|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
73-665 |
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: 1108.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 73 KNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAK 152
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 153 VNILLVENDQQLQKILSIpQSSLEPLKAIIQYRLPMK-KNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTS 231
Cdd:cd05933 81 ANILVVENQKQLQKILQI-QDKLPHLKAIIQYKEPLKeKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 232 GTTGIPKGVMLSHDNITWIAGAVTKDFKL---TDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVST 308
Cdd:cd05933 160 GTTGMPKGVMLSHDNITWTAKAASQHMDLrpaTVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGL 388
Cdd:cd05933 240 LREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 389 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWG 468
Cdd:cd05933 320 DRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 469 RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGD 548
Cdd:cd05933 400 RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 549 KLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKW 628
Cdd:cd05933 480 KRKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKW 559
|
570 580 590
....*....|....*....|....*....|....*..
gi 574584718 629 VILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:cd05933 560 VILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
48-665 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 549.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 48 ETPMTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAIL 127
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 128 AGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIpQSSLEPLKAIIQY-RLPMKKNNNLYSWDDFMELGRS 206
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV-RDELPSLRHIVVLdPRGLRDDPRLLSLDELLALGRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 207 I-PDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWV 285
Cdd:COG1022 167 VaDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP-GDRTLSFLPLAHVFERTVSYYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 286 pIKIGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKY 365
Cdd:COG1022 246 -LAAGATVAFAESPD---TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGKS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 366 NTP---VSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSC 442
Cdd:COG1022 322 PSLllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 443 GKILTGCKNMLfqqnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGE 522
Cdd:COG1022 401 GPPLPGVEVKI-----AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 523 NVPPIPVETLVkKKIPIISNAMLVGDKLKFLSMLLTlkcemnqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVkqQDP 601
Cdd:COG1022 476 NVAPQPIENAL-KASPLIEQAVVVGDGRPFLAALIV---------------PDFEALgEWAEENGLPYTSYAELA--QDP 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584718 602 LVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:COG1022 538 EVRALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
78-653 |
1.30e-139 |
|
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: 415.46 E-value: 1.30e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 78 WEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 157
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 158 VENdqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsiPDtqleqviesqkanQCAVLIYTSGTTGIP 237
Cdd:cd05907 83 VED-----------------------------------------------PD-------------DLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 238 KGVMLSHDNITWIAGAVTkDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVSTLKEVKPTVF 317
Cdd:cd05907 103 KGVMLSHRNILSNALALA-ERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 318 IGVPQIWEKIHEMVKKnsAKSMGLKKKAFVWArnigfkvnskkMLGKyntpvsyrmaktlvfskvktslgldhCHSFISG 397
Cdd:cd05907 179 LAVPRVWEKVYAAIKV--KAVPGLKRKLFDLA-----------VGGR--------------------------LRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 398 TAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKnmlFQQNKDGigEICLWGRHIFMGYLE 477
Cdd:cd05907 220 GAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVE---VRIADDG--EILVRGPNVMLGYYK 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 478 SETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDKLKFLSMLL 557
Cdd:cd05907 295 NPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVALI 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 558 TLKCEMNQMSGEPldklnfeainfcrgLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSI 637
Cdd:cd05907 374 VPDPEALEAWAEE--------------HGIAYTDVAELAA--NPAVRAEIEAAVEAANAR-LSRYEQIKKFLLLPEPFTI 436
|
570
....*....|....*.
gi 574584718 638 YGGELGPMMKLKRHFV 653
Cdd:cd05907 437 ENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
77-665 |
1.12e-86 |
|
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: 281.80 E-value: 1.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 77 KWEILNFNQYYEACRKAAKSLIKLGLERFHG--VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVN 154
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 155 ILLVENDQqlqkilsipqssleplkaiiqyrlpmkknnNLYSWDDFMELGRSIPdtqlEQVIESqKANQCAVLIYTSGTT 234
Cdd:cd05927 82 IVFCDAGV------------------------------KVYSLEEFEKLGKKNK----VPPPPP-KPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 235 GIPKGVMLSHDNI-TWIAGA--VTKDFKLTDKHETVVSYLPLSHIAAQMMdIWVPIKIGALTYFAQADALKgtLVSTLKE 311
Cdd:cd05927 127 GNPKGVMLTHGNIvSNVAGVfkILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 312 VKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNigFKVNSKKMLGKYNTPVSYRmaktLVFSKVKTSLGLdHC 391
Cdd:cd05927 204 LKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN--YKLAELRSGVVRASPFWDK----LVFNKIKQALGG-NV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 392 HSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML--------FQQNKDGIG 462
Cdd:cd05927 277 RLMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLvdvpemnyDAKDPNPRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 463 EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISN 542
Cdd:cd05927 357 EVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARS-PFVAQ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 543 AMLVGDKLKflSMLLTLKCemnqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEamNN 621
Cdd:cd05927 436 IFVYGDSLK--SFLVAIVV------------PDPDVLkEWAASKGGGTGSFEELCK--NPEVKKAILEDLVRLGKE--NG 497
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 574584718 622 AQRIE--KWVILEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:cd05927 498 LKGFEqvKAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
57-519 |
1.57e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 253.39 E-value: 1.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 57 FRESVNRFGTYPALaskNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIY 136
Cdd:pfam00501 1 LERQAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 137 ATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDfmelgrsiPDTQLEQVI 216
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAK--------PADVPPPPP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 217 ESQKANQCAVLIYTSGTTGIPKGVMLSHDNI----TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA- 291
Cdd:pfam00501 150 PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGP-DDRVLSTLPLFHDFGLSLGLLGPLLAGAt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 292 LTYFAQADALKGT-LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntpVS 370
Cdd:pfam00501 229 VVLPPGFPALDPAaLLELIERYKVTVLYGVPTLLNML-----------------------------------------LE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 371 YRMAKTLVFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLL---SCGKIL 446
Cdd:pfam00501 268 AGAPKRALLSSLRL---------VLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLDEDLRslgSVGRPL 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584718 447 TGCK------NMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 519
Cdd:pfam00501 339 PGTEvkivddETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
78-657 |
6.59e-76 |
|
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: 253.88 E-value: 6.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 78 WEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 157
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 158 VENDQQLQKILSIpQSSLEPLKAIIqYRLP--MKKNNN--LYSWDDFMELGRSI----PDtQLEQVIESQKANQCAVLIY 229
Cdd:cd17641 89 AEDEEQVDKLLEI-ADRIPSVRYVI-YCDPrgMRKYDDprLISFEDVVALGRALdrrdPG-LYEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 230 TSGTTGIPKGVMLSHDN-ITWIAGAVTKDFKLTDkhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVST 308
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNfLGHCAAYLAADPLGPG--DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE---TMMED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGK---YNTPVSYRMAKTLVFSKVKTS 385
Cdd:cd17641 241 LREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRpvsLWLRLASWLADALLFRPLRDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 386 LGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCknmlfQQNKDGIGEIC 465
Cdd:cd17641 321 LGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGT-----EVRIDEVGEIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 466 LWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAML 545
Cdd:cd17641 396 VRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEAVV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 546 VGDKLKFLSMLLTLKcemnqmsgepldklnFEAI-NFCRGLGSQASTVTEIVKQqdPLVYKAIQQGINAVNQEaMNNAQR 624
Cdd:cd17641 475 LGAGRPYLTAFICID---------------YAIVgKWAEQRGIAFTTYTDLASR--PEVYELIRKEVEKVNAS-LPEAQR 536
|
570 580 590
....*....|....*....|....*....|...
gi 574584718 625 IEKWVILEKDFSIYGGELGPMMKLKRHFVAQKY 657
Cdd:cd17641 537 IRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
75-657 |
1.93e-69 |
|
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: 235.06 E-value: 1.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 75 GKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVN 154
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 155 ILLV----ENDQQLQKILSIPQSSLEPlkaiiqyrlPMKKNNNLYSWDDFMELGrsipdtQLEQVIESQKANQCAVLIYT 230
Cdd:cd05932 81 ALFVgkldDWKAMAPGVPEGLISISLP---------PPSAANCQYQWDDLIAQH------PPLEERPTRFPEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 231 SGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQA-DalkgTLVSTL 309
Cdd:cd05932 146 SGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEE-NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESlD----TFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 310 KEVKPTVFIGVPQIWEKIHEmvkknsaksmglkkkafvwarNIGFKVNSKKMlgkyNTPVSYRMAKTLVFSKVKTSLGLD 389
Cdd:cd05932 221 QRARPTLFFSVPRLWTKFQQ---------------------GVQDKIPQQKL----NLLLKIPVVNSLVKRKVLKGLGLD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 390 HCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGEICLWGR 469
Cdd:cd05932 276 QCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 470 HIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVEtlvkKKI---PIISNAMLV 546
Cdd:cd05932 351 ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIE----NKLaehDRVEMVCVI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 547 GDKLKFLSMLLtlkcemnQMSGEPldklNFEAINFCRGlGSQASTvteivkqqdplvyKAIQQGINAvnqeAMNNAQRIE 626
Cdd:cd05932 427 GSGLPAPLALV-------VLSEEA----RLRADAFARA-ELEASL-------------RAHLARVNS----TLDSHEQLA 477
|
570 580 590
....*....|....*....|....*....|.
gi 574584718 627 KWVILEKDFSIYGGELGPMMKLKRHFVAQKY 657
Cdd:cd05932 478 GIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
85-583 |
8.68e-63 |
|
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: 215.77 E-value: 8.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 85 QYYEACRKAAKSLIKL---GLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND 161
Cdd:cd05914 9 TYKDLADNIAKFALLLkinGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 162 QQLqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPKGVM 241
Cdd:cd05914 89 DDV------------------------------------------------------------ALINYTSGTTGNSKGVM 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 242 LSHDNITWIAGAVtKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqaDALKGTLVSTLKEVKPTVFIGVP 321
Cdd:cd05914 109 LTYRNIVSNVDGV-KEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFAQVTPTLGVP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 322 QIW--EKIHEMVKKNsaksmglkkkafvwarnigfKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTA 399
Cdd:cd05914 186 VPLviEKIFKMDIIP--------------------KLTLKKFKFKLAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIGGA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 400 PLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQN-KDGIGEICLWGRHIFMGYLES 478
Cdd:cd05914 245 KINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRGPNVMKGYYKN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 479 ETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLSML- 556
Cdd:cd05914 325 PEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAkINNMPFVLESLVVVQEKKLVALAYId 404
|
490 500 510
....*....|....*....|....*....|....*
gi 574584718 557 ---LTLKCEMNQ-----MSGEPLDKLNFEAINFCR 583
Cdd:cd05914 405 pdfLDVKALKQRniidaIKWEVRDKVNQKVPNYKK 439
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
28-665 |
3.88e-59 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 210.34 E-value: 3.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 28 WTTCRDGEVLLRLSKHGPGHETPMTIPEFFRESVNRFGTYPALASK---NGK----KWeiLNFNQYYEAcRKAAKS-LIK 99
Cdd:PLN02736 21 WNVYRSARSPLKLVSRFPDHPEIGTLHDNFVYAVETFRDYKYLGTRirvDGTvgeyKW--MTYGEAGTA-RTAIGSgLVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 100 LGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVeNDQQLQKILSIpQSSLEPLK 179
Cdd:PLN02736 98 HGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSC-LSEIPSVR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 180 AIIQY--------RLPMKKNNNLYSWDDFMELGRSIPdtqleQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWI 250
Cdd:PLN02736 176 LIVVVggadeplpSLPSGTGVEIVTYSKLLAQGRSSP-----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNlIANV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 251 AGA-VTKDFKLTDKHetvVSYLPLSHI---AAQMMDIWVPIKIGaltyFAQADALKgtLVSTLKEVKPTVFIGVPQIWEK 326
Cdd:PLN02736 251 AGSsLSTKFYPSDVH---ISYLPLAHIyerVNQIVMLHYGVAVG----FYQGDNLK--LMDDLAALRPTIFCSVPRLYNR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 327 IHEMVKKNSAKSMGLKKKAFvwarNIGFkvNSKK---MLGKYNTPvsyrMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQ 403
Cdd:PLN02736 322 IYDGITNAVKESGGLKERLF----NAAY--NAKKqalENGKNPSP----MWDRLVFNKIKAKLG-GRVRFMSSGASPLSP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 404 ETAEFflsLDIPIG----ELYGLSESSGPHTISNQNNYrllSCGKI----------LTGCKNMLFqQNKDGI---GEICL 466
Cdd:PLN02736 391 DVMEF---LRICFGgrvlEGYGMTETSCVISGMDEGDN---LSGHVgspnpacevkLVDVPEMNY-TSEDQPyprGEICV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 467 WGRHIFMGYLESETETTEAIDDEGWLHSGDLGQ-LDGlGFLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAML 545
Cdd:PLN02736 464 RGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLwLPG-GRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 546 VGDKLKflSMLLTLkcemnqMSGEPLDKLNFEAINfcrglGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEAMNNAQRI 625
Cdd:PLN02736 542 YGDSLN--SSLVAV------VVVDPEVLKAWAASE-----GIKYEDLKQLCN--DPRVRAAVLADMDAVGREAQLRGFEF 606
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 574584718 626 EKWVILEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:PLN02736 607 AKAVTLVPEpFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
53-547 |
1.23e-57 |
|
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: 201.58 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 53 IPEFFRESVNRFGTYPALASKngkkWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLC 132
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 133 VGIYATNSAEVCQYVITHAKVNILLvendqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsipdtql 212
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 213 eqviesqkanqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA- 291
Cdd:COG0318 102 -----------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP-GDVVLVALPLFHVFGLTVGLLAPLLAGAt 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 292 ---LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntp 368
Cdd:COG0318 170 lvlLPRFDPERVLE-----LIERERVTVLFGVPTML-------------------------------------------- 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 369 vsYRMAKTLVFSKVKTSlgldHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNY--RLLSCGKI 445
Cdd:COG0318 201 --ARLLRHPEFARYDLS----SLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVNPEDPGerRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 446 LTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILIT 518
Cdd:COG0318 275 LPGVEVRIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
490 500
....*....|....*....|....*....
gi 574584718 519 aGGENVPPIPVETLVkKKIPIISNAMLVG 547
Cdd:COG0318 352 -GGENVYPAEVEEVL-AAHPGVAEAAVVG 378
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
81-653 |
2.41e-54 |
|
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: 193.97 E-value: 2.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYvithakvnillven 160
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIH-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 161 dqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGV 240
Cdd:cd17639 72 ---------------------------------------------SLNETECSAIFTDGKPDDLACIMYTSGSTGNPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 241 MLSHDNITW-IAGAVTKDFKLTDKHETVVSYLPLSHI---AAQMmdiwVPIKIGALTYFAQADAL--------KGTLVst 308
Cdd:cd17639 107 MLTHGNLVAgIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCLYRGGTIGYGSPRTLtdkskrgcKGDLT-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 309 lkEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarNIGFKVNSKKMLGKYNTPVsyrmAKTLVFSKVKTSLGl 388
Cdd:cd17639 181 --EFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLF----WTAYQSKLKALKEGPGTPL----LDELVFKKVRAALG- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 389 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML--------FQQNKDG 460
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLvdweeggySTDKPPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 461 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPII 540
Cdd:cd17639 330 RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSN-PLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 541 SNAMLVGD--KLKFLSMLLTlkcemNQmsgEPLDKlnfeainFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEA 618
Cdd:cd17639 409 NNICVYADpdKSYPVAIVVP-----NE---KHLTK-------LAEKHGVINSEWEELCE--DKKLQKAVLKSLAETARAA 471
|
570 580 590
....*....|....*....|....*....|....*...
gi 574584718 619 mnNAQRIE---KWVILEKDFSIYGGELGPMMKLKRHFV 653
Cdd:cd17639 472 --GLEKFEipqGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
40-665 |
3.89e-54 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 196.57 E-value: 3.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 40 LSKHG-PGHETPMTIP-EFFRESVNRFGTYPALA---SKNGK----KWEilNFNQYYEACRKAAKSLIKLGLERFHGVGI 110
Cdd:PLN02430 29 LSKKGfPPIDSDITTAwDIFSKSVEKYPDNKMLGwrrIVDGKvgpyMWK--TYKEVYEEVLQIGSALRASGAEPGSRVGI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 111 LGFNSAEWfITAVGAILAGGL-CVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQYRLPMK 189
Cdd:PLN02430 107 YGSNCPQW-IVAMEACAAHSLiCVPLYDTLGPGAVDYIVDHAEIDFVFVQ-DKKIKELLEPDCKSAKRLKAIVSFTSVTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 190 KNNN--------LYSWDDFMELGRSIPdtqlEQVIESQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAV---TKDF 258
Cdd:PLN02430 185 EESDkasqigvkTYSWIDFLHMGKENP----SETNPPKPLDICTIM-YTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 259 KLTDKHETV-VSYLPLSHIAAQMMDIWVPIKIGALTYF-AQADALKgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSA 336
Cdd:PLN02430 260 EDKMTHDDVyLSFLPLAHILDRMIEEYFFRKGASVGYYhGDLNALR----DDLMELKPTLLAGVPRVFERIHEGIQKALQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 337 KSMGLKKKAFvwarNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFF-LSLDIP 415
Cdd:PLN02430 336 ELNPRRRLIF----NALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEFLrVTSCAF 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 416 IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQ---------NKDGIGEICLWGRHIFMGYLESETETTEAI 486
Cdd:PLN02430 411 VVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEvpemgydplGEPPRGEICVRGKCLFSGYYKNPELTEEVM 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 487 DDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDKLKflSMLLTLKCemn 564
Cdd:PLN02430 491 KD-GWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYV---ALEYLenVYGQNPIVEDIWVYGDSFK--SMLVAVVV--- 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 565 qmsgepldkLNFEAINFCRGLGSQASTVTEIVKQqdPLVYKAIQQGINAVnqEAMNNAQRIE--KWVILE-KDFSIYGGE 641
Cdd:PLN02430 562 ---------PNEENTNKWAKDNGFTGSFEELCSL--PELKEHILSELKST--AEKNKLRGFEyiKGVILEtKPFDVERDL 628
|
650 660
....*....|....*....|....
gi 574584718 642 LGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:PLN02430 629 VTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
79-653 |
5.23e-52 |
|
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: 186.41 E-value: 5.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 79 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLV 158
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 159 ENDqqlqkilsipqssleplkaiiqyrlpmkkNNNLyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPK 238
Cdd:cd17640 84 END-----------------------------SDDL------------------------------ATIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 239 GVMLSHDNITWIAGAVTkDFKLTDKHETVVSYLPLSHIAAQmmdiwvpikigALTYFAqadALKG---------TLVSTL 309
Cdd:cd17640 105 GVMLTHANLLHQIRSLS-DIVPPQPGDRFLSILPIWHSYER-----------SAEYFI---FACGcsqaytsirTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 310 KEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIG-FKVNskkmlgkyntpvsyrmaktlvfskvktslgl 388
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGiFKFG------------------------------- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 389 dhchsfISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI------G 462
Cdd:cd17640 219 ------ISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 463 EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVE-TLVKKkiPIIS 541
Cdd:cd17640 293 IVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEeALMRS--PFIE 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 542 NAMLVGDKLKFLSMLLTlkcemnqmsgePldklNFEAINfcRGLGSQASTVTEIVKQ--QDPLVYKAIQQGINAV--NQE 617
Cdd:cd17640 371 QIMVVGQDQKRLGALIV-----------P----NFEELE--KWAKESGVKLANDRSQllASKKVLKLYKNEIKDEisNRP 433
|
570 580 590
....*....|....*....|....*....|....*.
