkplpGMFEETIRNLREISPTVYGNVPAGYAMLAEAMEKDDA----LRRSFF---KN 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 165 IGfkvnskkmlgkyntpvsyRMAktlvfskvktslgldhchsfiSGTAPLNQETAEFFLSL-------DIPIGELYGLSE 237
Cdd:PRK12582 348 LR------------------LMA---------------------YGGATLSDDLYERMQALavrttghRIPFYTGYGATE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 238 SSGPHTISNQNNYRLLSCGKILTGCKNMLFQqnkdgIG---EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQ-L 313
Cdd:PRK12582 389 TAPTTTGTHWDTERVGLIGLPLPGVELKLAP-----VGdkyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfV 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 314 D------GLGFlyvTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldk 386
Cdd:PRK12582 464 DpddpekGLIF---DGRVAEDFKLSTGTWVSVGTLRPdAVAACSPVIHDAVVAGQDRAFIGLLA---------------- 524
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584663 387 lnFEAINFCRGLGSQASTVTEIVKqQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 455
Cdd:PRK12582 525 --WPNPAACRQLAGDPDAAPEDVV-KHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEPPSIDAGEI 590
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
33-61 |
5.20e-06 |
|
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: 48.84 E-value: 5.20e-06
10 20
....*....|....*....|....*....
gi 574584663 33 KANQCAVLIYTSGTTGIPKGVMLSHDNIT 61
Cdd:cd17653 103 SPDDLAYIIFTSGSTGIPKGVMVPHRGVL 131
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
41-96 |
6.86e-06 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 48.58 E-value: 6.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 574584663 41 IYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDI 96
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR-PEDVVYDCLPLYHSAGGIMGV 164
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
34-75 |
7.13e-06 |
|
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: 48.46 E-value: 7.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 75
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNE 133
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
34-137 |
7.75e-06 |
|
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: 48.13 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADA 113
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERP 241
|
90 100
....*....|....*....|....
gi 574584663 114 LKGTLVSTLKEVKPTVFIGVPQIW 137
Cdd:cd05959 242 TPAAVFKRIRRYRPTVFFGVPTLY 265
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
16-104 |
8.71e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 48.06 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 16 LGRSIPDTQLEQVIESQKANQC----AVLIYTSGTTGIPKGVMLSHDNItWIAGAVTKDFKLTdKHETVVSYLPLSHIAA 91
Cdd:cd05938 121 LLDKVDAASDEPVPASLRAHVTikspALYIYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVT-ADDVIYITLPLYHSSG 198
|
90
....*....|...
gi 574584663 92 QMMDIWVPIKIGA 104
Cdd:cd05938 199 FLLGIGGCIELGA 211
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
31-351 |
1.50e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 47.40 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 31 SQKANQCAVLIYTSGTTGIPKGVMLSHDN-------ITWIAgavtkDFKLTDKhetVVSYLPLSHIAAQMMDIWVPIKIG 103
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSllanveqIKTIA-----DFTPNDR---FMSALPLFHSFGLTVGLFTPLLTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 104 AltyfaqadalkgtlvstlkevkpTVFIgvpqiwekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkYNTPVS 183
Cdd:PRK08043 433 A-----------------------EVFL----------------------------------------------YPSPLH 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 184 YRMAKTLVFSK-----VKTSLGLDHCHSF------------ISGTAPLNQETAEFFL-SLDIPIGELYGLSESSGPHTIS 245
Cdd:PRK08043 444 YRIVPELVYDRnctvlFGTSTFLGNYARFanpydfarlryvVAGAEKLQESTKQLWQdKFGLRILEGYGVTECAPVVSIN 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 246 NQNNYRLLSCGKILTGCKNMLFqqNKDGI---GEICLWGRHIFMGYLESE---------TETTEAIDDEGWLHSGDLGQL 313
Cdd:PRK08043 524 VPMAAKPGTVGRILPGMDARLL--SVPGIeqgGRLQLKGPNIMNGYLRVEkpgvlevptAENARGEMERGWYDTGDIVRF 601
|
330 340 350
....*....|....*....|....*....|....*...
