|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
125-715 |
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: 1126.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 125 KRQDKWEHISYSQYYLLARRAAKGFLK----QAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCC 200
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKlgleRFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 201 ANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSG 280
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 281 TTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVNTL 360
Cdd:cd05933 161 TTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 361 REVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFTT-RLADYLVLAKVRQALGFA 439
Cdd:cd05933 241 REVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFyRLAKKLVFKKVRKALGLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 440 KCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGR 519
Cdd:cd05933 321 RCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 520 TIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISNAMLIGDQ 599
Cdd:cd05933 401 HVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 600 RKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWA 679
Cdd:cd05933 481 RKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKWV 560
|
570 580 590
....*....|....*....|....*....|....*.
gi 313747580 680 ILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFY 715
Cdd:cd05933 561 ILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
102-718 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 578.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 102 PYTVHRMFYEALDKYGDLIALGFKRQDKWEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAG 177
Cdd:COG1022 10 ADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLlalgVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 178 GIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEV-P 256
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLSLDELLALGREVaD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 257 EEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWt 336
Cdd:COG1022 170 PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP----GDRTLSFLPLAHVFERTVSYY- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 337 GIQWGAQVCFAE-PDALkgslVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTC---- 411
Cdd:COG1022 245 ALAAGATVAFAEsPDTL----AEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARlagk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 412 -PGSDLKPfTTRLADYLVLAKVRQALG----FAKCqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYN 486
Cdd:COG1022 321 sPSLLLRL-KHALADKLVFSKLREALGgrlrFAVS-----GGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 487 YRLYSSGKLVPGCRVKLvnqdAEgIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELI 566
Cdd:COG1022 395 NRIGTVGPPLPGVEVKI----AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 567 ITAGGENVPPVPIEEAVKmELPIISNAMLIGDQRKFLSMLLtlkcTLDPdtsdqtdnltEQAMEFCQRVGSRATTVSEII 646
Cdd:COG1022 470 VTSGGKNVAPQPIENALK-ASPLIEQAVVVGDGRPFLAALI----VPDF----------EALGEWAEENGLPYTSYAELA 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313747580 647 ekKDEAVYQAIEEGIRRVNmNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQ 718
Cdd:COG1022 535 --QDPEVRALIQEEVDRAN-AGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
130-700 |
5.16e-145 |
|
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: 431.25 E-value: 5.16e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 130 WEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 205
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLialgVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VDTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqPNQCCVLVYTSGTTGNP 285
Cdd:cd05907 83 VED------------------------------------------------------------PDDLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 286 KGVMLSQDNITWTARYGSQAgdIRPAEvqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkgSLVNTLREVEP 365
Cdd:cd05907 103 KGVMLSHRNILSNALALAER--LPATE--GDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 366 TSHMGVPRVWEKIMERIQEVAAQSGfiRRKMLLWAmsvtleqnltcpgsdlkpfttrladylVLAKVRqalgFAKCqknf 445
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIKVKAVPGL--KRKLFDLA---------------------------VGGRLR----FAAS---- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 446 yGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiGEICLWGRTIFMGY 525
Cdd:cd05907 219 -GGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD-----GEILVRGPNVMLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 526 LNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISNAMLIGDQRKFLSM 605
Cdd:cd05907 293 YKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 606 LLTLKCtldpdtsdqtdnltEQAMEFCQRVGSRATTVSEIIekKDEAVYQAIEEGIRRVNmNAAARPYHIQKWAILERDF 685
Cdd:cd05907 372 LIVPDP--------------EALEAWAEEHGIAYTDVAELA--ANPAVRAEIEAAVEAAN-ARLSRYEQIKKFLLLPEPF 434
|
570
....*....|....*
gi 313747580 686 SISGGELGPTMKLKR 700
Cdd:cd05907 435 TIENGELTPTLKLKR 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
109-569 |
3.61e-101 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 316.95 E-value: 3.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 109 FYEALDKYGDLIALGFkrqDKWEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIY 184
Cdd:pfam00501 1 LERQAARTPDKTALEV---GEGRRLTYRELDERANRLAAGLralgVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 185 TTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEAldaii 264
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 265 dtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 344
Cdd:pfam00501 153 ---DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 345 CFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaqSGFIRRkmllwamsvtleqnltcpgsdlkpfttr 422
Cdd:pfam00501 230 VLPPGFPALdpAALLELIERYKVTVLYGVPTLLNMLLE--------AGAPKR---------------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 423 ladyLVLAKVRQALgfakcqknfYGAAPMMAETQHFFLGLNIR-LYAGYGLSETSGP---HFMSSPYNYRLYSSGKLVPG 498
Cdd:pfam00501 274 ----ALLSSLRLVL---------SGGAPLPPELARRFRELFGGaLVNGYGLTETTGVvttPLPLDEDLRSLGSVGRPLPG 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 499 CRVKLVNQD------AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITA 569
Cdd:pfam00501 341 TEVKIVDDEtgepvpPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
130-707 |
6.29e-88 |
|
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: 287.01 E-value: 6.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 130 WEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 205
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLlalgVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VDTQKQLEKILKIWKQLPHLKAVVIYKeppPNKMAN-----VYTMEEFMELGNEVPE---EALDAIIDTQQPNQCCVLVY 277
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIYCD---PRGMRKyddprLISFEDVVALGRALDRrdpGLYEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 278 TSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkgSLV 357
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDE----YVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE---TMM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 358 NTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSV---TLEQNLTCPGSDLKPFTTR-LADYLVLAKVR 433
Cdd:cd17641 239 EDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLglrALDRGKRGRPVSLWLRLASwLADALLFRPLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 434 QALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNqdaegIGE 513
Cdd:cd17641 319 DRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE-----VGE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 514 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISNA 593
Cdd:cd17641 394 ILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 594 MLIGDQRKFLSMLLtlkcTLDPDTsdqTDNLTEQAmefcqrvGSRATTVSEIIEKkdEAVYQAIEEGIRRVNMNAAArPY 673
Cdd:cd17641 473 VVLGAGRPYLTAFI----CIDYAI---VGKWAEQR-------GIAFTTYTDLASR--PEVYELIRKEVEKVNASLPE-AQ 535
|
570 580 590
....*....|....*....|....*....|....
gi 313747580 674 HIQKWAILERDFSISGGELGPTMKLKRLTVLEKY 707
Cdd:cd17641 536 RIRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
129-715 |
4.60e-82 |
|
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: 271.01 E-value: 4.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 129 KWEHISYSQYYLLARRAAKGFL------KQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCAN 202
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRslggkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 203 VIMVDtqkqlEKIlkiwkqlphlkavviykepppnkmaNVYTMEEFMELGNEVPEEALDAiidtqQPNQCCVLVYTSGTT 282
Cdd:cd05927 82 IVFCD-----AGV-------------------------KVYSLEEFEKLGKKNKVPPPPP-----KPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 283 GNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFAEPDALKgsLVNTLRE 362
Cdd:cd05927 127 GNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 363 VEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSvTLEQNLTCPGSdlkpFTTRLADYLVLAKVRQALGfAKCQ 442
Cdd:cd05927 204 LKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN-YKLAELRSGVV----RASPFWDKLVFNKIKQALG-GNVR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 443 KNFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLV-----NQDAEGI---GE 513
Cdd:cd05927 278 LMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVdvpemNYDAKDPnprGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 514 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIeEAVKMELPIISNA 593
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKI-ENIYARSPFVAQI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 594 MLIGDQRKflSMLLTLKCtLDPDTsdqtdnlteqAMEFCQRVGSRATTVSEIIekKDEAVYQAIEEGIRRVNMNAAARPY 673
Cdd:cd05927 437 FVYGDSLK--SFLVAIVV-PDPDV----------LKEWAASKGGGTGSFEELC--KNPEVKKAILEDLVRLGKENGLKGF 501
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 313747580 674 HIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKGIIDSFY 715
Cdd:cd05927 502 EQVKAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
105-597 |
6.03e-71 |
|
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: 238.56 E-value: 6.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 105 VHRMFYEALDKYGDLIALGFKrqdkWEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 180
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALralgVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 181 TGIYTTSSPEacqyiaydccanvimvdtqkQLEKILKiwkqlpHLKAVVIYkepppnkmanvytmeefmelgnevpeeal 260
Cdd:COG0318 77 VPLNPRLTAE--------------------ELAYILE------DSGARALV----------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 261 daiidtqqpnqCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQW 340
Cdd:COG0318 102 -----------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP----GDVVLVALPLFHVFGLTVGLLAPLLA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 341 GAQ-VCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcpgsdlkpf 419
Cdd:COG0318 167 GATlVLLPRFDP--ERVLELIERERVTVLFGVPTMLARLLRH-------------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 420 tTRLADYLvLAKVRQAlgfakcqknFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSgPHFMSSPYNY---RLYSSGKL 495
Cdd:COG0318 207 -PEFARYD-LSSLRLV---------VSGGAPLPPELLERFEErFGVRIVEGYGLTETS-PVVTVNPEDPgerRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 496 VPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIIT 568
Cdd:COG0318 275 LPGVEVRIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
490 500
....*....|....*....|....*....
gi 313747580 569 aGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:COG0318 352 -GGENVYPAEVEEVL-AAHPGVAEAAVVG 378
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
131-700 |
7.43e-66 |
|
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: 225.32 E-value: 7.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAKGFL----KQAHSVAILGFNSPEWFFSAVGTVFAGgivtgiyttsspeacqyiaydcCANVIMv 206
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRslgvKAGEKVALFADNSPRWLIADQGIMALG----------------------AVDVVR- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 207 DTQKQLEKILKIwkqLPHLKAVVIYKEPPPNKMAnvytmeefmelgnevpeealdaiidtqqpnqccVLVYTSGTTGNPK 286
Cdd:cd17640 61 GSDSSVEELLYI---LNHSESVALVVENDSDDLA---------------------------------TIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 287 GVMLSQDNITWTARygsQAGDIRPAEVQQeVVVSYLPLSHIAAQIYDlWTGIQWGAQVCFAEPDALKgslvNTLREVEPT 366
Cdd:cd17640 105 GVMLTHANLLHQIR---SLSDIVPPQPGD-RFLSILPIWHSYERSAE-YFIFACGCSQAYTSIRTLK----DDLKRVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 367 SHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpgsdlkpfttrladyLVLAKVRQALGFAkcqknfy 446
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF--------------------------LSGGIFKFGISGG------- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 447 GAAPMMAETqhFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI------GEICLWGRT 520
Cdd:cd17640 223 GALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRGPQ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 521 IFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGDQR 600
Cdd:cd17640 301 VMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEAL-MRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 601 KFLSMLLTlkctldPDtsdqtdnlTEQAMEFCQRVGSR-ATTVSEIIEKKDE-AVYQaiEEGIRRVNMNAAARPY-HIQK 677
Cdd:cd17640 380 KRLGALIV------PN--------FEELEKWAKESGVKlANDRSQLLASKKVlKLYK--NEIKDEISNRPGFKSFeQIAP 443
|
570 580
....*....|....*....|...
gi 313747580 678 WAILErDFSISGGELGPTMKLKR 700
Cdd:cd17640 444 FALLE-EPFIENGEMTQTMKIKR 465
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
271-584 |
1.33e-62 |
|
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: 212.53 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 271 QCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAaQIYDLWTGIQWGAQVCFAEPD 350
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE----GDVFLSTLPLFHIG-GLFGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 351 aLKGSLVNTLREVEPTSHMGVPRVWEKIMERIqevaaqsgfirrkmllwamsvtleqnltcpgsdlkpfttRLADYlVLA 430
Cdd:cd04433 76 -DPEAALELIEREKVTILLGVPTLLARLLKAP---------------------------------------ESAGY-DLS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 431 KVRQAlgfakcqknFYGAAPMMAETQHFFLGL-NIRLYAGYGLSETSGPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD 507
Cdd:cd04433 115 SLRAL---------VSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDdaRKPGSVGRPVPGVEVRIVDPD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 508 AE-----GIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 582
Cdd:cd04433 186 GGelppgEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAV 263
|
..
gi 313747580 583 VK 584
Cdd:cd04433 264 LL 265
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
129-706 |
5.97e-62 |
|
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: 215.80 E-value: 5.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 129 KWEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVI 204
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAALralgLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 205 MVDTqkqlekiLKIWKQLPHLKA--VVIYKEPPPNKMANVYTMEEFMELGNEVPEEAldaiidTQQPNQCCVLVYTSGTT 282
Cdd:cd05932 83 FVGK-------LDDWKAMAPGVPegLISISLPPPSAANCQYQWDDLIAQHPPLEERP------TRFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 283 GNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEpdALKgSLVNTLRE 362
Cdd:cd05932 150 GQPKGVMLTFGSFAWAAQAGIEHIGTEE----NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLD-TFVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 363 VEPTSHMGVPRVWEKIMERIQEVAAQSgfiRRKMLLWAmsvtleqnltcpgsdlkPFTTRLadylVLAKVRQALGFAKCQ 442
Cdd:cd05932 223 ARPTLFFSVPRLWTKFQQGVQDKIPQQ---KLNLLLKI-----------------PVVNSL----VKRKVLKGLGLDQCR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 443 KNFYGAAPMMAETQHFF--LGLNIrlYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiGEICLWGRT 520
Cdd:cd05932 279 LAGCGSAPVPPALLEWYrsLGLNI--LEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 521 IFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGDQr 600
Cdd:cd05932 352 LMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKL-AEHDRVEMVCVIGSG- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 601 kfLSMLLTLkCTLDPDTSDQTDNLTEQAMEfcqrvgsraTTVSEIIEKkdeavyqaieegirrvnMNAAARPY-HIQKWA 679
Cdd:cd05932 430 --LPAPLAL-VVLSEEARLRADAFARAELE---------ASLRAHLAR-----------------VNSTLDSHeQLAGIV 480
|
570 580
....*....|....*....|....*..
gi 313747580 680 ILERDFSISGGELGPTMKLKRlTVLEK 706
Cdd:cd05932 481 VVKDPWSIDNGILTPTLKIKR-NVLEK 506
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
131-630 |
4.54e-60 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 209.61 E-value: 4.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQyylLARRAAK--GFLKQA-----HSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIaydccanv 203
Cdd:cd05914 6 EPLTYKD---LADNIAKfaLLLKINgvgtgDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHI-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 204 imvdtqkqlekilkiwkqLPHLKAVVIYkepppnkmanvytmeefmelgnevpeealdaiidTQQPNQCCVLVYTSGTTG 283
Cdd:cd05914 75 ------------------LNHSEAKAIF----------------------------------VSDEDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 284 NPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAepDALKGSLVNTLREV 363
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVVLLGKGDK----ILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 364 EPTSHMGVPRVWE----KIMERIQEVAAqsgfirrKMLLWAMSVtleqnltcpgsdlKPFTTRLADyLVLAKVRQALGfa 439
Cdd:cd05914 177 QVTPTLGVPVPLViekiFKMDIIPKLTL-------KKFKFKLAK-------------KINNRKIRK-LAFKKVHEAFG-- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 440 kcqKNF----YGAAPMMAETQHFFLGLNIRLYAGYGLSETsGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAE-GIGE 513
Cdd:cd05914 234 ---GNIkefvIGGAKINPDVEEFLRTIGFPYTIGYGMTET-APIISYSPPNrIRLGSAGKVIDGVEVRIDSPDPAtGEGE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 514 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIE-EAVKMELPIISn 592
Cdd:cd05914 310 IIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEaKINNMPFVLES- 388
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 313747580 593 amLIGDQRKFLSMLLtlkcTLDPDTSD----QTDNLTEQAME 630
Cdd:cd05914 389 --LVVVQEKKLVALA----YIDPDFLDvkalKQRNIIDAIKW 424
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
262-700 |
1.74e-59 |
|
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: 208.99 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 262 AIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHI---AAQIydlwTGI 338
Cdd:cd17639 80 AIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLV--AGIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 339 QWGAQVCFAEPDAL-KGSLVNT---LREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGs 414
Cdd:cd17639 154 YRGGTIGYGSPRTLtDKSKRGCkgdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 415 dlkpftTRLADYLVLAKVRQALGfAKCQKNFYGAAPMMAETQHFflgLNI---RLYAGYGLSETSGPHFMSSPYNYRLYS 491
Cdd:cd17639 233 ------TPLLDELVFKKVRAALG-GRLRYMLSGGAPLSADTQEF---LNIvlcPVIQGYGLTETCAGGTVQDPGDLETGR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 492 SGKLVPGCRVKLVNQDAEGI--------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLK 563
Cdd:cd17639 303 VGPPLPCCEIKLVDWEEGGYstdkppprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 564 ELIITAGGENvppVPIE--EAVKMELPIISNAMLIGDQRKFLSMLLTLkctldPDTSdqtdnlteQAMEFCQRVGSRATT 641
Cdd:cd17639 383 DLVKLQNGEY---IALEklESIYRSNPLVNNICVYADPDKSYPVAIVV-----PNEK--------HLTKLAEKHGVINSE 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 642 VSEIIEKKD--EAVYQAIEEgirrvnmnaAARPYHIQKWAILERDFSISG------GELGPTMKLKR 700
Cdd:cd17639 447 WEELCEDKKlqKAVLKSLAE---------TARAAGLEKFEIPQGVVLLDEewtpenGLVTAAQKLKR 504
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
132-597 |
4.93e-58 |
|
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: 204.37 E-value: 4.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 132 HISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVD 207
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLrklgLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 208 tQKQLEKILKIWKQLPHLKAVVIYKEPPPnKMANVYTMEEFmELGNEVPEEALDAIIDtqqPNQCCVLVYTSGTTGNPKG 287
Cdd:cd05911 90 -PDGLEKVKEAAKELGPKDKIIVLDDKPD-GVLSIEDLLSP-TLGEEDEDLPPPLKDG---KDDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 288 VMLSQDNITWTArygSQAGDIRPAEVQ-QEVVVSYLPLSHIAAQIYDLWTgiqwgaqvcfaepdALKGSLVNTLREVEPt 366
Cdd:cd05911 164 VCLSHRNLIANL---SQVQTFLYGNDGsNDVILGFLPLYHIYGLFTTLAS--------------LLNGATVIIMPKFDS- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 367 shmgvprvwEKIMERIQEvaaqsgfiRRKMLLW---AMSVTLeqnLTCPgsDLKPFTtrladylvLAKVRQAlgfakcqk 443
Cdd:cd05911 226 ---------ELFLDLIEK--------YKITFLYlvpPIAAAL---AKSP--LLDKYD--------LSSLRVI-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 444 nFYGAAPMMAETQHFF--LGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN---QDAEGI---GEIC 515
Cdd:cd05911 268 -LSGGAPLSKELQELLakRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDddgKDSLGPnepGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 516 LWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML 595
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKEL-IKYKGFQVAPAEL-EAVLLEHPGVADAAV 424
|
..
gi 313747580 596 IG 597
Cdd:cd05911 425 IG 426
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
102-597 |
1.21e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 204.27 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 102 PYTVHRMFYEALDKYGDLIALgFKRQDKWehiSYSQYYLLARRAAKGFL----KQAHSVAILGFNSPEWFFSAVGTVFAG 177
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAV-YFDGRRT---TYAELDERVNRLANALRalgvKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 178 GIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ--KQLEKILKiwkQLPHLKAVVIYkEPPPNKMANVYTmEEFMELGNEV 255
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILP---QLPTVRTVIVE-GDGPAAPLAPEV-GEYEELLAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 256 PEEALDAIIDtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAqiydlW 335
Cdd:PRK06187 156 SDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR----DDVYLVIVPMFHVHA-----W 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 336 T----GIQWGA-QVCFAEPDAlkGSLVNTLREVEPT-SHMgVPRVWEkimeriqevaaqsgfirrkMLLwamsvtleQNL 409
Cdd:PRK06187 224 GlpylALMAGAkQVIPRRFDP--ENLLDLIETERVTfFFA-VPTIWQ-------------------MLL--------KAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 410 TCPGSDLkpfttrladylvlAKVRQALgfakcqknfYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSG-------PHFM 481
Cdd:PRK06187 274 RAYFVDF-------------SSLRLVI---------YGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvsvlppEDQL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 482 SSPYNYRlYSSGKLVPGCRVKLVNQ-------DAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADG 554
Cdd:PRK06187 332 PGQWTKR-RSAGRPLPGVEARIVDDdgdelppDGGEVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDG 409
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 313747580 555 FLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:PRK06187 410 YLYITDRIKDVIIS-GGENIYPRELEDAL-YGHPAVAEVAVIG 450
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
66-717 |
2.48e-53 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 195.32 E-value: 2.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 66 PEKVNNAQWDAPEEALWTTRADGRVrlridPSCPQLPyTVHRMFYEALDKYGDLIALGFKRQD-------KWehISYSQY 138
Cdd:PLN02736 13 PEKLQTGKWNVYRSARSPLKLVSRF-----PDHPEIG-TLHDNFVYAVETFRDYKYLGTRIRVdgtvgeyKW--MTYGEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 139 YllARRAAKGF------LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKqL 212
Cdd:PLN02736 85 G--TARTAIGSglvqhgIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQT-L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 213 EKILKIWKQLPHLKAVVIY-------KEPPPNKMANVYTMEEFMELGNEVPEEALdaiidTQQPNQCCVLVYTSGTTGNP 285
Cdd:PLN02736 162 NTLLSCLSEIPSVRLIVVVggadeplPSLPSGTGVEIVTYSKLLAQGRSSPQPFR-----PPKPEDVATICYTSGTTGTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 286 KGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAAQIYDLWTgIQWGAQVCFAEPDALKgsLVNTLREVEP 365
Cdd:PLN02736 237 KGVVLTHGNLIANVAGSSLSTKFYPSDVH----ISYLPLAHIYERVNQIVM-LHYGVAVGFYQGDNLK--LMDDLAALRP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 366 TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSV---TLEQnltcpGSDLKPfttrLADYLVLAKVRQALGfAKCQ 442
Cdd:PLN02736 310 TIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAkkqALEN-----GKNPSP----MWDRLVFNKIKAKLG-GRVR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 443 KNFYGAAPMMAETQHFflgLNI----RLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLV--------NQDAE- 509
Cdd:PLN02736 380 FMSSGASPLSPDVMEF---LRIcfggRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVdvpemnytSEDQPy 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 510 GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEaVKMELPI 589
Cdd:PLN02736 457 PRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKF 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 590 ISNAMLIGDQrkFLSMLLTLkCTLDPDT--------SDQTDNLTeqamEFCQRVGSRATTVSEIIEKKDEAVYQAIEEgi 661
Cdd:PLN02736 536 VAQCFVYGDS--LNSSLVAV-VVVDPEVlkawaaseGIKYEDLK----QLCNDPRVRAAVLADMDAVGREAQLRGFEF-- 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 313747580 662 rrvnmnaaARPYHIqkwaILErDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQE 717
Cdd:PLN02736 607 --------AKAVTL----VPE-PFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
133-597 |
1.23e-51 |
|
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: 185.51 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 133 ISYSQYYLLARRAAKGFLKQAHS----VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDT 208
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAkgdrVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLFDDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 209 qkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPKGV 288
Cdd:cd17631 101 ----------------------------------------------------------------ALLMYTSGTTGRPKGA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 289 MLSQDNITWTARYGSQAGDIRPAEVQqeVVVsyLPLSHIAA----QIYDLWTGiqwGAQVCFAEPDAlkGSLVNTLREVE 364
Cdd:cd17631 117 MLTHRNLLWNAVNALAALDLGPDDVL--LVV--APLFHIGGlgvfTLPTLLRG---GTVVILRKFDP--ETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 365 PTSHMGVPRVWEKImeriqevaaqsgfirrkmllwamsvtleqnLTCPGSDlkpfTTRLADylvLAKVrqalgfakcqkn 444
Cdd:cd17631 188 VTSFFLVPTMIQAL------------------------------LQHPRFA----TTDLSS---LRAV------------ 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 445 FYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYR--LYSSGKLVPGCRVKLVNQDAE-----GIGEICLW 517
Cdd:cd17631 219 IYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVDPDGRevppgEVGEIVVR 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 518 GRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd17631 299 GPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVL-YEHPAVAEVAVIG 375
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
108-719 |
1.69e-51 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 190.23 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 108 MFYEALDKYGDLIALGFK-----RQDKWEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGG 178
Cdd:PLN02614 50 VFRMSVEKYPNNPMLGRReivdgKPGKYVWQTYQEVYDIVIKLGNSLrsvgVKDEAKCGIYGANSPEWIISMEACNAHGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 179 IVTGIYTTSSPEACQYIAYDCCANVIMVDTQKqlekILKIWKQLP----HLKAVVIYKEPPPNKMAN-------VYTMEE 247
Cdd:PLN02614 130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKK----ISELFKTCPnsteYMKTVVSFGGVSREQKEEaetfglvIYAWDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 248 FMELGnevpeEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNI-TWTARYGSQAGDIRPAEVQQEVVVSYLPLSH 326
Cdd:PLN02614 206 FLKLG-----EGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIvTLIAGVIRLLKSANAALTVKDVYLSYLPLAH 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 327 IAAQIYDLWTgIQWGAQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLe 406
Cdd:PLN02614 281 IFDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKF- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 407 QNLTCPGSDLKpfTTRLADYLVLAKVRQALGfAKCQKNFYGAAPMMAETQHFflglnIRLYA------GYGLSETSGPHF 480
Cdd:PLN02614 357 GNMKKGQSHVE--ASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESF-----LRVVAcchvlqGYGLTESCAGTF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 481 MSSPYNYRLYSS-GKLVPGCRVKL-----VNQDAEGI---GEICLWGRTIFMGYLNMEDKTCEAIDeEGWLHTGDAGRLD 551
Cdd:PLN02614 429 VSLPDELDMLGTvGPPVPNVDIRLesvpeMEYDALAStprGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQ 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 552 ADGFLYITGRLKELIITAGGENVPPVPIEEaVKMELPIISNAMLIGDQrkFLSMLLTLKctldpDTSDQTdnLTEQAME- 630
Cdd:PLN02614 508 PNGSMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGNS--FESFLVAIA-----NPNQQI--LERWAAEn 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 631 --------FCQRVGSRATTVSEIIEKKDEAVYQAIEEgIRRVNMNAAARPyhiqkwaiLERDFsisggeLGPTMKLKRLT 702
Cdd:PLN02614 578 gvsgdynaLCQNEKAKEFILGELVKMAKEKKMKGFEI-IKAIHLDPVPFD--------MERDL------LTPTFKKKRPQ 642
|
650
....*....|....*..