gi 574584718 618 AMNNAQRIEKWVILEKDFsIYGGELGPMMKLKRHFV 653
Cdd:cd17640 434 GFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRNVV 468
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
55-665 |
1.21e-51 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 189.85 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 55 EFFRESVNRFGTYPALASK---NGK--KWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 129
Cdd:PLN02614 49 DVFRMSVEKYPNNPMLGRReivDGKpgKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 130 GLCVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQYR--LPMKKNNN------LYSWDDFM 201
Cdd:PLN02614 129 LYCVPLYDTLGAGAVEFIISHSEVSIVFVE-EKKISELFKTCPNSTEYMKTVVSFGgvSREQKEEAetfglvIYAWDEFL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 202 ELGRSipdTQLEQVIEsQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-----LTDKhETVVSYLPLSHI 276
Cdd:PLN02614 208 KLGEG---KQYDLPIK-KKSDICTIM-YTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVK-DVYLSYLPLAHI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 277 AAQMMDIWVpIKIGALTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKv 356
Cdd:PLN02614 282 FDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFG- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 357 NSKKmlGKYNTPVSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLD-IPIGELYGLSESSGPHTISNQN 435
Cdd:PLN02614 358 NMKK--GQSHVEASPLCDK-LVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCAGTFVSLPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 436 NYRLLscGKILTGCKNM------LFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLG 504
Cdd:PLN02614 434 ELDML--GTVGPPVPNVdirlesVPEMEYDALastprGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNG 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 505 FLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAMLVGDklKFLSMLLTLKCEMNQM----SGEPLDKLNFEAIn 580
Cdd:PLN02614 511 SMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGN--SFESFLVAIANPNQQIlerwAAENGVSGDYNAL- 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 581 fCRGLGSQASTVTEIVKQQDPLVYKAIQQgINAVNQEAMNnaqriekwVILEKDFsiyggeLGPMMKLKRHFVAQKYKKQ 660
Cdd:PLN02614 587 -CQNEKAKEFILGELVKMAKEKKMKGFEI-IKAIHLDPVP--------FDMERDL------LTPTFKKKRPQLLKYYQSV 650
|
....*
gi 574584718 661 IDHMY 665
Cdd:PLN02614 651 IDEMY 655
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
55-665 |
2.74e-50 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 185.82 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 55 EFFRESVNRF------GTYPALASKNGKK-WeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWfITAVGAIL 127
Cdd:PLN02861 47 QFFSDAVKKYpnnqmlGRRQVTDSKVGPYvW--LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEW-IIAMEACN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 128 AGGLC-VGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQY---RLPMKKNN-----NLYSWD 198
Cdd:PLN02861 124 SQGITyVPLYDTLGANAVEFIINHAEVSIAFVQ-ESKISSILSCLPKCSSNLKTIVSFgdvSSEQKEEAeelgvSCFSWE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 199 DFMELGRSipDTQLEQvieSQKANQCAVLiYTSGTTGIPKGVMLSHDNItwIAGAVTKD--FKLTDK----HETVVSYLP 272
Cdd:PLN02861 203 EFSLMGSL--DCELPP---KQKTDICTIM-YTSGTTGEPKGVILTNRAI--IAEVLSTDhlLKVTDRvateEDSYFSYLP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 273 LSHIAAQMMDIWVpIKIGALTYFAQADALkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNi 352
Cdd:PLN02861 275 LAHVYDQVIETYC-ISKGASIGFWQGDIR--YLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYN- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 353 gFKV-NSKKMLGKYNTpvSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIP-IGELYGLSESSGPHT 430
Cdd:PLN02861 351 -YKLgNLRKGLKQEEA--SPRLDR-LVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCF 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 431 ISNQNNYRLL-SCGKILTGCKNMLFQQNKDGI--------GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLD 501
Cdd:PLN02861 426 TSIANVFSMVgTVGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQ 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 502 GLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDklKFLSMLLTLKCEMNQmSGEPLDKLNFEAI 579
Cdd:PLN02861 505 PNGAMKIIDRKKNIFKLSQGEYV---AVENLenTYSRCPLIASIWVYGN--SFESFLVAVVVPDRQ-ALEDWAANNNKTG 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 580 NF---CrglgsqastvteivkqQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKD-FSIYGGELGPMMKLKRHFVAQ 655
Cdd:PLN02861 579 DFkslC----------------KNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLK 642
|
650
....*....|
gi 574584718 656 KYKKQIDHMY 665
Cdd:PLN02861 643 YYKDCIDQLY 652
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
81-532 |
2.30e-49 |
|
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: 179.72 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEN 160
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 161 DQqLQKILSIpQSSLEPLKAIIQYRLPMKKNNNLYSWDDFmELGRSIPDtQLEQVIESqkANQCAVLIYTSGTTGIPKGV 240
Cdd:cd05911 91 DG-LEKVKEA-AKELGPKDKIIVLDDKPDGVLSIEDLLSP-TLGEEDED-LPPPLKDG--KDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 241 MLSHDNIT-WIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKiGALTY----FAQADALKgtlvsTLKEVKPT 315
Cdd:cd05911 165 CLSHRNLIaNLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIimpkFDSELFLD-----LIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 316 VFIGVPQIwekiheMVkknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSYRMAktlvfskvktSLgldhcHSFI 395
Cdd:cd05911 239 FLYLVPPI------AA-----------------------------ALAKSPLLDKYDLS----------SL-----RVIL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 396 SGTAPLNQETAEFFLSLDIP--IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF------QQNKDGIGEICLW 467
Cdd:cd05911 269 SGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVdddgkdSLGPNEPGEICVR 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574584718 468 GRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETL 532
Cdd:cd05911 349 GPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAV 412
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
223-535 |
4.91e-47 |
|
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: 4.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 223 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAaQMMDIWVPIKIGA----LTYFAQA 298
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE-GDVFLSTLPLFHIG-GLFGLLGALLAGGtvvlLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 299 DALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwARNIGFKvnskkmlgkyntpvsyrmakTLV 378
Cdd:cd04433 79 AALE-----LIEREKVTILLGVPTLLARL---------------------LKAPESA--------------------GYD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 379 FSKVKTslgldhchsFISGTAPLNQETAEFFLSL-DIPIGELYGLSESSGPHTISN--QNNYRLLSCGKILTGCKNMLFQ 455
Cdd:cd04433 113 LSSLRA---------LVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPpdDDARKPGSVGRPVPGVEVRIVD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 456 QNKD-----GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:cd04433 184 PDGGelppgEIGELVVRGPSVMKGYWNNP-EATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVE 261
|
....*
gi 574584718 531 TLVKK 535
Cdd:cd04433 262 AVLLG 266
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
50-530 |
2.94e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 166.13 E-value: 2.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 50 PMTIPEFFRESVNRFGTYPALASkNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWF-----ITAVG 124
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYF-DGRRT---TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLeayfaVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 125 AILAgglcvgiyATN---SAEVCQYVITHAKVNILLVEND--QQLQKILSipqsSLEPLKAIIQYRLPMKKNNNLYsWDD 199
Cdd:PRK06187 81 AVLH--------PINirlKPEEIAYILNDAEDRVVLVDSEfvPLLAAILP----QLPTVRTVIVEGDGPAAPLAPE-VGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 200 FMELGRSIPDTQLEQVIEsqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAq 279
Cdd:PRK06187 148 YEELLAAASDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRD-DVYLVIVPMFHVHA- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 280 mmdiW----VPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEkihemvkknsaksmglkkkafvwarnigf 354
Cdd:PRK06187 223 ----WglpyLALMAGAkQVIPRRFDP--ENLLDLIETERVTFFFAVPTIWQ----------------------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 355 kvnskkMLGKYntPVSYRMAktlvFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSG------ 427
Cdd:PRK06187 268 ------MLLKA--PRAYFVD----FSSLRL---------VIYGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvsvlp 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 428 -PHTISNQNNYRlLSCGKILTGCK------NMLFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQ 499
Cdd:PRK06187 327 pEDQLPGQWTKR-RSAGRPLPGVEarivddDGDELPPDGGeVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGY 404
|
490 500 510
....*....|....*....|....*....|.
gi 574584718 500 LDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIIS-GGENIYPRELE 434
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
50-530 |
8.82e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 164.69 E-value: 8.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 50 PMTIPEFFRESVNRFGTYPALASKNGKkweiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 129
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQR----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 130 GLCVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQS--SLEpLKAIIQYRLPMKKNNNLYSWDDFMELGrsi 207
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFVL-GLFLGVDYSATTRlpALE-HVVICETEEDDPHTEKMKTFTDFLAAG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 208 pdTQLEQVIEsQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPI 287
Cdd:PRK07656 155 --DPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEG-DRYLAANPFFHVFGYKAGVNAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 288 KIGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIwekihemvkknsaksmglkkkafvwarnigfkvnskkmlg 363
Cdd:PRK07656 231 MRGAtilpLPVFDPDEVFR-----LIETERITVLPGPPTM---------------------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 364 kYNTPVSYRMAKTLVFSkvktSLGLdhchsFISGTAPLNQETAEFFLS-LDIP-IGELYGLSESSGPHTISNQNNYRLLS 441
Cdd:PRK07656 266 -YNSLLQHPDRSAEDLS----SLRL-----AVTGAASMPVALLERFESeLGVDiVLTGYGLSEASGVTTFNRLDDDRKTV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 442 CGKILTGCKNM-------LFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK 513
Cdd:PRK07656 336 AGTIGTAIAGVenkivneLGEEVPVGeVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKK 415
|
490
....*....|....*..
gi 574584718 514 EILITaGGENVPPIPVE 530
Cdd:PRK07656 416 DMFIV-GGFNVYPAEVE 431
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
48-666 |
2.18e-43 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 166.45 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 48 ETP----MTIPEFFRESVNRFGTYPAL-----------ASKNGKKWEILNFNQY--------YEACRKAAKSLIKLGLER 104
Cdd:PLN02387 51 ETPwegaTTLAALFEQSCKKYSDKRLLgtrklisrefeTSSDGRKFEKLHLGEYewitygqvFERVCNFASGLVALGHNK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 105 FHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENdQQLQKILSIpQSSLEPLKAII-- 182
Cdd:PLN02387 131 EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS-KQLKKLIDI-SSQLETVKRVIym 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 183 -------QYRLPMKKNNNLYSWDDFMELGRSIP-DTQLEqviesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAV 254
Cdd:PLN02387 209 ddegvdsDSSLSGSSNWTVSSFSEVEKLGKENPvDPDLP------SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 255 TKDFKLTDKHETVVSYLPLSHI---AAQ--MMDIWVPIKIG-ALTYFAQADALK-GTL--VSTLkevKPTVFIGVPQIWE 325
Cdd:PLN02387 283 MTVVPKLGKNDVYLAYLPLAHIlelAAEsvMAAVGAAIGYGsPLTLTDTSNKIKkGTKgdASAL---KPTLMTAVPAILD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 326 KIHEMVKKNSAKSMGLKKKAF--VWARNIGFKVNS-------KKMLgkYNtpvsyrmakTLVFSKVKTSLGlDHCHSFIS 396
Cdd:PLN02387 360 RVRDGVRKKVDAKGGLAKKLFdiAYKRRLAAIEGSwfgawglEKLL--WD---------ALVFKKIRAVLG-GRIRFMLS 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 397 GTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI---------GEICL 466
Cdd:PLN02387 428 GGAPLSGDTQRFInICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVI 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 467 WGRHIFMGYLESETETTEA--IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISN 542
Cdd:PLN02387 508 GGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVS-PYVDN 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 543 AMLVGDklKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRgLGSQASTVTEivkqqdplvykaIQQGINAVNQEAmnna 622
Cdd:PLN02387 587 IMVHAD--PFHSYCVALVVPSQQALEKWAKKAGIDYSNFAE-LCEKEEAVKE------------VQQSLSKAAKAA---- 647
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 574584718 623 qRIEKWVI------LEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH 666
Cdd:PLN02387 648 -RLEKFEIpakiklLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
53-530 |
9.16e-41 |
|
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: 155.03 E-value: 9.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 53 IPEFFRESVNRFGTYPALAskNGKKWeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLC 132
Cdd:cd05936 1 LADLLEEAARRFPDKTALI--FMGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 133 VgiyatnsaevcqyvithaKVNILLVEndQQLQKILSIPQSsleplKAIIQYRlpmkknnnlyswdDFMELGRSIPDTQL 212
Cdd:cd05936 77 V------------------PLNPLYTP--RELEHILNDSGA-----KALIVAV-------------SFTDLLAAGAPLGE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 213 EQVIesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA 291
Cdd:cd05936 119 RVAL---TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdLLEGDDVVLAALPLFHVFGLTVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 292 ----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsaksMGLKKKAFVWarnigfkvnskkmlgkynt 367
Cdd:cd05936 196 tivlIPRFRPIGVLK-----EIRKHRVTIFPGVPTMYIAL-----------LNAPEFKKRD------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 368 pvsyrmaktlvFSKVKTSlgldhchsfISGTAPLNQETAEFFLSL-DIPIGELYGLSESSgPHTISNQ--NNYRLLSCGK 444
Cdd:cd05936 241 -----------FSSLRLC---------ISGGAPLPVEVAERFEELtGVPIVEGYGLTETS-PVVAVNPldGPRKPGSIGI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 445 ILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILI 517
Cdd:cd05936 300 PLPGTEVKIV--DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDEDGYFFIVDRKKDMII 376
|
490
....*....|...
gi 574584718 518 tAGGENVPPIPVE 530
Cdd:cd05936 377 -VGGFNVYPREVE 388
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
46-532 |
3.97e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 147.82 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 46 GHETPMTIpEFFRESVNRfgTYPALaskngkkWE-ILNFnqyyeacrkaAKSLIKLGLERFHGVGILGFNSAEWFITAVG 124
Cdd:PTZ00216 106 GKERTMEV-THFNETRYI--TYAEL-------WErIVNF----------GRGLAELGLTKGSNVAIYEETRWEWLASIYG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 125 AILAGGLCVGIYATNSAEVCQYVI--THAKVnilLVENDQQLQKILSIPQSSLEPlKAIIQY--RLPM---KKNNNLYSW 197
Cdd:PTZ00216 166 IWSQSMVAATVYANLGEDALAYALreTECKA---IVCNGKNVPNLLRLMKSGGMP-NTTIIYldSLPAsvdTEGCRLVAW 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 198 DDFMELGRSIPDTQLEQVIESqkANQCAVLIYTSGTTGIPKGVMLSHDNITwiAGAVTKDFKLTD------KHETVVSYL 271
Cdd:PTZ00216 242 TDVVAKGHSAGSHHPLNIPEN--NDDLALIMYTSGTTGDPKGVMHTHGSLT--AGILALEDRLNDligppeEDETYCSYL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 272 PLSHIaaqmMDIWVP---IKIGALTYFAQADalkgTLVST-------LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGL 341
Cdd:PTZ00216 318 PLAHI----MEFGVTnifLARGALIGFGSPR----TLTDTfarphgdLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 342 KKKAFVWArnigFKVNSKKMLGKYNTPvsYRMAKtlVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYG 421
Cdd:PTZ00216 390 KRRVFDHA----YQSRLRALKEGKDTP--YWNEK--VFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 422 LSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNK-------DGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHS 494
Cdd:PTZ00216 461 LTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEykhtdtpEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHT 540
|
490 500 510
....*....|....*....|....*....|....*...
gi 574584718 495 GDLGQLDGLGFLYVTGHIKEILITAGGENvppIPVETL 532
Cdd:PTZ00216 541 GDVGSIAANGTLRIIGRVKALAKNCLGEY---IALEAL 575
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
51-530 |
2.56e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 134.94 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 51 MTIPEFFRESVNRFGTYPALASKN-GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEW----FITA-VG 124
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDqGLRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWvltqFATAkIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 125 AILagglcVGI----------YATNSAEvCQYVIT---------HAKVNILLVENDQQLQKILsipQSSLEP-LKAIIqy 184
Cdd:PRK08315 93 AIL-----VTInpayrlseleYALNQSG-CKALIAadgfkdsdyVAMLYELAPELATCEPGQL---QSARLPeLRRVI-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 185 RLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT----WIAGAVtkdfKL 260
Cdd:PRK08315 162 FLGDEKHPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILnngyFIGEAM----KL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 261 TDKhETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQA-DALKgTLVSTLKEvKPTVFIGVPQ--IWEKIHEMVKKnsa 336
Cdd:PRK08315 238 TEE-DRLCIPVPLYHCFGMVLGNLACVTHGAtMVYPGEGfDPLA-TLAAVEEE-RCTALYGVPTmfIAELDHPDFAR--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 337 ksmglkkkafvwarnigFKVNSKK---MLGKyNTPVSyrmaktlVFSKVKTSLGLDhchsfisgtaplnqetaefflslD 413
Cdd:PRK08315 312 -----------------FDLSSLRtgiMAGS-PCPIE-------VMKRVIDKMHMS-----------------------E 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 414 IPIGelYGLSESSGPHTISNQNN---YRLLSCGKIL-----------TGCKNMLFQQnkdgiGEICLWGRHIFMGYLESE 479
Cdd:PRK08315 344 VTIA--YGMTETSPVSTQTRTDDpleKRVTTVGRALphlevkivdpeTGETVPRGEQ-----GELCTRGYSVMKGYWNDP 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 574584718 480 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK08315 417 EKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIE 466
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
225-530 |
2.79e-33 |
|
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: 2.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLSHIAAQMMDIWVPIKIGALTYFAQA-DAlkG 303
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVV-APLFHIGGLGVFTLPTLLRGGTVVILRKfDP--E 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 304 TLVSTLKEVKPTVFIGVPQIWEKihemvkknsaksmglkkkafvwarnigfkvnskkMLgkyNTPVsyrmAKTLVFSKVK 383
Cdd:cd17631 178 TVLDLIERHRVTSFFLVPTMIQA----------------------------------LL---QHPR----FATTDLSSLR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 384 TslgldhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTI--SNQNNYRLLSCGKILTGCKNMLFQQNKD-- 459
Cdd:cd17631 217 A---------VIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFlsPEDHRRKLGSAGRPVFFVEVRIVDPDGRev 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584718 460 ---GIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:cd17631 288 ppgEVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVE 359
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
52-530 |
3.05e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 134.90 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 52 TIPEFFRESVNRFGTYPALASKN-GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGG 130
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHqALRY---TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 131 LCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLK-----AIIQYRLPMKKN---------NNLYS 196
Cdd:PRK12583 96 ILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAegqpgALACERLPELRGvvslapappPGFLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 197 WDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI 276
Cdd:PRK12583 176 WHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTE-HDRLCVPVPLYHC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 277 AAQMMDIWVPIKIGA-LTYFAQA-DALkGTLvSTLKEVKPTVFIGVPQIWekIHEMvkknsaksmglkkkafvwarnigf 354
Cdd:PRK12583 255 FGMVLANLGCMTVGAcLVYPNEAfDPL-ATL-QAVEEERCTALYGVPTMF--IAEL------------------------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 355 kvnSKKMLGKYNtpvsyrmaktlvFSKVKTSlgldhchsfISGTAPLNQET-----AEFFLSlDIPIGelYGLSESSGPH 429
Cdd:PRK12583 307 ---DHPQRGNFD------------LSSLRTG---------IMAGAPCPIEVmrrvmDEMHMA-EVQIA--YGMTETSPVS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 430 TISNQNN---YRLLSCGKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLD 501
Cdd:PRK12583 360 LQTTAADdleRRVETVGRTQPHLEVKVVDPDgatvpRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMD 439
|
490 500
....*....|....*....|....*....
gi 574584718 502 GLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK12583 440 EQGYVRIVGRSKDMIIR-GGENIYPREIE 467
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
68-530 |
8.02e-29 |
|
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: 120.49 E-value: 8.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 68 PALASKNGKKWeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 147
Cdd:cd05926 4 PALVVPGSTPA--LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 148 ITHAKVNILLVENDqqlqkilsipqSSLEPLKAIIQYRLPMKknnNLYsWDDFM--------ELGRSIPDTQLEQVIESQ 219
Cdd:cd05926 82 LADLGSKLVLTPKG-----------ELGPASRAASKLGLAIL---ELA-LDVGVlirapsaeSLSNLLADKKNAKSEGVP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 220 KANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVsYLPLSHIAAQMM----------DIWVPIKI 289
Cdd:cd05926 147 LPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLV-VMPLFHVHGLVAsllstlaaggSVVLPPRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 290 GALTYFAQadalkgtlvstLKEVKPTVFIGVPQIwekiHEMVKKNSAKSmglkkkafvwarnigfkvnskkmlgKYNTPV 369
Cdd:cd05926 226 SASTFWPD-----------VRDYNATWYTAVPTI----HQILLNRPEPN-------------------------PESPPP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 370 SYRmaktlvfskvktslgldhchsFI-SGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTiSNQ---NNYRLLSCGK 444
Cdd:cd05926 266 KLR---------------------FIrSCSASLPPAVLEALeATFGAPVLEAYGMTEAAHQMT-SNPlppGPRKPGSVGK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 445 IlTGCKNMLFQQN----KDG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITA 519
Cdd:cd05926 324 P-VGVEVRILDEDgeilPPGvVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKEL-INR 401
|
490
....*....|.
gi 574584718 520 GGENVPPIPVE 530
Cdd:cd05926 402 GGEKISPLEVD 412
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
52-533 |
1.88e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 117.29 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 52 TIPEFFRESVNRFGTYPALASkNGKKWEILNFNQYYEacRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL 131
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHS-FGKTITYREADQLVE--QFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 132 CVGIYATNSAEVCQYVITHAKVNILLVEND-----QQ--------------LQKILSIPQSSLepLKAIIQY---RLPMK 189
Cdd:PRK08751 103 VVNVNPLYTPRELKHQLIDSGASVLVVIDNfgttvQQviadtpvkqvittgLGDMLGFPKAAL--VNFVVKYvkkLVPEY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 190 KNNNLYSWDDFMELGR--SIPDTQLEqviesqkANQCAVLIYTSGTTGIPKGVMLSHDNIT--------WIAGAvtkdFK 259
Cdd:PRK08751 181 RINGAIRFREALALGRkhSMPTLQIE-------PDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqqahqWLAGT----GK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 260 LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksm 339
Cdd:PRK08751 250 LEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGL------------ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 340 glkkkafvwarnigfkvnskkmlgkYNTPvsyrMAKTLVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGE 418
Cdd:PRK08751 318 -------------------------LNTP----GFDQIDFSSLKMTLG---------GGMAVQRSVAERWKQVTgLTLVE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 419 LYGLSESS-----GPHTISNQNNYRLL------SCGKILTGCKNMLFQqnkdgIGEICLWGRHIFMGYLESETETTEAID 487
Cdd:PRK08751 360 AYGLTETSpaaciNPLTLKEYNGSIGLpipstdACIKDDAGTVLAIGE-----IGELCIKGPQVMKGYWKRPEETAKVMD 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 574584718 488 DEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETLV 533
Cdd:PRK08751 435 ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVI 479
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
79-547 |
2.07e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.50 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 79 EILNFNQYYEACRKAAKSLI-KLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 157
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 158 VENDQQ-----LQKILSI-PQSSLEPLKAIIQYRLpmkknnnlyswDDFMELGRSIPdtqleqviesqkanqcAVLIYTS 231
Cdd:PRK06839 106 VEKTFQnmalsMQKVSYVqRVISITSLKEIEDRKI-----------DNFVEKNESAS----------------FIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 232 GTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIaaqmmdiwvpikiGALTYFAQADALKGTLV----- 306
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLT-MHDRSIVLLPLFHI-------------GGIGLFAFPTLFAGGVIivprk 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 307 -------STLKEVKPTVFIGVPQIWEKIHEMVKKnsaksmglkkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvf 379
Cdd:PRK06839 225 feptkalSMIEKHKVTVVMGVPTIHQALINCSKF---------------------------------------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 380 skVKTSLglDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYR--LLSCGKILTGCKNMLFQQN 457
Cdd:PRK06839 259 --ETTNL--QSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDEN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 458 KD-----GIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETL 532
Cdd:PRK06839 335 KNkvevgEVGELLIRGPNVMKEYWNRPDATEETIQD-GWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQV 412
|
490
....*....|....*
gi 574584718 533 VkKKIPIISNAMLVG 547
Cdd:PRK06839 413 I-NKLSDVYEVAVVG 426
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
225-532 |
6.66e-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: 6.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVV-SYLPLSHIAAqmmdiwvpikigaLTYFAQAD-ALK 302
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFlCVLPMFHIYG-------------LSSFALGLlRLG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 303 GTLVStlkevkptvfigvpqiwekiheMVKKNSAKSMGLKKKafvwarnigFKVNSkkmlgkynTPVSYRMAKTLVFSKV 382
Cdd:cd05904 228 ATVVV----------------------MPRFDLEELLAAIER---------YKVTH--------LPVVPPIVLALVKSPI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 383 KTSLGLDHCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGP-HTISN--QNNYRLLSCGKILTGCKNMLFQQN 457
Cdd:cd05904 269 VDKYDLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvAMCFApeKDRAKYGSVGRLVPNVEAKIVDPE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 458 KDGI------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVET 531
Cdd:cd05904 349 TGESlppnqtGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKE-LIKYKGFQVAPAELEA 427
|
.