gi 574584663 314 DGLGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIP 351
Cdd:PRK08043 602 DEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALGVSP 638
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
22-60 |
2.58e-05 |
|
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: 46.62 E-value: 2.58e-05
10 20 30
....*....|....*....|....*....|....*....
gi 574584663 22 DTQLEQVIESQKanQCAVLIYTSGTTGIPKGVMLSHDNI 60
Cdd:cd17648 83 DTGARVVITNST--DLAYAIYTSGTTGKPKGVLVEHGSV 119
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
41-73 |
2.90e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.43 E-value: 2.90e-05
10 20 30
....*....|....*....|....*....|...
gi 574584663 41 IYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL 73
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL 181
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
254-358 |
4.20e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.14 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 254 SCGKILTGCKNMLFQQNKDGIGEIcLWGRHIFMGYLESETETT---EAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILI 330
Cdd:PRK13383 346 TVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTRYTDgggKAVVD-GMTSTGDMGYLDNAGRLFIVGR-EDDMI 422
|
90 100
....*....|....*....|....*...
gi 574584663 331 TAGGENVPPIPVETLVKKKIPIISNAML 358
Cdd:PRK13383 423 ISGGENVYPRAVENALAAHPAVADNAVI 450
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
8-333 |
4.83e-05 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 45.87 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 8 YSWDDFMELGRSIPDTqleqviESQKANQCAVLIYTSGTTGIPKGVMLSHdniTWIAGAVTKDFKLT-DKHE-------- 78
Cdd:COG0365 163 LDWDELLAAASAEFEP------EPTDADDPLFILYTSGTTGKPKGVVHTH---GGYLVHAATTAKYVlDLKPgdvfwcta 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 79 -----TVVSYL---PLSHIAAQ-MMDiwvpikiGALTYfaqADAlkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsa 149
Cdd:COG0365 234 digwaTGHSYIvygPLLNGATVvLYE-------GRPDF---PDP--GRLWELIEKYGVTVFFTAPTAI------------ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 150 ksMGLKKKAFVWARnigfkvnskkmlgKYNtpvsyrmaktlvFSKVKtslgldHChsfisGTA--PLNQETAEFFLS-LD 226
Cdd:COG0365 290 --RALMKAGDEPLK-------------KYD------------LSSLR------LL-----GSAgePLNPEVWEWWYEaVG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 227 IPIGELYGLSESSGpHTISnqnNYRLL-----SCGKILTGCKNMLFqqNKDG-------IGEICL---W-GrhIFMGYLE 290
Cdd:COG0365 332 VPIVDGWGQTETGG-IFIS---NLPGLpvkpgSMGKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWN 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 574584663 291 SETETTEAI--DDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAG 333
Cdd:COG0365 404 DPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSG 448
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
22-74 |
4.88e-05 |
|
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: 45.50 E-value: 4.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 574584663 22 DTQLeQVIESQKANqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 74
Cdd:cd17644 95 DAQI-SVLLTQPEN-LAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGIT 145
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-126 |
5.00e-05 |
|
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: 45.54 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhetvvsylplSHIAAQMMDIWVPIKIGAltyFAQADALKGT 117
Cdd:cd17650 96 AYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSF----------PVRLLQMASFSFDVFAGD---FARSLLNGGT 162
|
....*....
gi 574584663 118 LVSTLKEVK 126
Cdd:cd17650 163 LVICPDEVK 171
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
35-137 |
5.61e-05 |
|
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: 45.36 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 35 NQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT--DKHETVVSYlpLSHIAAqmMDIWVPIKIGALTYFAQAD 112
Cdd:cd12116 126 DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGpgDRLLAVTTY--AFDISL--LELLLPLLAGARVVIAPRE 201
|
90 100
....*....|....*....|....*..
gi 574584663 113 ALK--GTLVSTLKEVKPTVFIGVPQIW 137
Cdd:cd12116 202 TQRdpEALARLIEAHSITVMQATPATW 228
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
36-59 |
6.20e-05 |
|
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: 45.34 E-value: 6.20e-05
10 20
....*....|....*....|....
gi 574584663 36 QCAVLIYTSGTTGIPKGVMLSHDN 59
Cdd:cd12114 127 DLAYVIFTSGSTGTPKGVMISHRA 150
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
34-61 |
7.20e-05 |
|
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: 45.16 E-value: 7.20e-05
10 20
....*....|....*....|....*...