gi 313747580 703 VLEKYKGIIDSFYQEQK 719
Cdd:PLN02614 643 LLKYYQSVIDEMYKTTN 659
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
102-600 |
2.63e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 175.48 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 102 PYTVHRMFYEALDKYGDLIALGFKRQDkwehISYSQYYLLARRAAKGFL----KQAHSVAILGFNSPEWFFSAVGTVFAG 177
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQR----LTYAELNARVRRAAAALAalgiGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 178 GIVTGIYTTSSPEACQYIAYDCCANVIMVdTQKQLEKILKIWKQLPHLKAVVIYK-EPPPNKMANVYTMEEFMELGNEVP 256
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFV-LGLFLGVDYSATTRLPALEHVVICEtEEDDPHTEKMKTFTDFLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 257 EEAldaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIaaqiydlwt 336
Cdd:PRK07656 159 RAP------EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTE----GDRYLAANPFFHV--------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 337 giqWGAQVCFAEPdALKGSLVNTLREVEPtshmgvprvwEKIMERIQEvaaqsgfirRKMLLWAMSVTLEQNLtcpgsdl 416
Cdd:PRK07656 220 ---FGYKAGVNAP-LMRGATILPLPVFDP----------DEVFRLIET---------ERITVLPGPPTMYNSL------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 417 kpFTTRLADYLVLAKVRQALGfakcqknfyGAAPMMAETQHFF---LGLNIRLyAGYGLSETSGPHFMSSPYNYRL---Y 490
Cdd:PRK07656 270 --LQHPDRSAEDLSSLRLAVT---------GAASMPVALLERFeseLGVDIVL-TGYGLSEASGVTTFNRLDDDRKtvaG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 491 SSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKEL 565
Cdd:PRK07656 338 TIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDM 417
|
490 500 510
....*....|....*....|....*....|....*..
gi 313747580 566 IITaGGENVPPVPIEEaVKMELPIISNAMLIG--DQR 600
Cdd:PRK07656 418 FIV-GGFNVYPAEVEE-VLYEHPAVAEAAVIGvpDER 452
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
107-597 |
4.55e-46 |
|
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: 170.82 E-value: 4.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 107 RMFYEALDKYGDLIALGFkrQDKWehISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 182
Cdd:cd05936 3 DLLEEAARRFPDKTALIF--MGRK--LTYRELDALAEAFAAGLqnlgVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 183 IYTTSSPEACQYIAYDCCANVIMVDTQkqLEKILKIWkqlphlkavviykepppnkmanvytmeEFMELGNEVPEEALda 262
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVS--FTDLLAAG---------------------------APLGERVALTPEDV-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 263 iidtqqpnqcCVLVYTSGTTGNPKGVMLSQDNITWTARygSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGA 342
Cdd:cd05936 128 ----------AVLQYTSGTTGVPKGAMLTHRNLVANAL--QIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 343 QVCFaEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFIRRkmllwamsvtleqnltcpgsdlkpfttr 422
Cdd:cd05936 196 TIVL-IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLN-------APEFKKR---------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 423 ladylVLAKVRQALGfakcqknfyGAAPMMAETQHFFLGL-NIRLYAGYGLSETSgP--HFMSSPYNYRLYSSGKLVPGC 499
Cdd:cd05936 240 -----DFSSLRLCIS---------GGAPLPVEVAERFEELtGVPIVEGYGLTETS-PvvAVNPLDGPRKPGSIGIPLPGT 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 500 RVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADGFLYITGRLKELIItAGGE 572
Cdd:cd05936 305 EVKIV--DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGF 380
|
490 500
....*....|....*....|....*
gi 313747580 573 NVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd05936 381 NVYPREVEEVL-YEHPAVAEAAVVG 404
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
156-716 |
3.53e-45 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 171.92 E-value: 3.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 156 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYK--- 232
Cdd:PLN02430 104 VGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTsvt 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 233 EPPPNKMANV----YTMEEFMELGNEVPEEaldaiIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTAR----YGSQ 304
Cdd:PLN02430 184 EEESDKASQIgvktYSWIDFLHMGKENPSE-----TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlFMEQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 305 AGDIRPAEvqqEVVVSYLPLSHIAAQIYDLWTgIQWGAQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQE 384
Cdd:PLN02430 259 FEDKMTHD---DVYLSFLPLAHILDRMIEEYF-FRKGASVGYYHGDL--NALRDDLMELKPTLLAGVPRVFERIHEGIQK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 385 VAAQSGFIRRKM--------LLWamsvtleQNLTCPGSDLKPfttrLADYLVLAKVRQALGfAKCQKNFYGAAPMMAETQ 456
Cdd:PLN02430 333 ALQELNPRRRLIfnalykykLAW-------MNRGYSHKKASP----MADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 457 HFflgLNIR----LYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGC---RVKLVNQ---DAEG---IGEICLWGRTIFM 523
Cdd:PLN02430 401 EF---LRVTscafVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYnelRLEEVPEmgyDPLGeppRGEICVRGKCLFS 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 524 GYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVpPVPIEEAVKMELPIISNAMLIGDQrkFL 603
Cdd:PLN02430 478 GYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYV-ALEYLENVYGQNPIVEDIWVYGDS--FK 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 604 SMLLTLkCTLDPDTSDQ---TDNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEgIRRVNMNaaARPYHIqkwai 680
Cdd:PLN02430 554 SMLVAV-VVPNEENTNKwakDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEY-IKGVILE--TKPFDV----- 624
|
570 580 590
....*....|....*....|....*....|....*.
gi 313747580 681 lERDFsisggeLGPTMKLKRLTVLEKYKGIIDSFYQ 716
Cdd:PLN02430 625 -ERDL------VTATLKKRRNNLLKYYQVEIDEMYR 653
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
150-719 |
2.66e-44 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 169.25 E-value: 2.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 150 LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDtQKQLEKILKIWKQL-PHLKAV 228
Cdd:PLN02861 99 VNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ-ESKISSILSCLPKCsSNLKTI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 229 VIY-------KEPPPNKMANVYTMEEFMELGNevpeeaLDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARY 301
Cdd:PLN02861 178 VSFgdvsseqKEEAEELGVSCFSWEEFSLMGS------LDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 302 GSQAGDIRPAEVQQE-VVVSYLPLSHIAAQIYDLWTgIQWGAQVCFAEPDALkgSLVNTLREVEPTSHMGVPRVWEKIME 380
Cdd:PLN02861 252 TDHLLKVTDRVATEEdSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGDIR--YLMEDVQALKPTIFCGVPRVYDRIYT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 381 RIQEVAAQSGFIRRKMLLWAMSVTLeQNLT--CPGSDLKPFTtrlaDYLVLAKVRQALGfAKCQKNFYGAAPMMAETQHF 458
Cdd:PLN02861 329 GIMQKISSGGMLRKKLFDFAYNYKL-GNLRkgLKQEEASPRL----DRLVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEF 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 459 FLGLNIR-LYAGYGLSETSGPHFMSSPYNYRLYSS-GKLVPGCRVKLVNQDAEGI--------GEICLWGRTIFMGYLNM 528
Cdd:PLN02861 403 LRVTSCSvLSQGYGLTESCGGCFTSIANVFSMVGTvGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 529 EDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVpPVPIEEAVKMELPIISNAMLIGDQrkFLSMLLT 608
Cdd:PLN02861 483 QDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYV-AVENLENTYSRCPLIASIWVYGNS--FESFLVA 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 609 LkctLDPDTSDQTD-----NLTEQAMEFCQRVGSRattvseiiekkdeavyQAIEEGIRRVNMNAAARPYHIQKWAILER 683
Cdd:PLN02861 559 V---VVPDRQALEDwaannNKTGDFKSLCKNLKAR----------------KYILDELNSTGKKLQLRGFEMLKAIHLEP 619
|
570 580 590
....*....|....*....|....*....|....*..
gi 313747580 684 D-FSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQK 719
Cdd:PLN02861 620 NpFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
131-583 |
9.83e-43 |
|
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: 160.15 E-value: 9.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAKGFL----KQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 206
Cdd:cd05934 2 RRWTYAELLRESARIAAALAalgiRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 207 DTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 286
Cdd:cd05934 82 DP----------------------------------------------------------------ASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 287 GVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVcfaepdalkgslvnTLREVEPT 366
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFGLGE----DDVYLTVLPLFHINAQAVSVLAALSVGATL--------------VLLPRFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 367 ShmgvpRVWEKImeriQEVAAQSGFIRRKMllwaMSVTLEQnltcpgsdlkPFTTRLADylvlAKVRQAlgfakcqknfY 446
Cdd:cd05934 160 S-----RFWSDV----RRYGATVTNYLGAM----LSYLLAQ----------PPSPDDRA----HRLRAA----------Y 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 447 GAAPMMAETQHFFLGLNIRLYAGYGLSETSGPhFMSSPYNYRLYSS-GKLVPGCRVKLVNQD-----AEGIGEICL---W 517
Cdd:cd05934 203 GAPNPPELHEEFEERFGVRLLEGYGMTETIVG-VIGPRDEPRRPGSiGRPAPGYEVRIVDDDgqelpAGEPGELVIrglR 281
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313747580 518 GRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEAV 583
Cdd:cd05934 282 GWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDM-IRRRGENISSAEVERAI 345
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
165-718 |
1.14e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 162.07 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 165 EWFFSAVGTVFAGGIVTGIYTTSSPEACQY-IAYDCCANVIMVDtqKQLEKILKIWKQ--LPHlkAVVIY-KEPPPNKMA 240
Cdd:PTZ00216 158 EWLASIYGIWSQSMVAATVYANLGEDALAYaLRETECKAIVCNG--KNVPNLLRLMKSggMPN--TTIIYlDSLPASVDT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 241 ---NVYTMEEFMELGNEvpeEALDAIIDTQQPNQCCVLV-YTSGTTGNPKGVMLSQDNITwtarYGSQAGDIRPAEV--- 313
Cdd:PTZ00216 234 egcRLVAWTDVVAKGHS---AGSHHPLNIPENNDDLALImYTSGTTGDPKGVMHTHGSLT----AGILALEDRLNDLigp 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 314 --QQEVVVSYLPLSHI----AAQIYdlwtgIQWGAQVCFAEPDalkgSLVNT-------LREVEPTSHMGVPRVWEKIME 380
Cdd:PTZ00216 307 peEDETYCSYLPLAHImefgVTNIF-----LARGALIGFGSPR----TLTDTfarphgdLTEFRPVFLIGVPRIFDTIKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 381 RIQEVAAQSGFIRRKMLLWAmsvtleqnltcpgsdlkpFTTRLA-----------DYLVLAKVRQALGfAKCQKNFYGAA 449
Cdd:PTZ00216 378 AVEAKLPPVGSLKRRVFDHA------------------YQSRLRalkegkdtpywNEKVFSAPRAVLG-GRVRAMLSGGG 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 450 PMMAETQHFF---LGLNIRlyaGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQD-------AEGIGEICLWGR 519
Cdd:PTZ00216 439 PLSAATQEFVnvvFGMVIQ---GWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEeykhtdtPEPRGEILLRGP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 520 TIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENvppVPIE--EAVKMELPIISN---AM 594
Cdd:PTZ00216 516 FLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEY---IALEalEALYGQNELVVPngvCV 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 595 LIGDQRKFLSMLLtlkctldpdtsdqtdnLTEQ--AMEFCQRVGSRAtTVSEIIekKDEAVYQAIEEGIRRVNMNAAARP 672
Cdd:PTZ00216 593 LVHPARSYICALV----------------LTDEakAMAFAKEHGIEG-EYPAIL--KDPEFQKKATESLQETARAAGRKS 653
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 313747580 673 YHIQKWA-ILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQ 718
Cdd:PTZ00216 654 FEIVRHVrVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFADE 700
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
132-597 |
2.24e-39 |
|
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: 152.39 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 132 HISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVD 207
Cdd:cd05904 32 ALTYAELERRVRRLAAGLakrgGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 208 TQkQLEKILkiwkqlPHLKAVVIYKEPPPNKMANVytmeefmELGNEVPEEALDAIIDTQqpNQCCVLVYTSGTTGNPKG 287
Cdd:cd05904 112 AE-LAEKLA------SLALPVVLLDSAEFDSLSFS-------DLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 288 VMLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHIaaqiydlwtgiqWGAQVCFAEPDALKGSLVntlreVepts 367
Cdd:cd05904 176 VMLTHRNLI--AMVAQFVAGEGSNSDSEDVFLCVLPMFHI------------YGLSSFALGLLRLGATVV-----V---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 368 hmgVPR-VWEKIMERIQEVAAQSGFIRRKMLLwAMSvtleqnltcpgsdlkpfTTRLADYLVLAKVRQALGfakcqknfy 446
Cdd:cd05904 233 ---MPRfDLEELLAAIERYKVTHLPVVPPIVL-ALV-----------------KSPIVDKYDLSSLRQIMS--------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 447 GAAPMMAETQHFFLGL--NIRLYAGYGLSETSGP---HFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI------GEIC 515
Cdd:cd05904 283 GAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlppnqtGELW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 516 LWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML 595
Cdd:cd05904 363 IRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKEL-IKYKGFQVAPAEL-EALLLSHPEILDAAV 440
|
..
gi 313747580 596 IG 597
Cdd:cd05904 441 IP 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
100-582 |
4.23e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 150.49 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 100 QLPYTVHRMFYEALDKYGDLIALGF----KRQDKWEHISYSQyyLLAR--RAAKGFlkqaHS--------VAILGFNSPE 165
Cdd:PRK07529 22 DLPASTYELLSRAAARHPDAPALSFlldaDPLDRPETWTYAE--LLADvtRTANLL----HSlgvgpgdvVAFLLPNLPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 166 wffsAVGTVFAG---GIVTGIYTTSSPEACQYIAYDCCANVIM-------VDTQKQLEKILKiwkQLPHLKAVVIY---- 231
Cdd:PRK07529 96 ----THFALWGGeaaGIANPINPLLEPEQIAELLRAAGAKVLVtlgpfpgTDIWQKVAEVLA---ALPELRTVVEVdlar 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 232 KEPPPNKMAnvytmEEFMELGNEVPEEALDAIIDTQQ-----------PNQCCVLVYTSGTTGNPKGVMLSQDNITWTAR 300
Cdd:PRK07529 169 YLPGPKRLA-----VPLIRRKAHARILDFDAELARQPgdrlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 301 YGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVntlreveptshmgVPRVWeKIME 380
Cdd:PRK07529 244 LGALLLGLGP----GDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGV-------------IANFW-KIVE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 381 RIQeVAAQSGfirrkmLLWAMSVTLEqnltCP--GSDLkpfttrladylvlakvrQALGFAKCqknfyGAAPMMAET-QH 457
Cdd:PRK07529 306 RYR-INFLSG------VPTVYAALLQ----VPvdGHDI-----------------SSLRYALC-----GAAPLPVEVfRR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 458 FFLGLNIRLYAGYGLSETSGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAEG----------IGEICLWGRTIFMGYL 526
Cdd:PRK07529 353 FEAATGVRIVEGYGLTEATCVSSVNPPDGeRRIGSVGLRLPYQRVRVVILDDAGrylrdcavdeVGVLCIAGPNVFSGYL 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 313747580 527 NmEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 582
Cdd:PRK07529 433 E-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEA 486
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
129-598 |
1.30e-37 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 149.88 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 129 KWEHISYSQYYLLARRAAKGFLKQAHS----VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYiaydcCANVI 204
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNkeerVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCH-----SLNET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 205 MVDT----QKQLEKILKIWKQLPHLKAVVIYKEPPP------NKMAN--VYTMEEFMELGNEVPEEAldaiiDTQQPNQC 272
Cdd:PLN02387 178 EVTTvicdSKQLKKLIDISSQLETVKRVIYMDDEGVdsdsslSGSSNwtVSSFSEVEKLGKENPVDP-----DLPSPNDI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 273 CVLVYTSGTTGNPKGVMLSQDNITWTArygSQAGDIRPAEVQQEVVVSYLPLSHI---AAQIydlwTGIQWGAQVCFAEP 349
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATV---AGVMTVVPKLGKNDVYLAYLPLAHIlelAAES----VMAAVGAAIGYGSP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 350 DAL--------KGSL--VNTLRevePTSHMGVPRVWEKIMERIQE-VAAQSG---------FIRRKMLL---WAMSVTLE 406
Cdd:PLN02387 326 LTLtdtsnkikKGTKgdASALK---PTLMTAVPAILDRVRDGVRKkVDAKGGlakklfdiaYKRRLAAIegsWFGAWGLE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 407 QnltcpgsdlkpfttRLADYLVLAKVRQALG----FAKCqknfyGAAPMMAETQHFflgLNIRLYA----GYGLSETSGP 478
Cdd:PLN02387 403 K--------------LLWDALVFKKIRAVLGgrirFMLS-----GGAPLSGDTQRF---INICLGApigqGYGLTETCAG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 479 HFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI---------GEICLWGRTIFMGYLNMEDKTCEA--IDEEG--WLHTG 545
Cdd:PLN02387 461 ATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTG 540
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 313747580 546 DAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGD 598
Cdd:PLN02387 541 DIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAAL-SVSPYVDNIMVHAD 592
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
256-599 |
8.17e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 141.92 E-value: 8.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 256 PEEALDA-IIDTQQPNQ--CCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAaqiy 332
Cdd:PRK06839 132 LKEIEDRkIDNFVEKNEsaSFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLT----MHDRSIVLLPLFHIG---- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 333 dlwtGIQwgaqvCFAEPDALKGSLVNTLREVEPTSH------------MGVPRVWEKIMERIqevaaqsgfirrkmllwa 400
Cdd:PRK06839 204 ----GIG-----LFAFPTLFAGGVIIVPRKFEPTKAlsmiekhkvtvvMGVPTIHQALINCS------------------ 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 401 msvtleqnltcpgsdlKPFTTRLAdylvlaKVRQalgfakcqknFY-GAAPMMAETQHFFLGLNIRLYAGYGLSETSGPH 479
Cdd:PRK06839 257 ----------------KFETTNLQ------SVRW----------FYnGGAPCPEELMREFIDRGFLFGQGFGMTETSPTV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 480 FMSSPYNYR--LYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDA 552
Cdd:PRK06839 305 FMLSEEDARrkVGSIGKPVLFCDYELIDENKNkvevgEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDE 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 313747580 553 DGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISNAMLIGDQ 599
Cdd:PRK06839 384 DGFVYIVGRKKEMIIS-GGENIYPLEVEQVIN-KLSDVYEVAVVGRQ 428
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
277-646 |
8.25e-36 |
|
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: 138.77 E-value: 8.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 277 YTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSL 356
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDP----DDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRNPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 357 V--NTLREVE---PTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcPGSdlkpfttrlADylvLAK 431
Cdd:cd05944 85 LfdNFWKLVEryrITSLSTVPTVYAALLQV------------------------------PVN---------AD---ISS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 432 VRQALGfakcqknfyGAAPMMAETQHFF---LGLNIrlYAGYGLSETSGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQD 507
Cdd:cd05944 123 LRFAMS---------GAAPLPVELRARFedaTGLPV--VEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIKVLD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 508 AEG----------IGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPV 577
Cdd:cd05944 192 GVGrllrdcapdeVGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGHNIDPA 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313747580 578 PIEEAVkMELPIISNAMLIGDQRKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEfcqRVGSRATTVSEII 646
Cdd:cd05944 270 LIEEAL-LRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARD---HVPERAAVPKHIE 334
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
99-581 |
1.41e-35 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 142.26 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 99 PQLPYTVHRMFYEALDKYGDLIALGFKRQD-KWehiSYSQYYLLARRAAKGFL----KQAHSVAILGFNSPEWffsaVGT 173
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARYPDREALVYRDQGlRW---TYREFNEEVDALAKGLLalgiEKGDRVGIWAPNVPEW----VLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 174 VFAGGIVTGIYTTSSPeacqyiAY------------DCCANVIM--------VDTQKQLEKILKIW-------KQLPHLK 226
Cdd:PRK08315 85 QFATAKIGAILVTINP------AYrlseleyalnqsGCKALIAAdgfkdsdyVAMLYELAPELATCepgqlqsARLPELR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 227 AVVIYKEPPPNKManvYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAg 306
Cdd:PRK08315 159 RVIFLGDEKHPGM---LNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 307 dIRPAEvqQEVVVSYLPLSH--------IAAqiydLWTGiqwGAQVCFAEP-DALKgslvnTLREVEP---TSHMGVPrv 374
Cdd:PRK08315 235 -MKLTE--EDRLCIPVPLYHcfgmvlgnLAC----VTHG---ATMVYPGEGfDPLA-----TLAAVEEercTALYGVP-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 375 wekIMeriqevaaqsgFIrrkmllwAMsvtLEQ------NL-----------TCPGSDLKpfttrladylvlakvrqalg 437
Cdd:PRK08315 298 ---TM-----------FI-------AE---LDHpdfarfDLsslrtgimagsPCPIEVMK-------------------- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 438 faKCQKNFYgaapmMAETQhfflglnIrlyaGYGLSETSGPHFMSS---PYNYRLYSSGKLVPGCRVKLVnqDAEG---- 510
Cdd:PRK08315 334 --RVIDKMH-----MSEVT-------I----AYGMTETSPVSTQTRtddPLEKRVTTVGRALPHLEVKIV--DPETgetv 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313747580 511 ----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEE 581
Cdd:PRK08315 394 prgeQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIEE 467
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
133-597 |
5.84e-35 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 139.37 E-value: 5.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 133 ISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDT 208
Cdd:cd05926 15 LTYADLAELVDDLARQLaalgIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 209 QKQLEKI-LKIWKQLPHLKAVVIYKEPPPNKMANvytmeefmELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKG 287
Cdd:cd05926 95 GELGPASrAASKLGLAILELALDVGVLIRAPSAE--------SLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 288 VMLSQDNITWTARYGSQAGDIRPAEvqQEVVVsyLPLSHIAAQIYDLWTGIQWGAQVCFaePDALKGSLV-NTLREVEPT 366
Cdd:cd05926 167 VPLTHRNLAASATNITNTYKLTPDD--RTLVV--MPLFHVHGLVASLLSTLAAGGSVVL--PPRFSASTFwPDVRDYNAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 367 SHMGVPRVWEKIMERIQE----VAAQSGFIRrkmllwamsvtleqnlTCpGSDLKPFTtrladylvlakvrqalgFAKCQ 442
Cdd:cd05926 241 WYTAVPTIHQILLNRPEPnpesPPPKLRFIR----------------SC-SASLPPAV-----------------LEALE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 443 KNFygAAPMMaETqhfflglnirlyagYGLSETSgpHFMSS----PYNYRLYSSGKLVpGCRVKLVNQDAE-----GIGE 513
Cdd:cd05926 287 ATF--GAPVL-EA--------------YGMTEAA--HQMTSnplpPGPRKPGSVGKPV-GVEVRILDEDGEilppgVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 514 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNA 593
Cdd:cd05926 347 ICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR-GGEKISPLEVDG-VLLSHPAVLEA 424
|
....
gi 313747580 594 MLIG 597
Cdd:cd05926 425 VAFG 428
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-581 |
3.31e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 137.98 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 121 ALGFKRQDKweHISYSQYYLLARRAAKGFL----KQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-I 195
Cdd:PRK12583 36 ALVVRHQAL--RYTWRQLADAVDRLARGLLalgvQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYaL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 196 AYDCCANVIMVDTQKQ------LEKILK----------IWKQLPHLKAVVIY-KEPPPNKMAnvytMEEFMELGNEVPEE 258
Cdd:PRK12583 114 GQSGVRWVICADAFKTsdyhamLQELLPglaegqpgalACERLPELRGVVSLaPAPPPGFLA----WHELQARGETVSRE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 259 ALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQagdiRPAEVQQEVVVSYLPLSHIAAQIYDLWTGI 338
Cdd:PRK12583 190 ALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAE----SLGLTEHDRLCVPVPLYHCFGMVLANLGCM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 339 QWGAQVCFA----EPDAlkgslvnTLREVEP---TSHMGVPRVWEKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLTC 411
Cdd:PRK12583 266 TVGACLVYPneafDPLA-------TLQAVEEercTALYGVPTMFIAELDHPQ---------RGNFDLSSLRTGIMAGAPC 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 412 PGSDLKpfttRLADYLvlakvrqalgfakcqknfygaapMMAETQhfflglnirlyAGYGLSETSGPHFMSS---PYNYR 488
Cdd:PRK12583 330 PIEVMR----RVMDEM-----------------------HMAEVQ-----------IAYGMTETSPVSLQTTaadDLERR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 489 LYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLK 563
Cdd:PRK12583 372 VETVGRTQPHLEVKVVDPDGAtvprgEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSK 451
|
490
....*....|....*...