gi 574584718 532 L 532
Cdd:cd05904 428 L 428
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
202-547 |
8.13e-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: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 202 ELGRSIPDTQLEQVI---ESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAA 278
Cdd:cd05941 66 PLNPSYPLAELEYVItdsEPSLVLDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT-EDDVLLHVLPLHHVHG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 279 QMMDIWVPIKIGA----LTYFaqaDAlkgTLVSTLKEVKP-TVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarnig 353
Cdd:cd05941 145 LVNALLCPLFAGAsvefLPKF---DP---KEVAISRLMPSiTVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 354 fkvnsKKMlgkyntpvsyRMaktlvfskvktslgldhchsFISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgpHTIS 432
Cdd:cd05941 212 -----ERL----------RL--------------------MVSGSAALPVPTLEEWEAITgHTLLERYGMTEIG--MALS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 433 N--QNNYRLLSCGKILTGCKNMLFQQN------KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG 504
Cdd:cd05941 255 NplDGERRPGTVGMPLPGVQARIVDEEtgeplpRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDG 334
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 574584718 505 FLYVTGHIKEILITAGGENVPPIPVETLVkKKIPIISNAMLVG 547
Cdd:cd05941 335 YYWILGRSSVDIIKSGGYKVSALEIERVL-LAHPGVSECAVIG 376
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
83-530 |
1.01e-25 |
|
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: 110.46 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 83 FNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVendq 162
Cdd:cd05934 6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 163 qlqkilsipqssleplkaiiqyrlpmkknnnlyswDDFMelgrsipdtqleqviesqkanqcavLIYTSGTTGIPKGVML 242
Cdd:cd05934 82 -----------------------------------DPAS-------------------------ILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 243 SHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqadalkgTLVsTLKEVKPTVFIGVpq 322
Cdd:cd05934 102 THANLTFAGYYSARRFGLGED-DVYLTVLPLFHINAQAVSVLAALSVGA------------TLV-LLPRFSASRFWSD-- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 323 iwekihemVKKNSAksmglkkkafVWARNIGfkvnskKMLGK-YNTPVSYRMAktlvfskvktslglDHCHSFISGTAPL 401
Cdd:cd05934 166 --------VRRYGA----------TVTNYLG------AMLSYlLAQPPSPDDR--------------AHRLRAAYGAPNP 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 402 NQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF----QQNKDG-IGEICL-----WGrhI 471
Cdd:cd05934 208 PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVdddgQELPAGePGELVIrglrgWG--F 285
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 574584718 472 FMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 530
Cdd:cd05934 286 FKGYYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVE 342
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
52-530 |
3.88e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 109.64 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 52 TIPEFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL 131
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGD----RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 132 CVGI-YATNSAEVCqYVITHAKVNILLVEND--QQLQKILSIPQSSLEPLKAIIQYRLPMKknnnlySWDDFMELGRSIP 208
Cdd:PRK08316 88 HVPVnFMLTGEELA-YILDHSGARAFLVDPAlaPTAEAALALLPVDTLILSLVLGGREAPG------GWLDFADWAEAGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 209 DTQLEQVIESqkaNQCAVLIYTSGTTGIPKGVMLSHDNITW------IAGAVTKDfkltdkhETVVSYLPLSHiAAQMMD 282
Cdd:PRK08316 161 VAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHRALIAeyvsciVAGDMSAD-------DIPLHALPLYH-CAQLDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 283 IWVP-IKIGALTYFAQADALkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLkkkafvwARNIGFKVNSKKM 361
Cdd:PRK08316 230 FLGPyLYVGATNVILDAPDP-ELILRTIEAERITSFFAPPTVW--------------ISL-------LRHPDFDTRDLSS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 362 LGK--YNT-----PVSYRMAKTLvfskvkTSLGLDHChsfisgtaplnqetaefflsldipigelYGLSESSGPHTISNQ 434
Cdd:PRK08316 288 LRKgyYGAsimpvEVLKELRERL------PGLRFYNC----------------------------YGQTEIAPLATVLGP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 435 NNY--RLLSCGkiltgcKNMLFQQNK----DG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLD 501
Cdd:PRK08316 334 EEHlrRPGSAG------RPVLNVETRvvddDGndvapgeVGEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGVMD 406
|
490 500
....*....|....*....|....*....
gi 574584718 502 GLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK08316 407 EEGYITVVDRKKDMIKT-GGENVASREVE 434
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-530 |
5.46e-25 |
|
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: 109.26 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 82 NFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND 161
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 162 qqLQKILSIPQSSLEPLKAIIQY----RLPMKKNNNLYSWDDFmeLGRSIPDTQLEQVIEsqkaNQCAVLIYTSGTTGIP 237
Cdd:cd12119 107 --FLPLLEAIAPRLPTVEHVVVMtddaAMPEPAGVGVLAYEEL--LAAESPEYDWPDFDE----NTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 238 KGVMLSHDNITWIA-GAVTKDFKLTDKHETVVSYLPLSHIAAqmmdiW-VPIK---IGALTYFAQADALKGTLVSTLKEV 312
Cdd:cd12119 179 KGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMFHVNA-----WgLPYAaamVGAKLVLPGPYLDPASLAELIERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 313 KPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKkafvwarnigfkvnskkmlgkyntpvsyrmaktlvfskvktslgldhch 392
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEANGRDLSSLRR------------------------------------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 393 sFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTIS------------NQNNYRllscgkILTGCKNMLFQ---QN 457
Cdd:cd12119 285 -VVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVArppsehsnlsedEQLALR------AKQGRPVPGVElriVD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 458 KDG---------IGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIP 528
Cdd:cd12119 358 DDGrelpwdgkaVGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSVE 435
|
..
gi 574584718 529 VE 530
Cdd:cd12119 436 LE 437
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
42-547 |
3.39e-24 |
|
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: 106.84 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 42 KHGPGHETPM---TIPEFFRESVNRFGTYP-ALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAE 117
Cdd:cd17642 2 IVGPGPFYPLedgTAGEQLHKAMKRYASVPgTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 118 WFITAVGAILAGglcVGIYATNSAEVCQYVItHAkVNI----LLVENDQQLQKILSIpQSSLEPLKAIIQYrlpmkknNN 193
Cdd:cd17642 82 FFLPVIAGLFIG---VGVAPTNDIYNERELD-HS-LNIskptIVFCSKKGLQKVLNV-QKKLKIIKTIIIL-------DS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 194 LYSWDDFMEL----GRSIPDTQLEQVIESQKAN---QCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDKHE 265
Cdd:cd17642 149 KEDYKGYQCLytfiTQNLPPGFNEYDFKPPSFDrdeQVALIMNSSGSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 266 T-VVSYLPLSHiAAQMMDIWVPIKIGA----LTYFAQAdalkgTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmg 340
Cdd:cd17642 229 TaILTVIPFHH-GFGMFTTLGYLICGFrvvlMYKFEEE-----LFLRSLQDYKVQSALLVPTLF---------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 341 lkkkAFVwarnigfkvNSKKMLGKYNtpvsyrmaktlvfskvktslgLDHCHSFISGTAPLNQETAEFFLS-LDIP-IGE 418
Cdd:cd17642 287 ----AFF---------AKSTLVDKYD---------------------LSNLHEIASGGAPLSKEVGEAVAKrFKLPgIRQ 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 419 LYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI------GEICLWGRHIFMGYLESETETTEAIDDEGWL 492
Cdd:cd17642 333 GYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEATKALIDKDGWL 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 574584718 493 HSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:cd17642 413 HSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQH-PKIFDAGVAG 465
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
51-547 |
5.06e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 106.62 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 51 MTIPEFFRESVNRFGTYPALaskngkkwEILNFNQYY----EACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAI 126
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPAL--------DFFGATTTYaelgKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ-HIVAFYAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 127 LAGGLCV-------------GIYATNSAEVcqyVITHAKVNILLVE--NDQQLQKILSIPQSSLEPLKAIIQYRLPMKK- 190
Cdd:PRK05605 103 LRLGAVVvehnplytaheleHPFEDHGARV---AIVWDKVAPTVERlrRTTPLETIVSVNMIAAMPLLQRLALRLPIPAl 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 191 ----------NNNLYSWDDFMElGRSIPDTQLEQVIESQKANQcAVLIYTSGTTGIPKGVMLSHDNI--------TWIAG 252
Cdd:PRK05605 180 rkaraaltgpAPGTVPWETLVD-AAIGGDGSDVSHPRPTPDDV-ALILYTSGTTGKPKGAQLTHRNLfanaaqgkAWVPG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 253 avtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMV 331
Cdd:PRK05605 258 -------LGDGPERVLAALPMFHAYGLTLCLTLAVSIGGeLVLLPAPDI--DLILDAMKKHPPTWLPGVPPLYEKIAEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 332 KKnsaksmglkkkafvwaRNIGFKvnskkmlgkyntpvSYRMAktlvfskvktslgldhchsfISGTAPLNQETAEFFLS 411
Cdd:PRK05605 329 EE----------------RGVDLS--------------GVRNA--------------------FSGAMALPVSTVELWEK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 412 LdipIG----ELYGLSESSgPHTISN--QNNYRLLSCG------KILTGCKNMLFQQNKDG-IGEICLWGRHIFMGYLES 478
Cdd:PRK05605 359 L---TGgllvEGYGLTETS-PIIVGNpmSDDRRPGYVGvpfpdtEVRIVDPEDPDETMPDGeEGELLVRGPQVFKGYWNR 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584718 479 ETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKIPIISNAMLVG 547
Cdd:PRK05605 435 PEETAKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEE-VLREHPGVEDAAVVG 500
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
51-533 |
2.32e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 104.68 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 51 MTIPEFFRESVNRFGTYPALA-SKNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 129
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVeAVTGKAV---TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 130 GLCVGIYATN-SAEVCQYVitHAKVNILLVENDQQLQKILSIPqsslepLKAIIqyrLPMKKNNNLYSWDDFMELGRSIP 208
Cdd:PLN02330 105 GVFSGANPTAlESEIKKQA--EAAGAKLIVTNDTNYGKVKGLG------LPVIV---LGEEKIEGAVNWKELLEAADRAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 209 DTQLEQVIesQKANQCAvLIYTSGTTGIPKGVMLSHDNItwIAGAVTKDFKLTDK---HETVVSYLPLSHIAaqmmdiwv 285
Cdd:PLN02330 174 DTSDNEEI--LQTDLCA-LPFSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEmigQVVTLGLIPFFHIY-------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 286 pikigaltyfaqadALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVkknsaksmglkkkafvwARNIGFkvnskkmlgky 365
Cdd:PLN02330 241 --------------GITGICCATLRNKGKVVVMSRFELRTFLNALI-----------------TQEVSF----------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 366 nTPVSYRMAKTLVFSKVKTSLGLD--HCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESS-------GP---HTI 431
Cdd:PLN02330 279 -APIVPPIILNLVKNPIVEEFDLSklKLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHScitlthgDPekgHGI 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 432 SNQNnyrllSCGKILTGCKNMLFQQN------KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGF 505
Cdd:PLN02330 358 AKKN-----SVGFILPNLEVKFIDPDtgrslpKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGD 432
|
490 500
....*....|....*....|....*...
gi 574584718 506 LYVTGHIKEiLITAGGENVPPIPVETLV 533
Cdd:PLN02330 433 IFIVDRIKE-LIKYKGFQVAPAELEAIL 459
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
203-547 |
2.50e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 104.44 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 203 LGRSIPDTQLEQVIESQK---------ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPL 273
Cdd:PRK06087 159 LAPATSSLSLSQIIADYEplttaitthGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT-WQDVFMMPAPL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 274 SHIAAQMMDIWVPIKIGALTYFAQadalkgtlvstlkEVKPTVFIGVpqiwekihemvkknsaksmgLKKKAFVWarnig 353
Cdd:PRK06087 238 GHATGFLHGVTAPFLIGARSVLLD-------------IFTPDACLAL--------------------LEQQRCTC----- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 354 fkvnskkMLGKynTPVSYRMAKTLVFSKVK-TSLGLdhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTIS 432
Cdd:PRK06087 280 -------MLGA--TPFIYDLLNLLEKQPADlSALRF-----FLCGGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 433 NQNN---YRLLSCGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG 504
Cdd:PRK06087 345 NLDDplsRFMHTDGYAAAGVEIKVVDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAG 424
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 574584718 505 FLYVTGHIKEILITaGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PRK06087 425 YIKITGRKKDIIVR-GGENISSREVEDILLQH-PKIHDACVVA 465
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
225-547 |
2.57e-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: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAqmmdiwVPIKIGALTYfaqadALKGT 304
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED-DNWLCALPLFHISG------LSILMRSVIY-----GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 305 LVSTLKEvkptvfigvpqiwEKIHEMVKKNSAKSMGLKKKAFVWarnigfkvnskkMLGKYNTPVSYRMAKTLVfskvkt 384
Cdd:cd05912 148 LVDKFDA-------------EQVLHLINSGKVTIISVVPTMLQR------------LLEILGEGYPNNLRCILL------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 385 slgldhchsfisGTAPLNQETAEFFLSLDIPIGELYGLSE-SSGPHTISNQNNY-RLLSCGKILTGCKNMLFQ--QNKDG 460
Cdd:cd05912 197 ------------GGGPAPKPLLEQCKEKGIPVYQSYGMTEtCSQIVTLSPEDALnKIGSAGKPLFPVELKIEDdgQPPYE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 461 IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 540
Cdd:cd05912 265 VGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEEVL-LSHPAI 341
|
....*..
gi 574584718 541 SNAMLVG 547
Cdd:cd05912 342 KEAGVVG 348
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
81-533 |
7.26e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 103.19 E-value: 7.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL--- 157
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcld 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 158 --------VENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNL---YSWDDFMELGRSIP---DTQLEQVIESQkaNQ 223
Cdd:PRK06710 130 lvfprvtnVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLvvkVSESETIHLWNSVEkevNTGVEVPCDPE--ND 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 224 CAVLIYTSGTTGIPKGVMLSHDN--------ITWIagavtkdFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYF 295
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNlvsntlmgVQWL-------YNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 296 AQADALKgTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkafvwarnigfkvnskkmLGKYNTPvsyrMAK 375
Cdd:PRK06710 281 IPKFDMK-MVFEAIKKHKVTLFPGAPTIY-------------------------------------IALLNSP----LLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 376 TLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSldIPIGEL---YGLSESSgPHTISN----------------QNN 436
Cdd:PRK06710 319 EYDISSIRAC---------ISGSAPLPVEVQEKFET--VTGGKLvegYGLTESS-PVTHSNflwekrvpgsigvpwpDTE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 437 YRLLS--CGKILTGCKnmlfqqnkdgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKE 514
Cdd:PRK06710 387 AMIMSleTGEALPPGE----------IGEIVVKGPQIMKGYWNKPEETAAVLQD-GWLHTGDVGYMDEDGFFYVKDRKKD 455
|
490
....*....|....*....
gi 574584718 515 iLITAGGENVPPIPVETLV 533
Cdd:PRK06710 456 -MIVASGFNVYPREVEEVL 473
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
49-547 |
8.45e-22 |
|
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: 99.30 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 49 TPMTIPEFFRESVNRFGTYPALAskNGKKWeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILA 128
Cdd:cd12118 2 VPLTPLSFLERAAAVYPDRTSIV--YGDRR--YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 129 GGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQLQkilsipqssleplkaiiqyrlpmkknnnlysWDDFMELGRSIP 208
Cdd:cd12118 78 GAVLNALNTRLDAEEIAFILRHSEAKVLFV--DREFE-------------------------------YEDLLAEGDPDF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 209 DtqleqVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtdKHETVvsYL---PLSHiAAQMMDIWV 285
Cdd:cd12118 125 E-----WIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEM--KQHPV--YLwtlPMFH-CNGWCFPWT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 286 PIKIGaltyfaqadalkGTLVsTLKEVKPtvfigvPQIWEKIHE----------MVKKNSAKSMGLKKKAFVWARNIgfk 355
Cdd:cd12118 195 VAAVG------------GTNV-CLRKVDA------KAIYDLIEKhkvthfcgapTVLNMLANAPPSDARPLPHRVHV--- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 356 vnskkMLGKYNTPVSyrmaktlVFSKVkTSLGLDHCHSfisgtaplnqetaefflsldipigelYGLSESSGPHTI---- 431
Cdd:cd12118 253 -----MTAGAPPPAA-------VLAKM-EELGFDVTHV--------------------------YGLTETYGPATVcawk 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 432 ------SNQNNYRLlscgKILTGCKNMLFQQ------------NKDG--IGEICLWGRHIFMGYLESETETTEAIDDeGW 491
Cdd:cd12118 294 pewdelPTEERARL----KARQGVRYVGLEEvdvldpetmkpvPRDGktIGEIVFRGNIVMKGYLKNPEATAEAFRG-GW 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 574584718 492 LHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKIPIISNAMLVG 547
Cdd:cd12118 369 FHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEG-VLYKHPAVLEAAVVA 422
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
43-530 |
1.14e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 98.90 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 43 HGPGHETPMTIpeffrESVNRFGTYPALASKNGkkweILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITA 122
Cdd:PRK06188 9 HSGATYGHLLV-----SALKRYPDRPALVLGDT----RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 123 VGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIpQSSLEPLKAIiqyrLPMKKNNNLyswDDFME 202
Cdd:PRK06188 80 GAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALAL-LARVPSLKHV----LTLGPVPDG---VDLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 203 LGRSIPDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhetvVSYL---PLSHIAAQ 279
Cdd:PRK06188 152 AAAKFGPAPLVAAALPPDI---AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPAD----PRFLmctPLSHAGGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 280 MMdiwVP--IKIGALTYFAQADAlkGTLVSTLKEVKPTVFIGVP-QIWEKI-HEMVKKNSAKSMGLkkkafvwarnigfk 355
Cdd:PRK06188 225 FF---LPtlLRGGTVIVLAKFDP--AEVLRAIEEQRITATFLVPtMIYALLdHPDLRTRDLSSLET-------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 356 vnskkmlgkyntpVSYrmaktlvfskvktslgldhchsfisGTAPLN----QETAEFFLsldiPI-GELYGLSESsgPHT 430
Cdd:PRK06188 286 -------------VYY-------------------------GASPMSpvrlAEAIERFG----PIfAQYYGQTEA--PMV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 431 IS--------NQNNYRLLSCGKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDL 497
Cdd:PRK06188 322 ITylrkrdhdPDDPKRLTSCGRPTPGLRVALLDEDgrevaQGEVGEICVRGPLVMDGYWNRPEETAEAFRD-GWLHTGDV 400
|
490 500 510
....*....|....*....|....*....|...
gi 574584718 498 GQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK06188 401 AREDEDGFYYIVDRKKDMIVT-GGFNVFPREVE 432
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-530 |
2.16e-21 |
|
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: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIA--GAVTKDFKLTDkheTVVSYLPLSHIAAQMMDIWVPIKIGALTYFA-----Q 297
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAwmLALNSLFDPDD---VLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 298 ADALKGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkAFVWARNIGFKVNSkkmlgkyntpvsYRMAktl 377
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVY--------------------AALLQVPVNADISS------------LRFA--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 378 vfskvktslgldhchsfISGTAPLNQET-AEFFLSLDIPIGELYGLSESSGPHTISNQNN-YRLLSCG----------KI 445
Cdd:cd05944 127 -----------------MSGAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGlrlpyarvriKV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 446 LTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVP 525
Cdd:cd05944 190 LDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVAD-GWLNTGDLGRLDADGYLFITGRAKD-LIIRGGHNID 267
|
....*
gi 574584718 526 PIPVE 530
Cdd:cd05944 268 PALIE 272
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
227-547 |
7.28e-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: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 227 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT-DKHETVVSylPLSHIAAQMMDIWVPIKIGAlTYFAQA--DALKg 303
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTeDDRYLIIN--PFFHTFGYKAGIVACLLTGA-TVVPVAvfDVDA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 304 tLVSTLKEVKPTVFIGVPQIWEKI--HEMVKKnsaksmglkkkafvwarnigFKVNSKK--MLGKYNTPVSY--RMAKTL 377
Cdd:cd17638 81 -ILEAIERERITVLPGPPTLFQSLldHPGRKK--------------------FDLSSLRaaVTGAATVPVELvrRMRSEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 378 VFSKVKTSLGLDHChsfisGTAPLNQEtaefflsldipigelyglseSSGPHTISNqnnyrllSCGKILTGcknmlFQQN 457
Cdd:cd17638 140 GFETVLTAYGLTEA-----GVATMCRP--------------------GDDAETVAT-------TCGRACPG-----FEVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 458 KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILItAGGENVPPIPVETLVkKKI 537
Cdd:cd17638 183 IADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-AEH 260
|
330
....*....|
gi 574584718 538 PIISNAMLVG 547
Cdd:cd17638 261 PGVAQVAVIG 270
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
225-547 |
1.02e-20 |
|
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: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLSHIAAQMMdIWVPIKIGALTYFAQADALkgt 304
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLS-LPLYHVGGLAI-LVRSLLAGAELVLLERNQA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 305 LVSTLKEVKPTVFIGVP-QIWekiheMVKKNSAKSMGLKkkafvwarniGFKVnskkmlgkyntpvsyrmaktlVFSkvk 383
Cdd:cd17630 78 LAEDLAPPGVTHVSLVPtQLQ-----RLLDSGQGPAALK----------SLRA---------------------VLL--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 384 tslgldhchsfisGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGE 463
Cdd:cd17630 119 -------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----GE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 464 ICLWGRHIFMGYLESETEttEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNA 543
Cdd:cd17630 181 IWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAAL-AAHPAVRDA 256
|
....