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMLSHDNIT 61
Cdd:cd17656 127 SDDLLYIIYTSGTTGKPKGVQLEHKNMV 154
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
31-74 |
7.55e-05 |
|
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: 45.05 E-value: 7.55e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 574584663 31 SQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 74
Cdd:cd17649 90 THHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT 133
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
21-60 |
7.85e-05 |
|
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: 44.96 E-value: 7.85e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 574584663 21 PDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNI 60
Cdd:cd17646 127 PATPPLVPPRPDNL---AYVIYTSGSTGRPKGVMVTHAGI 163
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
10-91 |
8.05e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 45.25 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 10 WDDFMELGRSIPDTQLEqVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT----WIAGavtkdfkLTDKHETVVSY-- 83
Cdd:PRK08279 175 YEDLAAAAAGAPTTNPA-SRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLkamgGFGG-------LLRLTPDDVLYcc 246
|
....*...
gi 574584663 84 LPLSHIAA 91
Cdd:PRK08279 247 LPLYHNTG 254
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-74 |
8.96e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.54 E-value: 8.96e-05
10 20 30
....*....|....*....|....*....|....*....
gi 574584663 36 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 74
Cdd:PRK12467 657 NLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLA 695
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
38-93 |
9.07e-05 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 44.65 E-value: 9.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNItWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQM 93
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALI 138
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
34-70 |
1.33e-04 |
|
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: 44.23 E-value: 1.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMLSHDN----ITWIAGAVTKD 70
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQWAAAAFSAE 144
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
34-360 |
1.34e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 44.35 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLShiaaqmmdiwvpikiGALTYFAQADA 113
Cdd:PRK06164 180 PDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAA-LPFC---------------GVFGFSTLLGA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 114 LKGtlvstlkevkptvfiGVPQIWEKIHEMVKknSAKSMGLKKKAFVWARNIGFKvnskKMLGKYNTPVSYRMAKTLVFS 193
Cdd:PRK06164 244 LAG---------------GAPLVCEPVFDAAR--TARALRRHRVTHTFGNDEMLR----RILDTAGERADFPSARLFGFA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 194 kvktslgldhchSFISGTAplnqETAEFFLSLDIPIGELYGLSE-----SSGPHTISNQnnYRLLSCGKILTGCKNMLFQ 268
Cdd:PRK06164 303 ------------SFAPALG----ELAALARARGVPLTGLYGSSEvqalvALQPATDPVS--VRIEGGGRPASPEARVRAR 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 269 QNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG-FLYVT--GHIkeilITAGGENVP 338
Cdd:PRK06164 365 DPQDGallpdgeSGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQTrmGDS----LRLGGFLVN 440
|
330 340
....*....|....*....|..
gi 574584663 339 PIPVETLVkKKIPIISNAMLVG 360
Cdd:PRK06164 441 PAEIEHAL-EALPGVAAAQVVG 461
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
40-93 |
1.55e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 44.11 E-value: 1.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584663 40 LIYTSGTTGIPKGVMLSHDNItWIAGAVTKDF----KLTDKHETVVSYL-----------PLSHIAAQM 93
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDI-FRVLLGGRDFatgePIEDEEELAKRAAagpgmrrfpapPLMHGAGQW 235
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
40-100 |
1.57e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 44.25 E-value: 1.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584663 40 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdkhETVVSYL--PLSHIAAqMMDIWVPI 100
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT---RDDVCYVsmPLFHSNA-VMAGWAPA 213
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
10-57 |
2.72e-04 |
|
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: 43.49 E-value: 2.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 574584663 10 WDDFMELGRSIPDTqlEQVIESQKANQcAVLIYTSGTTGIPKGVMLSH 57
Cdd:cd17651 114 TLLDQPGAAAGADA--EPDPALDADDL-AYVIYTSGSTGRPKGVVMPH 158
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
40-99 |
3.11e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 43.13 E-value: 3.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574584663 40 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdkhETVVSYL--PLSHIAAQMMDiWVP 99
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLG---PDDVCYVsmPLFHSNAVMAG-WAV 214
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
38-71 |
3.80e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 3.80e-04
10 20 30
....*....|....*....|....*....|....