gi 313747580 564 ELIITaGGENVPPVPIEE 581
Cdd:PRK12583 452 DMIIR-GGENIYPREIEE 468
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
108-597 |
3.12e-33 |
|
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: 134.58 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 108 MFYeALDKYGDLI-ALGFKRQDKWEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 182
Cdd:cd17642 20 LHK-AMKRYASVPgTIAFTDAHTGVNYSYAEYLEMSVRLAEALkkygLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 183 IYTTSSpEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIykepppnkMANVYTMEEFMELGNEVpEEALDA 262
Cdd:cd17642 99 TNDIYN-ERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIII--------LDSKEDYKGYQCLYTFI-TQNLPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 263 IIDTQQ--PN------QCCVLVYTSGTTGNPKGVMLSQDNITwtARYGSQAGDIRPAEVQQEV-VVSYLPLSHiAAQIYD 333
Cdd:cd17642 169 GFNEYDfkPPsfdrdeQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHARDPIFGNQIIPDTaILTVIPFHH-GFGMFT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 334 LWTGIQWGAQVCFaepdalkgslvntlreveptshmgVPRVWEKI-MERIQEVAAQSGF-IRRKMLLWAMSVTLEQnltc 411
Cdd:cd17642 246 TLGYLICGFRVVL------------------------MYKFEEELfLRSLQDYKVQSALlVPTLFAFFAKSTLVDK---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 412 pgsdlkpftTRLADYLVLAKvrqalgfakcqknfyGAAPMMAETQHFF---LGLN-IRlyAGYGLSETSGPHFMSSPYNY 487
Cdd:cd17642 298 ---------YDLSNLHEIAS---------------GGAPLSKEVGEAVakrFKLPgIR--QGYGLTETTSAILITPEGDD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 488 RLYSSGKLVPGCRVKLVNQDAEGI------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGR 561
Cdd:cd17642 352 KPGAVGKVVPFFYAKVVDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDR 431
|
490 500 510
....*....|....*....|....*....|....*.
gi 313747580 562 LKELiITAGGENVPPVPIeEAVKMELPIISNAMLIG 597
Cdd:cd17642 432 LKSL-IKYKGYQVPPAEL-ESILLQHPKIFDAGVAG 465
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
274-601 |
9.55e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 130.89 E-value: 9.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTARYGsQA--GDIRPaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFAEPD 350
Cdd:PRK05605 223 LILYTSGTTGKPKGAQLTHRNLFANAAQG-KAwvPGLGD---GPERVLAALPMFHAYGLTLCLTLAVSIGGElVLLPAPD 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 351 AlkGSLVNTLREVEPTSHMGVPRVWEKIMEriqevAAQsgfirrkmllwamsvtlEQNLTcpgsdlkpfttrladylvLA 430
Cdd:PRK05605 299 I--DLILDAMKKHPPTWLPGVPPLYEKIAE-----AAE-----------------ERGVD------------------LS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 431 KVRQAlgfakcqknFYGAAPMMAETQHFFLGL-NIRLYAGYGLSETSgPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD 507
Cdd:PRK05605 337 GVRNA---------FSGAMALPVSTVELWEKLtGGLLVEGYGLTETS-PIIVGNPMSddRRPGYVGVPFPDTEVRIVDPE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 508 ------AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIE 580
Cdd:PRK05605 407 dpdetmPDGeEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVE 484
|
330 340
....*....|....*....|.
gi 313747580 581 EAVKmELPIISNAMLIGDQRK 601
Cdd:PRK05605 485 EVLR-EHPGVEDAAVVGLPRE 504
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-597 |
1.13e-31 |
|
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: 126.62 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 269 PNQCCVLVYTSGTTGNPKGVMLSQDNItwtARYGSQAGDiRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAE 348
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNI---VNNGYFIGE-RLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 349 P--DALKgslvnTLREVEP---TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnlTCPGSdlkpfttrl 423
Cdd:cd05917 77 PsfDPLA-----VLEAIEKekcTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGA---------PCPPE--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 424 adylVLAKVRQALGFAKCQknfygaapmmaetqhfflglnirlyAGYGLSETSGPHFMSS---PYNYRLYSSGKLVPGCR 500
Cdd:cd05917 134 ----LMKRVIEVMNMKDVT-------------------------IAYGMTETSPVSTQTRtddSIEKRVNTVGRIMPHTE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 501 VKLVnqDAEG--------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGE 572
Cdd:cd05917 185 AKIV--DPEGgivppvgvPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGE 261
|
330 340
....*....|....*....|....*
gi 313747580 573 NVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd05917 262 NIYPREIEEFL-HTHPKVSDVQVVG 285
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
134-597 |
2.59e-31 |
|
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: 128.90 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 134 SYSQYYLLARRAAKGF----LKQAHSVAILGFNSP---EWFFSAVGtvfAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 206
Cdd:cd12119 27 TYAEVAERARRLANALrrlgVKPGDRVATLAWNTHrhlELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 207 DtqKQLEKIL-KIWKQLPHLKAVVIYK---EPPPNKMANVYTMEEFMElgnevpEEALDAIIDTQQPNQCCVLVYTSGTT 282
Cdd:cd12119 104 D--RDFLPLLeAIAPRLPTVEHVVVMTddaAMPEPAGVGVLAYEELLA------AESPEYDWPDFDENTAAAICYTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 283 GNPKGVMLSQDNiTWTARYGSQAGDIRPAEvQQEVVVSYLPLSHIAAqiydlW----TGIQWGAQVCFAEPDALKGSLVN 358
Cdd:cd12119 176 GNPKGVVYSHRS-LVLHAMAALLTDGLGLS-ESDVVLPVVPMFHVNA-----WglpyAAAMVGAKLVLPGPYLDPASLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 359 TLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkMLLwamsvtleQNLTCPGSDLKPfttrladylvLAKVrqALGf 438
Cdd:cd12119 249 LIEREGVTFAAGVPTVWQ-------------------GLL--------DHLEANGRDLSS----------LRRV--VIG- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 439 akcqknfyGAA--PMMAETqhfFLGLNIRLYAGYGLSETS--------GPHFMSSPY----NYRLySSGKLVPGCRVKLV 504
Cdd:cd12119 289 --------GSAvpRSLIEA---FEERGVRVIHAWGMTETSplgtvarpPSEHSNLSEdeqlALRA-KQGRPVPGVELRIV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 505 NQ-------DAEGIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPV 577
Cdd:cd12119 357 DDdgrelpwDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDV-IKSGGEWISSV 434
|
490 500
....*....|....*....|
gi 313747580 578 PIEEAVkMELPIISNAMLIG 597
Cdd:cd12119 435 ELENAI-MAHPAVAEAAVIG 453
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
273-597 |
3.06e-31 |
|
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: 127.41 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 273 CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVvvsyLPLSHIAAQIYDLWTGIQWGAQVCF-AEPDA 351
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHV----LPLHHVHGLVNALLCPLFAGASVEFlPKFDP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 352 lkgSLVNTLREVEP-TSHMGVPRVWEKIMERIQEVAAQSGFIRrkmllwamsvtleqnltcpgsdlkpfttrladylvla 430
Cdd:cd05941 168 ---KEVAISRLMPSiTVFMGVPTIYTRLLQYYEAHFTDPQFAR------------------------------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 431 kvrqALGFAKCQKNFYGAAPMMAETQHFFLGLN-IRLYAGYGLSETSgphfM--SSPYN--YRLYSSGKLVPGCRVKLVN 505
Cdd:cd05941 208 ----AAAAERLRLMVSGSAALPVPTLEEWEAITgHTLLERYGMTEIG----MalSNPLDgeRRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 506 Q------DAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPI 579
Cdd:cd05941 280 EetgeplPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEI 359
|
330
....*....|....*...
gi 313747580 580 EEAVkMELPIISNAMLIG 597
Cdd:cd05941 360 ERVL-LAHPGVSECAVIG 376
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
116-597 |
4.18e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 128.18 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 116 YGDLIALGFKR-QDK----WEH--ISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIY 184
Cdd:PRK06188 14 YGHLLVSALKRyPDRpalvLGDtrLTYGQLADRISRYIQAFealgLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 185 TTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVViykepppnKMANVYTMEEFMELGNEVPEEALDAII 264
Cdd:PRK06188 94 PLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVL--------TLGPVPDGVDLLAAAAKFGPAPLVAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 265 DTQQPNqccVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrPAEVQqevvvsYL---PLSHIAAqiydlwtgiqwg 341
Cdd:PRK06188 166 LPPDIA---GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEW-PADPR------FLmctPLSHAGG------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 342 aqvCFAEPDALKGSLVNTLREVEPTShmgVPRVWEKimERIQEVaaqsgfirrkMLLWAMSVTLeqnLTCPGSdlkpftt 421
Cdd:PRK06188 224 ---AFFLPTLLRGGTVIVLAKFDPAE---VLRAIEE--QRITAT----------FLVPTMIYAL---LDHPDL------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 422 RLADYLVLAKVrqalgfakcqknFYGAAPMMAetqhfflglnIRLYAG-----------YGLSE--------TSGPHFMS 482
Cdd:PRK06188 276 RTRDLSSLETV------------YYGASPMSP----------VRLAEAierfgpifaqyYGQTEapmvitylRKRDHDPD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 483 SPYnyRLYSSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLY 557
Cdd:PRK06188 334 DPK--RLTSCGRPTPGLRVALLDEDgrevAQGeVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYY 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 313747580 558 ITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:PRK06188 411 IVDRKKDMIVT-GGFNVFPREVEDVL-AEHPAVAQVAVIG 448
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
273-582 |
2.57e-30 |
|
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: 122.05 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 273 CVLVYTSGTTGNPKGVMLSQDNITWTARyGSQAgdiRPAEVQQEVVVSYLPLSHIAAQiYDLWTGIQWGAQVCFAEPDAL 352
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAA-GLHS---RLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 353 kgsLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFirRKMLLwamsvtleqnltcpgsdlkpfttrladylvlakv 432
Cdd:cd17630 78 ---LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSL--RAVLL---------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 433 rqalgfakcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiG 512
Cdd:cd17630 119 --------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----G 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 513 EICLWGRTIFMGYLNMEdkTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 582
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAA 246
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
117-584 |
3.16e-30 |
|
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: 125.81 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 117 GDLIALGF--KRQDKWEHISYSQYYLLARRAAKGFL---KQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEA 191
Cdd:cd05931 7 PDRPAYTFldDEGGREETLTYAELDRRARAIAARLQavgKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 192 ---CQYIAYDCCANVIMVDTqkqlekilkiwkqlPHLKAVVIYKEPPPnkmanvytmeEFMELGNEVPEEALDAIIDTQQ 268
Cdd:cd05931 87 aerLAAILADAGPRVVLTTA--------------AALAAVRAFAASRP----------AAGTPRLLVVDLLPDTSAADWP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 269 PNQC-----CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHiaaqiyDLwtgiqwgaq 343
Cdd:cd05931 143 PPSPdpddiAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDP----GDVVVSWLPLYH------DM--------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 344 vcfaepdALKGSLVNTLreveptsHMGVPRVWekiMeriqevaAQSGFIRRKML-LWAMSvtlEQNLTCPGS-----DL- 416
Cdd:cd05931 204 -------GLIGGLLTPL-------YSGGPSVL---M-------SPAAFLRRPLRwLRLIS---RYRATISAApnfayDLc 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 417 -KPFTTRLADYLVLAKVRQALgfakcqkNfyGAAPMMAET-QHF---FLGLNIR---LYAGYGLSE-----TSGPHF--- 480
Cdd:cd05931 257 vRRVRDEDLEGLDLSSWRVAL-------N--GAEPVRPATlRRFaeaFAPFGFRpeaFRPSYGLAEatlfvSGGPPGtgp 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 481 ------------------MSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEG-IGEICLWGRTIFMGYLNMEDKTCE-- 534
Cdd:cd05931 328 vvlrvdrdalagravavaADDPAARELVSCGRPLPDQEVRIVDPEtgrelPDGeVGEIWVRGPSVASGYWGRPEATAEtf 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 313747580 535 ----AIDEEGWLHTGDAGRLdADGFLYITGRLKELIITAgGENVPPVPIEEAVK 584
Cdd:cd05931 408 galaATDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVR-GRNHYPQDIEATAE 459
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
134-597 |
2.29e-29 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 123.17 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 134 SYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG---IYTtsSPEAC-QYIAydccANVIM 205
Cdd:PLN02246 52 TYADVELLSRRVAAGLhklgIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTanpFYT--PAEIAkQAKA----SGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VDTQKQLEKILKIWKQLPHLKAVVIyKEPPPNKManvytmeEFMELGNEVPEEALDAIIDtqqPNQCCVLVYTSGTTGNP 285
Cdd:PLN02246 126 IITQSCYVDKLKGLAEDDGVTVVTI-DDPPEGCL-------HFSELTQADENELPEVEIS---PDDVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 286 KGVMLSQDN-ITWTArygsqagdirpaevQQ-------------EVVVSYLPLSHIAAQIYDLWTGIQWGAQVCfaepda 351
Cdd:PLN02246 195 KGVMLTHKGlVTSVA--------------QQvdgenpnlyfhsdDVILCVLPMFHIYSLNSVLLCGLRVGAAIL------ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 352 lkgslvntlreveptshmgvprvwekIMERIqEVAAQSGFIRRKMLLWAMSV-----TLEQNltcpgsdlkPFTTRlADy 426
Cdd:PLN02246 255 --------------------------IMPKF-EIGALLELIQRHKVTIAPFVppivlAIAKS---------PVVEK-YD- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 427 lvLAKVRQALGfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSEtSGP------HFMSSPYNYRLYSSGKLVPG 498
Cdd:PLN02246 297 --LSSIRMVLS---------GAAPLGKELEDAFRAKlpNAVLGQGYGMTE-AGPvlamclAFAKEPFPVKSGSCGTVVRN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 499 CRVKLVNQDAeGI-------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGG 571
Cdd:PLN02246 365 AELKIVDPET-GAslprnqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 443
|
490 500
....*....|....*....|....*.
gi 313747580 572 EnVPPVPIeEAVKMELPIISNAMLIG 597
Cdd:PLN02246 444 Q-VAPAEL-EALLISHPSIADAAVVP 467
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
130-717 |
2.50e-29 |
|
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: 123.31 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 130 WEHISYSQYYLLARRAAKGFLKQAHS----VAILGFNSPEWFFSAVGTVFAG---GIVTGIYTTSSPE--ACQYIAYDCC 200
Cdd:cd05921 23 WRRVTYAEALRQVRAIAQGLLDLGLSaerpLLILSGNSIEHALMALAAMYAGvpaAPVSPAYSLMSQDlaKLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 201 ANVIMVDTQKQLEKILKIWKqLPHLKAVVIYKEPPPNKMANvytmeeFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSG 280
Cdd:cd05921 103 PGLVFAQDAAPFARALAAIF-PLGTPLVVSRNAVAGRGAIS------FAELAATPPTAAVDAAFAAVGPDTVAKFLFTSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 281 TTGNPKGVMLSQDNITwtaryGSQAGDIRPAEVQQE---VVVSYLPLSHIAAQIYD----LWTG----IQWGAQVcfaeP 349
Cdd:cd05921 176 STGLPKAVINTQRMLC-----ANQAMLEQTYPFFGEeppVLVDWLPWNHTFGGNHNfnlvLYNGgtlyIDDGKPM----P 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 350 DALKGSLVNtLREVEPTSHMGVPRVWEKI---MERiQEVAAQSGFIRRKMLLWAmsvtleqnltcpGSDLKPFT-TRLad 425
Cdd:cd05921 247 GGFEETLRN-LREISPTVYFNVPAGWEMLvaaLEK-DEALRRRFFKRLKLMFYA------------GAGLSQDVwDRL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 426 ylvlakvrQALGFAKCqknfygaapmmaetqhfflGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN 505
Cdd:cd05921 311 --------QALAVATV-------------------GERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 506 QDaeGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRL----DADGFLYITGRLKELIITAGGENVPPVPIE- 580
Cdd:cd05921 364 SG--GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGPLRa 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 581 EAVKMELPIISNAMLIGDQRKFLSMLLTlkctldPDTSDqtdnlteqamefCQR-VGSRATTVSEIIekKDEAVYQAIEE 659
Cdd:cd05921 442 RAVAACAPLVHDAVVAGEDRAEVGALVF------PDLLA------------CRRlVGLQEASDAEVL--RHAKVRAAFRD 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 313747580 660 GIRRVNMNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQE 717
Cdd:cd05921 502 RLAALNGEATGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
274-597 |
2.79e-29 |
|
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: 120.91 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAepDALK 353
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT----EDDNWLCALPLFHISG-LSILMRSVIYGMTVYLV--DKFD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 354 GSLVNTLREVEPTSHMG-VPRVWEKIMERIQEVAAQSgfiRRKMLLWAmsvtleqnltcpgsdlkpfttrladylvlakv 432
Cdd:cd05912 154 AEQVLHLINSGKVTIISvVPTMLQRLLEILGEGYPNN---LRCILLGG-------------------------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 433 rqalGFAkcqknfygAAPMMAETQHfflgLNIRLYAGYGLSETSGPHFMSSPYNY--RLYSSGKLVPGCRVKLVN--QDA 508
Cdd:cd05912 199 ----GPA--------PKPLLEQCKE----KGIPVYQSYGMTETCSQIVTLSPEDAlnKIGSAGKPLFPVELKIEDdgQPP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 509 EGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEAVKmELP 588
Cdd:cd05912 263 YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLL-SHP 339
|
....*....
gi 313747580 589 IISNAMLIG 597
Cdd:cd05912 340 AIKEAGVVG 348
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
267-600 |
2.79e-29 |
|
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: 121.33 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 267 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqeVVVSylPLSHIAAQIYDLWTGIQWGAQVCF 346
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF--LVAS--PMAHQTGFVYGFTLPLLLGAPVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 347 AEP-DALKGslVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRrKMLlwamsvtleqnltCPGSDLKPFTTRLAD 425
Cdd:cd05903 166 QDIwDPDKA--LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLR-TFV-------------CGGATVPRSLARRAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 426 YLVLAKVRQALGfakcqknfygaapmMAETQHFFlglnirlyagyGLSEtsgphfmSSPYNYRLYSSGKLVPGCRVKLVN 505
Cdd:cd05903 230 ELLGAKVCSAYG--------------STECPGAV-----------TSIT-------PAPEDRRLYTDGRPLPGVEIKVVD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 506 QD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAiDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIE 580
Cdd:cd05903 278 DTgatlaPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVE 355
|
330 340
....*....|....*....|..
gi 313747580 581 EAVkMELPIISNAMLIG--DQR 600
Cdd:cd05903 356 DLL-LGHPGVIEAAVVAlpDER 376
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
271-599 |
5.04e-29 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 120.63 E-value: 5.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 271 QCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFAEPD 350
Cdd:TIGR01923 112 QIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGF----TEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 351 A-LKGSLVNtlrevEPTSHMG-VPrvwekimeriqevaaqsgfirrKMLLWamsvTLEQNLTCpgsdlkpfttrladyLV 428
Cdd:TIGR01923 187 NqLLEMIAN-----ERVTHISlVP----------------------TQLNR----LLDEGGHN---------------EN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 429 LAKVRqaLGFAKCqknfygAAPMMAETQHfflgLNIRLYAGYGLSETSGPHFMSSP--YNYRLySSGKLVPGCRVKLVNQ 506
Cdd:TIGR01923 221 LRKIL--LGGSAI------PAPLIEEAQQ----YGLPIYLSYGMTETCSQVTTATPemLHARP-DVGRPLAGREIKIKVD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 507 DAEGIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKmE 586
Cdd:TIGR01923 288 NKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIIS-GGENIYPEEIETVLY-Q 364
|
330
....*....|...
gi 313747580 587 LPIISNAMLIGDQ 599
Cdd:TIGR01923 365 HPGIQEAVVVPKP 377
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
274-597 |
1.05e-28 |
|
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: 117.37 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAAQIYDLWTGIQWGAQVC---FAEPD 350
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVY----LNMLPLFHIAGLNLALATFHAGGANVVmekFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 351 ALKgslvntLREVEPTSHMG--VPrvwekIMERIQEVAAQSGfirrkmllwamsvtleqnltcpgsdlkpfttrladyLV 428
Cdd:cd17637 80 ALE------LIEEEKVTLMGsfPP-----ILSNLLDAAEKSG------------------------------------VD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 429 LAKVRQALGFAkcqknfygaAPmmaETQHFFLGL-NIRLYAGYGLSETSGPHFMSsPYNYRLYSSGKLVPGCRVKLVNQD 507
Cdd:cd17637 113 LSSLRHVLGLD---------AP---ETIQRFEETtGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 508 -----AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADGFLYITGRL--KELIITaGGENVPPVPIE 580
Cdd:cd17637 180 drpvpAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVE 257
|
330
....*....|....*..
gi 313747580 581 EAVkMELPIISNAMLIG 597
Cdd:cd17637 258 KVI-LEHPAIAEVCVIG 273
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
115-597 |
1.22e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 120.81 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 115 KYGDLIALGFkRQDKWehiSYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPE 190
Cdd:PRK08316 23 RYPDKTALVF-GDRSW---TYAELDAAVNRVAAALldlgLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 191 ACQYIAYDCCANVIMVDTQ--KQLEKILKIWKQLPHLKAVVIYKEPPPNKMANvytmeeFMELGNEVPEEALDAIIDTQQ 268
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPAlaPTAEAALALLPVDTLILSLVLGGREAPGGWLD------FADWAEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 269 PNQccvLVYTSGTTGNPKGVMLSQDNITWtaRYGSQ--AGDIRPAEVQqevvVSYLPLSHiAAQIY-----DLWTGiqwG 341
Cdd:PRK08316 173 LAQ---ILYTSGTESLPKGAMLTHRALIA--EYVSCivAGDMSADDIP----LHALPLYH-CAQLDvflgpYLYVG---A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 342 AQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrkmllwamsVTLeqnLTCPGSDlkpfTT 421
Cdd:PRK08316 240 TNVILDAPDP--ELILRTIEAERITSFFAPPTVW---------------------------ISL---LRHPDFD----TR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 422 RLadylvlakvrQALgfakcQKNFYGAAPM----MAETQHFFLGLniRLYAGYGLSETSGPHFMSSPYNY--RLYSSGKL 495
Cdd:PRK08316 284 DL----------SSL-----RKGYYGASIMpvevLKELRERLPGL--RFYNCYGQTEIAPLATVLGPEEHlrRPGSAGRP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 496 VPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaG 570
Cdd:PRK08316 347 VLNVETRVVDDDgndvAPGeVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-G 424
|
490 500
....*....|....*....|....*..