gi 574584718 544 MLVG 547
Cdd:cd17630 257 FVVG 260
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
108-551 |
5.06e-19 |
|
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: 90.47 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 108 VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEndQQLQKILSIPQSSLEPLKAIIQYRLP 187
Cdd:cd05909 34 VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS--KQFIEKLKLHHLFDVEYDARIVYLED 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 188 MKKNnnlYSWDD----FMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDK 263
Cdd:cd05909 112 LRAK---ISKADkckaFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 264 hETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqADALKG-TLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLK 342
Cdd:cd05909 189 -DVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-PNPLDYkKIPELIYDKKATILLGTPTFL--------------RGYA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 343 KKAfvwarnigfkvnskkmlGKYNTPvSYRMAktlvfskvktslgldhchsfISGTAPLNQETAEFFLSL-DIPIGELYG 421
Cdd:cd05909 253 RAA-----------------HPEDFS-SLRLV--------------------VAGAEKLKDTLRQEFQEKfGIRILEGYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 422 LSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQ---QNKDGIGE---ICLWGRHIFMGYLESETETTEAIDDeGWLHS 494
Cdd:cd05909 295 TTECSPVISVNTPQSPNKEGTvGRPLPGMEVKIVSvetHEEVPIGEgglLLVRGPNVMLGYLNEPELTSFAFGD-GWYDT 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 574584718 495 GDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKIPIISN--AMLVGDKLK 551
Cdd:cd05909 374 GDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILSEILPEDNEvaVVSVPDGRK 431
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
59-549 |
1.33e-18 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 89.65 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 59 ESVNRFGTYPALAskNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLcvgIYAT 138
Cdd:PLN02246 31 ERLSEFSDRPCLI--DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV---TTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 139 N----SAEVC-QYVITHAKvniLLVENDQQLQKILSIPQSSLEPLKAIIQYRlpmkkNNNLYSWDDFMELGRSIPDTQLe 213
Cdd:PLN02246 106 NpfytPAEIAkQAKASGAK---LIITQSCYVDKLKGLAEDDGVTVVTIDDPP-----EGCLHFSELTQADENELPEVEI- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 214 qviesqKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWIAGAVTKD-----FKLTDkheTVVSYLPLSHIaaqmmdiwvpi 287
Cdd:PLN02246 177 ------SPDDVVALPYSSGTTGLPKGVMLTHKGlVTSVAQQVDGEnpnlyFHSDD---VILCVLPMFHI----------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 288 kigaltYfaqadALKGTLVSTLKeVKPTVFIgvpqiwekiheMVKKNSAKSMGLKKKafvwarnigFKVNskkmLGKYNT 367
Cdd:PLN02246 237 ------Y-----SLNSVLLCGLR-VGAAILI-----------MPKFEIGALLELIQR---------HKVT----IAPFVP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 368 PVSYRMAKtlvfSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSlDIP---IGELYGLSESsGPhtisnqnnyrLL---- 440
Cdd:PLN02246 281 PIVLAIAK----SPVVEKYDLSSIRMVLSGAAPLGKELEDAFRA-KLPnavLGQGYGMTEA-GP----------VLamcl 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 441 ------------SCG--------KIL---TGCKnmlFQQNKDGigEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 497
Cdd:PLN02246 345 afakepfpvksgSCGtvvrnaelKIVdpeTGAS---LPRNQPG--EICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDI 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 574584718 498 GQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVGDK 549
Cdd:PLN02246 420 GYIDDDDELFIVDRLKEL-IKYKGFQVAPAELEALLISH-PSIADAAVVPMK 469
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
199-530 |
1.46e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 90.01 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 199 DFMELGRSIPDTQLEQViESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT---WIAGAVTKDfkltDKHETVVSYLPLSH 275
Cdd:PRK07529 191 DFDAELARQPGDRLFSG-RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVanaWLGALLLGL----GPGDTVFCGLPLFH 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 276 IAAQMMDIWVPIKIGALTYFAQADALKG-TLVSTLKEV----KPTVFIGVPqiwekihemvkknSAKSMGLKKKafVWAR 350
Cdd:PRK07529 266 VNALLVTGLAPLARGAHVVLATPQGYRGpGVIANFWKIveryRINFLSGVP-------------TVYAALLQVP--VDGH 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 351 NIgfkvnskkmlgkyntpvsyrmaktlvfSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPH 429
Cdd:PRK07529 331 DI---------------------------SSLRY---------ALCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVS 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 430 TIsnqnNY-----RLLSCG--------KILTGCKNMLFQQN--KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHS 494
Cdd:PRK07529 375 SV----NPpdgerRIGSVGlrlpyqrvRVVILDDAGRYLRDcaVDEVGVLCIAGPNVFSGYLEAAHNKGLWLED-GWLNT 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 574584718 495 GDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 530
Cdd:PRK07529 450 GDLGRIDADGYFWLTGRAKD-LIIRGGHNIDPAAIE 484
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
219-541 |
1.61e-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: 89.08 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 219 QKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSH----IAAQMmdiwVPIKIGALTY 294
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK-DRILSWMPLTHdmglIAFHL----APLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 295 FAqadalkgtlvstlkevkPT-VFIGVPQIW-EKIHEmvkknsaksmglKKKAFVWARNIGFKVnskkMLGKYNTPVSYr 372
Cdd:cd05908 178 LM-----------------PTrLFIRRPILWlKKASE------------HKATIVSSPNFGYKY----FLKTLKPEKAN- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 373 maktlvfskvktSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESS--------GPHTI------ 431
Cdd:cd05908 224 ------------DWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrnailPVYGLAEASvgaslpkaQSPFKtitlgr 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 432 --------------SNQNNYRLLSCGKILTGCK-NMLFQQNK---DG-IGEICLWGRHIFMGYLESETETTEAIDDEGWL 492
Cdd:cd05908 292 rhvthgepepevdkKDSECLTFVEVGKPIDETDiRICDEDNKilpDGyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 574584718 493 HSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVETLVKKKIPIIS 541
Cdd:cd05908 372 KTGDLGFIRN-GRLVITGREKDIIFV-NGQNVYPHDIERIAEELEGVEL 418
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
229-547 |
1.86e-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: 87.33 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 229 YTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYlPLSHIAAQMMDIWVPIKIGALTYFAQA--DALkgTLV 306
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPV-PLFHCFGSVLGVLACLTHGATMVFPSPsfDPL--AVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 307 STLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkVNSKKMLgKYNtpvsyrmaktlvFSKVKTSl 386
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAE----------------------------LEHPDFD-KFD------------LSSLRTG- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 387 gldhchsfISGTAPLNQETAEFFLSL----DIPIGelYGLSESSGPHTISNQNN---YRLLSCGKIL----------TGC 449
Cdd:cd05917 124 --------IMAGAPCPPELMKRVIEVmnmkDVTIA--YGMTETSPVSTQTRTDDsieKRVNTVGRIMphteakivdpEGG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 450 KNMLFQQnkdgIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 529
Cdd:cd05917 194 IVPPVGV----PGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPREI 268
|
330
....*....|....*...
gi 574584718 530 ETLVKKKiPIISNAMLVG 547
Cdd:cd05917 269 EEFLHTH-PKVSDVQVVG 285
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
53-533 |
3.79e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 88.28 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 53 IPEFFRESVNRFGTYPALaSKNGKKweiLNFNQYYEACRKAAKSLIKL-GLERFHGVGILGFNSAEWFITAVGAILAGGL 131
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAF-SNLGKT---LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 132 CVG---IYATNSAEvCQYVITHAKVNILLVENDQQLQKILsiPQSSLE------------PLK-----AIIQYRLPMKKN 191
Cdd:PRK05677 102 VVNtnpLYTAREME-HQFNDSGAKALVCLANMAHLAEKVL--PKTGVKhvivtevadmlpPLKrllinAVVKHVKKMVPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 192 NNL---YSWDDFMELGRSIPDTQLeqvieSQKANQCAVLIYTSGTTGIPKGVMLSHDNItwIAGAV-TKDF---KLTDKH 264
Cdd:PRK05677 179 YHLpqaVKFNDALAKGAGQPVTEA-----NPQADDVAVLQYTGGTTGVAKGAMLTHRNL--VANMLqCRALmgsNLNEGC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 265 ETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIwekihemvkknsaksmglkkk 344
Cdd:PRK05677 252 EILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTL--------------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 345 aFV-WARNIGFKvnskkmlgkyntpvsyrmakTLVFSKVKTSLgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGL 422
Cdd:PRK05677 311 -FVaLCNNEAFR--------------------KLDFSALKLTL---------SGGMALQLATAERWKEVTgCAICEGYGM 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 423 SESSGPHTISNQNNYRLLSCGKIL--TGCKNMlfqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLH 493
Cdd:PRK05677 361 TETSPVVSVNPSQAIQVGTIGIPVpsTLCKVI----DDDGnelplgeVGELCVKGPQVMKGYWQRPEATDEILDSDGWLK 436
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 574584718 494 SGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETLV 533
Cdd:PRK05677 437 TGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
85-547 |
1.37e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.39 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 85 QYYEACRKAAKSLIKLGLERFHGVGILGFNSA---EWF--ITAVGAILAgglcvgiyATNSaevcQYVITHAKVNILLVE 159
Cdd:PLN02860 37 EFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDlylEWLlaVACAGGIVA--------PLNY----RWSFEEAKSAMLLVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 160 ndqqlQKILSIPQSsleplkaiIQYRLPMKKNNNLYS--WDDFME-LGRSI---------PDTQLEQVIESQKANQC--- 224
Cdd:PLN02860 105 -----PVMLVTDET--------CSSWYEELQNDRLPSlmWQVFLEsPSSSVfiflnsfltTEMLKQRALGTTELDYAwap 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 --AVLI-YTSGTTGIPKGVMLSHDNIT-------WIAGAVTKDFKLtdkHETvvsylPLSHIA------AQMMdiwvpik 288
Cdd:PLN02860 172 ddAVLIcFTSGTTGRPKGVTISHSALIvqslakiAIVGYGEDDVYL---HTA-----PLCHIGglssalAMLM------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 289 IGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIHEMvkknSAKSMGLKKKAFVwarnigfkvnsKKML-G 363
Cdd:PLN02860 237 VGAchvlLPKFDAKAALQ-----AIKQHNVTSMITVPAMMADLISL----TRKSMTWKVFPSV-----------RKILnG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 364 KYNTPVSYRMAKTLVF--SKVKTSLGL-DHCHSFIsgtaplnqetaefFLSLDIPIGELYGLSESSGPHTISNQNNYRLL 440
Cdd:PLN02860 297 GGSLSSRLLPDAKKLFpnAKLFSAYGMtEACSSLT-------------FMTLHDPTLESPKQTLQTVNQTKSSSVHQPQG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 441 SC-GKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITA 519
Cdd:PLN02860 364 VCvGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDR-IKT 442
|
490 500
....*....|....*....|....*...
gi 574584718 520 GGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PLN02860 443 GGENVYPEEVEAVLSQH-PGVASVVVVG 469
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
74-642 |
2.52e-17 |
|
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: 85.56 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 74 NGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGI---YATNSAEVC--QYVI 148
Cdd:cd05921 19 GNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQDLAklKHLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 149 THAKVNILLVENDQQLQKILSIPQSSLEPLkaIIQYRLPMKKNNNLyswddFMELGRSIPDTQLEQVIESQKANQCAVLI 228
Cdd:cd05921 99 ELLKPGLVFAQDAAPFARALAAIFPLGTPL--VVSRNAVAGRGAIS-----FAELAATPPTAAVDAAFAAVGPDTVAKFL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 229 YTSGTTGIPKGVMLSHDNITWIAGAVTKDF-KLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFaqaDALK----- 302
Cdd:cd05921 172 FTSGSTGLPKAVINTQRMLCANQAMLEQTYpFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYI---DDGKpmpgg 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 303 -GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmgLKKKAFvwarnigfkvnsKKMlgkyntpvsyrmaktlvfsk 381
Cdd:cd05921 249 fEETLRNLREISPTVYFNVPAGWEMLVAALEKDEA----LRRRFF------------KRL-------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 382 vktslgldhcHSFISGTAPLNQETAEfflSLD----------IPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKN 451
Cdd:cd05921 293 ----------KLMFYAGAGLSQDVWD---RLQalavatvgerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 452 MLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL----DGLGFLYVTGHIKEILITAGGENVPPI 527
Cdd:cd05921 360 KLVPS--GGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 528 PVET-LVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGL-GSQASTVTEIVKQqdPLVYK 605
Cdd:cd05921 438 PLRArAVAACAPLVHDAVVAGEDRAEVGALV------------------FPDLLACRRLvGLQEASDAEVLRH--AKVRA 497
|
570 580 590
....*....|....*....|....*....|....*..
gi 574584718 606 AIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 642
Cdd:cd05921 498 AFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEI 534
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
226-547 |
3.03e-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: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 226 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVpIKIGA----LTYFAQADAL 301
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTE-ADVYLNMLPLFHIAGLNLALAT-FHAGGanvvMEKFDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 302 KgtlvsTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKsmglkkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvFSK 381
Cdd:cd17637 82 E-----LIEEEKVTLMGSFPPILSNLLDAAEKSGVD-----------------------------------------LSS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 382 VKTSLGLDhchsfisgtAPlnqETAEFFLSL-DIPIGELYGLSESSGPHTISNQNNyRLLSCGKILTGCKNMLFQQNKDG 460
Cdd:cd17637 116 LRHVLGLD---------AP---ETIQRFEETtGATFWSLYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDDNDRP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 461 I-----GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHI--KEiLITAGGENVPPIPVETlV 533
Cdd:cd17637 183 VpagetGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKE-LIKPGGENVYPAEVEK-V 259
|
330
....*....|....
gi 574584718 534 KKKIPIISNAMLVG 547
Cdd:cd17637 260 ILEHPAIAEVCVIG 273
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
223-547 |
3.19e-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: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 223 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQA-DAL 301
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG-DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwDPD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 302 KGtlVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKkaFVWArnigfkvnskkmlGKYNTPVSYRMAKTLVFSK 381
Cdd:cd05903 173 KA--LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT--FVCG-------------GATVPRSLARRAAELLGAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 382 VKTSLGLDHCHSFISGTAPLNQETAEF-----FLSLDIPIGELYGLSESSGPhtisnqnnyrllscgkiltgcknmlfqq 456
Cdd:cd05903 236 VCSAYGSTECPGAVTSITPAPEDRRLYtdgrpLPGVEIKVVDDTGATLAPGV---------------------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 457 nkdgIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKK 536
Cdd:cd05903 288 ----EGELLSRGPSVFLGYLDRP-DLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLL-LG 360
|
330
....*....|.
gi 574584718 537 IPIISNAMLVG 547
Cdd:cd05903 361 HPGVIEAAVVA 371
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
75-547 |
3.65e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 84.63 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 75 GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFItavgAILA----GGLCVGIYATNSAEVCQYVITH 150
Cdd:PRK03640 25 EKKV---TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMIL----VIHAlqqlGAVAVLLNTRLSREELLWQLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 151 AKVNILLVenDQQLQKILSIPQSSLeplkaiiqyrlpmkknnnlysWDDFMELGRSIPDTQleqviESQKANQCAVLIYT 230
Cdd:PRK03640 98 AEVKCLIT--DDDFEAKLIPGISVK---------------------FAELMNGPKEEAEIQ-----EEFDLDEVATIMYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 231 SGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI---AAQMMDIWVPIKIGALTYFaqaDAlkgtlvs 307
Cdd:PRK03640 150 SGTTGKPKGVIQTYGNHWWSAVGSALNLGLTE-DDCWLAAVPIFHIsglSILMRSVIYGMRVVLVEKF---DA------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 308 tlkevkptvfigvpqiwEKIHEMVKKNSAKSMGlkkkafvwarnigfkvnskkmlgkyntpVSYRMAKTLVfskvkTSLG 387
Cdd:PRK03640 219 -----------------EKINKLLQTGGVTIIS----------------------------VVSTMLQRLL-----ERLG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 388 LDHCHS----FISGTAPLNQETAEFFLSLDIPIGELYGLSESSG------PHTISNqnnyRLLSCGKILTGC-----KNM 452
Cdd:PRK03640 249 EGTYPSsfrcMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASqivtlsPEDALT----KLGSAGKPLFPCelkieKDG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 453 LFQQNKDgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETl 532
Cdd:PRK03640 325 VVVPPFE-EGEIVVKGPNVTKGYLNREDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEE- 400
|
490
....*....|....*
gi 574584718 533 VKKKIPIISNAMLVG 547
Cdd:PRK03640 401 VLLSHPGVAEAGVVG 415
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
225-526 |
8.35e-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: 8.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQadalkgt 304
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDP-GDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 305 lvstlkevkPTVFIGVPQIWekiHEMVKKNSAKSMGlkkkafvwARNIGF-----KVNSKKM----LGKYNT------PV 369
Cdd:cd05931 224 ---------PAAFLRRPLRW---LRLISRYRATISA--------APNFAYdlcvrRVRDEDLegldLSSWRValngaePV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 370 SyrmAKTL-VFSKVKTSLGLD-HCHS----------FISGTAPLNQETAEFFLSLdipigELYGLSESSGPHTisnQNNY 437
Cdd:cd05931 284 R---PATLrRFAEAFAPFGFRpEAFRpsyglaeatlFVSGGPPGTGPVVLRVDRD-----ALAGRAVAVAADD---PAAR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 438 RLLSCGKILTGcknMLF--------QQNKDG-IGEICLWGRHIFMGYL--ESETETT----EAIDDEGWLHSGDLGQLDG 502
Cdd:cd05931 353 ELVSCGRPLPD---QEVrivdpetgRELPDGeVGEIWVRGPSVASGYWgrPEATAETfgalAATDEGGWLRTGDLGFLHD 429
|
330 340
....*....|....*....|....
gi 574584718 503 lGFLYVTGHIKEILITAgGENVPP 526
Cdd:cd05931 430 -GELYITGRLKDLIIVR-GRNHYP 451
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
225-533 |
1.26e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 83.56 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNI-------TWIAGAVtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaq 297
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMlanleqaKAAYGPL-----LHPGKELVVTALPLYHIFALTVNCLLFIELGG------ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 298 adalKGTLVSTLKEvkptvfigvpqiwekIHEMVKKnsaksmgLKKKAFVWARNigfkVNSkkmlgKYNTPVSYRMAKTL 377
Cdd:PRK08974 278 ----QNLLITNPRD---------------IPGFVKE-------LKKYPFTAITG----VNT-----LFNALLNNEEFQEL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 378 VFSKVKTSLGldhchsfisGTAPLNQETAEFFLSL-DIPIGELYGLSESS-----GPHTISNQNNyrllSCG-------- 443
Cdd:PRK08974 323 DFSSLKLSVG---------GGMAVQQAVAERWVKLtGQYLLEGYGLTECSplvsvNPYDLDYYSG----SIGlpvpstei 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 444 KILTGCKNMLFQqnkDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGEN 523
Cdd:PRK08974 390 KLVDDDGNEVPP---GEPGELWVKGPQVMLGYWQRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDM-ILVSGFN 464
|
330
....*....|
gi 574584718 524 VPPIPVETLV 533
Cdd:PRK08974 465 VYPNEIEDVV 474
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
79-533 |
1.39e-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: 83.10 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 79 EILNFNQYYEACRKAAKSLIKLGLERFHGVgILGFNSAEWFITAV-GAILAGGLCV-----GIYATNSAEvcqyvITHAK 152
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFwACVLAGFVPApltvpPTYDEPNAR-----LRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 153 vNILlvendQQLQK--ILSIPqSSLEPLKAIIQYRlpmkknnnlySWDDFMELGRSI-PDTQLEQVIESQKANQCAVLIY 229
Cdd:cd05906 112 -HIW-----QLLGSpvVLTDA-ELVAEFAGLETLS----------GLPGIRVLSIEElLDTAADHDLPQSRPDDLALLML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 230 TSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALkgtlvstL 309
Cdd:cd05906 175 TSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ-DVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEI-------L 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 310 KEvkPTVFIgvpqiwekihEMVKKNSAksmglkkkAFVWARNigFkvnskkMLGKYNTPVSYRMAKTLVFSKVKtslgld 389
Cdd:cd05906 247 AD--PLRWL----------DLIDRYRV--------TITWAPN--F------AFALLNDLLEEIEDGTWDLSSLR------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 390 hchSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-------SSGPHTISNQNNYRLLSCGKILTGCKNMLFQ 455
Cdd:cd05906 293 ---YLVNAGEAVVAKTIRRLLRLLEPYGlppdairPAFGMTEtcsgviySRSFPTYDHSQALEFVSLGRPIPGVSMRIVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 456 QNKDG-----IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:cd05906 370 DEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIV-NGVNYYSHEIE 447
|
...
gi 574584718 531 TLV 533
Cdd:cd05906 448 AAV 450
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-520 |
1.63e-16 |
|
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: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKGT 304
Cdd:cd05922 120 ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI-TADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 305 LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaKSMGLKKKAFVWARnigfkvnskkmlgkYNTPVSYRMAKTLVfskvkt 384
Cdd:cd05922 198 FWEDLREHGATGLAGVPSTYAML---------TRLGFDPAKLPSLR--------------YLTQAGGRLPQETI------ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 385 slgldhchsfisgtaplnQETAEFFLSLDIPIgeLYGLSESSG------PHTISNqnnyRLLSCGKILTGCKnmLFQQNK 458
Cdd:cd05922 249 ------------------ARLRELLPGAQVYV--MYGQTEATRrmtylpPERILE----KPGSIGLAIPGGE--FEILDD 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584718 459 DG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAG 520
Cdd:cd05922 303 DGtptppgePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFG 371
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
225-497 |
2.46e-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: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDfkLTDKHETVVSYLPLSHIAAQMmdiwvpIKIGALT-----YFAQ 297
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLVAtfWLKVSSIQD--IRPPASITLNFMPMSHIAGRI------SLYGTLArggtaYFAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 298 ADALKgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVsyrmaktl 377
Cdd:cd17632 298 ASDMS-TLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLAAV-------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 378 vfskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELYGLSEsSGPHTISNQ------NNYRLLSC---GKILT 447
Cdd:cd17632 369 ------------------CGSAPLSAEMKAFMESlLDLDLHDGYGSTE-AGAVILDGVivrppvLDYKLVDVpelGYFRT 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 574584718 448 gcknmlfqQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 497
Cdd:cd17632 430 --------DRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
81-547 |
2.63e-15 |
|
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: 79.06 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILlVEN 160
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-VTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 161 DQQLQKILSIPQSSLEPLKAII----QYRLPMKKNNNLYSWDDFMELGRSIPdtqLEQVIESQkanqCAVLIYTSGTTGI 236
Cdd:TIGR03098 105 SERLDLLHPALPGCHDLRTLIIvgdpAHASEGHPGEEPASWPKLLALGDADP---PHPVIDSD----MAAILYTSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 237 PKGVMLSHDNItwIAGA--VTKDFKLTDKhETVVSYLPLSHIAA--QMMDIWVpikIGA----LTYFAQADALKgtlvsT 308
Cdd:TIGR03098 178 PKGVVLSHRNL--VAGAqsVATYLENRPD-DRLLAVLPLSFDYGfnQLTTAFY---VGAtvvlHDYLLPRDVLK-----A 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkkafvwARNIGFKVNSKKmlgkyntpvsyRMAKTLVfSKVKTSLGL 388
Cdd:TIGR03098 247 LEKHGITGLAAVPPLWAQLAQLDWPESA------------APSLRYLTNSGG-----------AMPRATL-SRLRSFLPN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 389 dhchsfisgtaplnqetAEFFLsldipigeLYGLSESSGPHTISNQN-NYRLLSCGKILTGCKNMLFqqNKDG------- 460
Cdd:TIGR03098 303 -----------------ARLFL--------MYGLTEAFRSTYLPPEEvDRRPDSIGKAIPNAEVLVL--REDGsecapge 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 461 IGEICLWGRHIFMGYLESETETTEAI------DDEGWLH-----SGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPV 529
Cdd:TIGR03098 356 EGELVHRGALVAMGYWNDPEKTAERFrplppfPGELHLPelavwSGDTVRRDEEGFLYFVGR-RDEMIKTSGYRVSPTEV 434
|
490
....*....|....*...
gi 574584718 530 ETlVKKKIPIISNAMLVG 547
Cdd:TIGR03098 435 EE-VAYATGLVAEAVAFG 451
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
225-530 |
2.74e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 79.27 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqaDALKGT 304
Cdd:PRK07768 155 ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGA-------ELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 305 lvstlkevkPTVFIGVPQIWekihemvkknsAKSMGLKKKAFVWARNIGFKVNSKKmLGKYNTPVSYRMaktlvfSKVKT 384
Cdd:PRK07768 228 ---------PMDFLRDPLLW-----------AELISKYRGTMTAAPNFAYALLARR-LRRQAKPGAFDL------SSLRF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 385 SLgldhchsfiSGTAPLNQETAEFFLSLDIPIG-------ELYGLSESSGPHTIS------------------------- 432
Cdd:PRK07768 281 AL---------NGAEPIDPADVEDLLDAGARFGlrpeailPAYGMAEATLAVSFSpcgaglvvdevdadllaalrravpa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 433 -NQNNYRLLSCGKILTGCKNMLFQQNKD-----GIGEICLWGRHIFMGYLESETeTTEAIDDEGWLHSGDLGQLDGLGFL 506
Cdd:PRK07768 352 tKGNTRRLATLGPPLPGLEVRVVDEDGQvlpprGVGVIELRGESVTPGYLTMDG-FIPAQDADGWLDTGDLGYLTEEGEV 430
|
330 340
....*....|....*....|....