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDF 71
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF 2369
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
40-112 |
4.42e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 42.50 E-value: 4.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574584663 40 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHEtvvsYLPLSHIAAQMM--DIWVPIKIGALTYFAQAD 112
Cdd:cd17647 114 LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK----FTMLSGIAHDPIqrDMFTPLFLGAQLLVPTQD 184
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
272-356 |
6.68e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 42.32 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 272 DGIGEIC-LWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKI 350
Cdd:PRK13388 349 EAIGELVnTAGAGFFEGYYNNPEATAERMRH-GMYWSGDLAYRDADGWIYFAGR-TADWMRVDGENLSAAPIERILLRHP 426
|
....*.
gi 574584663 351 PIISNA 356
Cdd:PRK13388 427 AINRVA 432
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
286-343 |
1.08e-03 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 41.53 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 574584663 286 MGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK05857 386 LGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPDEVD 441
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
38-60 |
1.19e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 1.19e-03
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
274-345 |
1.35e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 41.22 E-value: 1.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584663 274 IGEICLWGRHIFMgYLESETETTEAID-DEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 345
Cdd:PRK13391 353 PGTIWFEGGRPFE-YLNDPAKTAEARHpDGTWSTVGDIGYVDEDGYLYLTDR-AAFMIISGGVNIYPQEAENL 423
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
38-91 |
1.36e-03 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 40.88 E-value: 1.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAA 91
Cdd:cd05937 90 AILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNG-DRTYTCMPLYHGTA 142
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
40-129 |
1.60e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 41.20 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584663 40 LIYTSGTTGIPKGVMLSHDNIT----WIAgavtKDFKLTDKHEtvvsYLPLSHIAAQMM--DIWVPIKIGALTYFAQADA 113
Cdd:TIGR03443 420 LSFTSGSEGIPKGVLGRHFSLAyyfpWMA----KRFGLSENDK----FTMLSGIAHDPIqrDMFTPLFLGAQLLVPTADD 491
|
90
....*....|....*...
gi 574584663 114 L--KGTLVSTLKEVKPTV 129
Cdd:TIGR03443 492 IgtPGRLAEWMAKYGATV 509
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
38-105 |
1.62e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 41.30 E-value: 1.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNIT----WIAGAvtkdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAL 105
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALAnhlcWIAEA-----YELDANDRVLLFMSFSFDGAQERFLWTLICGGCL 3306
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-60 |
1.88e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 40.91 E-value: 1.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 574584663 21 PDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDNI 60
Cdd:PRK12467 1707 SDSNPAVNLAPQ---NLAYVIYTSGSTGRPKGAGNRHGAL 1743
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
34-60 |
2.03e-03 |
|
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: 40.62 E-value: 2.03e-03
10 20
....*....|....*....|....*..
gi 574584663 34 ANQCAVLIYTSGTTGIPKGVMLSHDNI 60
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNL 129
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
272-343 |
3.04e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.05 E-value: 3.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584663 272 DGIGEIC-LWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILiTAGGENVPPIPVE 343
Cdd:PRK07867 350 EAIGELVnTAGPGGFEGYYNDPEADAERMRG-GVYWSGDLAYRDADGYAYFAGRLGDWM-RVDGENLGTAPIE 420
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
38-75 |
3.61e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 39.88 E-value: 3.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 574584663 38 AVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDFKLTD 75
Cdd:PRK04319 208 AILHYTSGSTGKPKGVLHVHNAMLqhYQTGKYVLDLHEDD 247
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
275-343 |
4.05e-03 |
|
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: 39.21 E-value: 4.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584663 275 GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVE 343
Cdd:cd17636 190 GEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAEVE 256
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
288-345 |
4.48e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 39.50 E-value: 4.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 574584663 288 YLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 345
Cdd:PRK08276 354 YHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENL 410
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
294-343 |
8.38e-03 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 38.53 E-value: 8.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 574584663 294 ETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 343
Cdd:PRK12406 370 EKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIE 418
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
37-59 |
8.38e-03 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 38.73 E-value: 8.38e-03
|
| |