gi 313747580 571 GENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:PRK08316 425 GENVASREVEEAL-YTHPAVAEVAVIG 450
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
104-597 |
6.84e-28 |
|
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: 118.35 E-value: 6.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 104 TVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGI 179
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDR----TLTYAALSERVLALASGLrglgLARGERVAIYLDKRLETVTAMFGAALAGGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 180 VTGIYTTSSPEACQYIAYDCCANvIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKmanvytmeEFMELGNEVPEEA 259
Cdd:TIGR03098 77 FVPINPLLKAEQVAHILADCNVR-LLVTSSERLDLLHPALPGCHDLRTLIIVGDPAHAS--------EGHPGEEPASWPK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 260 LDAIIDTQQPNQC------CVLvYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqEVVVSYLPLSHIAAQiYD 333
Cdd:TIGR03098 148 LLALGDADPPHPVidsdmaAIL-YTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPD----DRLLAVLPLSFDYGF-NQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 334 LWTGIQWGAQVCFAEPdALKGSLVNTLREVEPTSHMGVPRVWEKIME-RIQEVAAQSgfIRRkmllwamsvtleqnLTCP 412
Cdd:TIGR03098 222 LTTAFYVGATVVLHDY-LLPRDVLKALEKHGITGLAAVPPLWAQLAQlDWPESAAPS--LRY--------------LTNS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 413 GSDLKPFTtrladylvLAKVRQALGfakcqknfygaapmmaetqhfflglNIRLYAGYGLSETsgphFMSS---P--YNY 487
Cdd:TIGR03098 285 GGAMPRAT--------LSRLRSFLP-------------------------NARLFLMYGLTEA----FRSTylpPeeVDR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 488 RLYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCE----AIDEEGWLH-------TGDAGRLD 551
Cdd:TIGR03098 328 RPDSIGKAIPNAEVLVLREDGSecapgEEGELVHRGALVAMGYWNDPEKTAErfrpLPPFPGELHlpelavwSGDTVRRD 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 313747580 552 ADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:TIGR03098 408 EEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA-YATGLVAEAVAFG 451
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
131-597 |
1.22e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 117.29 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAkGFLK-----QAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 205
Cdd:PRK06145 26 QEISYAEFHQRILQAA-GMLHargigQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VDTQkqlekiLKIWKQLPHLKAVViykepppNKMANVYTmEEFMELGNEVPEEALDAiidtqqPNQCCVLVYTSGTTGNP 285
Cdd:PRK06145 105 VDEE------FDAIVALETPKIVI-------DAAAQADS-RRLAQGGLEIPPQAAVA------PTDLVRLMYTSGTTDRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 286 KGVMLSQDNITW-----TARYGSQAGDirpaevqQEVVVSylPLSHIAAqiYDLwTGIQWGAQvcfaepdalkGSLVNTL 360
Cdd:PRK06145 165 KGVMHSYGNLHWksidhVIALGLTASE-------RLLVVG--PLYHVGA--FDL-PGIAVLWV----------GGTLRIH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 361 REVEPtshmgvprvwEKIMERIQEvaaqsgfiRRKMLLWAMSVTLEQNLTCPgsdlkpftTRlaDYLVLAKVRQALGFAK 440
Cdd:PRK06145 223 REFDP----------EAVLAAIER--------HRLTCAWMAPVMLSRVLTVP--------DR--DRFDLDSLAWCIGGGE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 441 cqknfygAAPMMAETQHFFLGLNIRLYAGYGLSET-SGPHFMSSPYNY-RLYSSGKLVPGCRVKLVNQDAEGI-----GE 513
Cdd:PRK06145 275 -------KTPESRIRDFTRVFTRARYIDAYGLTETcSGDTLMEAGREIeKIGSTGRALAHVEIRIADGAGRWLppnmkGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 514 ICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNA 593
Cdd:PRK06145 348 ICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVI-YELPEVAEA 424
|
....
gi 313747580 594 MLIG 597
Cdd:PRK06145 425 AVIG 428
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
140-628 |
1.42e-27 |
|
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: 117.05 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 140 LLARRAAKgFLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILKIW 219
Cdd:cd05909 19 ALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL--TSKQFIEKLKLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 220 KQLPHLK-AVVIYKEpppNKMANVYTMEE-FMELGNEVPEEALDAI--IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNI 295
Cdd:cd05909 96 HLFDVEYdARIVYLE---DLRAKISKADKcKAFLAGKFPPKWLLRIfgVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 296 TWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAePDALKG-SLVNTLREVEPTSHMGVPRV 374
Cdd:cd05909 173 LANVEQITAIFDPNP----EDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-PNPLDYkKIPELIYDKKATILLGTPTF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 375 WekimeriqevaaqSGFIRRKMllwamsvtleqnltcpGSDLkpFTTRLAdylvlakvrqalgfakcqknFYGAAPMMAE 454
Cdd:cd05909 248 L-------------RGYARAAH----------------PEDF--SSLRLV--------------------VAGAEKLKDT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 455 TQHFFLGL-NIRLYAGYGLSETSGPHFMSSP-YNYRLYSSGKLVPGCRVKLVnqDAEG-----IGE---ICLWGRTIFMG 524
Cdd:cd05909 277 LRQEFQEKfGIRILEGYGTTECSPVISVNTPqSPNKEGTVGRPLPGMEVKIV--SVETheevpIGEgglLLVRGPNVMLG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 525 YLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEAVKMELPIISN--AMLIGDQRKF 602
Cdd:cd05909 355 YLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRF-AKIAGEMVSLEAIEDILSEILPEDNEvaVVSVPDGRKG 432
|
490 500
....*....|....*....|....*.
gi 313747580 603 LSMLLtlkCTLDPDTSdqTDNLTEQA 628
Cdd:cd05909 433 EKIVL---LTTTTDTD--PSSLNDIL 453
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
212-600 |
3.53e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 116.39 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 212 LEKILKIWKQLPHLKAVVIykepppnkmanvytmeeFMELGNEVPEEALDAIIDTQQPNQ----------CCVLvYTSGT 281
Cdd:PRK06087 137 VDLILPLQNQLPQLQQIVG-----------------VDKLAPATSSLSLSQIIADYEPLTtaitthgdelAAVL-FTSGT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 282 TGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIaaqiydlwTGIQWGAQVCFaepdaLKGSLVntlr 361
Cdd:PRK06087 199 EGLPKGVMLTHNNILASERAYCARLNL----TWQDVFMMPAPLGHA--------TGFLHGVTAPF-----LIGARS---- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 362 eveptshmgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVTleqnltcpgsdlkPFTtrladYLVLAKVRQ------A 435
Cdd:PRK06087 258 ----------------VLLDIFTPDACLALLEQQRCTCMLGAT-------------PFI-----YDLLNLLEKqpadlsA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 436 LGFAKCqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFM---SSPYNYRLYSSGKLVPGCRVKLVNQDAEGI- 511
Cdd:PRK06087 304 LRFFLC-----GGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVvnlDDPLSRFMHTDGYAAAGVEIKVVDEARKTLp 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 512 ----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMEL 587
Cdd:PRK06087 378 pgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSREVEDIL-LQH 455
|
410
....*....|....*
gi 313747580 588 PIISNAMLIG--DQR 600
Cdd:PRK06087 456 PKIHDACVVAmpDER 470
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
141-597 |
8.64e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 114.67 E-value: 8.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 141 LARRAAKGFLKQAHSVAILGFNSPEWFFSavgtvfaggivtgIYttsspeACQYIAydccANVIMVDTQKQLEKILkiWk 220
Cdd:PRK03640 40 VAGKLAALGVKKGDRVALLMKNGMEMILV-------------IH------ALQQLG----AVAVLLNTRLSREELL--W- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 221 QLPHLKA-VVIYKEPPPNKMANVY--TMEEFMELGNEVPEealdaIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITW 297
Cdd:PRK03640 94 QLDDAEVkCLITDDDFEAKLIPGIsvKFAELMNGPKEEAE-----IQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 298 TAR-----YGSQAGDIRPAEVqqevvvsylPLSHIAAqIYDLWTGIQWGAQVCFAEP-DALKgslVNTLREVEPTSHMG- 370
Cdd:PRK03640 169 SAVgsalnLGLTEDDCWLAAV---------PIFHISG-LSILMRSVIYGMRVVLVEKfDAEK---INKLLQTGGVTIISv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 371 VPRVWEKIMERIQEVAAQSGFirRKMLLW---AMSVTLEQnltcpgsdlkpfttrladylvlakvrqalgfakCQknfyg 447
Cdd:PRK03640 236 VSTMLQRLLERLGEGTYPSSF--RCMLLGggpAPKPLLEQ---------------------------------CK----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 448 aapmmaetQHfflglNIRLYAGYGLSETSG------PHFMSSpynyRLYSSGKLVPGCRVKLVNQDAEG----IGEICLW 517
Cdd:PRK03640 276 --------EK-----GIPVYQSYGMTETASqivtlsPEDALT----KLGSAGKPLFPCELKIEKDGVVVppfeEGEIVVK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 518 GRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNAMLIG 597
Cdd:PRK03640 339 GPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEI-EEVLLSHPGVAEAGVVG 415
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
110-597 |
1.41e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 114.82 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 110 YEALDKY----GDLIALGFKRQDKWE-HISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 180
Cdd:COG0365 12 YNCLDRHaegrGDKVALIWEGEDGEErTLTYAELRREVNRFANALralgVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 181 TGIYTTSSPEACQYIAYDCCANVIMVD--------TQKQLEKILKIWKQLPHLKAVVIYKEP-PPNKMANVYTMEEFMEL 251
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITAdgglrggkVIDLKEKVDEALEELPSLEHVIVVGRTgADVPMEGDLDWDELLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 252 -GNEVPEEALDAiidtqqpNQCCVLVYTSGTTGNPKGVMLSQD----NITWTARYGSqagDIRPAEVqqevvvsYLPLSH 326
Cdd:COG0365 172 aSAEFEPEPTDA-------DDPLFILYTSGTTGKPKGVVHTHGgylvHAATTAKYVL---DLKPGDV-------FWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 327 IAaqiydlWTGIQW---------GAQVCFAE-----PDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFI 392
Cdd:COG0365 235 IG------WATGHSyivygpllnGATVVLYEgrpdfPDP--GRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 393 RRKMLlwaMSVtleqnltcpGSDLKPfttrladyLVLAKVRQALGfakcqknfygaapmmaetqhfflglnIRLYAGYGL 472
Cdd:COG0365 307 SLRLL---GSA---------GEPLNP--------EVWEWWYEAVG--------------------------VPIVDGWGQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 473 SETSGpHFMSSPYNYRLY--SSGKLVPGCRVKLVnqDAEG-------IGEICL---W-GrtIFMGYLNMEDKTCEAI--D 537
Cdd:COG0365 341 TETGG-IFISNLPGLPVKpgSMGKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPERYRETYfgR 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 538 EEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:COG0365 416 FPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESAL-VSHPAVAEAAVVG 473
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
128-582 |
1.75e-26 |
|
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: 114.00 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 128 DKWEHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANV 203
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALralgVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 204 IMVdTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMAnvytmeeFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTG 283
Cdd:cd05959 105 VVV-SGELAPVLAAALTKSEHTLVVLIVSGGAGPEAG-------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 284 NPKGVMLSQDNITWTAR-YGSQAGDIRPAevqqEVVVSYLPLSHI----AAQIYDLWTGiqwGAQVCFAE---PDAlkgs 355
Cdd:cd05959 177 RPKGVVHLHADIYWTAElYARNVLGIRED----DVCFSAAKLFFAyglgNSLTFPLSVG---ATTVLMPErptPAA---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 356 LVNTLREVEPTSHMGVPRVWEKIMEriQEVAAQSGFIRRKMLLWAMSVTleqnltcPGSDLKPFTTRladylvlakvrqa 435
Cdd:cd05959 246 VFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEAL-------PAEVGERWKAR------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 436 lgfakcqknfygaapmmaetqhffLGLNIRlyagYGLSETSGPH-FMSS-PYNYRLYSSGKLVPGCRVKLVNQDAE---- 509
Cdd:cd05959 304 ------------------------FGLDIL----DGIGSTEMLHiFLSNrPGRVRYGTTGKPVPGYEVELRDEDGGdvad 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313747580 510 -GIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEA 582
Cdd:cd05959 356 gEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDM-LKVSGIWVSPFEVESA 427
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
100-664 |
2.06e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 114.36 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 100 QLPYTV-------HRMFYEALDKYGDLIALGFKRQDkwehISYSQYYLLARRAA----KGFLKQAHSVAILGFNSPEWFF 168
Cdd:PRK06710 14 EIPSTIsydiqplHKYVEQMASRYPEKKALHFLGKD----ITFSVFHDKVKRFAnylqKLGVEKGDRVAIMLPNCPQAVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 169 SAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM-----------VDTQKQLEKIL--KIWKQLPHLKAVV--IYKE 233
Cdd:PRK06710 90 GYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKIEHVIvtRIADFLPFPKNLLypFVQK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 234 PPPNKMANVyTMEEFMELGNEVPEE---ALDAIIDTQqpNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAgdIRP 310
Cdd:PRK06710 170 KQSNLVVKV-SESETIHLWNSVEKEvntGVEVPCDPE--NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW--LYN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 311 AEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKgSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaqsg 390
Cdd:PRK06710 245 CKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMK-MVFEAIKKHKVTLFPGAPTIYIALLN---------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 391 firrkmllwamsvtleqnltcpgsdlkpfTTRLADYLVlAKVRQALGfakcqknfyGAAPMMAETQHFFLGLNI-RLYAG 469
Cdd:PRK06710 314 -----------------------------SPLLKEYDI-SSIRACIS---------GSAPLPVEVQEKFETVTGgKLVEG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 470 YGLSEtsgphfmSSPYNYRLYSSGKLVPGC-RVKLVNQDAE-------------GIGEICLWGRTIFMGYLNMEDKTCeA 535
Cdd:PRK06710 355 YGLTE-------SSPVTHSNFLWEKRVPGSiGVPWPDTEAMimsletgealppgEIGEIVVKGPQIMKGYWNKPEETA-A 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 536 IDEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEaVKMELPIISNAMLIGDQRKFLSMLLTLKCTLDP 615
Cdd:PRK06710 427 VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEE-VLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE 504
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 313747580 616 DTSDQTDNLTEQAMEFCQrvgsrATTVSEIIEKKDEAVYQAIEEGIRRV 664
Cdd:PRK06710 505 GTECSEEELNQFARKYLA-----AYKVPKVYEFRDELPKTTVGKILRRV 548
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
131-590 |
2.77e-26 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 113.53 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAKGfLKQAH----SVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSpeacqyiAYDCCANvimv 206
Cdd:cd05906 38 EFQSYQDLLEDARRLAAG-LRQLGlrpgDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPP-------TYDEPNA---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 207 dtqkQLEKILKIWKQLPhlKAVVIykepppnkmANVYTMEEFMELGNE---------VPEEALDAIIDT----QQPNQCC 273
Cdd:cd05906 106 ----RLRKLRHIWQLLG--SPVVL---------TDAELVAEFAGLETLsglpgirvlSIEELLDTAADHdlpqSRPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAA----QIYDLWTGIQwgaQVcfaep 349
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTP----QDVFLNWVPLDHVGGlvelHLRAVYLGCQ---QV----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 350 dalkgslvNTlrevePTSHM-GVPRVWEKIMERIQevAAQSgfirrkmllWA----MSVTLEQnltcpgsdLKPFTTRLA 424
Cdd:cd05906 239 --------HV-----PTEEIlADPLRWLDLIDRYR--VTIT---------WApnfaFALLNDL--------LEEIEDGTW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 425 DylvLAKVRQALGfakcqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSET-SGPHFMSSPYNY------RLY 490
Cdd:cd05906 287 D---LSSLRYLVN---------AGEAVVAKTIRRLLrllepyGLPPDaIRPAFGMTETcSGVIYSRSFPTYdhsqalEFV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 491 SSGKLVPGCRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDaDGFLYITGRLKEL 565
Cdd:cd05906 355 SLGRPIPGVSMRIVDDEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDT 433
|
490 500
....*....|....*....|....*
gi 313747580 566 IITaGGENVPPVPIEEAVKmELPII 590
Cdd:cd05906 434 IIV-NGVNYYSHEIEAAVE-EVPGV 456
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
134-583 |
2.90e-25 |
|
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: 110.08 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 134 SYSQYYLLARRAAKGFLKQAHS----VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ 209
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISrgdtVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 210 kqlekilkiwkqlphlkavviykepppnkmanvYTMEEFMELGN-----EVPEEALDAIidtqqpnqccVLVYTSGTTGN 284
Cdd:cd12118 111 ---------------------------------FEYEDLLAEGDpdfewIPPADEWDPI----------ALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 285 PKGVMLSQDNItwtarYGSQAGDIRPAEVQQEVVvsYL---PLSHIAAqiydlWTGIqWGaqvcfaePDALKGSLVnTLR 361
Cdd:cd12118 148 PKGVVYHHRGA-----YLNALANILEWEMKQHPV--YLwtlPMFHCNG-----WCFP-WT-------VAAVGGTNV-CLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 362 EVEPtshmgvPRVWEKI-MERIQEVAAqsgfirrkmllwamSVTLEQNLT-CPGSDLKPFTTRladylvlakVRQALGfa 439
Cdd:cd12118 207 KVDA------KAIYDLIeKHKVTHFCG--------------APTVLNMLAnAPPSDARPLPHR---------VHVMTA-- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 440 kcqknfyGAAP---MMAETQHfflgLNIRLYAGYGLSETSGPHF----------MSSPYNYRLYS----SGKLVPGCRV- 501
Cdd:cd12118 256 -------GAPPpaaVLAKMEE----LGFDVTHVYGLTETYGPATvcawkpewdeLPTEERARLKArqgvRYVGLEEVDVl 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 502 -----KLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPP 576
Cdd:cd12118 325 dpetmKPVPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISS 402
|
....*..
gi 313747580 577 VPIEEAV 583
Cdd:cd12118 403 VEVEGVL 409
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
104-597 |
3.71e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 110.16 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 104 TVHRMFYEALDKYGDLIALGFK-RQDKWEHISYSQYYLLARRAAKGFL----KQAHSVAILGFNSPEWFFSAVGTVFAGG 178
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFEsSGGVVRRYSYLELNEEINRTANLFYslgiRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 179 IVTGIYTTSSPEACQYIAYDCCANVIMVDtqkqlEKILKIWKQLPH-----LKAVVIYKEPPPnKMANVYtmeEFMELGN 253
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTS-----AQFYPMYRQIQQedatpLRHICLTRVALP-ADDGVS---SFTQLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 254 EVPEEALDAII----DTQQpnqccvLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAA 329
Cdd:PRK08008 159 QQPATLCYAPPlstdDTAE------ILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALR----DDDVYLTVMPAFHIDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 330 QiydlwtgiqwgaqvCFAEPDALkgSLVNTLREVEPTShmgVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNl 409
Cdd:PRK08008 229 Q--------------CTAAMAAF--SAGATFVLLEKYS---ARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQH- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 410 tcpgsdlkpfttRLAD---YLVLAKvrqalgfakcqknfygaapmmAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYN 486
Cdd:PRK08008 289 ------------CLREvmfYLNLSD---------------------QEKDAFEERFGVRLLTSYGMTETIVGIIGDRPGD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 487 YRLYSS-GKLVPGCRVKLVNQD-----AEGIGEICLWG---RTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLY 557
Cdd:PRK08008 336 KRRWPSiGRPGFCYEAEIRDDHnrplpAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFY 415
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 313747580 558 ITGRlKELIITAGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:PRK08008 416 FVDR-RCNMIKRGGENVSCVELENII-ATHPKIQDIVVVG 453
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
76-692 |
1.38e-24 |
|
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: 108.70 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 76 APEEALwtTRADGRVRLRIdpscPQLPYTVhrmfyeaLDKYGDLIALGFKRQD----------------KWEHISYSQYY 139
Cdd:cd17632 8 APLEAV--TEAIRRPGLRL----AQIIATV-------MTGYADRPALGQRATElvtdpatgrttlrllpRFETITYAELW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 140 -----LLARRAAKGFLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkQLEK 214
Cdd:cd17632 75 ervgaVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAE-HLDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 215 ILKIWKQLPHLKAVVIY----------------KEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPnqCCVLVYT 278
Cdd:cd17632 154 AVEAVLEGGTPPRLVVFdhrpevdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDP--LALLIYT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 279 SGTTGNPKGVMLSQDNIT--WTARYGSQAGDIRPAevqqeVVVSYLPLSHIAAQIYdLWTGIQWGAQVCF-AEPDAlkGS 355
Cdd:cd17632 232 SGSTGTPKGAMYTERLVAtfWLKVSSIQDIRPPAS-----ITLNFMPMSHIAGRIS-LYGTLARGGTAYFaAASDM--ST 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 356 LVNTLREVEPTSHMGVPRVWEKIMERIQEVaaqsgfIRRKMLLWAMSVTLEQNltcpgsdlkpfttrladylVLAKVRQA 435
Cdd:cd17632 304 LFDDLALVRPTELFLVPRVCDMLFQRYQAE------LDRRSVAGADAETLAER-------------------VKAELRER 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 436 LGFAKCQKNFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSGphfmsspynyrLYSSGKLV--PGCRVKLVNQDAEGI- 511
Cdd:cd17632 359 VLGGRLLAAVCGSAPLSAEMKAFMESlLDLDLHDGYGSTEAGA-----------VILDGVIVrpPVLDYKLVDVPELGYf 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 512 --------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDA-GRLDADGFLYITgRLKELIITAGGENVpPVPIEEA 582
Cdd:cd17632 428 rtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVmAELGPDRLVYVD-RRNNVLKLSQGEFV-TVARLEA 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 583 VKMELPIISNAMLIGD-QRKFLSMLLTlkctldPdTSDQTDNLTEQAMefcqrvgsRAttvseiiekkdeavyqAIEEGI 661
Cdd:cd17632 506 VFAASPLVRQIFVYGNsERAYLLAVVV------P-TQDALAGEDTARL--------RA----------------ALAESL 554
|
650 660 670
....*....|....*....|....*....|..
gi 313747580 662 RRVNMNAAARPYHIQKWAILERD-FSISGGEL 692
Cdd:cd17632 555 QRIAREAGLQSYEIPRDFLIETEpFTIANGLL 586
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
261-597 |
2.16e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 107.82 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 261 DAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQDNITWTARygSQAGDIRPAEVQQEVVVSYLPLSHIAaqiydlwtGIQw 340
Cdd:PRK07470 157 NAAVDHDDP---CWFFFTSGTTGRPKAAVLTHGQMAFVIT--NHLADLMPGTTEQDASLVVAPLSHGA--------GIH- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 341 gaqvcfaepdalkgSLVNTLREVE----PTSHMGVPRVWEKIME-RIQEVAAQSGFIrrKMLLWAMSVTleqnlTCPGSD 415
Cdd:PRK07470 223 --------------QLCQVARGAAtvllPSERFDPAEVWALVERhRVTNLFTVPTIL--KMLVEHPAVD-----RYDHSS 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 416 LKpfttrladYLVlakvrqalgfakcqknfYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSG------PHFMSS---Py 485
Cdd:PRK07470 282 LR--------YVI-----------------YAGAPMYRADQKRALAkLGKVLVQYFGLGEVTGnitvlpPALHDAedgP- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 486 NYRLYSSGKLVPGCRVKLvnQDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYI 558
Cdd:PRK07470 336 DARIGTCGFERTGMEVQI--QDDEGrelppgeTGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYI 412
|
330 340 350
....*....|....*....|....*....|....*....
gi 313747580 559 TGRLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG 597
Cdd:PRK07470 413 TGRASDMYIS-GGSNVYPREIEEKLLTH-PAVSEVAVLG 449
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
274-645 |
6.29e-24 |
|
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: 105.60 E-value: 6.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK 353
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA----DDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 354 GSLVNTLREVEPTSHMGVPRVWEkIMERIqevaaqsgfIRRKMLLwamsVTLeQNLTCPGSDLKP-FTTRLADYLVLAkv 432
Cdd:cd05922 196 DAFWEDLREHGATGLAGVPSTYA-MLTRL---------GFDPAKL----PSL-RYLTQAGGRLPQeTIARLRELLPGA-- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 433 rqalgfakcqknfygaapmmaetqhfflglniRLYAGYGLSETSG------PHFMSSpynyRLYSSGKLVPGCRVKLVNQ 506
Cdd:cd05922 259 --------------------------------QVYVMYGQTEATRrmtylpPERILE----KPGSIGLAIPGGEFEILDD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 507 D----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEE 581
Cdd:cd05922 303 DgtptPPGePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEA 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 582 AVkMELPIISNAMLIGDQRKF---LSMLLTLKCTLDPDtsDQTDNLTEQAMEFcqRVGSRATTVSEI 645
Cdd:cd05922 382 AA-RSIGLIIEAAAVGLPDPLgekLALFVTAPDKIDPK--DVLRSLAERLPPY--KVPATVRVVDEL 443
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
269-600 |
8.99e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 105.66 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 269 PNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA- 347
Cdd:PRK09088 134 PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVD----AHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSn 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 348 --EPDALKGSLVNTLREVepTSHMGVPrvweKIMERIQevaAQSGFirrkmllwamsvtleqnltcPGSDLKPFTtrlad 425
Cdd:PRK09088 210 gfEPKRTLGRLGDPALGI--THYFCVP----QMAQAFR---AQPGF--------------------DAAALRHLT----- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 426 ylvlakvrqALgfakcqknFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMS---SPYNYRLYSSGKLVPGCRVK 502
Cdd:PRK09088 256 ---------AL--------FTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVFGMSvdcDVIRAKAGAAGIPTPTVQTR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 503 LVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPV 577
Cdd:PRK09088 319 VVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPA 397
|
330 340
....*....|....*....|....*
gi 313747580 578 PIeEAVKMELPIISNAMLIG--DQR 600
Cdd:PRK09088 398 EI-EAVLADHPGIRECAVVGmaDAQ 421
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
222-600 |
1.38e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.52 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 222 LPHLKAVVIYKEPPPNKMANVYTMEEFMElgnevpEEALDAIIDTQQ--PNQCCVLVYTSGTTGNPKGVM-----LSQDN 294
Cdd:PRK13295 153 LPALRHVVVVGGDGADSFEALLITPAWEQ------EPDAPAILARLRpgPDDVTQLIYTSGTTGEPKGVMhtantLMANI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 295 ITWTARYGSQAGDirpaevqqeVVVSYLPLSHIaaqiydlwTGIQWGAQVcfaePDALKGSLVntLREVeptshmgvprv 374
Cdd:PRK13295 227 VPYAERLGLGADD---------VILMASPMAHQ--------TGFMYGLMM----PVMLGATAV--LQDI----------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 375 WEkimeriqeVAAQSGFIRRKMLLWAMSVTleqnltcpgsdlkPFTTRLADYLVL-AKVRQALGFAKCQknfyGAA--PM 451
Cdd:PRK13295 273 WD--------PARAAELIRTEGVTFTMAST-------------PFLTDLTRAVKEsGRPVSSLRTFLCA----GAPipGA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 452 MAETQHFFLGLNIrlYAGYGLSETSGP--HFMSSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLWGRTIF 522
Cdd:PRK13295 328 LVERARAALGAKI--VSAWGMTENGAVtlTKLDDPDERASTTDGCPLPGVEVRVV--DADGaplpagqIGRLQVRGCSNF 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 523 MGYLNMEDKTceAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNAMLIG--DQR 600
Cdd:PRK13295 404 GGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEI-EALLYRHPAIAQVAIVAypDER 479
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
268-585 |
2.06e-23 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 104.96 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 268 QPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQ----AGDIRPAevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAq 343
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagTGKLEEG---CEVVITALPLYHIFALTANGLVFMKIGG- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 344 vC---FAEPDALKGsLVNTLREVEPTSHMGVPRVWEKImeriqevaaqsgfirrkmllwamsvtleqnLTCPGSDLKPFT 420
Cdd:PRK08751 282 -CnhlISNPRDMPG-FVKELKKTRFTAFTGVNTLFNGL------------------------------LNTPGFDQIDFS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 421 TrladylvlakVRQALGfakcqknfYGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFMSSPYNYRLY--SSGKLVPG 498
Cdd:PRK08751 330 S----------LKMTLG--------GGMAVQRSVAERWKQVTGLTLVEAYGLTETS-PAACINPLTLKEYngSIGLPIPS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 499 CRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeN 573
Cdd:PRK08751 391 TDACIKDDAGTVlaigeIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGF-N 469
|
330
....*....|..