gi 574584718 507 YVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK07768 431 VVCGRVKDVIIM-AGRNIYPTDIE 453
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
225-533 |
7.36e-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: 76.53 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKgT 304
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK-S 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 305 LVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLkkkafvwaRNIGFkvnskkmlgkyntpvsyrmaktlvfskvkt 384
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSL--------RLIGY------------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 385 slgldhchsfiSGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLL-SCGKILTGCK-----NMLFQQNK 458
Cdd:cd17635 125 -----------GGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEInAVGRPYPGVDvylaaTDGIAGPS 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574584718 459 DGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLV 533
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLGERREDGFLFITGRSSES-INCGGVKIAPDEVERIA 266
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
68-547 |
1.58e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 76.46 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 68 PALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 147
Cdd:PRK06145 19 AALVYRD----QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 148 ITHAKVNILLVenDQQLQKIlsipqSSLEPLKAIIqyrlpmkknnNLYSWDDFMELGRS-IPDTQLEQVIESQKANqcav 226
Cdd:PRK06145 95 LGDAGAKLLLV--DEEFDAI-----VALETPKIVI----------DAAAQADSRRLAQGgLEIPPQAAVAPTDLVR---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 227 LIYTSGTTGIPKGVMLSHDNITW------IAGAVTKDFKLTdkhetVVSylPLSHIAA-QMMDIWVPIKIGALTYFAQAD 299
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWksidhvIALGLTASERLL-----VVG--PLYHVGAfDLPGIAVLWVGGTLRIHREFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 300 AlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSaksmgLKKKAFVWArnIGfkvnskkmlGKYNTPVSYRMAKTLVF 379
Cdd:PRK06145 227 P--EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDR-----FDLDSLAWC--IG---------GGEKTPESRIRDFTRVF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 380 SKVKtslgldhchsFISGtaplnqetaefflsldipigelYGLSESSGPHTISNQNNY--RLLSCGK--------ILTGC 449
Cdd:PRK06145 289 TRAR----------YIDA----------------------YGLTETCSGDTLMEAGREieKIGSTGRalahveirIADGA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 450 KNMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 529
Cdd:PRK06145 337 GRWLPPNMK---GEICMRGPKVTKGYWKDPEKTAEAFYG-DWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEV 411
|
490
....*....|....*...
gi 574584718 530 ETLVkKKIPIISNAMLVG 547
Cdd:PRK06145 412 ERVI-YELPEVAEAAVIG 428
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
225-530 |
2.55e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 76.08 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVsYLPLSH----IAAQMMDIwvpIKIGALTYFAQADA 300
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVA-VMPLYHghglIAALLATL---ASGGAVLLPARGRF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 301 LKGTLVSTLKEVKPTVFIGVPqiweKIHEMvkknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSYRMAKTLVFS 380
Cdd:PRK05852 255 SAHTFWDDIKAVGATWYTAVP----TIHQI------------------------------LLERAATEPSGRKPAALRFI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 381 KvktslgldhchsfiSGTAPLNQETAEF----FLSldiPIGELYGLSE---------------------SSGPHTISNQN 435
Cdd:PRK05852 301 R--------------SCSAPLTAETAQAlqteFAA---PVVCAFGMTEathqvtttqiegigqtenpvvSTGLVGRSTGA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 436 NYRLL-SCGKILTgcknmlfqqnKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKE 514
Cdd:PRK05852 364 QIRIVgSDGLPLP----------AGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKE 432
|
330
....*....|....*.
gi 574584718 515 iLITAGGENVPPIPVE 530
Cdd:PRK05852 433 -LINRGGEKISPERVE 447
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
85-545 |
5.35e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.06 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 85 QYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND--- 161
Cdd:PLN03102 44 QTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSfep 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 162 --QQLQKILSIPQSSLEPLKAII-QYRLPMKKNNNLYSWDDFMELGRSIPdTQLEQVIESQKANQCAVLIYTSGTTGIPK 238
Cdd:PLN03102 124 laREVLHLLSSEDSNLNLPVIFIhEIDFPKRPSSEELDYECLIQRGEPTP-SLVARMFRIQDEHDPISLNYTSGTTADPK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 239 GVMLSHDnitwiaGAvtkdfkltdkhetvvsYL-PLSHIAAQMMDIWvPIKIGALTYF-------AQADALKGTLVSTLK 310
Cdd:PLN03102 203 GVVISHR------GA----------------YLsTLSAIIGWEMGTC-PVYLWTLPMFhcngwtfTWGTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 311 EVKptvfigVPQIWEKIhEMvkkNSAKSMGLKKKAFvwarNIGFKVNSkkmlgkynTPVSYRMAKTLVfskvktslgldh 390
Cdd:PLN03102 260 HVT------APEIYKNI-EM---HNVTHMCCVPTVF----NILLKGNS--------LDLSPRSGPVHV------------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 391 chsfISGTAPLNQETAEFFLSLDIPIGELYGLSESSGP------------------HTISNQNNYRLLSCGKILTGCKNM 452
Cdd:PLN03102 306 ----LTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPvlfcewqdewnrlpenqqMELKARQGVSILGLADVDVKNKET 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 453 LFQQNKDG--IGEICLWGRHIFMGYLESETETTEAIDdEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PLN03102 382 QESVPRDGktMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVE 459
|
490
....*....|....*
gi 574584718 531 TLVKKKIPIISNAML 545
Cdd:PLN03102 460 NVLYKYPKVLETAVV 474
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
81-547 |
5.35e-14 |
|
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: 74.44 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVen 160
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 161 dqqlqkilsipQSSLEPLkaiiqyrlpmkknnnlyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPKGV 240
Cdd:cd05935 80 -----------GSELDDL----------------------------------------------ALIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 241 MLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGAlTYFAQADALKGTLVSTLKEVKPTVfigv 320
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLTPS-DVILACLPLFHVTGFVGSLNTAVYVGG-TYVLMARWDRETALELIEKYKVTF---- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 321 pqiWEKIHEMVKKNSAkSMGLKKKAFvwarnigfkvNSKKMLGKYNTPVSYRMAKtlvfsKVKTSLGLDHChsfisgtap 400
Cdd:cd05935 177 ---WTNIPTMLVDLLA-TPEFKTRDL----------SSLKVLTGGGAPMPPAVAE-----KLLKLTGLRFV--------- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 401 lnqetaefflsldipigELYGLSESSgPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI-------GEICLWGRHIFM 473
Cdd:cd05935 229 -----------------EGYGLTETM-SQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRelppnevGEIVVRGPQIFK 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574584718 474 GYLESETETTEA-IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:cd05935 291 GYWNRPEETEESfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKR-MINVSGFKVWPAEVEAKLYKH-PAI*EVCVIS 365
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
225-547 |
8.22e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 74.46 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNitwiAGAVTKDFKLTDKHETVVSYL---PLSHIaaqmmdiwvpikIGALTYFAQADAL 301
Cdd:PRK09088 138 SLILFTSGTSGQPKGVMLSERN----LQQTAHNFGVLGRVDAHSSFLcdaPMFHI------------IGLITSVRPVLAV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 302 KGT-LVSTLKEVKPTV------------FIGVPQIWEKIHemvkknsaksmglkkkafvwaRNIGFKVNSkkmlgkyntp 368
Cdd:PRK09088 202 GGSiLVSNGFEPKRTLgrlgdpalgithYFCVPQMAQAFR---------------------AQPGFDAAA---------- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 369 vsyrmaktlvfskvktslgLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSE-------SSGPHTISNqnnyRLLS 441
Cdd:PRK09088 251 -------------------LRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEagtvfgmSVDCDVIRA----KAGA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 442 CGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIL 516
Cdd:PRK09088 308 AGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF 387
|
330 340 350
....*....|....*....|....*....|.
gi 574584718 517 ITaGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PRK09088 388 IS-GGENVYPAEIEAVLADH-PGIRECAVVG 416
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
420-547 |
9.12e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.31 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 420 YGLSESSG-----P---HTISNQNNYRLLSCGKILTGcknMLFQ-QNKDG-------IGEICLWGRHIFMGYLESETETT 483
Cdd:PRK07470 312 FGLGEVTGnitvlPpalHDAEDGPDARIGTCGFERTG---MEVQiQDDEGrelppgeTGEICVIGPAVFAGYYNNPEANA 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574584718 484 EAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVEtlvkKKI---PIISNAMLVG 547
Cdd:PRK07470 389 KAFRD-GWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIE----EKLlthPAVSEVAVLG 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
206-512 |
1.27e-13 |
|
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: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 206 SIPDTQLEQVIESQKA-------NQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVtKDFKLTDkHETVVSYLPLSHIA 277
Cdd:cd05945 74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDNLvSFTNWML-SDFPLGP-GDVFLNQAPFSFDL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 278 AqMMDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIWEkihemvkknsaksMGLKKKAFvwarnigfk 355
Cdd:cd05945 152 S-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAA-------------MCLLSPTF--------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 356 vNSKKMlgkyntpvsyrmaKTLVfskvktslgldhcHSFISGTaPLNQETAEFFLSL--DIPIGELYGLSESSGP---HT 430
Cdd:cd05945 209 -TPESL-------------PSLR-------------HFLFCGE-VLPHKTARALQQRfpDARIYNTYGPTEATVAvtyIE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 431 ISNQ--NNYRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLG 498
Cdd:cd05945 261 VTPEvlDGYDRLPIGYAKPGAKLVIL--DEDGrpvppgeKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLV 338
|
330
....*....|....
gi 574584718 499 QLDGLGFLYVTGHI 512
Cdd:cd05945 339 RLEADGLLFYRGRL 352
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
207-547 |
1.32e-13 |
|
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: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 207 IPDTQLEQVIESQKAnqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSylplshiAAQMM----- 281
Cdd:cd05919 78 ARDCEARLVVTSADD--IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFS-------SAKMFfgygl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 282 --DIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWekihemvkKNSAKSMGLKKKAFVWARnigfkvnsk 359
Cdd:cd05919 149 gnSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFY--------ANLLDSCAGSPDALRSLR--------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 360 kmlgkyntpvsyrmaktlvfskvktslgldHChsfISGTAPLNQETAEFFLS-LDIPIGELYGLSESSgpHT-ISNQ-NN 436
Cdd:cd05919 212 ------------------------------LC---VSAGEALPRGLGERWMEhFGGPILDGIGATEVG--HIfLSNRpGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 437 YRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESeTETTEAIDDEGWLHSGDLGQLDGLGFLYVT 509
Cdd:cd05919 257 WRLGSTGRPVPGYEIRLV--DEEGhtippgeEGDLLVRGPSAAVGYWNN-PEKSRATFNGGWYRTGDKFCRDADGWYTHA 333
|
330 340 350
....*....|....*....|....*....|....*...
gi 574584718 510 GHIKEILITaGGENVPPIPVETLVkKKIPIISNAMLVG 547
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, ... |
229-547 |
3.91e-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: 70.90 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 229 YTSGTTGIPKGVMLSHDniTWIAGAVT--KDFKLtDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGtlV 306
Cdd:cd17633 7 FTSGTTGLPKAYYRSER--SWIESFVCneDLFNI-SGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSW--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 307 STLKEVKPTVFIGVPQiwekiheMVKknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSyrmaktlvfsKVKtsl 386
Cdd:cd17633 82 RKINQYNATVIYLVPT-------MLQ----------------------------ALARTLEPES----------KIK--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 387 gldhchSFISGTAPLNQETAEFF--LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEI 464
Cdd:cd17633 114 ------SIFSSGQKLFESTKKKLknIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 465 CLWGRHIFMGYLESEtetteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNAM 544
Cdd:cd17633 188 FVKSEMVFSGYVRGG-----FSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVL-KAIPGIEEAI 260
|
...
gi 574584718 545 LVG 547
Cdd:cd17633 261 VVG 263
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
216-662 |
6.57e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 72.06 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 216 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTK-DFKLTDKHETVVSYLPLSHI-------AAQMMDIWVPI 287
Cdd:PTZ00342 298 IQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKhSIFKKYNPKTHLSYLPISHIyerviayLSFMLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 288 KIGALTYFAqadalkgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKK---KAFVWARNIGFKVNSKKMLGK 364
Cdd:PTZ00342 378 WSKDINYFS----------KDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRflvKKILSLRKSNNNGGFSKFLEG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 365 YnTPVSYRMAktlvfSKVKTSLGLdhchsFISGTAPLNQETA-EFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCG 443
Cdd:PTZ00342 448 I-THISSKIK-----DKVNPNLEV-----ILNGGGKLSPKIAeELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIG 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 444 KILtgCKNMLFQ-------QNKDGI--GEICLWGRHIFMGY-LESETeTTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK 513
Cdd:PTZ00342 517 GPI--SPNTKYKvrtwetyKATDTLpkGELLIKSDSIFSGYfLEKEQ-TKNAFTEDGYFKTGDIVQINKNGSLTFLDRSK 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 514 EILITAGGENvppIPVETL--VKKKIPIISNAMLVGDK-----LKFLSM--LLTLKC----EMNQMSG----EPLDKLNF 576
Cdd:PTZ00342 594 GLVKLSQGEY---IETDMLnnLYSQISFINFCVVYGDDsmdgpLAIISVdkYLLFKClkddNMLESTGinekNYLEKLTD 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 577 EAINfcrglgsqASTVTEIVKQQDPLVYKaiQQGINAVNqeAMNNAQRIEK-WvilekDFSIYggeLGPMMKLKRHFVAQ 655
Cdd:PTZ00342 671 ETIN--------NNIYVDYVKGKMLEVYK--KTNLNRYN--IINDIYLTSKvW-----DTNNY---LTPTFKVKRFYVFK 730
|
....*..
gi 574584718 656 KYKKQID 662
Cdd:PTZ00342 731 DYAFFID 737
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
225-547 |
8.16e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 71.39 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK---------LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGaltyf 295
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIAPLPLYHIYAFTANCMCMMVSG----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 296 aqadalkgtlvstlkevKPTVFIGVPQiweKIHEMVKKnsaksmgLKKKAFvwarnigfkvnsKKMLGkYNTPVSYRMA- 374
Cdd:PRK12492 285 -----------------NHNVLITNPR---DIPGFIKE-------LGKWRF------------SALLG-LNTLFVALMDh 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 375 ---KTLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgphTISNQNNY----RLLSCGKIL 446
Cdd:PRK12492 325 pgfKDLDFSALKLT---------NSGGTALVKATAERWEQLTgCTIVEGYGLTETS---PVASTNPYgelaRLGTVGIPV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 447 TGCKNMLFqqNKDGI-------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 519
Cdd:PRK12492 393 PGTALKVI--DDDGNelplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
|
330 340
....*....|....*....|....*...
gi 574584718 520 GGeNVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PRK12492 471 GF-NVYPNEIEDVVMAH-PKVANCAAIG 496
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
92-547 |
1.21e-12 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 70.87 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 92 KAAKSLIKLGLERFHGVGILGFNSAE----WFITA-VGAILagglcVGIYATNSAEVCQYVITHAKVNiLLVENDQQLQK 166
Cdd:PRK08008 49 RTANLFYSLGIRKGDKVALHLDNCPEfifcWFGLAkIGAIM-----VPINARLLREESAWILQNSQAS-LLVTSAQFYPM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 167 ILSIPQSSLEPLKAIIQYRLPMKKNNNLYswdDFMELGRSIPDTQLEQVIESqkANQCAVLIYTSGTTGIPKGVMLSHDN 246
Cdd:PRK08008 123 YRQIQQEDATPLRHICLTRVALPADDGVS---SFTQLKAQQPATLCYAPPLS--TDDTAEILFTSGTTSRPKGVVITHYN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 247 I-------TWiAGAVTKDfkltDKHETVvsyLPLSHIAAQMMDIWVPIKIGAltyfaqadalkgTLVstlkevkptvfig 319
Cdd:PRK08008 198 LrfagyysAW-QCALRDD----DVYLTV---MPAFHIDCQCTAAMAAFSAGA------------TFV------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 320 vpqiwekiheMVKKNSAKsmglkkkAFvWarnigfkvnskKMLGKYNTPVSYRMA---KTLVFSKVkTSLGLDHCHSFIS 396
Cdd:PRK08008 245 ----------LLEKYSAR-------AF-W-----------GQVCKYRATITECIPmmiRTLMVQPP-SANDRQHCLREVM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 397 GTAPL-NQETAEFFLSLDIPIGELYGLSES-SGPHTISNQNNYRLLSCGKILTGCKNMLfqQNKDG-------IGEICLW 467
Cdd:PRK08008 295 FYLNLsDQEKDAFEERFGVRLLTSYGMTETiVGIIGDRPGDKRRWPSIGRPGFCYEAEI--RDDHNrplpageIGEICIK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 468 G---RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKiPIISNAM 544
Cdd:PRK08008 373 GvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR-RCNMIKRGGENVSCVELENIIATH-PKIQDIV 450
|
...
gi 574584718 545 LVG 547
Cdd:PRK08008 451 VVG 453
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
221-547 |
3.91e-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: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 221 ANQCAVLIYTSGTTGIPKGVMLSHdnitwiagavtkdfkltdkhetvvSYlPLSHIAAqmMDIWVPIKIGALtYFAQADA 300
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTH------------------------SY-PLGHIPT--AAYWLGLRPDDI-HWNIADP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 301 --LKGTLvSTLKEVkptVFIGVPQIwekIHEMVKKNSAKSMGLKKKafvwarnigFKVNSKkmlgkYNTPVSYRM-AKTL 377
Cdd:cd05972 132 gwAKGAW-SSFFGP---WLLGATVF---VYEGPRFDAERILELLER---------YGVTSF-----CGPPTAYRMlIKQD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 378 VFSKVKTSLgldhcHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSEssgphTISNQNNYRLL-----SCGKILTGCKN 451
Cdd:cd05972 191 LSSYKFSHL-----RLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTE-----TGLTVGNFPDMpvkpgSMGRPTPGYDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 452 MLFQQNKDGI-----GEICL-WGRH-IFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENV 524
Cdd:cd05972 261 AIIDDDGRELppgeeGDIAIkLPPPgLFLGYVGDPEKTEASIRG-DYYLTGDRAYRDEDGYFWFVGRADDI-IKSSGYRI 338
|
330 340
....*....|....*....|....
gi 574584718 525 PPIPVE-TLVKKkiPIISNAMLVG 547
Cdd:cd05972 339 GPFEVEsALLEH--PAVAEAAVVG 360
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
225-547 |
4.05e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 69.04 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAA-----QMMDIWVPIKIGALTYFaqaD 299
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGigsmlPGLLLGAPTVIYPLGAF---D 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 300 AlkGTLVSTLKEVKPTVFIGVPQIWEKIhemVKKNSAKSMGLKKKAFVWarnigfkvnskkmlgkyntpvsyrmaktlvf 379
Cdd:PRK07786 254 P--GQLLDVLEAEKVTGIFLVPAQWQAV---CAEQQARPRDLALRVLSW------------------------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 380 skvktslgldhchsfisGTAP----LNQETAEFFLslDIPIGELYGLSESSgPHT--ISNQNNYRLL-SCGKILTGCKNM 452
Cdd:PRK07786 298 -----------------GAAPasdtLLRQMAATFP--EAQILAAFGQTEMS-PVTcmLLGEDAIRKLgSVGKVIPTVAAR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 453 LFQQNKDG-----IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPI 527
Cdd:PRK07786 358 VVDENMNDvpvgeVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCA 435
|
330 340
....*....|....*....|
gi 574584718 528 PVETLVKKKiPIISNAMLVG 547
Cdd:PRK07786 436 EVENVLASH-PDIVEVAVIG 454
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
200-533 |
6.92e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 68.36 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 200 FMELGRSIPDTqLEQVieSQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPL------ 273
Cdd:PRK07514 137 LLEAAAAAPDD-FETV--PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPD-DVLIHALPIfhthgl 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 274 ---SHIA----AQMmdIWVPiKIGA---LTYFAQAdalkgtlvstlkevkpTVFIGVPQIWEKI--HEMVKKNSAKSMGL 341
Cdd:PRK07514 213 fvaTNVAllagASM--IFLP-KFDPdavLALMPRA----------------TVMMGVPTFYTRLlqEPRLTREAAAHMRL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 342 kkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvfskvktslgldhchsFISGTAPLNQET-AEFFLSLDIPIGELY 420
Cdd:PRK07514 274 ----------------------------------------------------FISGSAPLLAEThREFQERTGHAILERY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 421 GLSEssgphTISNQNN-Y------------------RLLSC--GKILTgcknmlfqqnKDGIGEICLWGRHIFMGYLESE 479
Cdd:PRK07514 302 GMTE-----TNMNTSNpYdgerragtvgfplpgvslRVTDPetGAELP----------PGEIGMIEVKGPNVFKGYWRMP 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 574584718 480 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 533
Cdd:PRK07514 367 EKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEGEI 419
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
216-538 |
7.36e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 68.80 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 216 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHiaaqmmdiwvpikigaltyf 295
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNL-RNDDVILSSLPFFH-------------------- 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 296 aqADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMgLKKKAF--VWARNIgfKVNsKKMLGkyntpvSYRM 373
Cdd:PRK08633 835 --SFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATIL-LGTPTFlrLYLRNK--KLH-PLMFA------SLRL 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 374 AktlvfskvktslgldhchsfISGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQNnyRLLSCGKILTGCKN- 451
Cdd:PRK08633 903 V--------------------VAGAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVNLPD--VLAADFKRQTGSKEg 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 452 ----------------MLFQQNKDGI-GEICLWGRHIFMGYLESETETTEAI---DDEGWLHSGDLGQLDGLGFLYVTGH 511
Cdd:PRK08633 961 svgmplpgvavrivdpETFEELPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
330 340 350
....*....|....*....|....*....|
gi 574584718 512 IK---EIlitaGGENVPPIPVETLVKKKIP 538
Cdd:PRK08633 1041 YSrfaKI----GGEMVPLGAVEEELAKALG 1066
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
81-324 |
1.03e-11 |
|
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: 67.78 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEn 160
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 161 dQQLQKILSIPQSSLEPLKAIiqyrlpMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGV 240
Cdd:cd05959 109 -GELAPVLAAALTKSEHTLVV------LIVSGGAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 241 MLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGV 320
Cdd:cd05959 182 VHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRPTVFFGV 261
|
....
gi 574584718 321 PQIW 324
Cdd:cd05959 262 PTLY 265
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
225-521 |
1.13e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 67.32 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIG---------ALTYF 295
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD-DVLVHGLPLFHVHGLVLGVLGPLRIGnrfvhtgrpTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 296 AQADALKGTLvstlkevkptvFIGVPQIWEKIHEmvKKNSAKSMglkkkafvwarnigfkvnskkmlgkyntpvsyRMAK 375
Cdd:PRK07787 210 AQALSEGGTL-----------YFGVPTVWSRIAA--DPEAARAL--------------------------------RGAR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 376 TLVfskvktslgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGLSES--------SGPHtisnqnnyRLLSCGKIL 446
Cdd:PRK07787 245 LLV-----------------SGSAALPVPVFDRLAALTgHRPVERYGMTETlitlstraDGER--------RPGWVGLPL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 447 TGCKNMLFQQN-----KDG--IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 519
Cdd:PRK07787 300 AGVETRLVDEDggpvpHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKS 379
|
..
gi 574584718 520 GG 521
Cdd:PRK07787 380 GG 381
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
208-339 |
3.18e-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: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 208 PDTQLEQVIESQKA-------NQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAqM 280
Cdd:cd05930 72 PAERLAYILEDSGAklvltdpDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLT-PGDRVLQFTSFSFDVS-V 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574584718 281 MDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSM 339
Cdd:cd05930 150 WEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL 210
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
225-547 |
4.56e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 65.83 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADALkg 303
Cdd:PRK06178 212 AALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGAtLVLLARWDAV-- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 304 TLVSTLKEVKPTVFIG-VPQIWEKI-HEMVKKNSAKSmgLKKK---AFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTlv 378
Cdd:PRK06178 290 AFMAAVERYRVTRTVMlVDNAVELMdHPRFAEYDLSS--LRQVrvvSFVKKLNPDYRQRWRALTGSVLAEAAWGMTET-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 379 fskvktslgldH-CHSFISG--TAPLNQETAEFFLSLDIPIGELYGLSESSGphtisnqnnyRLLSCGkiltgcknmlfq 455
Cdd:PRK06178 366 -----------HtCDTFTAGfqDDDFDLLSQPVFVGLPVPGTEFKICDFETG----------ELLPLG------------ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 456 qnkdGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAgGENVPPIPVETLVKK 535
Cdd:PRK06178 413 ----AEGEIVVRTPSLLKGYWNKPEATAEALRD-GWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQ 486
|
330
....*....|..
gi 574584718 536 KiPIISNAMLVG 547
Cdd:PRK06178 487 H-PAVLGSAVVG 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
225-533 |
6.17e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 65.43 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNI--------TWIAGAVTKdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALtyfa 296
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWLQPAFEK--KPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGR---- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 297 qadalkgtlvstlkevkpTVFIGVPQiweKIHEMVKKnsaksmgLKKKAFvwarNIGFKVNSkkmlgKYNTPVSYRMAKT 376
Cdd:PRK07059 281 ------------------NILIPNPR---DIPGFIKE-------LKKYQV----HIFPAVNT-----LYNALLNNPDFDK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 377 LVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGELYGLSESSgPHTISNQNNyrllscGKILTGCKNM--- 452
Cdd:PRK07059 324 LDFSKLIVANG---------GGMAVQRPVAERWLEMTgCPITEGYGLSETS-PVATCNPVD------ATEFSGTIGLplp 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 453 ---LFQQNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGE 522
Cdd:PRK07059 388 steVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKD-MILVSGF 466
|
330
....*....|.
gi 574584718 523 NVPPIPVETLV 533
Cdd:PRK07059 467 NVYPNEIEEVV 477
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
200-549 |
8.00e-11 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 64.86 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 200 FMELGRSIPDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTK----DFKLTDKHETVVSYLPLSH 275
Cdd:PLN02574 179 FYELIKEDFDFVPKPVIKQDDV---AAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEYPGSDNVYLAALPMFH 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 276 IAAQMMDIWVPIKIG-ALTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLKKKAfvwarnigf 354
Cdd:PLN02574 256 IYGLSLFVVGLLSLGsTIVVMRRFDA--SDMVKVIDRFKVTHFPVVPPIL--------------MALTKKA--------- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 355 kvnskkmlgkynTPVSYRMAKTLVfskvktslgldhchSFISGTAPLNQETAEFFLS----LDIPIGelYGLSESS--GP 428
Cdd:PLN02574 311 ------------KGVCGEVLKSLK--------------QVSCGAAPLSGKFIQDFVQtlphVDFIQG--YGMTESTavGT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 429 HTISNQNNYRLLSCG--------KIL---TGCknMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 497
Cdd:PLN02574 363 RGFNTEKLSKYSSVGllapnmqaKVVdwsTGC--LLPPGNC---GELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDI 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 574584718 498 GQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKIPIISNAML-VGDK 549
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEI-IKYKGFQIAPADLEAVLISHPEIIDAAVTaVPDK 489
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
81-533 |
8.72e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 64.95 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSaEWFITAVGAilAGGLCVGIYATNS-------AEVCQyvitHAKV 153
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNH-RGFVLALYA--AGKVGARIILLNTgfsgpqlAEVAA----REGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 154 NILLVenDQQLQKILSIPQSSLEPLKAIIQYRlpmkknnnlyswDDFMELGRSIPDtqLEQVIESQKAN-------QCAV 226
Cdd:PRK07788 148 KALVY--DDEFTDLLSALPPDLGRLRAWGGNP------------DDDEPSGSTDET--LDDLIAGSSTAplpkppkPGGI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 227 LIYTSGTTGIPKGVMLSHDNI-TWIAGAVTK-DFKltdKHETVVsylplshIAAQMMDIWvpikigALTYFAQADALKGT 304
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPEPSPlAPLAGLLSRvPFR---AGETTL-------LPAPMFHAT------GWAHLTLAMALGST 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 305 LV--------STLKEV---KPTVFIGVPQIwekIHEMVKKnsaksmglkkkafvwarnigfkvnSKKMLGKYNTPvSYRM 373
Cdd:PRK07788 276 VVlrrrfdpeATLEDIakhKATALVVVPVM---LSRILDL------------------------GPEVLAKYDTS-SLKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 374 AktlvfskvktslgldhchsFISG---TAPLNQETAEFFlsldipiGE----LYGLSESSGPhTISNQNNYRL--LSCGK 444
Cdd:PRK07788 328 I-------------------FVSGsalSPELATRALEAF-------GPvlynLYGSTEVAFA-TIATPEDLAEapGTVGR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 445 ILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYleSETETTEAIDdeGWLHSGDLGQLDGLGFLYVTGHIKEiLITA 519
Cdd:PRK07788 381 PPKGVTVKILDENGNEVprgvvGRIFVGNGFPFEGY--TDGRDKQIID--GLLSSGDVGYFDEDGLLFVDGRDDD-MIVS 455
|
490
....*....|....
gi 574584718 520 GGENVPPIPVETLV 533
Cdd:PRK07788 456 GGENVFPAEVEDLL 469
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
55-321 |
1.07e-10 |
|
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: 64.27 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 55 EFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVG 134
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 135 IYATNSAEVCQYVITHAKVNILLVendqqlqkilsipQSSLEPLKAIIQYRLPMKKNNnlyswddfmelGRSIPDTQLEQ 214
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLT-------------QSHLQPPIAFIGLIDLLDEDT-----------IYHEESENLEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 215 VIesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLShIAAQMMDIWVPIKIGA-LT 293
Cdd:cd17655 133 VS---KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQ-GEHLRVALFASIS-FDASVTEIFASLLSGNtLY 207
|
250 260
....*....|....*....|....*....
gi 574584718 294 YFAQADALKG-TLVSTLKEVKPTVFIGVP 321
Cdd:cd17655 208 IVRKETVLDGqALTQYIRQNRITIIDLTP 236
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
33-642 |
1.22e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 64.68 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 33 DGEVLLRlSKHGPGhETPMTIPEFFRESVNRFGTYPALASKNG--KKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGI 110
Cdd:PRK12582 33 DGSIVIK-SRHPLG-PYPRSIPHLLAKWAAEAPDRPWLAQREPghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 111 LGFNSAEWFITAVGAILAGGLCVGI---YATNSAEVCQ--YVITHAKVNILLVENDQQLQKILSIPQssLEPLKAIIQYR 185
Cdd:PRK12582 111 LSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDHAKlkHLFDLVKPRVVFAQSGAPFARALAALD--LLDVTVVHVTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 186 LPmkknnnlyswDD-----FMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSH----DNITWIAGavTK 256
Cdd:PRK12582 189 PG----------EGiasiaFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQrmmcANIAMQEQ--LR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 257 DFKLTDKHETVVSYLPLSHIAAQMMdIWVPIKIGALTYFAQAD----ALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVK 332
Cdd:PRK12582 257 PREPDPPPPVSLDWMPWNHTMGGNA-NFNGLLWGGGTLYIDDGkplpGMFEETIRNLREISPTVYGNVPAGYAMLAEAME 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 333 KNSAksmgLKKKAFvwaRNIGfkvnskkmlgkyntpvsyRMAktlvfskvktslgldhchsfiSGTAPLNQETAEFFLSL 412
Cdd:PRK12582 336 KDDA----LRRSFF---KNLR------------------LMA---------------------YGGATLSDDLYERMQAL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 413 -------DIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQqnkdgIG---EICLWGRHIFMGYLESETET 482
Cdd:PRK12582 370 avrttghRIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAP-----VGdkyEVRVKGPNVTPGYHKDPELT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 483 TEAIDDEGWLHSGDLGQ-LD------GLGFlyvTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLS 554
Cdd:PRK12582 445 AAAFDEEGFYRLGDAARfVDpddpekGLIF---DGRVAEDFKLSTGTWVSVGTLRPdAVAACSPVIHDAVVAGQDRAFIG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 555 MLLtlkcemnqmsgepldklnFEAINFCRGLGSQASTVTEIVKqQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKD 634
Cdd:PRK12582 522 LLA------------------WPNPAACRQLAGDPDAAPEDVV-KHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEP 582
|
....*...
gi 574584718 635 FSIYGGEL 642
Cdd:PRK12582 583 PSIDAGEI 590
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
199-589 |
1.45e-10 |
|
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: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 199 DFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDFKLTDKHETVVSylPlSHI 276
Cdd:cd05969 66 DRLENSEAKVLITTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIfyYFTGKYVLDLHPDDIYWCTAD--P-GWV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 277 AAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVfigvpqiwekihemvkknsaksmglkkkafvWarnigfkv 356
Cdd:cd05969 143 TGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTV-------------------------------W-------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 357 nskkmlgkYNTPVSYRMAKTLVFSKVKtSLGLDHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESsGPHTISNQ- 434
Cdd:cd05969 184 --------YTAPTAIRMLMKEGDELAR-KYDLSSLRFIHSVGEPLNPEAIRWGMEvFGVPIHDTWWQTET-GSIMIANYp 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 435 -NNYRLLSCGKILTGCKNMLFQQNKDGI-----GEICL---WGRhIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGF 505
Cdd:cd05969 254 cMPIKPGSMGKPLPGVKAAVVDENGNELppgtkGILALkpgWPS-MFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 506 LYVTGHIKEILITAgGENVPPIPVETLVKKKiPIISNAMLVG--DKLK--FLSMLLTLKcemnqmSG-EPLDKLNFEAIN 580
Cdd:cd05969 332 FWFVGRADDIIKTS-GHRVGPFEVESALMEH-PAVAEAGVIGkpDPLRgeIIKAFISLK------EGfEPSDELKEEIIN 403
|
410
....*....|
gi 574584718 581 FCR-GLGSQA 589
Cdd:cd05969 404 FVRqKLGAHV 413
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
108-325 |
1.64e-10 |
|
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: 63.44 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 108 VGILGFNSAeWFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQLQkilsiPQSSLEPLKAIIqyrl 186
Cdd:TIGR01733 28 VAVLLERSA-ELVVAILAVLkAGAAYVPLDPAYPAERLAFILEDAGARLLLT--DSALA-----SRLAGLVLPVIL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 187 pmkknnnlyswDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDkhE 265
Cdd:TIGR01733 96 -----------LDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLvNLLAWLARRYGLDPD--D 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584718 266 TVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKGTLVST---LKEVKPTVFIGVPQIWE 325
Cdd:TIGR01733 163 RVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERDDAALLaalIAEHPVTVLNLTPSLLA 224
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
225-540 |
3.93e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.84 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSH----DNITWIAGAVtkdfKLTDKHETVVSYLPLSHIAAQMMdIWVPikigaltyfaqadA 300
Cdd:PRK12476 196 SHLQYTSGSTRPPVGVEITHravgTNLVQMILSI----DLLDRNTHGVSWLPLYHDMGLSM-IGFP-------------A 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 301 LKG---TLVStlkevkPTVFIGVPQIWekIHEMVKKNSAKSM--GLKKKAFVWARNIGFKVN------SKKMLGKYNTPV 369
Cdd:PRK12476 258 VYGghsTLMS------PTAFVRRPQRW--IKALSEGSRTGRVvtAAPNFAYEWAAQRGLPAEgddidlSNVVLIIGSEPV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 370 SyrMAKTLVFSK-----------VKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTISNqnnyr 438
Cdd:PRK12476 330 S--IDAVTTFNKafapyglprtaFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADA-PNAVAH----- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 439 lLSCGKIL-----------TGCknmlfqQNKDG-IGEICLWGRHIFMGYLE--SETETT----------------EAIDD 488
Cdd:PRK12476 402 -VSCGQVArsqwavivdpdTGA------ELPDGeVGEIWLHGDNIGRGYWGrpEETERTfgaklqsrlaegshadGAADD 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 574584718 489 EGWLHSGDLG-QLDGLgfLYVTGHIKEiLITAGGENVPPIPVETLVKKKIPII 540
Cdd:PRK12476 475 GTWLRTGDLGvYLDGE--LYITGRIAD-LIVIDGRNHYPQDIEATVAEASPMV 524
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
225-642 |
4.01e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.97 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-LTDKHETVVSYLPLSHIaaqmmdiwvpikIGALTYFAQADALKG 303
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfLAEEPPVLVDWLPWNHT------------FGGNHNLGIVLYNGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 304 TL---------------VSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkkafvwarnigfkvnskkmlgkyntp 368
Cdd:PRK08180 280 TLyiddgkptpggfdetLRNLREISPTVYFNVPKGWEMLVPALERDAA-------------------------------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 369 vsyrMAKTLvFSKVKtslgldhchSFISGTAPLNQETAEfflSLD----------IPIGELYGLSESSGPHTISNQNNYR 438
Cdd:PRK08180 328 ----LRRRF-FSRLK---------LLFYAGAALSQDVWD---RLDrvaeatcgerIRMMTGLGMTETAPSATFTTGPLSR 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 439 LLSCGKILTGCKNMLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL-D----GLGFLYvTGHIK 513
Cdd:PRK08180 391 AGNIGLPAPGCEVKLVPV--GGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDpadpERGLMF-DGRIA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 514 EILITAGGE--NVPPIPVEtLVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGLGSQAST 591
Cdd:PRK08180 468 EDFKLSSGTwvSVGPLRAR-AVSAGAPLVQDVVITGHDRDEIGLLV------------------FPNLDACRRLAGLLAD 528
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 574584718 592 VTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 642
Cdd:PRK08180 529 ASLAEVLAHPAVRAAFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEI 579
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
83-600 |
4.08e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 62.83 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 83 FNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDq 162
Cdd:cd05915 27 YAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 163 qlqkILSIPQSSLEPLKAIIQYRLPMKKNNNlysWDDFMELGRsiPDTQleqviESQKANQC--AVLIYTSGTTGIPKGV 240
Cdd:cd05915 106 ----LLPLVEAIRGELKTVQHFVVMDEKAPE---GYLAYEEAL--GEEA-----DPVRVPERaaCGMAYTTGTTGLPKGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 241 MLSHDNITWIAGAVTKDFKLTDKHETV-VSYLPLSHIAAQMMdIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIG 319
Cdd:cd05915 172 VYSHRALVLHSLAASLVDGTALSEKDVvLPVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 320 VPQIWEKIhemvkKNSAKSMglkKKAFVWARNIgfkvnskkMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFisGTA 399
Cdd:cd05915 251 VPTVWLAL-----ADYLEST---GHRLKTLRRL--------VVGGSAAPRSLIARFERMGVEVRQGYGLTETSPV--VVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 400 PLNQETAEfflslDIPIGELYGLSESSGPHTISNQNNyrllscgkiLTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESE 479
Cdd:cd05915 313 NFVKSHLE-----SLSEEEKLTLKAKTGLPIPLVRLR---------VADEEGRPVPKDGKALGEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 480 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG--DKLKFLSMLL 557
Cdd:cd05915 379 EATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL-IKSGGEWISSVDLENALMGH-PKVKEAAVVAipHPKWQERPLA 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 574584718 558 TLKCEMNQMSGEpldklnfEAINFC-RGLGSQASTVTEIVKQQD 600
Cdd:cd05915 457 VVVPRGEKPTPE-------ELNEHLlKAGFAKWQLPDAYVFAEE 493
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
82-547 |
7.31e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.08 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 82 NFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVenD 161
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT--D 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 162 QQLQKILSIPQSSLEPLKAIIQY----RLPMKKNNNLYSWDDFMELGRSipDTQLEQVIESQKANQCavliYTSGTTGIP 237
Cdd:PRK06018 119 LTFVPILEKIADKLPSVERYVVLtdaaHMPQTTLKNAVAYEEWIAEADG--DFAWKTFDENTAAGMC----YTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 238 KGVMLSH-DNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPiKIGALTYFAQADALKGTLVSTLKEVKPTV 316
Cdd:PRK06018 193 KGVLYSHrSNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVMPGAKLDGASVYELLDTEKVTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 317 FIGVPQIWEKIHEMVKKNSAKSMGLKKKAfvwarnIGFKVNSKKMLG---KYNTPV--SYRMAKTlvfSKVKTSLGLDHC 391
Cdd:PRK06018 272 TAGVPTVWLMLLQYMEKEGLKLPHLKMVV------CGGSAMPRSMIKafeDMGVEVrhAWGMTEM---SPLGTLAALKPP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 392 HSFISGTAPLN----QETAEFFLSLDipigelyglsessgphtISNQNNYRLLSCGKILtgcknmlfqqnkdgiGEICLW 467
Cdd:PRK06018 343 FSKLPGDARLDvlqkQGYPPFGVEMK-----------------ITDDAGKELPWDGKTF---------------GRLKVR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 468 GRHIFMGYLESETETteaIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PRK06018 391 GPAVAAAYYRVDGEI---LDDDGFFDTGDVATIDAYGYMRITDRSKDV-IKSGGEWISSIDLENLAVGH-PKVAEAAVIG 465
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
461-547 |
8.08e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 61.61 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 461 IGEICLWGRHIFMGYLESETETteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKiPII 540
Cdd:PRK13295 392 IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEIEALLYRH-PAI 467
|
....*..
gi 574584718 541 SNAMLVG 547
Cdd:PRK13295 468 AQVAIVA 474
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
85-533 |
1.35e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 61.01 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 85 QYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL--CVGIYAtnSAEVCQYVITHAKVNILLVEN-- 160
Cdd:PLN02479 50 QTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVvnCVNIRL--NAPTIAFLLEHSKSEVVMVDQef 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 161 ----DQQLQKILSIPQSSLEPLKAII-----------QYRLpmkkNNNLYSWDDFMELGRsiPDTQLEQvieSQKANQCA 225
Cdd:PLN02479 128 ftlaEEALKILAEKKKSSFKPPLLIVigdptcdpkslQYAL----GKGAIEYEKFLETGD--PEFAWKP---PADEWQSI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 226 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAqmmdiWVpikigaltYFAQADALKGTL 305
Cdd:PLN02479 199 ALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEG-AVYLWTLPMFHCNG-----WC--------FTWTLAALCGTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 306 VStLKEVKPTvfigvpqiweKIHEMVKKNSAKSMGlkkKAFVWARNIgfkvnskkmlgkYNTPVSyrmaktlvfskvKTS 385
Cdd:PLN02479 265 IC-LRQVTAK----------AIYSAIANYGVTHFC---AAPVVLNTI------------VNAPKS------------ETI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 386 LGLDH-CHSFISGTAPlnqeTAEFFLSLDIP---IGELYGLSESSGPHTISN----------QNNYRLLSCGKI----LT 447
Cdd:PLN02479 307 LPLPRvVHVMTAGAAP----PPSVLFAMSEKgfrVTHTYGLSETYGPSTVCAwkpewdslppEEQARLNARQGVryigLE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 448 GCKNMLFQQNK----DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGG 521
Cdd:PLN02479 383 GLDVVDTKTMKpvpaDGktMGEIVMRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GG 460
|
490
....*....|..
gi 574584718 522 ENVPPIPVETLV 533
Cdd:PLN02479 461 ENISSLEVENVV 472
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
55-291 |
5.10e-09 |
|
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: 59.14 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 55 EFFRESVNRFGTYPALASKNGKkweiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAIL-AGGLCV 133
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRS----LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPE-LVVALLAVLkAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 134 GIYATNSAEVCQYVITHAKVNILLVENdqqlqkilSIPQSSLEPLKAIIQYRLPMKKnnnlyswddfmelgrsiPDTQLE 213
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTDR--------SLAGRAGGLEVAVVIDEALDAG-----------------PAGNPA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584718 214 QVIEsqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVtkDFKLTDKHETVVSYLPLSHIAAqMMDIWVPIKIGA 291
Cdd:cd12117 131 VPVS---PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT--NYVTLGPDDRVLQTSPLAFDAS-TFEIWGALLNGA 202
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
459-530 |
5.21e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 59.19 E-value: 5.21e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584718 459 DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK08162 384 DGetIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVE 455
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
209-520 |
9.08e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 58.42 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 209 DTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFkLTDKHE------TVVSYLPLSHIAAQMMD 282
Cdd:PRK05850 147 DSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY-FGDTGGvpppdtTVVSWLPFYHDMGLVLG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 283 IWVPIKIGALTYfaqadalkgtLVStlkevkPTVFIGVPQIWekIHeMVKKNSAksmglkkkAFVWARNIGFKVNSKK-- 360
Cdd:PRK05850 226 VCAPILGGCPAV----------LTS------PVAFLQRPARW--MQ-LLASNPH--------AFSAAPNFAFELAVRKts 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 361 ---MLGkyntpvsyrmaktlvfskvktsLGLDHCHSFISGTAPLNQET--------AEFFLSlDIPIGELYGLSE----- 424
Cdd:PRK05850 279 dddMAG----------------------LDLGGVLGIISGSERVHPATlkrfadrfAPFNLR-ETAIRPSYGLAEatvyv 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 425 -----SSGPHTIS---------------NQNNYRLLSCG-------KILTGCKNMlfqQNKDG-IGEICLWGRHIFMGYL 476
Cdd:PRK05850 336 atrepGQPPESVRfdyeklsaghakrceTGGGTPLVSYGsprsptvRIVDPDTCI---ECPAGtVGEIWVHGDNVAAGYW 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 574584718 477 E--SETETT--EAIDD------EG-WLHSGDLGQLDGlGFLYVTGHIKEILITAG 520
Cdd:PRK05850 413 QkpEETERTfgATLVDpspgtpEGpWLRTGDLGFISE-GELFIVGRIKDLLIVDG 466
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
99-547 |
2.12e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 57.28 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 99 KLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITH--AKVNILLVE---------NDQQLQKI 167
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDsgARVAIVGSElapkvapavGNLRLRHV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 168 LS------IPQSSLEPLKAIIQYR--LPMKKNNNLYSWDDFMELGRSIPDTQLeqviesqKANQCAVLIYTSGTTGIPKG 239
Cdd:PRK08314 135 IVaqysdyLPAEPEIAVPAWLRAEppLQALAPGGVVAWKEALAAGLAPPPHTA-------GPDDLAVLPYTSGTTGVPKG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 240 VMLSHDNItwIAGAVTKDFKLTDKHETVV-SYLPLSHIAAQMMDIWVPIKIGA-LTYFAQAD-ALKGTLVSTLkevKPTV 316
Cdd:PRK08314 208 CMHTHRTV--MANAVGSVLWSNSTPESVVlAVLPLFHVTGMVHSMNAPIYAGAtVVLMPRWDrEAAARLIERY---RVTH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 317 figvpqiWEKIHEMVkknsaksmglkkkafvwarnIGFKVNSKkmLGKYNtpvsyrmaktlvFSKVKTSLGldhchsfis 396
Cdd:PRK08314 283 -------WTNIPTMV--------------------VDFLASPG--LAERD------------LSSLRYIGG--------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 397 GTAPLNQETAEFFLSL-DIPIGELYGLSESSGPhTISNQNNYRLLSCGKILTgcknmlfqQNKDG--------------- 460
Cdd:PRK08314 313 GGAAMPEAVAERLKELtGLDYVEGYGLTETMAQ-THSNPPDRPKLQCLGIPT--------FGVDArvidpetleelppge 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 461 IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKi 537
Cdd:PRK08314 384 VGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKR-MINASGFKVWPAEVENLLYKH- 461
|
490
....*....|
gi 574584718 538 PIISNAMLVG 547
Cdd:PRK08314 462 PAIQEACVIA 471
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
80-533 |
4.22e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 56.36 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 80 ILNFNQYYEACRKAAKSLIKLGLERfhgVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVE 159
Cdd:PRK06334 45 KLSYNQVRKAVIALATKVSKYPDQH---IGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 160 ndQQLQKILSIPQSSLEPLKAIIQYRLPMKKNnnlYSWDDFMELG--RSIPDTQLEQV--IESQKANQCAVLIYTSGTTG 235
Cdd:PRK06334 122 --KQLMQHLAQTHGEDAEYPFSLIYMEEVRKE---LSFWEKCRIGiyMSIPFEWLMRWfgVSDKDPEDVAVILFTSGTEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 236 IPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPT 315
Cdd:PRK06334 197 LPKGVPLTHANLLANQRACLKFFSPKED-DVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 316 VFIGVPQIWEKIHEMVKKNSAKSMGLKkkaFVWARNIGFKvnskkmlgkyntpvsyrmaktlvfskvktslgldhcHSfi 395
Cdd:PRK06334 276 FLGSTPVFFDYILKTAKKQESCLPSLR---FVVIGGDAFK------------------------------------DS-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 396 sgtapLNQETAEFFLSLDIPIGelYGLSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQQ------NKDGIGEICLWG 468
Cdd:PRK06334 315 -----LYQEALKTFPHIQLRQG--YGTTECSPVITINTVNSPKHESCvGMPIRGMDVLIVSEetkvpvSSGETGLVLTRG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574584718 469 RHIFMGYL-ESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLV 533
Cdd:PRK06334 388 TSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSR-FVKIGAEMVSLEALESIL 452
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
79-248 |
4.50e-08 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 55.94 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 79 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILL 157
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAE-MIVGILGILkAGGAFVPIDPEYPEERRIYIMLDSGVRVVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 158 VENDQQlqkilsipqSSLEPLKAIIqyrlpmkknnnLYSWDDfmelgrsIPDTQLEQVIESQKANQCAVLIYTSGTTGIP 237
Cdd:cd17656 91 TQRHLK---------SKLSFNKSTI-----------LLEDPS-------ISQEDTSNIDYINNSDDLLYIIYTSGTTGKP 143
|
170
....*....|.