gi 313747580 574 VPPVPIEEAVKM 585
Cdd:PRK08751 470 VYPNEIEDVIAM 481
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
274-600 |
5.13e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 103.75 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWT-----ARYGSQAGDIRPA-EVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCF 346
Cdd:PRK12492 211 VLQYTGGTTGLAKGAMLTHGNLVANmlqvrACLSQLGPDGQPLmKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHnVLI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 347 AEPDALKGsLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFirRKMLLWAMSVTleqnltcpgsdlkpfttrlady 426
Cdd:PRK12492 291 TNPRDIPG-FIKELGKWRFSALLGLNTLFVALMD-------HPGF--KDLDFSALKLT---------------------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 427 lvlakvrqalgfakcqkNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFMSSPYN--YRLYSSGKLVPGCRVKLV 504
Cdd:PRK12492 339 -----------------NSGGTALVKATAERWEQLTGCTIVEGYGLTETS-PVASTNPYGelARLGTVGIPVPGTALKVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 505 NQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPPVPI 579
Cdd:PRK12492 401 DDDGNELplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF-NVYPNEI 479
|
330 340
....*....|....*....|...
gi 313747580 580 EEAVkMELPIISNAMLIG--DQR 600
Cdd:PRK12492 480 EDVV-MAHPKVANCAAIGvpDER 501
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
133-596 |
1.03e-22 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 102.75 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 133 ISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDt 208
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALrslgLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 209 QKQLEKILKIwkQLPhlkaVVIYKEpppNKMANVYTMEEFMELGNEVPEEALDAIIdtqQPNQCCVLVYTSGTTGNPKGV 288
Cdd:PLN02330 135 DTNYGKVKGL--GLP----VIVLGE---EKIEGAVNWKELLEAADRAGDTSDNEEI---LQTDLCALPFSSGTTGISKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 289 MLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHIaaqiYDLwTGIqwgaqvCFAepdalkgslvnTLREVeptsh 368
Cdd:PLN02330 203 MLTHRNLV--ANLCSSLFSVGPEMIGQVVTLGLIPFFHI----YGI-TGI------CCA-----------TLRNK----- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 369 mgvprvwekimeriQEVAAQSGFIRRKML--LWAMSVTLEQnlTCPGSDLKPFTTRLADYLVLAKVrqalgfaKCQKNFY 446
Cdd:PLN02330 254 --------------GKVVVMSRFELRTFLnaLITQEVSFAP--IVPPIILNLVKNPIVEEFDLSKL-------KLQAIMT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 447 GAAPMMAETQHFFLGL--NIRLYAGYGLSETSGPHFMSSPYN-----YRLYSSGKLVPGCRVKLVNQDA------EGIGE 513
Cdd:PLN02330 311 AAAPLAPELLTAFEAKfpGVQVQEAYGLTEHSCITLTHGDPEkghgiAKKNSVGFILPNLEVKFIDPDTgrslpkNTPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 514 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISNA 593
Cdd:PLN02330 391 LCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ-VAPAEL-EAILLTHPSVEDA 468
|
...
gi 313747580 594 MLI 596
Cdd:PLN02330 469 AVV 471
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
134-561 |
2.49e-22 |
|
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: 100.03 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 134 SYSQyylLARRAAK--GFLKQAHS------VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 205
Cdd:TIGR01733 1 TYRE---LDERANRlaRHLRAAGGvgpgdrVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VDTQKQLEkilkiwkqLPHLKAVVIYKEPPPNKMANvytmeefmelgNEVPEEALDAiiDTQQPNQCCVLvYTSGTTGNP 285
Cdd:TIGR01733 78 TDSALASR--------LAGLVLPVILLDPLELAALD-----------DAPAPPPPDA--PSGPDDLAYVI-YTSGSTGRP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 286 KGVMLSQDNI----TWTAR-YGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVN 358
Cdd:TIGR01733 136 KGVVVTHRSLvnllAWLARrYGLDPDD---------RVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERddAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 359 TLREVEPTSHM-GVPRVWEKIMEriqevAAQSGFIRRKMLlwamsvtleqnltCPGSDlkPFTTRLADylvlaKVRQALG 437
Cdd:TIGR01733 206 ALIAEHPVTVLnLTPSLLALLAA-----ALPPALASLRLV-------------ILGGE--ALTPALVD-----RWRARGP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 438 fakcqknfygaapmmaetqhfflglNIRLYAGYGLSETS----------GPHFMSSPYNYrlyssGKLVPGCRVKLVNQD 507
Cdd:TIGR01733 261 -------------------------GARLINLYGPTETTvwstatlvdpDDAPRESPVPI-----GRPLANTRLYVLDDD 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 508 -----AEGIGEICLWGRTIFMGYLNMEDKTCEAI--------DEEGWLHTGDAGRLDADGFLYITGR 561
Cdd:TIGR01733 311 lrpvpVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGR 377
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
275-600 |
2.55e-22 |
|
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: 98.73 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 275 LVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEvqqevvvSYL---PLSHIaaqiydlwTGIQWGAQVCFaepda 351
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD-------RYLiinPFFHT--------FGYKAGIVACL----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 352 LKGSlvntlrEVEPTSHMGVPrvweKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLtcpgsdLKPFTTRLADylvLAK 431
Cdd:cd17638 65 LTGA------TVVPVAVFDVD----AILEAIE---------RERITVLPGPPTLFQSL------LDHPGRKKFD---LSS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 432 VRQALGfakcqknfyGAA---PMMAETQHFFLGLNIRLYAgYGLSEtSGPHFMSSPYNYRL---YSSGKLVPGCRVKLVN 505
Cdd:cd17638 117 LRAAVT---------GAAtvpVELVRRMRSELGFETVLTA-YGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 506 QdaegiGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEAVkM 585
Cdd:cd17638 186 D-----GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-A 258
|
330
....*....|....*..
gi 313747580 586 ELPIISNAMLIG--DQR 600
Cdd:cd17638 259 EHPGVAQVAVIGvpDER 275
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
76-718 |
3.25e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 101.49 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 76 APEEALWTTRADGRVRLRidpsCPQLPYTVHRMFYEALDKY----GDLIALGfKRQDK--WEHISYSQYYLLARRAAKGF 149
Cdd:PRK08180 12 APPAVEVERRADGTIYLR----SAEPLGDYPRRLTDRLVHWaqeaPDRVFLA-ERGADggWRRLTYAEALERVRAIAQAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 150 LKQAHS----VAILGFNSPEWFFSAVGTVFAGGIVTGI---YTTSS--PEACQYIAYDCCANVIMVDTQKQLEKILKIwk 220
Cdd:PRK08180 87 LDRGLSaerpLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKLRHVLELLTPGLVFADDGAAFARALAA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 221 qLPHLKAVVIYKEPPPNKMANVytmeEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTAR 300
Cdd:PRK08180 165 -VVPADVEVVAVRGAVPGRAAT----PFAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 301 YGSQAgdIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGaqvcfaepdalkGSL---------------VNTLREVEP 365
Cdd:PRK08180 240 MLAQT--FPFLAEEPPVLVDWLPWNHTFGGNHNLGIVLYNG------------GTLyiddgkptpggfdetLRNLREISP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 366 TSHMGVPRVWEkimeriqevaaqsgfirrkMLLWAmsvtLEQNltcpgsdlkpfttrladylvlAKVRQALgFAKCQKNF 445
Cdd:PRK08180 306 TVYFNVPKGWE-------------------MLVPA----LERD---------------------AALRRRF-FSRLKLLF 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 446 YGAAPM----------MAEtQHffLGLNIRLYAGYGLSETSgPHFMSSpyNYRLYSSGKL---VPGCRVKLVnqDAEGIG 512
Cdd:PRK08180 341 YAGAALsqdvwdrldrVAE-AT--CGERIRMMTGLGMTETA-PSATFT--TGPLSRAGNIglpAPGCEVKLV--PVGGKL 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 513 EICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRL-DAD----GFLYiTGRLKELIITAGGE--NVPPVPIeEAVKM 585
Cdd:PRK08180 413 EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPAdperGLMF-DGRIAEDFKLSSGTwvSVGPLRA-RAVSA 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 586 ELPIISNAMLIGDQRKFLSMLLTLKctldpdtsdqtdnlteqaMEFCQRVG--SRATTVSEIIEkkDEAVYQAIEEGIRR 663
Cdd:PRK08180 491 GAPLVQDVVITGHDRDEIGLLVFPN------------------LDACRRLAglLADASLAEVLA--HPAVRAAFRERLAR 550
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 664 VNMNAAARPYHIQKWAILERDFSISGGELgpTMK--LKRLTVLEKYKGIIDSFYQEQ 718
Cdd:PRK08180 551 LNAQATGSSTRVARALLLDEPPSLDAGEI--TDKgyINQRAVLARRAALVEALYADE 605
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
107-582 |
1.74e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 98.87 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 107 RMFYEALDK--------------------YGDLIALGFKRQdkweHISYSQYYLLARRAAKGfLKQA-----HSVAILGF 161
Cdd:PRK08162 2 NIYEQGLDRnaanyvpltplsfleraaevYPDRPAVIHGDR----RRTWAETYARCRRLASA-LARRgigrgDTVAVLLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 162 NSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQlEKILKIWKQLPHLKAVVIY---KEPPPNK 238
Cdd:PRK08162 77 NIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFA-EVAREALALLPGPKPLVIDvddPEYPGGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 239 MANVYTMEEFMELGN-----EVPEEALDAIidtqqpnqccVLVYTSGTTGNPKGV--------MLSQDNI-TWTARygsq 304
Cdd:PRK08162 156 FIGALDYEAFLASGDpdfawTLPADEWDAI----------ALNYTSGTTGNPKGVvyhhrgayLNALSNIlAWGMP---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 305 agdirpaevQQEVVVSYLPLSHIAAQIYDlWT-GIQWGAQVCfaepdalkgslvntLREVEPtshmgvprvwEKIMERIQ 383
Cdd:PRK08162 222 ---------KHPVYLWTLPMFHCNGWCFP-WTvAARAGTNVC--------------LRKVDP----------KLIFDLIR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 384 E--VAAQSGF-IRRKMLLWAmsvtleqnltcPGSDLKPFttrlaDYLVLAKVRqalgfakcqknfyGAAP------MMAE 454
Cdd:PRK08162 268 EhgVTHYCGApIVLSALINA-----------PAEWRAGI-----DHPVHAMVA-------------GAAPpaaviaKMEE 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 455 tqhfflgLNIRLYAGYGLSETSGP--------HFMSSPYNYRLYSSGK------LVPGCRV------KLVNQDAEGIGEI 514
Cdd:PRK08162 319 -------IGFDLTHVYGLTETYGPatvcawqpEWDALPLDERAQLKARqgvrypLQEGVTVldpdtmQPVPADGETIGEI 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313747580 515 CLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 582
Cdd:PRK08162 392 MFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVEDV 457
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
141-597 |
4.40e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 97.54 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 141 LARRAAkGFlkqAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkqLEKILKIWK 220
Cdd:PRK07786 59 LSRRGV-GF---GDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA--LAPVATAVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 221 QL-PHLKAVVIYKEPPPnkmANVYTMEEFMELGNEVPeealdAIIDTqqPNQCCVLV-YTSGTTGNPKGVMLSQDNITWT 298
Cdd:PRK07786 133 DIvPLLSTVVVAGGSSD---DSVLGYEDLLAEAGPAH-----APVDI--PNDSPALImYTSGTTGRPKGAVLTHANLTGQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 299 ARYGsqagdIRPAEVQQEVVVSYL--PLSHIAAqIYDLWTGIQWGAQVCFAEPDALK-GSLVNTLREVEPTSHMGVPRVW 375
Cdd:PRK07786 203 AMTC-----LRTNGADINSDVGFVgvPLFHIAG-IGSMLPGLLLGAPTVIYPLGAFDpGQLLDVLEAEKVTGIFLVPAQW 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 376 ekimeriQEVAAQSGFIRRKMLLWAMSvtleqnltcpgsdlkpfttrladylvlakvrqalgfakcqknfYGAAPM---- 451
Cdd:PRK07786 277 -------QAVCAEQQARPRDLALRVLS-------------------------------------------WGAAPAsdtl 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 452 ---MAETqhfFLGLNIrlYAGYGLSETSGPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTI 521
Cdd:PRK07786 307 lrqMAAT---FPEAQI--LAAFGQTEMSPVTCMLLGEDaiRKLGSVGKVIPTVAARVVDENmndvPVGeVGEIVYRAPTL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313747580 522 FMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNAMLIG 597
Cdd:PRK07786 382 MSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAEVEN-VLASHPDIVEVAVIG 454
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
134-603 |
2.19e-20 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 95.59 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 134 SYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ 209
Cdd:PRK06018 41 TYAQIHDRALKVSQALdrdgIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 210 --KQLEKILKiwkQLPHLKAVVIYKEP---PPNKMANVYTMEEFMElgnevpEEALDAIIDTQQPNQCCVLVYTSGTTGN 284
Cdd:PRK06018 121 fvPILEKIAD---KLPSVERYVVLTDAahmPQTTLKNAVAYEEWIA------EADGDFAWKTFDENTAAGMCYTSGTTGD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 285 PKGVMLSQDNITWTARYGSQAGDIrpAEVQQEVVVSYLPLSHIAAqiydlwtgiqWGaqVCFAEPDA----------LKG 354
Cdd:PRK06018 192 PKGVLYSHRSNVLHALMANNGDAL--GTSAADTMLPVVPLFHANS----------WG--IAFSAPSMgtklvmpgakLDG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 355 SLVNTLREVEPTSH-MGVPRVWEkimeriqevaaqsgfirrkMLLWAMSvtlEQNLTCPgsDLKpfttrladylvlakvR 433
Cdd:PRK06018 258 ASVYELLDTEKVTFtAGVPTVWL-------------------MLLQYME---KEGLKLP--HLK---------------M 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 434 QALGFAKCQKNFYGAapmmaetqhfFLGLNIRLYAGYGLSETS--------GPHFMSSPYNYRL---YSSGKLVPGCRVK 502
Cdd:PRK06018 299 VVCGGSAMPRSMIKA----------FEDMGVEVRHAWGMTEMSplgtlaalKPPFSKLPGDARLdvlQKQGYPPFGVEMK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 503 LVNQDAEGI-------GEICLWGRTIFMGYLNMEDktcEAIDEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVP 575
Cdd:PRK06018 369 ITDDAGKELpwdgktfGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKD-VIKSGGEWIS 444
|
490 500 510
....*....|....*....|....*....|....*
gi 313747580 576 PVPIEE-AVKMelPIISNAMLIG------DQRKFL 603
Cdd:PRK06018 445 SIDLENlAVGH--PKVAEAAVIGvyhpkwDERPLL 477
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
131-597 |
2.69e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 95.29 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAKGF-----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 205
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLyhvmgVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VDTQKqLEKilkiwkqLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQpnqCCVLVYTSGTTGNP 285
Cdd:PLN02574 145 TSPEN-VEK-------LSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPVIKQDD---VAAIMYSSGTTGAS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 286 KGVMLSQDNITWT---------ARYGSQAGDirpaevqqEVVVSYLPLSHI------AAQIYDLWTGIqwgaqVCFAEPD 350
Cdd:PLN02574 214 KGVVLTHRNLIAMvelfvrfeaSQYEYPGSD--------NVYLAALPMFHIyglslfVVGLLSLGSTI-----VVMRRFD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 351 AlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSgfirrkmllwamsvtleqnLTCpgsdLKPFTTrladylvla 430
Cdd:PLN02574 281 A--SDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEV-------------------LKS----LKQVSC--------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 431 kvrqalgfakcqknfyGAAPMMAET-QHFFLGL-NIRLYAGYGLSETS--GPHFMSSPYNYRLYSSGKLVPGCRVKLVNQ 506
Cdd:PLN02574 327 ----------------GAAPLSGKFiQDFVQTLpHVDFIQGYGMTESTavGTRGFNTEKLSKYSSVGLLAPNMQAKVVDW 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 507 DAE------GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIe 580
Cdd:PLN02574 391 STGcllppgNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKE-IIKYKGFQIAPADL- 468
|
490
....*....|....*..
gi 313747580 581 EAVKMELPIISNAMLIG 597
Cdd:PLN02574 469 EAVLISHPEIIDAAVTA 485
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
275-597 |
5.26e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.79 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 275 LVYTSGTTGNPKGVMLSQDNITWTAR-----YGSQAGDirpaevqqeVVVSYLPLSH-----IAAQIYDLWtgiqwGAQV 344
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALtlvdyWRFTPDD---------VLIHALPIFHthglfVATNVALLA-----GASM 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 345 CFA---EPDALKGSLVNTlrevepTSHMGVPRVWEKIMeriqevaAQSGFIR---RKMLLwamsvtleqnltcpgsdlkp 418
Cdd:PRK07514 227 IFLpkfDPDAVLALMPRA------TVMMGVPTFYTRLL-------QEPRLTReaaAHMRL-------------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 419 FTTrladylvlakvrqalgfakcqknfyGAAPMMAETQHFF---LGLNI--RlyagYGLSETSgphfM--SSPYN--YRL 489
Cdd:PRK07514 274 FIS-------------------------GSAPLLAETHREFqerTGHAIleR----YGMTETN----MntSNPYDgeRRA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 490 YSSGKLVPGCRVKLVNQD------AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLK 563
Cdd:PRK07514 321 GTVGFPLPGVSLRVTDPEtgaelpPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
330 340 350
....*....|....*....|....*....|....
gi 313747580 564 ELIITaGGENVPPVPIEEAVKmELPIISNAMLIG 597
Cdd:PRK07514 401 DLIIS-GGYNVYPKEVEGEID-ELPGVVESAVIG 432
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
145-583 |
8.87e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 93.67 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 145 AAKGfLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkQLEKILKIWKQLPH 224
Cdd:PRK06155 64 AAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA-LLAALEAADPGDLP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 225 LKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALdaiidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQ 304
Cdd:PRK06155 142 LPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAV-------QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 305 AGDIRPaevqQEVVVSYLPLSHIAAQiydlwtgiqwgaqvcfaepDALKGSLVNTLREVEpTSHMGVPRVWEkimeRIQE 384
Cdd:PRK06155 215 DLEIGA----DDVLYTTLPLFHTNAL-------------------NAFFQALLAGATYVL-EPRFSASGFWP----AVRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 385 VAAQSGFirrkmLLWAMSVTLeqnltcpgsDLKPFTTRLADYlvlaKVRQALGfakcqknfyGAAPMmAETQHFFLGLNI 464
Cdd:PRK06155 267 HGATVTY-----LLGAMVSIL---------LSQPARESDRAH----RVRVALG---------PGVPA-ALHAAFRERFGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 465 RLYAGYGLSETSGPhFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFM---GYLNMEDKTCEAI 536
Cdd:PRK06155 319 DLLDGYGSTETNFV-IAVTHGSQRPGSMGRLAPGFEARVVDEHDQELpdgepGELLLRADEPFAfatGYFGMPEKTVEAW 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 313747580 537 dEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAV 583
Cdd:PRK06155 398 -RNLWFHTGDRVVRDADGWFRFVDRIKD-AIRRRGENISSFEVEQVL 442
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
278-583 |
1.21e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 93.14 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 278 TSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFaepdalkgslv 357
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEF---DVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVK----------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 358 ntlreVEPTSHMGVPRVWEKIMERiqevaaqsgfiRRKmllwamSVTLEQNLTcpgsdlkpfttrladYLVLAKV--RQA 435
Cdd:PRK07768 226 -----VTPMDFLRDPLLWAELISK-----------YRG------TMTAAPNFA---------------YALLARRlrRQA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 436 ---------LGFAKCqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSETS----------GPHF--------- 480
Cdd:PRK07768 269 kpgafdlssLRFALN-----GAEPIDPADVEDLLdagarfGLRPEaILPAYGMAEATlavsfspcgaGLVVdevdadlla 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 481 -------MSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMeDKTCEAIDEEGWLHTGDAG 548
Cdd:PRK07768 344 alrravpATKGNTRRLATLGPPLPGLEVRVVDEDgqvlpPRGVGVIELRGESVTPGYLTM-DGFIPAQDADGWLDTGDLG 422
|
330 340 350
....*....|....*....|....*....|....*
gi 313747580 549 RLDADGFLYITGRLKELIITaGGENVPPVPIEEAV 583
Cdd:PRK07768 423 YLTEEGEVVVCGRVKDVIIM-AGRNIYPTDIERAA 456
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
132-580 |
1.82e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 92.72 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 132 HISYSQYYLLARRAAkGFLKQAHS------VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 205
Cdd:PRK08314 35 AISYRELLEEAERLA-GYLQQECGvrkgdrVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VdTQKQLEKILKIWKQLPhLKAVVIYK----------EPPPNKMANVYTMEEFMELGNEVPEEALDAIID----TQQPNQ 271
Cdd:PRK08314 114 V-GSELAPKVAPAVGNLR-LRHVIVAQysdylpaepeIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAppphTAGPDD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 272 CCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFaepda 351
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTP----ESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 352 lkgslvntlreveptshmgVPRvWEKimeriqEVAAQsgFIRR-KMLLW----AMSVTLeqnLTCPGsdlkpfttrLADY 426
Cdd:PRK08314 263 -------------------MPR-WDR------EAAAR--LIERyRVTHWtnipTMVVDF---LASPG---------LAER 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 427 lVLAKVRQALGfakcqknfyGAAPM---MAETQHFFLGLniRLYAGYGLSETSGPHFMSSPYNYRLYSSGklvpgcrVKL 503
Cdd:PRK08314 303 -DLSSLRYIGG---------GGAAMpeaVAERLKELTGL--DYVEGYGLTETMAQTHSNPPDRPKLQCLG-------IPT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 504 VNQDAEGI-------------GEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRLKELiI 567
Cdd:PRK08314 364 FGVDARVIdpetleelppgevGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRM-I 442
|
490
....*....|...