gi 574584718 238 KGVMLSHDNIT 248
Cdd:cd17656 144 KGVQLEHKNMV 154
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
79-520 |
5.60e-08 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 55.89 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 79 EILNFNQYYEACRKAAKSLIKLGLERfhG--VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNIL 156
Cdd:COG0365 38 RTLTYAELRREVNRFANALRALGVKK--GdrVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 157 LVENDQ-------QLQKILSIPQSSLEPLKAIIQYRLPMKKNN--NLYSWDDFMELGRSIPDTqleqviESQKANQCAVL 227
Cdd:COG0365 116 ITADGGlrggkviDLKEKVDEALEELPSLEHVIVVGRTGADVPmeGDLDWDELLAAASAEFEP------EPTDADDPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 228 IYTSGTTGIPKGVMLSHdniTWIAGAVTKDFKLT-DKHE-------------TVVSYL---PLSHIAAQ-MMDiwvpiki 289
Cdd:COG0365 190 LYTSGTTGKPKGVVHTH---GGYLVHAATTAKYVlDLKPgdvfwctadigwaTGHSYIvygPLLNGATVvLYE------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 290 GALTYfaqADAlkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLKKKAFVWARnigfkvnskkmlgKYNtpv 369
Cdd:COG0365 260 GRPDF---PDP--GRLWELIEKYGVTVFFTAPTAI--------------RALMKAGDEPLK-------------KYD--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 370 syrmaktlvFSKVKtslgldHChsfisGTA--PLNQETAEFFLS-LDIPIGELYGLSESSGpHTISnqnNYRLL-----S 441
Cdd:COG0365 305 ---------LSSLR------LL-----GSAgePLNPEVWEWWYEaVGVPIVDGWGQTETGG-IFIS---NLPGLpvkpgS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 442 CGKILTGCKNMLFqqNKDG-------IGEICL---W-GrhIFMGYLESETETTEAI--DDEGWLHSGDLGQLDGLGFLYV 508
Cdd:COG0365 361 MGKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWI 436
|
490
....*....|..
gi 574584718 509 TGHIKEILITAG 520
Cdd:COG0365 437 LGRSDDVINVSG 448
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
90-547 |
7.87e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 55.52 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 90 CRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYAT-NSAEVcQYVITHAKVNILLVE---NDQQLQ 165
Cdd:PRK06164 45 VDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRyRSHEV-AHILGRGRARWLVVWpgfKGIDFA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 166 KILS-IPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSH 244
Cdd:PRK06164 124 AILAaVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 245 DNITWIAGAVTKDFKLTDKHETVVSyLPLShiaaqmmdiwvpikiGALTYFAQADALKGtlvstlkevkptvfiGVPQIW 324
Cdd:PRK06164 204 ATLLRHARAIARAYGYDPGAVLLAA-LPFC---------------GVFGFSTLLGALAG---------------GAPLVC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 325 EKIHEMVKknSAKSMGLKKKAFVWARNIGFKvnskKMLGKYNTPVSYRMAKTLVFSkvktslgldhchSFISGTAplnqE 404
Cdd:PRK06164 253 EPVFDAAR--TARALRRHRVTHTFGNDEMLR----RILDTAGERADFPSARLFGFA------------SFAPALG----E 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 405 TAEFFLSLDIPIGELYGLSE-----SSGPHTISNQnnYRLLSCGKILTGCKNMLFQQNKDG-------IGEICLWGRHIF 472
Cdd:PRK06164 311 LAALARARGVPLTGLYGSSEvqalvALQPATDPVS--VRIEGGGRPASPEARVRARDPQDGallpdgeSGEIEIRAPSLM 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584718 473 MGYLESETETTEAIDDEGWLHSGDLGQLDGLG-FLYVT--GHIkeilITAGGENVPPIPVETLVkKKIPIISNAMLVG 547
Cdd:PRK06164 389 RGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQTrmGDS----LRLGGFLVNPAEIEHAL-EALPGVAAAQVVG 461
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
225-533 |
8.11e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 55.74 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTK-DFKLTDKhetVVSYLPLSHiaaqmmdiwvpiKIGaLTyfaqadalK 302
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLlANRAQVAARiDFSPEDK---VFNALPVFH------------SFG-LT--------G 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 303 GTLVSTLKEVkPTVFIGVPQIWEKIHEMVkknsaksmglkkkafvwarnigFKVNSKKMLG---------KYNTPVSYRM 373
Cdd:PRK06814 852 GLVLPLLSGV-KVFLYPSPLHYRIIPELI----------------------YDTNATILFGtdtflngyaRYAHPYDFRS 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 374 AKtLVFskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNM 452
Cdd:PRK06814 909 LR-YVF----------------AGAEKVKEETRQTWMEkFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYR 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 453 LfqQNKDGI---GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK---EIlitaGGENVPP 526
Cdd:PRK06814 972 L--EPVPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKrfaKI----AGEMISL 1045
|
....*..
gi 574584718 527 IPVETLV 533
Cdd:PRK06814 1046 AAVEELA 1052
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
91-530 |
8.28e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 55.48 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 91 RKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEndqqlqkilsi 170
Cdd:PRK07008 50 KQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD----------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 171 pqSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGrSIPDTQLEQVIESQKA---------NQCAVLIYTSGTTGIPKGVM 241
Cdd:PRK07008 119 --LTFLPLVDALAPQCPNVKGWVAMTDAAHLPAG-STPLLCYETLVGAQDGdydwprfdeNQASSLCYTSGTTGNPKGAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 242 LSHDNITWIA-GAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIkIGALTYFAqADALKGTLVSTLKEVKPTVF-IG 319
Cdd:PRK07008 196 YSHRSTVLHAyGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLP-GPDLDGKSLYELIEAERVTFsAG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 320 VPQIWEKIHEMVKKNSAKSMGLKkkafvwarnigfkvnsKKMLGKYNTPVSyrMAKTLvfskvKTSLGLDHCHSF-ISGT 398
Cdd:PRK07008 274 VPTVWLGLLNHMREAGLRFSTLR----------------RTVIGGSACPPA--MIRTF-----EDEYGVEVIHAWgMTEM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 399 APLNQETAEFFLSLDIPIGELYGLSESSGpHTIsnqnnyrllsCG---KILTGCKNMLfqqNKDGI--GEICLWGRHIFM 473
Cdd:PRK07008 331 SPLGTLCKLKWKHSQLPLDEQRKLLEKQG-RVI----------YGvdmKIVGDDGREL---PWDGKafGDLQVRGPWVID 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 574584718 474 GYLESETETTeaidDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVE 530
Cdd:PRK07008 397 RYFRGDASPL----VDGWFPTGDVATIDADGFMQITDRSKDV-IKSGGEWISSIDIE 448
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
416-547 |
9.55e-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: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 416 IGELYGLSESSGPHTISNQNnyrLL----SCGKILTGCKNMLfqqNKDG-------IGEICLWGRHIFMgYLESETETTE 484
Cdd:cd05929 272 IWEYYGGTEGQGLTIINGEE---WLthpgSVGRAVLGKVHIL---DEDGnevppgeIGEVYFANGPGFE-YTNDPEKTAA 344
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584718 485 AIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:cd05929 345 ARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAH-PKVLDAAVVG 405
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
43-325 |
1.13e-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: 55.25 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 43 HGPGHETP--MTIPEFFRESVNRFGTYPALASKNGKkweiLNfnqYYEACRKA---AKSLIKLGLERFHGVGILGFNSAE 117
Cdd:COG1020 466 NATAAPYPadATLHELFEAQAARTPDAVAVVFGDQS----LT---YAELNARAnrlAHHLRALGVGPGDLVGVCLERSLE 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 118 wFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQLQKILsiPQSSLEPLkaiiqyrlpmkknnnlyS 196
Cdd:COG1020 539 -MVVALLAVLkAGAAYVPLDPAYPAERLAYMLEDAGARLVLT--QSALAARL--PELGVPVL-----------------A 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 197 WDDfmELGRSIPDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI 276
Cdd:COG1020 597 LDA--LALAAEPATNPPVPVTPD---DLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGP-GDRVLQFASLSFD 670
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 574584718 277 AAqMMDIWVPIKIGALTYFAQADALKGT--LVSTLKEVKPTVFIGVPQIWE 325
Cdd:COG1020 671 AS-VWEIFGALLSGATLVLAPPEARRDPaaLAELLARHRVTVLNLTPSLLR 720
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
225-525 |
1.59e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 54.35 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHIAAQMMdIWVPIKIGAltYFaqadalkgT 304
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEG-QEGDRGVSWLPFFHDMGLIT-VLLPALLGH--YI--------T 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 305 LVStlkevkPTVFIGVPQIWekIHEMVKKNsaksmGLKKKAFVWARNIGFKVNSKKMLGKYNTPvsyrmaktlvfskvkt 384
Cdd:PRK07769 251 FMS------PAAFVRRPGRW--IRELARKP-----GGTGGTFSAAPNFAFEHAAARGLPKDGEP---------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 385 SLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-----SSGPHTISNQ---------NNYRLL--- 440
Cdd:PRK07769 302 PLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGlpptaikPSYGMAEatlfvSTTPMDEEPTviyvdrdelNAGRFVevp 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 441 ----------SCGKIL-----------TGcknmlfQQNKDG-IGEICLWGRHIFMGYLESETETTE-------------- 484
Cdd:PRK07769 382 adapnavaqvSAGKVGvsewavivdpeTA------SELPDGqIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlsesh 455
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 574584718 485 ---AIDDEGWLHSGDLGQ-LDglGFLYVTGHIKEILITAGGENVP 525
Cdd:PRK07769 456 aegAPDDALWVRTGDYGVyFD--GELYITGRVKDLVIIDGRNHYP 498
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
51-530 |
2.07e-07 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 53.99 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 51 MTIPEFFRESVNRFGTYPaLASKNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGG 130
Cdd:PRK06155 21 RTLPAMLARQAERYPDRP-LLVFGGTRW---TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 131 LCVGIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsipqsSLEPLKAIIQYRLPMKK-----NNNLYSWDDFMELGR 205
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAA------------LLAALEAADPGDLPLPAvwlldAPASVSVPAGWSTAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 206 SIPDTQLEQVIESQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMdiwv 285
Cdd:PRK06155 165 LPPLDAPAPAAAVQPGDTAAIL-YTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGAD-DVLYTTLPLFHTNALNA---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 286 pikigaltyFAQADALKGTLVSTlkevkptvfigvpqiwekihemvKKNSAKSMglkkkafvWARnigfkvnskkmLGKY 365
Cdd:PRK06155 239 ---------FFQALLAGATYVLE-----------------------PRFSASGF--------WPA-----------VRRH 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 366 NTPVSY---RMAKTLVFSKVKTSlglDHCHSFISGTAP--LNQETAEFFLSLDIPIGELYGLSESSGP--HTISNQnnyR 438
Cdd:PRK06155 268 GATVTYllgAMVSILLSQPARES---DRAHRVRVALGPgvPAALHAAFRERFGVDLLDGYGSTETNFViaVTHGSQ---R 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 439 LLSCGKILTGCKNMLFQQNKDGI-----GEICLWGR--HIFM-GYLESETETTEAIDDEgWLHSGDLGQLDGLGFLYVTG 510
Cdd:PRK06155 342 PGSMGRLAPGFEARVVDEHDQELpdgepGELLLRADepFAFAtGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVD 420
|
490 500
....*....|....*....|
gi 574584718 511 HIKEIlITAGGENVPPIPVE 530
Cdd:PRK06155 421 RIKDA-IRRRGENISSFEVE 439
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
223-547 |
2.53e-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: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 223 QCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDKHETVVSYLPLSHIaaqmmdiwvpikIGALTYFAQADAL 301
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAeSRVLFMSTQAGLRHGRHNVVLGLMPLYHV------------IGFFAVLVAALAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 302 KGTLVsTLKEVKPtvfigvpqiwekihemvkknsaksmglkKKAFVWarnigfkVNSKKMLGKYNTPVSYrmaKTLVFSK 381
Cdd:cd05923 219 DGTYV-VVEEFDP----------------------------ADALKL-------IEQERVTSLFATPTHL---DALAAAA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 382 VKTSLGLDHCHSFISGTAPLNQ---ETAEFFLSldIPIGELYGLSESSgpHTISNQN-------------NYRLLSCGki 445
Cdd:cd05923 260 EFAGLKLSSLRHVTFAGATMPDavlERVNQHLP--GEKVNIYGTTEAM--NSLYMRDartgtemrpgffsEVRIVRIG-- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 446 ltGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVP 525
Cdd:cd05923 334 --GSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQD-GWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIH 409
|
330 340
....*....|....*....|..
gi 574584718 526 PIPVETLVKKKiPIISNAMLVG 547
Cdd:cd05923 410 PSEIERVLSRH-PGVTEVVVIG 430
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
220-540 |
2.72e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 220 KANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL-TDKHETVVSYLPLSHiaaqmmDIWVpikIGALtyfaqa 298
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdLNPDDVIVSWLPLYH------DMGL---IGGL------ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 299 dalkgtlvstlkeVKPtVFIGVPQIwekihemvkknsaksmgLKKKAFVWARnigfKVNSKKMLGKYNTPVS------YR 372
Cdd:PRK05691 229 -------------LQP-IFSGVPCV-----------------LMSPAYFLER----PLRWLEAISEYGGTISggpdfaYR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 373 MAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESS----------GPHTIS--- 432
Cdd:PRK05691 274 LCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGfdpdsffASYGLAEATlfvsggrrgqGIPALElda 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 433 ---NQNNYR------LLSCGK------ILTGCKNMLFQQNKDGIGEICLWGRHIFMGYL---ESETETTEAIDDEGWLHS 494
Cdd:PRK05691 354 ealARNRAEpgtgsvLMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWrnpEASAKTFVEHDGRTWLRT 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 574584718 495 GDLGQLDGlGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIPII 540
Cdd:PRK05691 434 GDLGFLRD-GELFVTGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
146-522 |
2.99e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 53.63 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 146 YVITHAKVNILLVenDQQLQKILSIPQSSLEPLKAII--------QYRLPMKKNNNLYSWDDFMElGRSI----PDtqle 213
Cdd:PRK05620 105 HIINHAEDEVIVA--DPRLAEQLGEILKECPCVRAVVfigpsdadSAAAHMPEGIKVYSYEALLD-GRSTvydwPE---- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 214 qviesQKANQCAVLIYTSGTTGIPKGVMLSHDNItWIAGA---VTKDFKLTDKhETVVSYLPLSHIAAqmmdiW-VPIKI 289
Cdd:PRK05620 178 -----LDETTAAAICYSTGTTGAPKGVVYSHRSL-YLQSLslrTTDSLAVTHG-ESFLCCVPIYHVLS-----WgVPLAA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 290 ---GALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLkKKAFV------------WARNIGF 354
Cdd:PRK05620 246 fmsGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSL-QEIYVggsavppilikaWEERYGV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 355 KVNSkkmlgkyntpvSYRMAKTLVFSKVKtslgldHCHSFISGTAPLNqetaefflsldipigelYGLSESSGPHTIsnq 434
Cdd:PRK05620 325 DVVH-----------VWGMTETSPVGTVA------RPPSGVSGEARWA-----------------YRVSQGRFPASL--- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 435 nNYRLLSCGKILTGcknmlfqqNKDGIGEICLWGRHIFMGYLESETETT---------EAIDDE-------GWLHSGDLG 498
Cdd:PRK05620 368 -EYRIVNDGQVMES--------TDRNEGEIQVRGNWVTASYYHSPTEEGggaastfrgEDVEDAndrftadGWLRTGDVG 438
|
410 420
....*....|....*....|....
gi 574584718 499 QLDGLGFLYVTGHIKEIlITAGGE 522
Cdd:PRK05620 439 SVTRDGFLTIHDRARDV-IRSGGE 461
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
460-533 |
3.82e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.09 E-value: 3.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584718 460 GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEiLITAGGENVPPIPVETLV 533
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKD-LIIINGRNIWPQDIEWIA 480
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
227-547 |
4.22e-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: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 227 LIYTSGTTGIPKGVMLSHDNI-------TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDiwvpikiGALTYFAQAD 299
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmlmggADFGTGEFTPSEDAH-KAAAAAAGTVMFPAPPLMH-------GTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 300 ALKGTLVstlkeVKPTVFIGVPQIWEKIHEMvkknsaksmglkkkafvwarnigfKVNSKKMLGKyntpvsyRMAKTLV- 378
Cdd:cd05924 80 LLGGQTV-----VLPDDRFDPEEVWRTIEKH------------------------KVTSMTIVGD-------AMARPLId 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 379 -FSKVKTsLGLDHCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGPHTISNQNN------YRLLSCGKILTGC 449
Cdd:cd05924 124 aLRDAGP-YDLSSLFAISSGGALLSPEVKQGLLELvpNITLVDAFGSSETGFTGSGHSAGSgpetgpFTRANPDTVVLDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 450 KNMLFQQNKDGIGEICLWGrHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPP 526
Cdd:cd05924 203 DGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR-GSVCINTGGEKVFP 280
|
330 340
....*....|....*....|.
gi 574584718 527 IPVETLVKKKiPIISNAMLVG 547
Cdd:cd05924 281 EEVEEALKSH-PAVYDVLVVG 300
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
210-531 |
4.36e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.85 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 210 TQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHiaaqmmDIwvpiki 289
Cdd:PRK05851 140 TNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYH------DM------ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 290 gALTyFAQADALKGTlvsTLKEVKPTVFIGVPQIWekihemvkknsAKSMGLKKKAFVWARNIGFKvnskkMLGKYNTPV 369
Cdd:PRK05851 208 -GLA-FLLTAALAGA---PLWLAPTTAFSASPFRW-----------LSWLSDSRATLTAAPNFAYN-----LIGKYARRV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 370 SYRMAKTLVFSkvktslgldhchsfISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESSGPHTIS---------- 432
Cdd:PRK05851 267 SDVDLGALRVA--------------LNGGEPVDCDGFERFATAMAPFGfdagaaaPSYGLAESTCAVTVPvpgiglrvde 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 433 -----NQNNYRLLSCGKILTG------CKNMLFQQNKDGIGEICLWGRHIFMGYLESETetteaIDDEGWLHSGDLGQLd 501
Cdd:PRK05851 333 vttddGSGARRHAVLGNPIPGmevrisPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL- 406
|
330 340 350
....*....|....*....|....*....|
gi 574584718 502 GLGFLYVTGHIKEiLITAGGENVPPIPVET 531
Cdd:PRK05851 407 VDGGLVVCGRAKE-LITVAGRNIFPTEIER 435
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
458-547 |
5.91e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 52.47 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 458 KDGIGEICLWGRHIFMGYLeSETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKI 537
Cdd:PRK07638 330 KGEIGTVYVKSPQFFMGYI-IGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEH 406
|
90
....*....|
gi 574584718 538 PIISNAMLVG 547
Cdd:PRK07638 407 PAVDEIVVIG 416
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-291 |
8.75e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 57 FRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWfITAVGAIL-AGGLCVGI 135
Cdd:PRK12316 517 FEEQVERTPEAPALAFGE----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEM-VVALLAILkAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 136 YATNSAEVCQYVITHAKVNILLveNDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNlyswddfmelgrsiPDTQLEqv 215
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLL--SQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEEN--------------PGTELN-- 653
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574584718 216 iesqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLShIAAQMMDIWVPIKIGA 291
Cdd:PRK12316 654 -----PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGL-GVGDTVLQKTPFS-FDVSVWEFFWPLMSGA 722
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
412-533 |
1.49e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 51.15 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 412 LDIPIGELYGLSESSG------PHTISNQNNyrllSCGKILTGCKNMLFQQNkdgIGEICLWGRHIFMGYLEsetettEA 485
Cdd:PRK07445 253 LQLRLAPTYGMTETASqiatlkPDDFLAGNN----SSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QI 319
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 574584718 486 IDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 533
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
221-547 |
2.29e-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: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 221 ANQCAVLIYTSGTTGIPKGVMlsHdnitwiagavtkdfkltdKHETVVSYLPLSHIAAQMMDiwvpiKIGALtYFAQAD- 299
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGAL--H------------------AHRVLLGHLPGVQFPFNLFP-----RDGDL-YWTPADw 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 300 ALKGTLVSTLKevkPTVFIGVPQIwekIHEMVKKNSAKSMglkkkafvwarnigfkvnskKMLGKYN------TPVSYRM 373
Cdd:cd05971 141 AWIGGLLDVLL---PSLYFGVPVL---AHRMTKFDPKAAL--------------------DLMSRYGvttaflPPTALKM 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 374 AKtlvFSKVKTSLGLDHCHSFISGTAPLNQE-TAEFFLSLDIPIGELYGLSESSgpHTISNQNNY---RLLSCGKILTGC 449
Cdd:cd05971 195 MR---QQGEQLKHAQVKLRAIATGGESLGEElLGWAREQFGVEVNEFYGQTECN--LVIGNCSALfpiKPGSMGKPIPGH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 450 KNMLFQQN-----KDGIGEICLW--GRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGE 522
Cdd:cd05971 270 RVAIVDDNgtplpPGEVGEIAVElpDPVAFLGYWNNP-SATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV-ITSSGY 347
|
330 340
....*....|....*....|....*
gi 574584718 523 NVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:cd05971 348 RIGPAEIEECLLKH-PAVLMAAVVG 371
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
89-246 |
2.46e-06 |
|
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: 50.35 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 89 ACRKAAKsLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKIL 168
Cdd:cd12114 22 ARRVAGA-LKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDGPDAQLDVA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584718 169 sIPQSSLEPLKAIIQyrlpmkknnnlyswddfmelgrsiPDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDN 246
Cdd:cd12114 101 -VFDVLILDLDALAA------------------------PAPPPPVDVAPD---DLAYVIFTSGSTGTPKGVMISHRA 150
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
454-530 |
2.57e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 50.53 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584718 454 FQQNKDG-IGEICLWGRHIFMGYLESETETTEaiddEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 530
Cdd:PRK13382 383 FREVPTGeVGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFVVGRDDE-MIVSGGENVYPIEVE 455
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
48-278 |
3.28e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 50.26 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 48 ETPMTIPEFFRESVNRFGTYPALASkNGKKWEILNFNQYyeaCRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAIL 127
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPALLF-EDQSISYAELNAR---ANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 128 AGGlCVGIYATN-SAEVCQYVITHAKVNILLVENDQqLQKILSIPQsslEPLKAIIQYRLPMKKNNNLYSWDDFMELGRS 206
Cdd:PRK08279 110 LGA-VVALLNTQqRGAVLAHSLNLVDAKHLIVGEEL-VEAFEEARA---DLARPPRLWVAGGDTLDDPEGYEDLAAAAAG 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584718 207 IPDTQLEqVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT----WIAGavtkdfkLTDKHETVVSY--LPLSHIAA 278
Cdd:PRK08279 185 APTTNPA-SRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLkamgGFGG-------LLRLTPDDVLYccLPLYHNTG 254
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
214-262 |
3.35e-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: 3.35e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 574584718 214 QVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 262
Cdd:cd05918 98 KVVLTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTS 146
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
461-547 |
3.90e-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: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 461 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 540
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVENLL-LRHPAV 412
|
....*..
gi 574584718 541 SNAMLVG 547
Cdd:cd05920 413 HDAAVVA 419
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
461-547 |
4.07e-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: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 461 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPII 540
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-QINRGGEKIAAEEVENLLLAH-PAV 457
|
....*..
gi 574584718 541 SNAMLVG 547
Cdd:COG1021 458 HDAAVVA 464
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
202-547 |
4.53e-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: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 202 ELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQM- 280
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALg 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 281 MDIWVPikigALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEmvkknsaksmglkkkafvWARNIGFKVNSKK 360
Cdd:cd05910 145 LTSVIP----DMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVAR------------------YCAQHGITLPSLR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 361 MLGKYNTPVsyRMAKTLVFSK-------VKTSLGLDHC--------HSFISGTAPLNQETAEFFLSLDIPIGELYGLSES 425
Cdd:cd05910 203 RVLSAGAPV--PIALAARLRKmlsdeaeILTPYGATEAlpvssigsRELLATTTAATSGGAGTCVGRPIPGVRVRIIEID 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 426 SGPhtISNQNNYRLLSCGkiltgcknmlfqqnkdGIGEICLWGRHIFMGYLESETETTEA-IDDEG---WLHSGDLGQLD 501
Cdd:cd05910 281 DEP--IAEWDDTLELPRG----------------EIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLD 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 574584718 502 GLGFLYVTGHIKEILITAGGeNVPPIPVETlVKKKIPIISNAMLVG 547
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) ... |
225-261 |
4.59e-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: 4.59e-06
10 20 30
....*....|....*....|....*....|....*..
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 261
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG 132
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
178-291 |
5.77e-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: 49.21 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 178 LKAIIQYRLPMKKNNNLYSW--------DDFMELGRSIPDTQLEQVIESQKANQC----AVLIYTSGTTGIPKGVMLSHD 245
Cdd:cd05938 88 LQEAVEEVLPALRADGVSVWylshtsntEGVISLLDKVDAASDEPVPASLRAHVTikspALYIYTSGTTGLPKAARISHL 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 574584718 246 NItWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDIWVPIKIGA 291
Cdd:cd05938 168 RV-LQCSGFLSLCGVT-ADDVIYITLPLYHSSGFLLGIGGCIELGA 211
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
88-286 |
5.80e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 49.29 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 88 EACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEV---------CQYVITHAKVNILLv 158
Cdd:PRK07867 37 GSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAAlardiahadCQLVLTESAHAELL- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 159 enDQQLQKILSIPQSSLEPLKAIIQYRlpmkknnnlyswDDFMELGRSIPDTQLeqviesqkanqcaVLIYTSGTTGIPK 238
Cdd:PRK07867 116 --DGLDPGVRVINVDSPAWADELAAHR------------DAEPPFRVADPDDLF-------------MLIFTSGTSGDPK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 574584718 239 GVMLSHDNITWIAGAVTKDFKLTdkhETVVSYL--PLSHIAAQMMDiWVP 286
Cdd:PRK07867 169 AVRCTHRKVASAGVMLAQRFGLG---PDDVCYVsmPLFHSNAVMAG-WAV 214
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
220-248 |
8.42e-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: 8.42e-06
10 20
....*....|....*....|....*....
gi 574584718 220 KANQCAVLIYTSGTTGIPKGVMLSHDNIT 248
Cdd:cd17653 103 SPDDLAYIIFTSGSTGIPKGVMVPHRGVL 131
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
68-261 |
9.29e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 49.39 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 68 PALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 147
Cdd:PRK12467 529 PALVFGE----QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYM 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 148 ITHAKVNILLveNDQQLQKILSIPqssleplkaiiqyrlpmkknnnlyswDDFMELGRSIPDTQLEQVIE-----SQKAN 222
Cdd:PRK12467 605 LDDSGVRLLL--TQSHLLAQLPVP--------------------------AGLRSLCLDEPADLLCGYSGhnpevALDPD 656
|
170 180 190
....*....|....*....|....*....|....*....
gi 574584718 223 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 261
Cdd:PRK12467 657 NLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLA 695
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
228-283 |
1.11e-05 |
|
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: 1.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 574584718 228 IYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDI 283
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR-PEDVVYDCLPLYHSAGGIMGV 164
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
221-262 |
1.15e-05 |
|
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: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 574584718 221 ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 262
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNE 133
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
81-313 |
1.72e-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: 47.85 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEn 160
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 161 dqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsiPDtqleqviesqkanQCAVLIYTSGTTGIPKGV 240
Cdd:cd17650 92 -----------------------------------------------PE-------------DLAYVIYTSGTTGKPKGV 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584718 241 MLSHDNITWIAGAVTKDFKLTDKhetvvsylplSHIAAQMMDIWVPIKIGAltyFAQADALKGTLVSTLKEVK 313
Cdd:cd17650 112 MVEHRNVAHAAHAWRREYELDSF----------PVRLLQMASFSFDVFAGD---FARSLLNGGTLVICPDEVK 171
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
108-324 |
2.26e-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: 47.29 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 108 VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsipqsSLEPLKAIIqyrlp 187
Cdd:cd12116 40 VAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDA------------LPDRLPAGL----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 188 mkknnnlyswdDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT--DKHE 265
Cdd:cd12116 103 -----------PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGpgDRLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574584718 266 TVVSYlpLSHIAAqmMDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIW 324
Cdd:cd12116 172 AVTTY--AFDISL--LELLLPLLAGARVVIAPRETQRdpEALARLIEAHSITVMQATPATW 228
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
88-287 |
2.27e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 47.33 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 88 EACRKAAkSLIKL--GLERFHgVGILGFNSAEwFITAV-GAILAGGLCVGIYATN-----SAEV----CQYVITHAK--- 152
Cdd:PRK13388 35 EAAARAA-ALIALadPDRPLH-VGVLLGNTPE-MLFWLaAAALGGYVLVGLNTTRrgaalAADIrradCQLLVTDAEhrp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 153 ---------VNILLVENDQQLQKILsiPQSSLEPLKAIIqyrlpmkknnnlyswddfmelgrsiPDTQLeqviesqkanq 223
Cdd:PRK13388 112 lldgldlpgVRVLDVDTPAYAELVA--AAGALTPHREVD-------------------------AMDPF----------- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574584718 224 caVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdkhETVVSYL--PLSHIAAqMMDIWVPI 287
Cdd:PRK13388 154 --MLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT---RDDVCYVsmPLFHSNA-VMAGWAPA 213
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
218-538 |
2.44e-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: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 218 SQKANQCAVLIYTSGTTGIPKGVMLSHDN-------ITWIAgavtkDFKLTDKhetVVSYLPLSHIAAQMMDIWVPIKIG 290
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSllanveqIKTIA-----DFTPNDR---FMSALPLFHSFGLTVGLFTPLLTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 291 AltyfaqadalkgtlvstlkevkpTVFIgvpqiwekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkYNTPVS 370
Cdd:PRK08043 433 A-----------------------EVFL----------------------------------------------YPSPLH 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 371 YRMAKTLVFSK-----VKTSLGLDHCHSF------------ISGTAPLNQETAEFFL-SLDIPIGELYGLSESSGPHTIS 432
Cdd:PRK08043 444 YRIVPELVYDRnctvlFGTSTFLGNYARFanpydfarlryvVAGAEKLQESTKQLWQdKFGLRILEGYGVTECAPVVSIN 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 433 NQNNYRLLSCGKILTGCKNMLFqqNKDGI---GEICLWGRHIFMGYLESE---------TETTEAIDDEGWLHSGDLGQL 500
Cdd:PRK08043 524 VPMAAKPGTVGRILPGMDARLL--SVPGIeqgGRLQLKGPNIMNGYLRVEkpgvlevptAENARGEMERGWYDTGDIVRF 601
|
330 340 350
....*....|....*....|....*....|....*...
gi 574584718 501 DGLGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIP 538
Cdd:PRK08043 602 DEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALGVSP 638
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
57-244 |
2.64e-05 |
|
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: 47.34 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 57 FRESVNRFGTYPALASkNGKKWEilnfnqYYEACRKA---AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCV 133
Cdd:cd17651 1 FERQAARTPDAPALVA-EGRRLT------YAELDRRAnrlAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 134 GIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsiPQSSLEPLKAIIqyrlpmkknnnlysWDDFMELGRSIPDTqlE 213
Cdd:cd17651 74 PLDPAYPAERLAFMLADAGPVLVLTHPA---------LAGELAVELVAV--------------TLLDQPGAAAGADA--E 128
|
170 180 190
....*....|....*....|....*....|.
gi 574584718 214 QVIESQKANQcAVLIYTSGTTGIPKGVMLSH 244
Cdd:cd17651 129 PDPALDADDL-AYVIYTSGSTGRPKGVVMPH 158
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
228-260 |
3.99e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.81 E-value: 3.99e-05
10 20 30
....*....|....*....|....*....|...
gi 574584718 228 IYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL 260
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL 181
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
209-247 |
4.14e-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: 4.14e-05
10 20 30
....*....|....*....|....*....|....*....
gi 574584718 209 DTQLEQVIESQKanQCAVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:cd17648 83 DTGARVVITNST--DLAYAIYTSGTTGKPKGVLVEHGSV 119
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
79-532 |
5.91e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 46.22 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 79 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAILAGGL---CVGIYATnsAEVCQYVITHAKVNI 155
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLR-YLEVCWAAERSGLyytCVNSHLT--PAEAAYIVDDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 156 LLVENDQqlqkiLSIPQSSLEPLKAIiQYRLPMKKNNNLYSWDDFMELGRSIPDTqleqVIESQKANQcaVLIYTSGTTG 235
Cdd:PRK13391 100 LITSAAK-----LDVARALLKQCPGV-RHRLVLDGDGELEGFVGYAEAVAGLPAT----PIADESLGT--DMLYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 236 IPKGVM--LSHDNI---TWIAGAVTKDFKLTDkhETVvsYL---PLSHIAAQMmdiWVPIKIgaltyfaqadALKGTLVs 307
Cdd:PRK13391 168 RPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRS--DMV--YLspaPLYHSAPQR---AVMLVI----------RLGGTVI- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 308 TLKEVKPTVFIGVPQIWEKIHEMVkknsAKSMglkkkaFVwarnigfkvnskKMLgkyNTPVSYRMAKTLvfSKVKTSlg 387
Cdd:PRK13391 230 VMEHFDAEQYLALIEEYGVTHTQL----VPTM------FS------------RML---KLPEEVRDKYDL--SSLEVA-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 388 ldhchsfISGTAPLNQETAEFFLSLDIP-IGELYGLSESSGPHTI-SNQNNYRLLSCGKILTGCKNMLFQQNKD----GI 461
Cdd:PRK13391 281 -------IHAAAPCPPQVKEQMIDWWGPiIHEYYAATEGLGFTACdSEEWLAHPGTVGRAMFGDLHILDDDGAElppgEP 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574584718 462 GEICLWGRHIFMgYLESETETTEAID-DEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 532
Cdd:PRK13391 354 GTIWFEGGRPFE-YLNDPAKTAEARHpDGTWSTVGDIGYVDEDGYLYLTDR-AAFMIISGGVNIYPQEAENL 423
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
441-545 |
6.73e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.14 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 441 SCGKILTGCKNMLFQQNKDGIGEIcLWGRHIFMGYLESETETT---EAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILI 517
Cdd:PRK13383 346 TVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTRYTDgggKAVVD-GMTSTGDMGYLDNAGRLFIVGR-EDDMI 422
|
90 100
....*....|....*....|....*...
gi 574584718 518 TAGGENVPPIPVETLVKKKIPIISNAML 545
Cdd:PRK13383 423 ISGGENVYPRAVENALAAHPAVADNAVI 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
209-261 |
8.79e-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: 8.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 574584718 209 DTQLeQVIESQKANqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 261
Cdd:cd17644 95 DAQI-SVLLTQPEN-LAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGIT 145
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
92-240 |
9.52e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 45.46 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 92 KAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND--QQLQKIL- 168
Cdd:PRK12406 23 RAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADllHGLASALp 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574584718 169 -SIPQSSLEPLKAIIQ-YRLP---MKKNNNLYSWDDFMELGRSIPDTQLEQViesqkanqcAVLIYTSGTTGIPKGV 240
Cdd:PRK12406 103 aGVTVLSVPTPPEIAAaYRISpalLTPPAGAIDWEGWLAQQEPYDGPPVPQP---------QSMIYTSGTTGHPKGV 170
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-262 |
9.54e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 45.66 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 69 ALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAE-VCQYV 147
Cdd:PRK04319 62 ALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEaVRDRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 148 -ITHAKVnilLVENDQQLQKIlsiPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGrsipDTQLEqvIESQKANQCAV 226
Cdd:PRK04319 142 eDSEAKV---LITTPALLERK---PADDLPSLKHVLLVGEDVEEGPGTLDFNALMEQA----SDEFD--IEWTDREDGAI 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 574584718 227 LIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDFKLTD 262
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAMLqhYQTGKYVLDLHEDD 247
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
218-261 |
1.20e-04 |
|
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: 1.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 574584718 218 SQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 261
Cdd:cd17649 90 THHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT 133
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
94-280 |
1.23e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 45.26 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 94 AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGI-YATNSAEVcQYVITHAKVNILLVEnDQQLQKILSIPq 172
Cdd:PRK07798 42 AHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDEL-RYLLDDSDAVALVYE-REFAPRVAEVL- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 173 SSLEPLKAIIQYrlpmkknnnlyswDDFMELGRSIPDTQLEQVIESQKANQCAV--------LIYTSGTTGIPKGVMLSH 244
Cdd:PRK07798 119 PRLPKLRTLVVV-------------EDGSGNDLLPGAVDYEDALAAGSPERDFGerspddlyLLYTGGTTGMPKGVMWRQ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 574584718 245 DNItWIAGAVTKDF----KLTDKHETVVSYL-----------PLSHIAAQM 280
Cdd:PRK07798 186 EDI-FRVLLGGRDFatgePIEDEEELAKRAAagpgmrrfpapPLMHGAGQW 235
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
208-247 |
1.25e-04 |
|
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: 1.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 574584718 208 PDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:cd17646 127 PATPPLVPPRPDNL---AYVIYTSGSTGRPKGVMVTHAGI 163
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
225-280 |
1.44e-04 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 44.65 E-value: 1.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNItWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQM 280
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALI 138
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
221-257 |
2.10e-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: 2.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 574584718 221 ANQCAVLIYTSGTTGIPKGVMLSHDN----ITWIAGAVTKD 257
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQWAAAAFSAE 144
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
55-309 |
2.70e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.56 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 55 EFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVG 134
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 135 IYATNSAEVCQYVITHAKVNILLVendqqlQKILSIPQSsleplkaiiqyrlpmKKNNNLYSWDDFMELGRSIPDTQLEq 214
Cdd:PRK12316 3137 LDPEYPEERLAYMLEDSGAQLLLS------QSHLRLPLA---------------QGVQVLDLDRGDENYAEANPAIRTM- 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 215 viesqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDIWVPIKIGALTY 294
Cdd:PRK12316 3195 ------PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLG-VGDRVLQFTTFSFDVFVEELFWPLMSGARVVL 3267
|
250
....*....|....*
gi 574584718 295 FAQADALKGTLVSTL 309
Cdd:PRK12316 3268 AGPEDWRDPALLVEL 3282
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-244 |
3.86e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.18 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 86 YYEACRKA---AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDq 162
Cdd:PRK12316 2031 YAELDSRAnrlAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH- 2109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 163 qLQKILSIPQSSLeplkaiiqyRLPMKKNNNLYSWDDFMELGRSIPDTqleqviesqkanqCAVLIYTSGTTGIPKGVML 242
Cdd:PRK12316 2110 -LLERLPLPAGVA---------RLPLDRDAEWADYPDTAPAVQLAGEN-------------LAYVIYTSGSTGLPKGVAV 2166
|
..
gi 574584718 243 SH 244
Cdd:PRK12316 2167 SH 2168
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
225-258 |
6.07e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 6.07e-04
10 20 30
....*....|....*....|....*....|....
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDF 258
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF 2369
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
227-299 |
6.97e-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: 6.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574584718 227 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHEtvvsYLPLSHIAAQMM--DIWVPIKIGALTYFAQAD 299
Cdd:cd17647 114 LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK----FTMLSGIAHDPIqrDMFTPLFLGAQLLVPTQD 184
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-292 |
1.05e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 42.46 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 86 YYEACRKA---AKSLIKLGL--ERFhgVGILGFNSAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVE 159
Cdd:PRK12467 3123 YAELNRRAnrlAHRLIAIGVgpDVL--VGVAVERSVE-MIVALLAVLkAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ 3199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 160 ndqqlqkilsipQSSLEplkaiiqyRLPMKKNNNLYSWDDFMELGrsIPDTQLEQVIESQkanQCAVLIYTSGTTGIPKG 239
Cdd:PRK12467 3200 ------------AHLLE--------QLPAPAGDTALTLDRLDLNG--YSENNPSTRVMGE---NLAYVIYTSGSTGKPKG 3254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 574584718 240 VMLSHDNIT----WIAGAvtkdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAL 292
Cdd:PRK12467 3255 VGVRHGALAnhlcWIAEA-----YELDANDRVLLFMSFSFDGAQERFLWTLICGGCL 3306
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
473-530 |
1.69e-03 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 41.53 E-value: 1.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 574584718 473 MGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK05857 386 LGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPDEVD 441
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-247 |
1.77e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 41.69 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 35 EVLLRLSKHGPGHETPMTIPEFFRESVNRfgTYPALASKNGKkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFN 114
Cdd:PRK12467 1558 QILEGWNATHTGYPLARLVHQLIEDQAAA--TPEAVALVFGE--QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVER 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 115 SAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVendqqlqkilsipQSSLEPlkaiiqyRLPMKKNNN 193
Cdd:PRK12467 1634 SLE-MVVGLLAILkAGGAYVPLDPEYPRERLAYMIEDSGIELLLT-------------QSHLQA-------RLPLPDGLR 1692
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 574584718 194 LYSWDDFMELGRSIPDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:PRK12467 1693 SLVLDQEDDWLEGYSDSNPAVNLAPQ---NLAYVIYTSGSTGRPKGAGNRHGAL 1743
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
225-247 |
1.88e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 1.88e-03
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
225-278 |
2.13e-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: 2.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 574584718 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAA 278
Cdd:cd05937 90 AILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNG-DRTYTCMPLYHGTA 142
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
227-316 |
2.52e-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: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584718 227 LIYTSGTTGIPKGVMLSHDNIT----WIAgavtKDFKLTDKHEtvvsYLPLSHIAAQMM--DIWVPIKIGALTYFAQADA 300
Cdd:TIGR03443 420 LSFTSGSEGIPKGVLGRHFSLAyyfpWMA----KRFGLSENDK----FTMLSGIAHDPIqrDMFTPLFLGAQLLVPTADD 491
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90
....*....|....*...
gi 574584718 301 L--KGTLVSTLKEVKPTV 316
Cdd:TIGR03443 492 IgtPGRLAEWMAKYGATV 509
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| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
221-247 |
3.16e-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: 3.16e-03
10 20
....*....|....*....|....*..
gi 574584718 221 ANQCAVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNL 129
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
459-530 |
4.74e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.05 E-value: 4.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584718 459 DGIGEIC-LWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILiTAGGENVPPIPVE 530
Cdd:PRK07867 350 EAIGELVnTAGPGGFEGYYNDPEADAERMRG-GVYWSGDLAYRDADGYAYFAGRLGDWM-RVDGENLGTAPIE 420
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
462-530 |
6.22e-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: 6.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584718 462 GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVE 530
Cdd:cd17636 190 GEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAEVE 256
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
475-532 |
6.96e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 39.50 E-value: 6.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 574584718 475 YLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 532
Cdd:PRK08276 354 YHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENL 410
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