gi 313747580 568 TAGGENVPPVPIE 580
Cdd:PRK08314 443 NASGFKVWPAEVE 455
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
275-581 |
1.97e-19 |
|
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: 90.40 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 275 LVYTSGTTGNPKGVMLSQDN-ITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALK 353
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNW----VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 354 gSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqsgfirrkmllwamSVTLEQNLTCPgsdlkpfttrladylvlaKVR 433
Cdd:cd17635 82 -SLFKILTTNAVTTTCLVPTLLSKLV----------------------SELKSANATVP------------------SLR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 434 qALGFAkcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMssPYNYRLY---SSGKLVPGCRVKLVNQD-AE 509
Cdd:cd17635 121 -LIGYG-------GSRAIAADVRFIEATGLTNTAQVYGLSETGTALCL--PTDDDSIeinAVGRPYPGVDVYLAATDgIA 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313747580 510 GI----GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEE 581
Cdd:cd17635 191 GPsasfGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSE-SINCGGVKIAPDEVER 264
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
224-583 |
2.10e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 92.52 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 224 HLKAVViykepPPNKMANVYTMEEFMELGNEVPEEALDAiidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWT----- 298
Cdd:PRK05677 171 HVKKMV-----PAYHLPQAVKFNDALAKGAGQPVTEANP-----QADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqcr 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 299 ARYGSQAGDIRpaevqqEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFAEPDALKGsLVNTLREVEPTSHMGVPRVWEK 377
Cdd:PRK05677 241 ALMGSNLNEGC------EILIAPLPLYHIYAFTFHCMAMMLIGNHnILISNPRDLPA-MVKELGKWKFSGFVGLNTLFVA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 378 IMERiqevaaqSGFirRKMLLWAMSVTLEQNLTcpgsdlkpfttrladyLVLAKvrqalgfAKCQKNFYGAApmmaetqh 457
Cdd:PRK05677 314 LCNN-------EAF--RKLDFSALKLTLSGGMA----------------LQLAT-------AERWKEVTGCA-------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 458 fflglnirLYAGYGLSETSgPHFMSSPYNY-RLYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDK 531
Cdd:PRK05677 354 --------ICEGYGMTETS-PVVSVNPSQAiQVGTIGIPVPSTLCKVIDDDGNelplgEVGELCVKGPQVMKGYWQRPEA 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 313747580 532 TCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPPVPIEEAV 583
Cdd:PRK05677 425 TDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
269-597 |
6.15e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 90.43 E-value: 6.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 269 PNQCCVLVYTSGTTGNPKGVMLSQDNIT-----------WTARygsqagdirpaevqqEVVVSYLPLSHIAAQIYDLWTG 337
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAadldalaeawqWTAD---------------DVLVHGLPLFHVHGLVLGVLGP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 338 IQWGAQV---------CFAEPDALKGSLVntlreveptshMGVPRVWEkimeRIQEVAAQSGFIRRKMLLWAMSVTLeqn 408
Cdd:PRK07787 192 LRIGNRFvhtgrptpeAYAQALSEGGTLY-----------FGVPTVWS----RIAADPEAARALRGARLLVSGSAAL--- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 409 ltcpgsdlkPFTtrladylVLAKVRQALGFAKCQKnfYGaapmMAETqhfFLGLNIRlyagyglseTSGPHfmsspynyR 488
Cdd:PRK07787 254 ---------PVP-------VFDRLAALTGHRPVER--YG----MTET---LITLSTR---------ADGER--------R 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 489 LYSSGKLVPGCRVKLVNQ-------DAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGR 561
Cdd:PRK07787 292 PGWVGLPLAGVETRLVDEdggpvphDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGR 371
|
330 340 350
....*....|....*....|....*....|....*.
gi 313747580 562 LKELIITAGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:PRK07787 372 ESTDLIKSGGYRIGAGEIETAL-LGHPGVREAAVVG 406
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
275-583 |
2.00e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 90.37 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 275 LVYTSGTTGNPKGVMLSQDNITWTARygsQAGDIRPAEvQQEVVVSYLPLSH----IAAQIYDLWTGIqwgAQVCFAEP- 349
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLSHHNILSNIE---QISDVFNLR-NDDVILSSLPFFHsfglTVTLWLPLLEGI---KVVYHPDPt 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 350 DALKgslvntlreveptshmgvprvwekimerIQEVAAQsgfiRRKMLLWAMSvtleqnltcpgsdlkpftTRLADYLVL 429
Cdd:PRK08633 860 DALG----------------------------IAKLVAK----HRATILLGTP------------------TFLRLYLRN 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 430 AKVrQALGFAKCQKNFYGA---APMMAETqhFFLGLNIRLYAGYGLSETSG------PHFMSSPYNY----RLYSSGKLV 496
Cdd:PRK08633 890 KKL-HPLMFASLRLVVAGAeklKPEVADA--FEEKFGIRILEGYGATETSPvasvnlPDVLAADFKRqtgsKEGSVGMPL 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 497 PGCRVKLVNQD-----AEGI-GEICLWGRTIFMGYLNMEDKTCEAI---DEEGWLHTGDAGRLDADGFLYITGRLKEL-- 565
Cdd:PRK08633 967 PGVAVRIVDPEtfeelPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFak 1046
|
330
....*....|....*...
gi 313747580 566 IitaGGENVPPVPIEEAV 583
Cdd:PRK08633 1047 I---GGEMVPLGAVEEEL 1061
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
254-562 |
2.09e-18 |
|
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: 88.46 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 254 EVPEEALDAIIDTQQP-------NQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSH 326
Cdd:cd05945 74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGP----GDVFLNQAPFSF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 327 IAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqsgfiRRKMLLWAMSVT 404
Cdd:cd05945 150 DLS-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAAMCL-------------LSPTFTPESLPS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 405 LEQNLTCpGsdlKPFTTRLADYLVlakvrqalgfakcqknfyGAAPmmaetqhfflglNIRLYAGYGLSET----SGPHF 480
Cdd:cd05945 216 LRHFLFC-G---EVLPHKTARALQ------------------QRFP------------DARIYNTYGPTEAtvavTYIEV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 481 MSSPY--NYRLYSsGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRL 550
Cdd:cd05945 262 TPEVLdgYDRLPI-GYAKPGAKLVILDEDGRpvppgEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRL 340
|
330
....*....|..
gi 313747580 551 DADGFLYITGRL 562
Cdd:cd05945 341 EADGLLFYRGRL 352
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
156-632 |
3.14e-18 |
|
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: 87.90 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 156 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTqkqlekilkiwkqlphlkavviykepp 235
Cdd:cd05919 38 VLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA--------------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 236 pnkmanvytmeefmelgnevpeealDAIidtqqpnqcCVLVYTSGTTGNPKGVMLSQDNITWTAR-YGSQAGDIRPaevq 314
Cdd:cd05919 91 -------------------------DDI---------AYLLYSSGTTGPPKGVMHAHRDPLLFADaMAREALGLTP---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 315 QEVVVSylplshiAAQIY-------DLWTGIQWGAQVCFAE--PDAlkGSLVNTLREVEPTSHMGVPRVWEKIMeriqev 385
Cdd:cd05919 133 GDRVFS-------SAKMFfgyglgnSLWFPLAVGASAVLNPgwPTA--ERVLATLARFRPTVLYGVPTFYANLL------ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 386 aAQSGFIRRKMllwamsvtleqnltcpgSDLKPFTTRladylvlakvrqalgfakcqknfyGAAPMMAETQHFFLGLNIR 465
Cdd:cd05919 198 -DSCAGSPDAL-----------------RSLRLCVSA------------------------GEALPRGLGERWMEHFGGP 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 466 LYAGYGLSETsGPHFMSS-PYNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTcEAIDEE 539
Cdd:cd05919 236 ILDGIGATEV-GHIFLSNrPGAWRLGSTGRPVPGYEIRLVDEEGHTIppgeeGDLLVRGPSAAVGYWNNPEKS-RATFNG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 540 GWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIGDQRKF----LSMLLTLKCTLDP 615
Cdd:cd05919 314 GWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLI-IQHPAVAEAAVVAVPESTglsrLTAFVVLKSPAAP 391
|
490
....*....|....*..
gi 313747580 616 DTSdqtdnLTEQAMEFC 632
Cdd:cd05919 392 QES-----LARDIHRHL 403
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
463-597 |
3.39e-18 |
|
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: 86.31 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 463 NIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGRTIFMGYLNMEdktceAIDEEGWL 542
Cdd:cd17633 136 KANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGG-----FSNPDGWM 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 313747580 543 HTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISNAMLIG 597
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLK-AIPGIEEAIVVG 263
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
275-585 |
1.03e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 87.03 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 275 LVYTSGTTGNPKGVMLSQDNITwtARYGSQAGDIRPA-EVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQvcfaepdalk 353
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHRNML--ANLEQAKAAYGPLlHPGKELVVTALPLYHIFALTVNCLLFIELGGQ---------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 354 GSLVNTLREVEptshmgvprvwekimeriqevaaqsGFIRrkmllwamsvtleqnltcpgsDLK--PFTT-----RLADY 426
Cdd:PRK08974 279 NLLITNPRDIP-------------------------GFVK---------------------ELKkyPFTAitgvnTLFNA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 427 LVLAKVRQALGFAKCQKNFYGAAPM---MAETQHFFLGLNirLYAGYGLSETSgPHFMSSPYNYRLY--SSGKLVPGCRV 501
Cdd:PRK08974 313 LLNNEEFQELDFSSLKLSVGGGMAVqqaVAERWVKLTGQY--LLEGYGLTECS-PLVSVNPYDLDYYsgSIGLPVPSTEI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 502 KLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPP 576
Cdd:PRK08974 390 KLVDDDGNEVppgepGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGF-NVYP 467
|
....*....
gi 313747580 577 VPIEEAVKM 585
Cdd:PRK08974 468 NEIEDVVML 476
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
142-588 |
1.76e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 86.29 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 142 ARRAAKGF----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM--VDTQKQLEKI 215
Cdd:PRK12406 21 AARAAGGLaalgVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahADLLHGLASA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 216 LKiwkqlPHLKAVVIykePPPNKMANVYTMEEFMElgnEVPEEALD--------AIIDTQQPNQCCVLVYTSGTTGNPKG 287
Cdd:PRK12406 101 LP-----AGVTVLSV---PTPPEIAAAYRISPALL---TPPAGAIDwegwlaqqEPYDGPPVPQPQSMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 288 VMLSQDNITWTARYGSQAGDIRPAEvQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA--EPDALkgsLVNTLREVEP 365
Cdd:PRK12406 170 VRRAAPTPEQAAAAEQMRALIYGLK-PGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPrfDPEEL---LQLIERHRIT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 366 TSHMgVPRVWEKIMERIQEVaaqsgfiRRKMLLWAMSVTLEQNLTCPgsdlkpfttrladylvlAKVRQALgfakcqKNF 445
Cdd:PRK12406 246 HMHM-VPTMFIRLLKLPEEV-------RAKYDVSSLRHVIHAAAPCP-----------------ADVKRAM------IEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 446 YGaaPMMAETqhfflglnirlyagYGLSETSGPHFMSSP-YNYRLYSSGKLVPGCRVKLVNQDAE-----GIGEIC--LW 517
Cdd:PRK12406 295 WG--PVIYEY--------------YGSTESGAVTFATSEdALSHPGTVGKAAPGAELRFVDEDGRplpqgEIGEIYsrIA 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313747580 518 GRTIFMgYLNMEDKTCEaIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELP 588
Cdd:PRK12406 359 GNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEI-EAVLHAVP 425
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
256-601 |
1.15e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 83.94 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 256 PEEALDAIidtqqpnqcCVLVYTSGTTGNPKGVMLSQDNITWTArygSQAGDIRPAEVQQEVVVSYLPLSHIAAQ----I 331
Cdd:PRK06178 204 PPPALDAL---------AALNYTGGTTGMPKGCEHTQRDMVYTA---AAAYAVAVVGGEDSVFLSFLPEFWIAGEnfglL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 332 YDLWTGI------QWGAQVCFAEPDALK----GSLVNTLREVeptshMGVPRVWEKIMERIQEVAAQSgFIRRkmllwam 401
Cdd:PRK06178 272 FPLFSGAtlvllaRWDAVAFMAAVERYRvtrtVMLVDNAVEL-----MDHPRFAEYDLSSLRQVRVVS-FVKK------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 402 svtleqnltcpgsdLKPfttrlaDYlvlakvRQALgfakcqKNFYGAapMMAEtqhfflglnirlyAGYGLSET------ 475
Cdd:PRK06178 339 --------------LNP------DY------RQRW------RALTGS--VLAE-------------AAWGMTEThtcdtf 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 476 ------------SGPHFMSSPynyrlyssgklVPGCRVKLVNQDAEGI------GEICLWGRTIFMGYLNMEDKTCEAId 537
Cdd:PRK06178 372 tagfqdddfdllSQPVFVGLP-----------VPGTEFKICDFETGELlplgaeGEIVVRTPSLLKGYWNKPEATAEAL- 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 538 EEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPvpiE-EAVKMELPIISNAMLIG--DQRK 601
Cdd:PRK06178 440 RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPS---EvEALLGQHPAVLGSAVVGrpDPDK 503
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
76-717 |
1.19e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.94 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 76 APEEALWTTRADGRVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQD--KWEHISYSQYYLLARRAAKGFLKQA 153
Cdd:PRK12582 22 KPPDISVERRADGSIVIKSRHPLGPYPRSIPHLLAKWAAEAPDRPWLAQREPGhgQWRKVTYGEAKRAVDALAQALLDLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 154 ----HSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTTSSPE--ACQYIAYDCCANVIMVDTQKQLEKILKIwkqLPH 224
Cdd:PRK12582 102 ldpgRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVVFAQSGAPFARALAA---LDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 225 LKAVVIYKEPPPNKMANVytmeEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITwTARYGSQ 304
Cdd:PRK12582 179 LDVTVVHVTGPGEGIASI----AFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMC-ANIAMQE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 305 AGDIRPAEVQQEVVVSYLPLSHIAA--QIYD--LWTG----IQWGAQVcfaePdALKGSLVNTLREVEPTSHMGVPRVWE 376
Cdd:PRK12582 254 QLRPREPDPPPPVSLDWMPWNHTMGgnANFNglLWGGgtlyIDDGKPL----P-GMFEETIRNLREISPTVYGNVPAGYA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 377 KIMERIQ--EVAAQSGFIRRKMLLWAmsvtleqnltcpGSdlkpfttRLADYLvLAKVrQALGfakcqknfygaapmMAE 454
Cdd:PRK12582 329 MLAEAMEkdDALRRSFFKNLRLMAYG------------GA-------TLSDDL-YERM-QALA--------------VRT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 455 TQHfflglNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEgiGEICLWGRTIFMGYLNMEDKTCE 534
Cdd:PRK12582 374 TGH-----RIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPVGDK--YEVRVKGPNVTPGYHKDPELTAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 535 AIDEEGWLHTGDAGR-LDAD----GfLYITGRLKELIITAGGE--NVPPVPIeEAVKMELPIISNAMLIGDQRKFLSMLl 607
Cdd:PRK12582 447 AFDEEGFYRLGDAARfVDPDdpekG-LIFDGRVAEDFKLSTGTwvSVGTLRP-DAVAACSPVIHDAVVAGQDRAFIGLL- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 608 tlkCTLDPDTsdqtdnlteqamefCQRVGSRATTVSEIIeKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWAILERDFSI 687
Cdd:PRK12582 524 ---AWPNPAA--------------CRQLAGDPDAAPEDV-VKHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEPPSI 585
|
650 660 670
....*....|....*....|....*....|
gi 313747580 688 SGGELGPTMKLKRLTVLEKYKGIIDSFYQE 717
Cdd:PRK12582 586 DAGEITDKGYINQRAVLERRAALVERLYAE 615
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-586 |
1.50e-16 |
|
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: 83.31 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 267 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSH----IAAQIYDLWTGIQwga 342
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK----TKDRILSWMPLTHdmglIAFHLAPLIAGMN--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 343 qvcfaepdalkgslvntlreveptshmgvprvwekimeriQEVAAQSGFIRRKML-LWAMSVTLEQNLTCP--GSD--LK 417
Cdd:cd05908 176 ----------------------------------------QYLMPTRLFIRRPILwLKKASEHKATIVSSPnfGYKyfLK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 418 PFTTRLADYLVLAKVRQALGfakcqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSETS--------GPHFM- 481
Cdd:cd05908 216 TLKPEKANDWDLSSIRMILN---------GAEPIDYELCHEFLdhmskyGLKRNaILPVYGLAEASvgaslpkaQSPFKt 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 482 -------------------SSPYNYRLYSSGKLVPGCRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAID 537
Cdd:cd05908 287 itlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKIlpdgyIGHIQIRGKNVTPGYYNNPEATAKVFT 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 313747580 538 EEGWLHTGDAGrLDADGFLYITGRLKELIITaGGENVPPVPIEE-AVKME 586
Cdd:cd05908 367 DDGWLKTGDLG-FIRNGRLVITGREKDIIFV-NGQNVYPHDIERiAEELE 414
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
248-572 |
1.93e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 83.61 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 248 FMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVvvSYLPLSHI 327
Cdd:PTZ00342 282 IILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHL--SYLPISHI 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 328 AAQIY---DLWTGIQ---WGAQVCFAEPDAL--KGSLVntlreveptshMGVPRVWEKIMERIQEVAAQSGFIRRKMLLW 399
Cdd:PTZ00342 360 YERVIaylSFMLGGTiniWSKDINYFSKDIYnsKGNIL-----------AGVPKVFNRIYTNIMTEINNLPPLKRFLVKK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 400 AMSVTLEQNLTCPGSDLKPFTTrladylVLAKVRQALGfAKCQKNFYGAAPMMAE-TQHFFLGLNIRLYAGYGLSETSGP 478
Cdd:PTZ00342 429 ILSLRKSNNNGGFSKFLEGITH------ISSKIKDKVN-PNLEVILNGGGKLSPKiAEELSVLLNVNYYQGYGLTETTGP 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 479 HFMSSPYNYRLYS-SGKLVPGCRVKLVN------QDAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLD 551
Cdd:PTZ00342 502 IFVQHADDNNTESiGGPISPNTKYKVRTwetykaTDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQIN 581
|
330 340
....*....|....*....|.
gi 313747580 552 ADGFLYITGRLKELIITAGGE 572
Cdd:PTZ00342 582 KNGSLTFLDRSKGLVKLSQGE 602
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
108-597 |
2.61e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 82.64 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 108 MFYEALDKY-----GDLIALGFKRQDKWEHISYSQYYLLARRAA-----KGFLKQAHsVAILGFNSPEWFFSAVGTVFAG 177
Cdd:PRK04319 44 IAYEAIDRHadggrKDKVALRYLDASRKEKYTYKELKELSNKFAnvlkeLGVEKGDR-VFIFMPRIPELYFALLGALKNG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 178 GIVTGIYTTSSPEACQYIAYDCCANVImVDTQKQLEKilKIWKQLPHLKAVVIYKEPPPNKmANVYTMEEFMELGNEVPE 257
Cdd:PRK04319 123 AIVGPLFEAFMEEAVRDRLEDSEAKVL-ITTPALLER--KPADDLPSLKHVLLVGEDVEEG-PGTLDFNALMEQASDEFD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 258 -EALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITW---TARYgsqAGDIRPAEvqqevvvsylplshiaaqIYd 333
Cdd:PRK04319 199 iEWTD-------REDGAILHYTSGSTGKPKGVLHVHNAMLQhyqTGKY---VLDLHEDD------------------VY- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 334 lWtgiqwgaqvCFAEPDALKGS-----------LVNTLREVEPTshmgvPRVWEKIMERiQEV----AAQSGFirrKMLL 398
Cdd:PRK04319 250 -W---------CTADPGWVTGTsygifapwlngATNVIDGGRFS-----PERWYRILED-YKVtvwyTAPTAI---RMLM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 399 WAmsvtleqnltcpGSDLkpfttrLADYlVLAKVRQALGFAKcqknfygaaPMMAETQHFflG---LNIRLYAGYGLSET 475
Cdd:PRK04319 311 GA------------GDDL------VKKY-DLSSLRHILSVGE---------PLNPEVVRW--GmkvFGLPIHDNWWMTET 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 476 SGpHFMSspyNY-----RLYSSGKLVPGCRVKLV-NQDAEG----IGEICL---WgRTIFMGYLNMEDKTcEAIDEEGWL 542
Cdd:PRK04319 361 GG-IMIA---NYpamdiKPGSMGKPLPGIEAAIVdDQGNELppnrMGNLAIkkgW-PSMMRGIWNNPEKY-ESYFAGDWY 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 313747580 543 HTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:PRK04319 435 VSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKL-MEHPAVAEAGVIG 487
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
274-600 |
2.77e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.86 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTA-----RYGSQAgdirpaevqQEVVVsyLPLSHIAaqiydlwtgiqwGAQVcfae 348
Cdd:PRK07824 39 LVVATSGTTGTPKGAMLTAAALTASAdathdRLGGPG---------QWLLA--LPAHHIA------------GLQV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 349 pdalkgsLV-NTLREVEPTShMGVPRVWEkIMERIQEVAAQSGFiRRKMLLWAMSvtLEQNLTCPGSdlkpfTTRLADY- 426
Cdd:PRK07824 92 -------LVrSVIAGSEPVE-LDVSAGFD-PTALPRAVAELGGG-RRYTSLVPMQ--LAKALDDPAA-----TAALAELd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 427 LVLAkvrqalgfakcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGphfmSSPYNyrlyssGKLVPGCRVKLVNq 506
Cdd:PRK07824 155 AVLV----------------GGGPAPAPVLDAAAAAGINVVRTYGMSETSG----GCVYD------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 507 daegiGEICLWGRTIFMGYLNMEDKtcEAIDEEGWLHTGDAGRLDaDGFLYITGRLKElIITAGGENVPPVPIEEAVkME 586
Cdd:PRK07824 208 -----GRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALD-DGVLTVLGRADD-AISTGGLTVLPQVVEAAL-AT 277
|
330
....*....|....*.
gi 313747580 587 LPIISNAMLIG--DQR 600
Cdd:PRK07824 278 HPAVADCAVFGlpDDR 293
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
141-597 |
3.93e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 82.15 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 141 LARRAAKGFLKQAHSVAILGFNSP---EWFFsAVgtVFAGGIVTGI-YTTSSPEACQyiAYDCCANVIMV-DTQKQLEKI 215
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDlylEWLL-AV--ACAGGIVAPLnYRWSFEEAKS--AMLLVRPVMLVtDETCSSWYE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 216 LKIWKQLPHLKAVVIYKEPPP---NKMANVYTMEEFMELGNEVPEEALdaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQ 292
Cdd:PLN02860 120 ELQNDRLPSLMWQVFLESPSSsvfIFLNSFLTTEMLKQRALGTTELDY-----AWAPDDAVLICFTSGTTGRPKGVTISH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 293 DNITW-----TARYGSQAGDIrpaevqqevvvsYL---PLSHI---AAQIYDLWTGiqwGAQVCFAEPDAlkGSLVNTLR 361
Cdd:PLN02860 195 SALIVqslakIAIVGYGEDDV------------YLhtaPLCHIgglSSALAMLMVG---ACHVLLPKFDA--KAALQAIK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 362 EVEPTSHMGVPrvweKIMERIQEVAaqsgfirRKMLLWAMSVTLEQNLTCPGSdlkpFTTRLADYLVLAKVRQALGFAkc 441
Cdd:PLN02860 258 QHNVTSMITVP----AMMADLISLT-------RKSMTWKVFPSVRKILNGGGS----LSSRLLPDAKKLFPNAKLFSA-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 442 qknfYGaapmMAET--QHFFLGLNI-RLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWG 518
Cdd:PLN02860 321 ----YG----MTEAcsSLTFMTLHDpTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRVGRILTRG 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313747580 519 RTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNAMLIG 597
Cdd:PLN02860 393 PHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYPEEV-EAVLSQHPGVASVVVVG 469
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
274-597 |
4.13e-16 |
|
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: 81.37 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCfaepdalk 353
Cdd:cd05935 88 LIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDV----ILACLPLFHVTGFVGSLNTAVYVGGTYV-------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 354 gslvntlreveptshmgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTcpgSDLKPFTTRLADYLVLAKvr 433
Cdd:cd05935 156 ------------------------LMARWDRETALELIEKYKVTFWTNIPTMLVDLL---ATPEFKTRDLSSLKVLTG-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 434 qalgfakcqknfyGAAPMMAETQHFFLGL-NIRLYAGYGLSETSGPHFMSSPYNYRLYSSGklVPGCRVKLVNQDAEG-- 510
Cdd:cd05935 207 -------------GGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTNPPLRPKLQCLG--IP*FGVDARVIDIETgr 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 511 ------IGEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGEnVPPVPIeE 581
Cdd:cd05935 272 elppneVGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK-VWPAEV-E 349
|
330
....*....|....*.
gi 313747580 582 AVKMELPIISNAMLIG 597
Cdd:cd05935 350 AKLYKHPAI*EVCVIS 365
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
273-597 |
4.46e-16 |
|
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: 81.23 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 273 CVLVYTSGTTGNPKGVmlsqdnitwtarygsqagdirpaevqqEVVVSYlPLSHI--AAQIYDL------WTGIQWGAQV 344
Cdd:cd05972 84 ALIYFTSGTTGLPKGV---------------------------LHTHSY-PLGHIptAAYWLGLrpddihWNIADPGWAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 345 C----FAEPdALKGS--LVNTLREVEPtshmgvpRVWEKIMERIQevaaqsgfirrkmllwamsVTleqNLTCPGSDLKP 418
Cdd:cd05972 136 GawssFFGP-WLLGAtvFVYEGPRFDA-------ERILELLERYG-------------------VT---SFCGPPTAYRM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 419 FTTRLADYLVLAKVRQALGfakcqknfyGAAPMMAETQHFF---LGLNIRlyAGYGLSETSGPHFMSSPYNYRLYSSGKL 495
Cdd:cd05972 186 LIKQDLSSYKFSHLRLVVS---------AGEPLNPEVIEWWraaTGLPIR--DGYGQTETGLTVGNFPDMPVKPGSMGRP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 496 VPGCRVKLVNQDAEGI-----GEICLWGRTI--FMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIIT 568
Cdd:cd05972 255 TPGYDVAIIDDDGRELppgeeGDIAIKLPPPglFLGYVGDPEKT-EASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKS 333
|
330 340
....*....|....*....|....*....
gi 313747580 569 AgGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd05972 334 S-GYRIGPFEVESAL-LEHPAVAEAAVVG 360
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
254-561 |
4.88e-16 |
|
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: 81.03 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 254 EVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDirpaevqqeVVVSY 321
Cdd:cd05930 70 SYPAERLAYILeDSGaklvltDPDDLAYVIYTSGSTGKPKGVMVEHRGLVnlllwMQEAYPLTPGD---------RVLQF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 322 LPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrkmllw 399
Cdd:cd05930 141 TSFSFDVS-VWEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLL------------------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 400 amSVTLEQNLTCPGSDLKpfttrladYLVLA--KVRQALgfakcQKNFYGAAPmmaetqhfflglNIRLYAGYGLSETS- 476
Cdd:cd05930 196 --RLLLQELELAALPSLR--------LVLVGgeALPPDL-----VRRWRELLP------------GARLVNLYGPTEATv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 477 GPHFMSSPYNYRLYSS---GKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAI-----DEEGWLH 543
Cdd:cd05930 249 DATYYRVPPDDEEDGRvpiGRPIPNTRVYVLDENlrpvpPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfGPGERMY 328
|
330
....*....|....*....
gi 313747580 544 -TGDAGRLDADGFLYITGR 561
Cdd:cd05930 329 rTGDLVRWLPDGNLEFLGR 347
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
270-597 |
2.88e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 79.37 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 270 NQCCVLVYTSGTTGNPKGVMLSQDNITWTArYGSQAGDIRPAEVqQEVVVSYLPLSHIAAqiydlWtGIQW-----GAQV 344
Cdd:PRK07008 176 NQASSLCYTSGTTGNPKGALYSHRSTVLHA-YGAALPDAMGLSA-RDAVLPVVPMFHVNA-----W-GLPYsapltGAKL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 345 CFAEPDaLKGSLVNTLREVEP-TSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvTLEQNLTCPGSDLKPFTtrl 423
Cdd:PRK07008 248 VLPGPD-LDGKSLYELIEAERvTFSAGVPTVWLGLLNHMREAGLRFSTLRR---------TVIGGSACPPAMIRTFE--- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 424 ADYLVlaKVRQALGfakcqknfygaapmMAETQHffLGLNIRLYAGY-GLSETSGPHfmsspynyRLYSSGKLVPGCRVK 502
Cdd:PRK07008 315 DEYGV--EVIHAWG--------------MTEMSP--LGTLCKLKWKHsQLPLDEQRK--------LLEKQGRVIYGVDMK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 503 LVNQ-------DAEGIGEICLWGRTIFMGYLNMEDKTCeaIDeeGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVP 575
Cdd:PRK07008 369 IVGDdgrelpwDGKAFGDLQVRGPWVIDRYFRGDASPL--VD--GWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWIS 443
|
330 340
....*....|....*....|..
gi 313747580 576 PVPIEEaVKMELPIISNAMLIG 597
Cdd:PRK07008 444 SIDIEN-VAVAHPAVAEAACIA 464
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
274-580 |
4.20e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 78.78 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSH----IAAQIYDLWTGiqwGAQVCFAEP 349
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSP----RDATVAVMPLYHghglIAALLATLASG---GAVLLPARG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 350 DALKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSG-----FIRrkmllwamsvtleqnlTCPGsdlkPFTTRLA 424
Cdd:PRK05852 253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKpaalrFIR----------------SCSA----PLTAETA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 425 dylvlakvrQALgfakcQKNFygAAPM-----MAETQHFFLGLNIRlyaGYGLSE----TSGPHFMSSPYNYRLY-SSGK 494
Cdd:PRK05852 313 ---------QAL-----QTEF--AAPVvcafgMTEATHQVTTTQIE---GIGQTEnpvvSTGLVGRSTGAQIRIVgSDGL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 495 LVPgcrvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENV 574
Cdd:PRK05852 374 PLP----------AGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKEL-INRGGEKI 441
|
....*.
gi 313747580 575 PPVPIE 580
Cdd:PRK05852 442 SPERVE 447
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
131-633 |
6.27e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 78.35 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAKGFLKQA----HSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 206
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSigpgSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 207 DTQ--KQLEKILKIW--KQLPHLKA---VVIYKE---PPPNKMA---NVYTMEEFMELGNevPEEALdaiidtQQPN--- 270
Cdd:PLN02479 124 DQEffTLAEEALKILaeKKKSSFKPpllIVIGDPtcdPKSLQYAlgkGAIEYEKFLETGD--PEFAW------KPPAdew 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 271 QCCVLVYTSGTTGNPKGVMLSQ---------DNITWTARYGSqagdirpaevqqeVVVSYLPLSHIAAQIYDLWTGIQWG 341
Cdd:PLN02479 196 QSIALGYTSGTTASPKGVVLHHrgaylmalsNALIWGMNEGA-------------VYLWTLPMFHCNGWCFTWTLAALCG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 342 AQVCfaepdalkgslvntLREVEPTShmgvprvwekimerIQEVAAQSGFIRrkmlLWAMSVTLEQNLTCPGSDLKPFTT 421
Cdd:PLN02479 263 TNIC--------------LRQVTAKA--------------IYSAIANYGVTH----FCAAPVVLNTIVNAPKSETILPLP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 422 RLADYLVLakvrqalgfakcqknfyGAAP----MMAETQHFFlglniRLYAGYGLSETSGPHFMSS--PYNYRLYSSGKL 495
Cdd:PLN02479 311 RVVHVMTA-----------------GAAPppsvLFAMSEKGF-----RVTHTYGLSETYGPSTVCAwkPEWDSLPPEEQA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 496 VPGCR------------------VKLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLY 557
Cdd:PLN02479 369 RLNARqgvryiglegldvvdtktMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 558 ITGRLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG--DQRKFLS--MLLTLKCtlDPDTSDQTdNLTEQAMEFCQ 633
Cdd:PLN02479 448 IKDRSKDIIIS-GGENISSLEVENVVYTH-PAVLEASVVArpDERWGESpcAFVTLKP--GVDKSDEA-ALAEDIMKFCR 522
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
268-601 |
7.57e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 78.85 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 268 QPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHiaaqiydlwtgiqwgaqvCFA 347
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSP----EDKVFNALPVFH------------------SFG 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 348 epdaLKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFirrkmllwamsvtleqnltcpGSDlkpftTRLADYl 427
Cdd:PRK06814 849 ----LTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILF---------------------GTD-----TFLNGY- 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 428 vlAKVRQALGFAKCQKNFYGAAPMMAETQHFFL-GLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLvnQ 506
Cdd:PRK06814 898 --ARYAHPYDFRSLRYVFAGAEKVKEETRQTWMeKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRL--E 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 507 DAEGI---GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEAV 583
Cdd:PRK06814 974 PVPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRF-AKIAGEMISLAAVEELA 1052
|
330
....*....|....*....
gi 313747580 584 KMELP-IISNAMLIGDQRK 601
Cdd:PRK06814 1053 AELWPdALHAAVSIPDARK 1071
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
273-597 |
1.26e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 75.80 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 273 CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevvvsYL---PLSHIaaqiydlwtgiqwgaqvcfaep 349
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTV-------FLnsgPLFHI---------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 350 dalkGSLVNTLrevePTSHMG-----VPRV-WEKIMERIQEVAAQSGFIrrkmllwaMSVTLEQNLtcpgsdlKPFTTRL 423
Cdd:cd17636 54 ----GTLMFTL----ATFHAGgtnvfVRRVdAEEVLELIEAERCTHAFL--------LPPTIDQIV-------ELNADGL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 424 ADYLVLAKVRQALGFAkcqknfygaAPMMAETQHFFLGLnirlyAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKL 503
Cdd:cd17636 111 YDLSSLRSSPAAPEWN---------DMATVDTSPWGRKP-----GGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 504 VnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRlKELIITAGGENVPP 576
Cdd:cd17636 177 L--DEDGrevpdgeVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYP 252
|
330 340
....*....|....*....|.
gi 313747580 577 VPIEEAVKmELPIISNAMLIG 597
Cdd:cd17636 253 AEVERCLR-QHPAVADAAVIG 272
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
156-595 |
1.62e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 76.98 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 156 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ-----KQLEKILKIWKQLPHLKAVVI 230
Cdd:PLN03102 67 VSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSfeplaREVLHLLSSEDSNLNLPVIFI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 231 YK-EPPPNKMANVYTMEEFMELGNEVPEeALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNI---TWTARYGSQAG 306
Cdd:PLN03102 147 HEiDFPKRPSSEELDYECLIQRGEPTPS-LVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAylsTLSAIIGWEMG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 307 dIRPaevqqeVVVSYLPLSHIAAQIYDLWTGIQWGAQVCF---AEPDALKGSlvntlrEVEPTSHMG-VPRVWEKIME-R 381
Cdd:PLN03102 226 -TCP------VYLWTLPMFHCNGWTFTWGTAARGGTSVCMrhvTAPEIYKNI------EMHNVTHMCcVPTVFNILLKgN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 382 IQEVAAQSGFIrrkmllwamsvtleQNLTcpGSDLKPfttrladyLVLAKVRQALGFakcqknfygaapmmaETQHfflg 461
Cdd:PLN03102 293 SLDLSPRSGPV--------------HVLT--GGSPPP--------AALVKKVQRLGF---------------QVMH---- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 462 lnirlyaGYGLSETSGPHFMSS--------PYNYRLYSSGKlvPGCRV--------------KLVNQDAEGIGEICLWGR 519
Cdd:PLN03102 330 -------AYGLTEATGPVLFCEwqdewnrlPENQQMELKAR--QGVSIlgladvdvknketqESVPRDGKTMGEIVIKGS 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313747580 520 TIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKMELPIISNAML 595
Cdd:PLN03102 401 SIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVENVLYKYPKVLETAVV 474
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
266-585 |
2.81e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.21 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 266 TQQPNQCCVLVYTSGTTGNPKGVMLSQDNI--------TWTarygsQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTG 337
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWL-----QPAFEKKPRPDQLNFVCALPLYHIFALTVCGLLG 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 338 IQWGA-QVCFAEPDALKGsLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFirRKMllwamsvtleqnltcpgsDL 416
Cdd:PRK07059 275 MRTGGrNILIPNPRDIPG-FIKELKKYQVHIFPAVNTLYNALLN-------NPDF--DKL------------------DF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 417 KPFttrladylvlaKVRQALGFAkCQKNfygaapmMAETQHFFLGLNIrlYAGYGLSETSgPHFMSSPYNYRLYSSGKLV 496
Cdd:PRK07059 327 SKL-----------IVANGGGMA-VQRP-------VAERWLEMTGCPI--TEGYGLSETS-PVATCNPVDATEFSGTIGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 497 PGCRVKLVNQDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITA 569
Cdd:PRK07059 385 PLPSTEVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
330
....*....|....*.
gi 313747580 570 GGeNVPPVPIEEAVKM 585
Cdd:PRK07059 465 GF-NVYPNEIEEVVAS 479
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
250-632 |
4.04e-14 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 75.62 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 250 ELGNEVPEEALDAIIDTQ-QPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGS-QAGDIRPAevqQEVVVSYLPLSHI 327
Cdd:cd05923 129 LVGLGEPESAGPLIEDPPrEPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMStQAGLRHGR---HNVVLGLMPLYHV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 328 AAQIYDLWTGIQWGAQVCFAEPDAlKGSLVNTLREVEPTSHMGVPrvwekimeriqevaaqsgfirrkMLLWAMSVTLEQ 407
Cdd:cd05923 206 IGFFAVLVAALALDGTYVVVEEFD-PADALKLIEQERVTSLFATP-----------------------THLDALAAAAEF 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 408 NltcpGSDLKPFTTrladylvlakvrqaLGFAkcqknfyGAA---PMMAETQHFFLGLNIRLYagyGLSETsgphfMSSP 484
Cdd:cd05923 262 A----GLKLSSLRH--------------VTFA-------GATmpdAVLERVNQHLPGEKVNIY---GTTEA-----MNSL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 485 YNYRLYSSGKLVPG--CRVKLVN-----QDAEGIGE-----ICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDA 552
Cdd:cd05923 309 YMRDARTGTEMRPGffSEVRIVRiggspDEALANGEegeliVAAAADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 553 DGFLYITGRLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG--DQRKFLSMLLTLKCTLDPDTSDQTDnlteqamE 630
Cdd:cd05923 388 SGDVRILGRVDDMIIS-GGENIHPSEIERVLSRH-PGVTEVVVIGvaDERWGQSVTACVVPREGTLSADELD-------Q 458
|
..
gi 313747580 631 FC 632
Cdd:cd05923 459 FC 460
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
242-586 |
7.48e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 75.04 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 242 VYTMEEFMELgnevpeEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAG-DIRPAEVqqevVVS 320
Cdd:PRK09192 154 VLSHAWFKAL------PEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlKVRPGDR----CVS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 321 YLPLSHiaaqiyDLwtgiqwGAQVCFAEPDALKGSlVNTLrevePTSHMGV-PRVWEKIMERIQEVAAQS---GF---IR 393
Cdd:PRK09192 224 WLPFYH------DM------GLVGFLLTPVATQLS-VDYL----PTRDFARrPLQWLDLISRNRGTISYSppfGYelcAR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 394 RkmllwAMSVTLEQ-NLTC-----PGSD------LKPFTTRLADylvlakvrqaLGFAkcQKNF---YG------AAPMM 452
Cdd:PRK09192 287 R-----VNSKDLAElDLSCwrvagIGADmirpdvLHQFAEAFAP----------AGFD--DKAFmpsYGlaeatlAVSFS 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 453 AETQHF-FLGLNIRLYAGYGLSETSGphfmSSPYNYRLY-SSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGY 525
Cdd:PRK09192 350 PLGSGIvVEEVDRDRLEYQGKAVAPG----AETRRVRTFvNCGKALPGHEIEIRNEAGMplperVVGHICVRGPSLMSGY 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313747580 526 LNMEDkTCEAIDEEGWLHTGDAGRLdADGFLYITGRLKELIITaGGENVPPVPIEEAVKME 586
Cdd:PRK09192 426 FRDEE-SQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIII-NGRNIWPQDIEWIAEQE 483
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
493-597 |
1.40e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 73.81 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 493 GKLVPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKtcEAIDeeGWLHTGDAGRLDADGFLYITGRLKEL 565
Cdd:PRK07788 379 GRPPKGVTVKIL--DENGnevprgvVGRIFVGNGFPFEGYTDGRDK--QIID--GLLSSGDVGYFDEDGLLFVDGRDDDM 452
|
90 100 110
....*....|....*....|....*....|..
gi 313747580 566 IITaGGENVPPVPIEEAVKmELPIISNAMLIG 597
Cdd:PRK07788 453 IVS-GGENVFPAEVEDLLA-GHPDVVEAAVIG 482
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
131-582 |
2.47e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 73.01 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTT------SSPEAcQYIAYDCC 200
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLralgLREGDVVAILLENNPEFF-----EVYWAARRSGLYYTpinwhlTAAEI-AYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 201 ANVIMVDtQKQLEKILKIWKQLPHlkavviykepppnkmanvyTMEEFMELGNEVP-----EEALDAIIDTQQPNQC--C 273
Cdd:PRK08276 84 AKVLIVS-AALADTAAELAAELPA-------------------GVPLLLVVAGPVPgfrsyEEALAAQPDTPIADETagA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVM--LSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAqiydlwtgIQWGAQVcfaepDA 351
Cdd:PRK08276 144 DMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAP--------LRFGMSA-----LA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 352 LKGSLV--------NTLREVE----PTSHMgVPrvwekIMeriqevaaqsgFIRrkMLlwamsvtleqnltcpgsdlkpf 419
Cdd:PRK08276 211 LGGTVVvmekfdaeEALALIEryrvTHSQL-VP-----TM-----------FVR--ML---------------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 420 ttRLADylvlaKVRQALGFAKCQKNFYGAAP--------MMAetqhfFLGLNIRLYagYGLSETSGPHFMSS------PY 485
Cdd:PRK08276 250 --KLPE-----EVRARYDVSSLRVAIHAAAPcpvevkraMID-----WWGPIIHEY--YASSEGGGVTVITSedwlahPG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 486 nyrlySSGKLVPGcRVKLVNQDAEGI--GEIclwGrTIFM-------GYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFL 556
Cdd:PRK08276 316 -----SVGKAVLG-EVRILDEDGNELppGEI---G-TVYFemdgypfEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYL 385
|
490 500
....*....|....*....|....*.
gi 313747580 557 YITGRLKELIITaGGENVPPVPIEEA 582
Cdd:PRK08276 386 YLTDRKSDMIIS-GGVNIYPQEIENL 410
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
462-583 |
4.68e-13 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 71.95 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 462 LNIRLYAGYGLSETSGPHFMSSPYNYRL--YSSGKLVPGCRVKLVNQDaegIGEICLWGRTIFMGYLNmedktcEAIDEE 539
Cdd:PRK07445 253 LQLRLAPTYGMTETASQIATLKPDDFLAgnNSSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QILDSQ 323
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 313747580 540 GWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAV 583
Cdd:PRK07445 324 GIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
265-651 |
6.47e-13 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 71.38 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 265 DTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 344
Cdd:cd05969 84 ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHP----DDIYWCTADPGWVTGTVYGIWAPWLNGVTN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 345 CFAEPDAlkgslvntlreveptshmgVPRVWEKIMERIqevaaqsgfirrKMLLWAMSVTLEQNLTcpgsdlkpfttRLA 424
Cdd:cd05969 160 VVYEGRF-------------------DAESWYGIIERV------------KVTVWYTAPTAIRMLM-----------KEG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 425 DYLVLAKVRQALGFAKCqknfyGAAPMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSP-YNYRLYSSGKLVPGCRVK 502
Cdd:cd05969 198 DELARKYDLSSLRFIHS-----VGEPLNPEAIRWGMEvFGVPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 503 LVNQDAEGI-----GEICL---WgRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENV 574
Cdd:cd05969 273 VVDENGNELppgtkGILALkpgW-PSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRV 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 575 PPVPIEEAVkMELPIISNAMLIGDQRKFLSMLLTLKCTLDPDTSdQTDNLTEQAMEFCqRVGSRATTVSEIIEKKDE 651
Cdd:cd05969 350 GPFEVESAL-MEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE-PSDELKEEIINFV-RQKLGAHVAPREIEFVDN 423
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
131-597 |
1.31e-12 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 70.58 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAA-----KGFLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 205
Cdd:cd05958 9 REWTYRDLLALANRIAnvlvgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VDtqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeEALDAIIDTqqpnqcCVLVYTSGTTGNP 285
Cdd:cd05958 89 CA--------------------------------------------------HALTASDDI------CILAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 286 KGVM-LSQDNITWTARYGSQAgdIRPAEvqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQvCFAEPDALKGSLVNTLREVE 364
Cdd:cd05958 113 KATMhFHRDPLASADRYAVNV--LRLRE--DDRFVGSPPLAFTFGLGGVLLFPFGVGAS-GVLLEEATPDLLLSAIARYK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 365 PTSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvtleqnLTCPGSDLKPFTTRLADYLVLAKVRQALGfakCQKN 444
Cdd:cd05958 188 PTVLFTAPTAYRAMLAHPDAAGPDLSSLRK--------------CVSAGEALPAALHRAWKEATGIPIIDGIG---STEM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 445 FygaapmmaetqHFFLGlnirlyagyglsetsgphfmSSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLW 517
Cdd:cd05958 251 F-----------HIFIS--------------------ARPGDARPGATGKPVPGYEAKVV--DDEGnpvpdgtIGRLAVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 518 GRTifmGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd05958 298 GPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVL-LQHPAVAECAVVG 372
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
266-597 |
3.75e-12 |
|
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: 69.00 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 266 TQQPNQCCVLVYTSGTTGNPKGVMLSQdnitwtarygsqagdirpaevqqEVVVSYLPLSHIAAQIY----DL-WTGIQW 340
Cdd:cd05971 84 TDGSDDPALIIYTSGTTGPPKGALHAH-----------------------RVLLGHLPGVQFPFNLFprdgDLyWTPADW 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 341 gaqvcfaepdALKGSLVNTLRevePTSHMGVPRVWEKiMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFT 420
Cdd:cd05971 141 ----------AWIGGLLDVLL---PSLYFGVPVLAHR-MTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 421 TRL---------ADYLVLAKVRQALGFAKCQknFYGaapmMAETqHFFLGLNirlyagyglsetsgphfmSSPYNYRLYS 491
Cdd:cd05971 207 VKLraiatggesLGEELLGWAREQFGVEVNE--FYG----QTEC-NLVIGNC------------------SALFPIKPGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 492 SGKLVPGCRVKLVNQDAE-----GIGEICLwgRT----IFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRL 562
Cdd:cd05971 262 MGKPIPGHRVAIVDDNGTplppgEVGEIAV--ELpdpvAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRD 338
|
330 340 350
....*....|....*....|....*....|....*
gi 313747580 563 KElIITAGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd05971 339 DD-VITSSGYRIGPAEIEECL-LKHPAVLMAAVVG 371
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
463-597 |
4.19e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 69.04 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 463 NIRLYAGYGLSETSGPHFMSSPYNYRLYSS-GKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNmEDKTCEAI 536
Cdd:PRK07638 279 YAKLYEFYGASELSFVTALVDEESERRPNSvGRPFHNVQVRICNEAGEevqkgEIGTVYVKSPQFFMGYII-GGVLAREL 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313747580 537 DEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNAMLIG 597
Cdd:PRK07638 358 NADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEHPAVDEIVVIG 416
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
254-561 |
4.84e-12 |
|
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: 68.49 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 254 EVPEEALDAIIDTQQPNQC---------CVLVYTSGTTGNPKGVMLSQDNIT----WT-ARYGSQAGDiRPAEVqqevvv 319
Cdd:cd17653 80 KLPSARIQAILRTSGATLLlttdspddlAYIIFTSGSTGIPKGVMVPHRGVLnyvsQPpARLDVGPGS-RVAQV------ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 320 sylpLShIA--AQIYDLWTGIQWGAQVCFAEPDalkgslvntlrevEPTSHMgvprvwekimeriqevaaqsgfirrkml 397
Cdd:cd17653 153 ----LS-IAfdACIGEIFSTLCNGGTLVLADPS-------------DPFAHV---------------------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 398 lwAMSVTLeqnLTCPGSDLKpfTTRLADYLVLAKVrqALGfakcqknfyGAAPMMAETQHFflGLNIRLYAGYGLSETSG 477
Cdd:cd17653 187 --ARTVDA---LMSTPSILS--TLSPQDFPNLKTI--FLG---------GEAVPPSLLDRW--SPGRRLYNAYGPTECTI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 478 PHFMSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAI----DEEGWLH--TGD 546
Cdd:cd17653 247 SSTMTELLPGQPVTIGKPIPNSTCYILDADlqpvpEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGD 326
|
330
....*....|....*
gi 313747580 547 AGRLDADGFLYITGR 561
Cdd:cd17653 327 YGRWTEDGGLEFLGR 341
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
491-583 |
1.11e-11 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 67.79 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 491 SSGKLVPGcRVKLVNQDAEG-----IGEICLWGRTIFMgYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKEL 565
Cdd:cd05929 298 SVGRAVLG-KVHILDEDGNEvppgeIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDM 375
|
90
....*....|....*...
gi 313747580 566 IITaGGENVPPVPIEEAV 583
Cdd:cd05929 376 IIS-GGVNIYPQEIENAL 392
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
256-601 |
4.01e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 65.92 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 256 PEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLW 335
Cdd:PRK06164 167 PAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAV----LLAALPFCGVFGFSTLLG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 336 TGIQWGAQVCFAEPDAlkGSLVNTLREVEPTSHMGVprvwEKIMERIQEVAAQSG-FIRRKMLLWAmsvtleqnltcpgs 414
Cdd:PRK06164 243 ALAGGAPLVCEPVFDA--ARTARALRRHRVTHTFGN----DEMLRRILDTAGERAdFPSARLFGFA-------------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 415 dlkPFTTRLADYLVLAKVRQALgfakcQKNFYGAApmmaETQHFFLGlnirlyagyglsetsgpHFMSSPYNYRLYSSGK 494
Cdd:PRK06164 303 ---SFAPALGELAALARARGVP-----LTGLYGSS----EVQALVAL-----------------QPATDPVSVRIEGGGR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 495 LV-PGCRVKLVNQDAEGI------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADG-FLYITgRLKElI 566
Cdd:PRK06164 354 PAsPEARVRARDPQDGALlpdgesGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQT-RMGD-S 431
|
330 340 350
....*....|....*....|....*....|....*
gi 313747580 567 ITAGGENVPPVPIEEAVKmELPIISNAMLIGDQRK 601
Cdd:PRK06164 432 LRLGGFLVNPAEIEHALE-ALPGVAAAQVVGATRD 465
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
267-570 |
4.83e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 66.27 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 267 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVcF 346
Cdd:PRK08043 362 QQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTP----NDRFMSALPLFHSFGLTVGLFTPLLTGAEV-F 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 347 AEPDALKGSLVNTLreveptshmgvprVWEkimeriqevaaqsgfiRRKMLLWAMSvtleqnltcpgsdlkpftTRLADY 426
Cdd:PRK08043 437 LYPSPLHYRIVPEL-------------VYD----------------RNCTVLFGTS------------------TFLGNY 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 427 lvlAKVRQALGFAKCQKNFYGAAPMMAET-QHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN 505
Cdd:PRK08043 470 ---ARFANPYDFARLRYVVAGAEKLQESTkQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS 546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 506 qdAEGI---GEICLWGRTIFMGYLNMED---------KTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAG 570
Cdd:PRK08043 547 --VPGIeqgGRLQLKGPNIMNGYLRVEKpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
466-633 |
6.96e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 65.40 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 466 LYAGYGLSETsGPHFMSSPYNYRLY--SSGKLVPGCRVKLVNQDAEGIGEIcLWGRTIFMGYLNME---DKTCEAIdEEG 540
Cdd:PRK13383 320 LYNGYGSTEV-GIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTrytDGGGKAV-VDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 541 WLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKMELPIISNAML-IGDQR--KFLSMLLTLKCTLDPDT 617
Cdd:PRK13383 397 MTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAHPAVADNAVIgVPDERfgHRLAAFVVLHPGSGVDA 475
|
170
....*....|....*.
gi 313747580 618 SDQTDNLTEQAMEFCQ 633
Cdd:PRK13383 476 AQLRDYLKDRVSRFEQ 491
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
131-597 |
8.30e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 65.10 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAKGF----LKQAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTTS-----SPEACQYIAYDCCA 201
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFrslgLKRGDHVAIFMENNLRYL-----EVCWAAERSGLYYTCvnshlTPAEAAYIVDDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 202 NViMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPpnkmanvyTMEEFMELgnevpEEALDAIIDTQQPNQC--CVLVYTS 279
Cdd:PRK13391 98 RA-LITSAAKLDVARALLKQCPGVRHRLVLDGDG--------ELEGFVGY-----AEAVAGLPATPIADESlgTDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 280 GTTGNPKGVM--LS----QDNITWTA----RYGSQAGDIrpaevqqevvvsYL---PLSHIAAQIYDLwTGIQWGAQVCF 346
Cdd:PRK13391 164 GTTGRPKGIKrpLPeqppDTPLPLTAflqrLWGFRSDMV------------YLspaPLYHSAPQRAVM-LVIRLGGTVIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 347 AEP-DAlkgslvntlreveptshmgvprvwEKIMERIQEVAaqsgfIRRKMLLWAMSVTLeqnLTCPgsdlkpfttrlad 425
Cdd:PRK13391 231 MEHfDA------------------------EQYLALIEEYG-----VTHTQLVPTMFSRM---LKLP------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 426 ylvlAKVRQALGFAKCQKNFYGAAPMMAETQHFFL---GLNIRLYagYGLSETSGPHFMSSP-YNYRLYSSGKLVPGcrv 501
Cdd:PRK13391 266 ----EEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIdwwGPIIHEY--YAATEGLGFTACDSEeWLAHPGTVGRAMFG--- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 502 KLVNQDAEG-------IGEICLWGRTIFMgYLNMEDKTCEAIDEEG-WLHTGDAGRLDADGFLYITGRLKELIITaGGEN 573
Cdd:PRK13391 337 DLHILDDDGaelppgePGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIIS-GGVN 414
|
490 500
....*....|....*....|....
gi 313747580 574 VPPVPIEEAVkMELPIISNAMLIG 597
Cdd:PRK13391 415 IYPQEAENLL-ITHPKVADAAVFG 437
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
89-561 |
1.30e-10 |
|
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: 65.26 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 89 RVRLRIDPSCPQLPY----TVHRMFYEALDKYGDLIALGFKRQdkweHISYSQyylLARRAAK--GFLKQAHS-----VA 157
Cdd:COG1020 458 RQQLLAEWNATAAPYpadaTLHELFEAQAARTPDAVAVVFGDQ----SLTYAE---LNARANRlaHHLRALGVgpgdlVG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 158 ILGFNSPEWFFSAVGTVFAGGIvtgiYT---TSSPEA-CQYIAYDCCANVIMvdTQKQLEKilkiwkQLPHLKAVVIYKE 233
Cdd:COG1020 531 VCLERSLEMVVALLAVLKAGAA----YVpldPAYPAErLAYMLEDAGARLVL--TQSALAA------RLPELGVPVLALD 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 234 PPpnkmanvytmeefmELGNEvPEEALDAIIDTQQPnqCCVLvYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDi 308
Cdd:COG1020 599 AL--------------ALAAE-PATNPPVPVTPDDL--AYVI-YTSGSTGRPKGVMVEHRALVnllawMQRRYGLGPGD- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 309 rpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTS-HMgVPRVWEKIMEriqev 385
Cdd:COG1020 660 --------RVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEARRdpAALAELLARHRVTVlNL-TPSLLRALLD----- 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 386 AAQSGFIRRKMLLW---AMSVTLeqnltcpgsdlkpfttrladylvLAKVRQALGfakcqknfygaapmmaetqhfflgl 462
Cdd:COG1020 725 AAPEALPSLRLVLVggeALPPEL-----------------------VRRWRARLP------------------------- 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 463 NIRLYAGYGLSETS-----------GPHFMSSPY-----NYRLY---SSGKLVP-GCrvklvnqdaegIGEICLWGRTIF 522
Cdd:COG1020 757 GARLVNLYGPTETTvdstyyevtppDADGGSVPIgrpiaNTRVYvldAHLQPVPvGV-----------PGELYIGGAGLA 825
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 313747580 523 MGYLNMEDKTCEA-----IDEEG--WLHTGDAGRLDADGFLYITGR 561
Cdd:COG1020 826 RGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGR 871
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-590 |
1.46e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 268 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT---WTARYGSqAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 344
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVaneQLIRHGF-GIDLNP----DDVIVSWLPLYHDMGLIGGLLQPIFSGVPC 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 345 CFAEPDALkgsLVNTLREVEPTSHM-----GVPR-VWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNltcpgsDLKP 418
Cdd:PRK05691 239 VLMSPAYF---LERPLRWLEAISEYggtisGGPDfAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQD------SLER 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 419 FTTRLAdylvlakvrqALGFAkcQKNFYgAAPMMAETQHFFLG-----------LNIRLYAGYGLSETSGPHFMSSpyny 487
Cdd:PRK05691 310 FAEKFA----------ACGFD--PDSFF-ASYGLAEATLFVSGgrrgqgipaleLDAEALARNRAEPGTGSVLMSC---- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 488 rlyssGKLVPGCRVKLVN-QDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAI---DEEGWLHTGDAGRLdADGFLYI 558
Cdd:PRK05691 373 -----GRSQPGHAVLIVDpQSLEVlgdnrVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLGFL-RDGELFV 446
|
330 340 350
....*....|....*....|....*....|..
gi 313747580 559 TGRLKELIITAgGENVPPVPIEEAVKMELPII 590
Cdd:PRK05691 447 TGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
101-597 |
2.37e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 63.49 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 101 LPYTVHRMFYEALDKYGDLIALgfKRQDKWEHISYSQYYLLARRAAKGFLKQAHS----VAILGFNSPEWFFSAVGTVFA 176
Cdd:PRK05857 12 LPSTVLDRVFEQARQQPEAIAL--RRCDGTSALRYRELVAEVGGLAADLRAQSVSrgsrVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 177 GGIVtgiyttsspeacqyiaydccanvIMVDTQKQLEKILKiWKQLPHLKAVVIYK------EPPPNKMANVYTMEEFME 250
Cdd:PRK05857 90 GAIA-----------------------VMADGNLPIAAIER-FCQITDPAAALVAPgskmasSAVPEALHSIPVIAVDIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 251 LGNEVPEEALDAIIDTQQPN----QCCVLVYTSGTTGNPKGVMLSqdNITWTArygsqAGDIRPAE-------VQQEVVV 319
Cdd:PRK05857 146 AVTRESEHSLDAASLAGNADqgseDPLAMIFTSGTTGEPKAVLLA--NRTFFA-----VPDILQKEglnwvtwVVGETTY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 320 SYLPLSHIAAqiydLW---TGIQWGAqVCFAepdalKGSLVNTLREVeptshmgvprvwekimeriqevaaqsgfirrkm 396
Cdd:PRK05857 219 SPLPATHIGG----LWwilTCLMHGG-LCVT-----GGENTTSLLEI--------------------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 397 llwamSVTLEQNLTCpgsdLKP-FTTRLADYLVLAKVR-QALGFAKcqknfYGAAPMMAETQHFFLGLNIRLYAGYGLSE 474
Cdd:PRK05857 256 -----LTTNAVATTC----LVPtLLSKLVSELKSANATvPSLRLVG-----YGGSRAIAADVRFIEATGVRTAQVYGLSE 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 475 TSG-----PHFMSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEGIGEIC----LWGRTI--FMGYLNMEDKTCEAIdE 538
Cdd:PRK05857 322 TGCtalclPTDDGSIVKIEAGAVGRPYPGVDVYLAATDgigptAPGAGPSAsfgtLWIKSPanMLGYWNNPERTAEVL-I 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313747580 539 EGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPP---------VP-IEEAVKMELPIISNAMLIG 597
Cdd:PRK05857 401 DGWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPdevdriaegVSgVREAACYEIPDEEFGALVG 468
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
131-597 |
3.91e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 62.72 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQY----YLLARRAAKGFLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 206
Cdd:PRK13390 23 EQVSYRQLdddsAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 207 DTQkqlekilkiwkqLPHLKAVViyKEPPPNKMANVYTMEEFMELgnevpEEALDAIID--TQQPnqC-CVLVYTSGTTG 283
Cdd:PRK13390 103 SAA------------LDGLAAKV--GADLPLRLSFGGEIDGFGSF-----EAALAGAGPrlTEQP--CgAVMLYSSGTTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 284 NPKGvmlsqdnitwtarygsqagdIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQW--GAQVCFAEPdalkgslvntLR 361
Cdd:PRK13390 162 FPKG--------------------IQPDLPGRDVDAPGDPIVAIARAFYDISESDIYysSAPIYHAAP----------LR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 362 EVEPTSHMGVPRVWEKIMEriqeVAAQSGFIRRkmllwaMSVTLEQnltcpgsdLKPftTRLADYLVL-AKVRQALGFAK 440
Cdd:PRK13390 212 WCSMVHALGGTVVLAKRFD----AQATLGHVER------YRITVTQ--------MVP--TMFVRLLKLdADVRTRYDVSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 441 CQKNFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSP-YNYRLYSSGKLVPGcRVKLVNQD-----AEGIGE 513
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTEAHGMTFIDSPdWLAHPGSVGRSVLG-DLHICDDDgnelpAGRIGT 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 514 ICLWGRTIFMGYLNMEDKTCEAIDEEG--WLHTGDAGRLDADGFLYITGRlKELIITAGGENVPPVPIEEAVKMElPIIS 591
Cdd:PRK13390 351 VYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADR-KSFMIISGGVNIYPQETENALTMH-PAVH 428
|
....*.
gi 313747580 592 NAMLIG 597
Cdd:PRK13390 429 DVAVIG 434
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
139-600 |
4.96e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 62.60 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 139 YLLARraakGFLKQAHsVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTtssPEACQYIAYDCCANVIMVDTQkQLEKI 215
Cdd:PRK07798 44 YLIAQ----GLGPGDH-VGIYARNRIEYVEAMLGAFKARAVPVNVnyrYV---EDELRYLLDDSDAVALVYERE-FAPRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 216 LKIWKQLPHLKAVVIYKEPPPNKmanvytmeefmELGNEVP-EEALDAIIDTQQPNQCC----VLVYTSGTTGNPKGVML 290
Cdd:PRK07798 115 AEVLPRLPKLRTLVVVEDGSGND-----------LLPGAVDyEDALAAGSPERDFGERSpddlYLLYTGGTTGMPKGVMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 291 SQDNItwtarYGSQAGDIRPA---EVQQEVVVSYL-------------PLSHIAAQiydlWTGiqWGAqvcfaepdALKG 354
Cdd:PRK07798 184 RQEDI-----FRVLLGGRDFAtgePIEDEEELAKRaaagpgmrrfpapPLMHGAGQ----WAA--FAA--------LFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 355 SLVNTLREVEPTSHmgvpRVWEKI-MERIQEVAaqsgfirrkMLLWAMSVTLEQNLTCPGsdlkpfTTRLADYLVLAKvr 433
Cdd:PRK07798 245 QTVVLLPDVRFDAD----EVWRTIeREKVNVIT---------IVGDAMARPLLDALEARG------PYDLSSLFAIAS-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 434 qalgfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSET-SGPHFMSSPYNYRlySSGKLV-PGCRVKLVNQD-- 507
Cdd:PRK07798 304 -------------GGALFSPSVKEALLELlpNVVLTDSIGSSETgFGGSGTVAKGAVH--TGGPRFtIGPRTVVLDEDgn 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 508 -----AEGIGEICLWGRtIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRlKELIITAGGENVPPVPI 579
Cdd:PRK07798 369 pvepgSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGR-GSVCINTGGEKVFPEEV 446
|
490 500
....*....|....*....|...
gi 313747580 580 EEAVKMElPIISNAMLIG--DQR 600
Cdd:PRK07798 447 EEALKAH-PDVADALVVGvpDER 468
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-600 |
9.01e-10 |
|
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: 61.24 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 275 LVYTSGTTGNPKGVMLSQDNItwtarYGSQAG-------------DIRPAEVQQEVVVSYL--PLSHIAAQIydLWTGIQ 339
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDI-----FRMLMGgadfgtgeftpseDAHKAAAAAAGTVMFPapPLMHGTGSW--TAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 340 WGAQVCFAEPDALKGslVNTLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkmllwAMSVTLEQNLTCPGsdlkpf 419
Cdd:cd05924 81 LGGQTVVLPDDRFDP--EEVWRTIEKHKVTSMTIVGD-----------------------AMARPLIDALRDAG------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 420 TTRLADYLVLAKvrqalgfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSETSgphFMSSPYN-YRLYSSGKLV 496
Cdd:cd05924 130 PYDLSSLFAISS---------------GGALLSPEVKQGLLELvpNITLVDAFGSSETG---FTGSGHSaGSGPETGPFT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 497 ---PGCRV-----KLVNQDAEGIGEICLWGRtIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRlKEL 565
Cdd:cd05924 192 ranPDTVVldddgRVVPPGSGGVGWIARRGH-IPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR-GSV 269
|
330 340 350
....*....|....*....|....*....|....*..
gi 313747580 566 IITAGGENVPPVPIEEAVKMElPIISNAMLIG--DQR 600
Cdd:cd05924 270 CINTGGEKVFPEEVEEALKSH-PAVYDVLVVGrpDER 305
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
464-593 |
1.01e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 61.43 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 464 IRLYAGYGLSEtsgphfMSSPYNYRLYSS----GKLVPGCRVKLVNqdaegiGEICLWGRTIFMGYLnMEDKTCEAIDEE 539
Cdd:PRK09029 265 IRCWCGYGLTE------MASTVCAKRADGlagvGSPLPGREVKLVD------GEIWLRGASLALGYW-RQGQLVPLVNDE 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 313747580 540 GWLHTGDAGRLDaDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNA 593
Cdd:PRK09029 332 GWFATRDRGEWQ-NGELTILGRLDNLFFS-GGEGIQPEEI-ERVINQHPLVQQV 382
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
501-597 |
1.88e-09 |
|
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: 60.54 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 501 VKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVP 575
Cdd:COG1021 365 VRIVDEDgnpvPPGeVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIA 443
|
90 100
....*....|....*....|..
gi 313747580 576 PVPIEEAVkMELPIISNAMLIG 597
Cdd:COG1021 444 AEEVENLL-LAHPAVHDAAVVA 464
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
269-602 |
4.63e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 59.39 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 269 PNQCCVLVYTSGTTGNPKGvmlsqdnitwtARYgSQAGDIRPAEVqqevVVSYLPLSH-----IAAQIYDLWtGIqwgAQ 343
Cdd:PRK13382 195 GRKGRVILLTSGTTGTPKG-----------ARR-SGPGGIGTLKA----ILDRTPWRAeeptvIVAPMFHAW-GF---SQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 344 VCFAEpdALKGSLVN--------TLREVE---PTSHMGVPRVWEKIMERIQEVAAQsgFIRRKMLLWAMSvtleqnltcp 412
Cdd:PRK13382 255 LVLAA--SLACTIVTrrrfdpeaTLDLIDrhrATGLAVVPVMFDRIMDLPAEVRNR--YSGRSLRFAAAS---------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 413 GSDLKP-----FTTRLADYLVlakvrqalgfakcqkNFYGA--APMMAetqhfflglnirlyagyglseTSGPHFMSSPY 485
Cdd:PRK13382 321 GSRMRPdvviaFMDQFGDVIY---------------NNYNAteAGMIA---------------------TATPADLRAAP 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 486 NyrlySSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEaideEGWLHTGDAGRLDADGFLYITG 560
Cdd:PRK13382 365 D----TAGRPAEGTEIRILDQDfrevPTGeVGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFVVG 436
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 313747580 561 RLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG-DQRKF 602
Cdd:PRK13382 437 RDDEMIVS-GGENVYPIEVEKTL-ATHPDVAEAAVIGvDDEQY 477
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
464-583 |
1.00e-08 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 58.28 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 464 IRLYAGYGLSET-----SGPHFMSSPYnyrlySSGKLVPGCRVKLVNQDAEGI-----GEICLwgRT-------IFMGYL 526
Cdd:cd05970 327 IKLMEGFGQTETtltiaTFPWMEPKPG-----SMGKPAPGYEIDLIDREGRSCeageeGEIVI--RTskgkpvgLFGGYY 399
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 527 NMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAV 583
Cdd:cd05970 400 KDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPFEVESAL 454
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
89-329 |
1.12e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 58.35 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 89 RVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKQAHS----VAILGFNSP 164
Cdd:PRK08279 23 RGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGkgdvVALLMENRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 165 EWFFSAVGTVFAGGIVTGIYTTSSPEA---CQYIAYdccANVIMV--DTQKQLEKIlkiwkqLPHLKAVVIYKEPPPNKM 239
Cdd:PRK08279 99 EYLAAWLGLAKLGAVVALLNTQQRGAVlahSLNLVD---AKHLIVgeELVEAFEEA------RADLARPPRLWVAGGDTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 240 ANVYTMEEFMELGNEVPEEALDAiidTQ--QPNQCCVLVYTSGTTGNPKGVMLSQdnITWTARYGSQAGDIRPAEvqQEV 317
Cdd:PRK08279 170 DDPEGYEDLAAAAAGAPTTNPAS---RSgvTAKDTAFYIYTSGTTGLPKAAVMSH--MRWLKAMGGFGGLLRLTP--DDV 242
|
250
....*....|..
gi 313747580 318 VVSYLPLSHIAA 329
Cdd:PRK08279 243 LYCCLPLYHNTG 254
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
107-561 |
1.43e-08 |
|
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: 57.72 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 107 RMFYEALDKYGDLIALGFKRQdkweHISYSQyylLARRAA--------KGfLKQAHSVAILGFNSPEWFFSAVGTVFAGG 178
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQ----TLTYRE---LNERANqlartlreKG-VGPDTIVGIMAERSLEMIVGILGILKAGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 179 IVTGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKilkiwkQLPHLKAVVIYKEpppnkmanvytmeefmELGNEVPEE 258
Cdd:cd17655 73 AYLPIDPDYPEERIQYILEDSGADILL--TQSHLQP------PIAFIGLIDLLDE----------------DTIYHEESE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 259 ALDAIIdtqQPNQCCVLVYTSGTTGNPKGVMLSQDN----ITWTARYGSQAGDIRpaevqqevVVSYLPLShIAAQIYDL 334
Cdd:cd17655 129 NLEPVS---KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlVEWANKVIYQGEHLR--------VALFASIS-FDASVTEI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 335 WTGIQWGAQVCFAEPDALKG--SLVNTLREVEPTSHMGVPRVwekiMERIQEVAAQSGFIRRKMLLwamsvtleqnltcP 412
Cdd:cd17655 197 FASLLSGNTLYIVRKETVLDgqALTQYIRQNRITIIDLTPAH----LKLLDAADDSEGLSLKHLIV-------------G 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 413 GSDLKPfttrladylVLAKVRQALGFAKCQ-KNFYGAapmmAETQhffLGLNIRLYAGYGLSETSGPhfMSSPY-NYRLY 490
Cdd:cd17655 260 GEALST---------ELAKKIIELFGTNPTiTNAYGP----TETT---VDASIYQYEPETDQQVSVP--IGKPLgNTRIY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 491 ---SSGKLVPgcrvklvnqdaEGI-GEICLWGRTIFMGYLNMEDKTCEA-IDE-----EGWLHTGDAGRLDADGFLYITG 560
Cdd:cd17655 322 ildQYGRPQP-----------VGVaGELYIGGEGVARGYLNRPELTAEKfVDDpfvpgERMYRTGDLARWLPDGNIEFLG 390
|
.
gi 313747580 561 R 561
Cdd:cd17655 391 R 391
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
131-616 |
2.50e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 57.00 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSqyyllARRAA--KGFL---KQAHsVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-IAY-DCcaNV 203
Cdd:PRK07867 33 EHIRGS-----AARAAalRARLdptRPPH-VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARdIAHaDC--QL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 204 IMVDTqkqlekilkiwKQLPHLKAVviykePPPNKMANVYTMEEFMELGNEvPEEALDAIIDtqQPNQCCVLVYTSGTTG 283
Cdd:PRK07867 105 VLTES-----------AHAELLDGL-----DPGVRVINVDSPAWADELAAH-RDAEPPFRVA--DPDDLFMLIFTSGTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 284 NPKGVMLSQDNITWTARYGSQAGDIRPAEVqqeVVVSyLPLSHIAAQIYDLWTGIQWGAQvcfaepdalkgslvntlrev 363
Cdd:PRK07867 166 DPKAVRCTHRKVASAGVMLAQRFGLGPDDV---CYVS-MPLFHSNAVMAGWAVALAAGAS-------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 364 eptshMGVPRVWekimeriqevaAQSGFIrrkmllwamsvtleqnltcpgSDLKPFTTRLADYL------VLAK------ 431
Cdd:PRK07867 222 -----IALRRKF-----------SASGFL---------------------PDVRRYGATYANYVgkplsyVLATperpdd 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 432 ----VRQALGfakcqkNfYGAAPMMAETQHFFlglNIRLYAGYGLSETsGPHFMSSPyNYRLYSSGKLVPGcrVKLVNQD 507
Cdd:PRK07867 265 adnpLRIVYG------N-EGAPGDIARFARRF---GCVVVDGFGSTEG-GVAITRTP-DTPPGALGPLPPG--VAIVDPD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 508 ------------------AEGIGEIC-LWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiIT 568
Cdd:PRK07867 331 tgtecppaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDW-MR 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 313747580 569 AGGENVPPVPIEEAVkMELPIISNAML-------IGDQrKFLSMLLTLKCTLDPD 616
Cdd:PRK07867 409 VDGENLGTAPIERIL-LRYPDATEVAVyavpdpvVGDQ-VMAALVLAPGAKFDPD 461
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
248-561 |
3.31e-08 |
|
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: 56.78 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 248 FMELGNEVPEEALDAIID--------TQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqevvV 319
Cdd:cd05918 76 FVPLDPSHPLQRLQEILQdtgakvvlTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSE-------S 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 320 SYLPLSHIA--AQIYDLWTGIQWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVwekimeriqevaaqsgfirrkml 397
Cdd:cd05918 149 RVLQFASYTfdVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSV----------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 398 lwAMSVTLEQnltCPgsDLKpfttrladYLVLA--KVRQALGFAKCQK----NFYGAA--PMMAETQHFFLGLNIRLyAG 469
Cdd:cd05918 206 --ARLLDPED---VP--SLR--------TLVLGgeALTQSDVDTWADRvrliNAYGPAecTIAATVSPVVPSTDPRN-IG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 470 YGLSETSgphFMSSPYNYrlyssGKLVP-GCrvklvnqdaegIGEICLWGRTIFMGYLNMEDKTCEA-IDEEGWLH---- 543
Cdd:cd05918 270 RPLGATC---WVVDPDNH-----DRLVPiGA-----------VGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegs 330
|
330 340
....*....|....*....|....*.
gi 313747580 544 --------TGDAGRLDADGFLYITGR 561
Cdd:cd05918 331 grgrrlyrTGDLVRYNPDGSLEYVGR 356
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
488-583 |
4.47e-08 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 56.55 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 488 RLYSSGKLVPGCRVKLVNQDAE-----GIGEIC------------LWG---RTIfMGYLNMEDktceaideeGWLHTGDA 547
Cdd:cd05967 409 KAGSPGKPVPGYQVQVLDEDGEpvgpnELGNIViklplppgclltLWKndeRFK-KLYLSKFP---------GYYDTGDA 478
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 313747580 548 GRLDADGFLYITGRLKELIITAG-----GEnvppvpIEEAV 583
Cdd:cd05967 479 GYKDEDGYLFIMGRTDDVINVAGhrlstGE------MEESV 513
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
268-596 |
4.63e-08 |
|
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: 55.94 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 268 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDIRpaevqqevvvsylpLSHIAAQIYDLWTG----- 337
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAhaahaWRREYELDSFPVR--------------LLQMASFSFDVFAGdfars 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 338 IQWGAQ--VCfaePDALK---GSLVNTLREVEPTSHMGVPRVWEKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLTCP 412
Cdd:cd17650 157 LLNGGTlvIC---PDEVKldpAALYDLILKSRITLMESTPALIRPVMAYVY---------RNGLDLSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 413 GSDLKPFTTRLADYLVLAkvrqalgfakcqkNFYGAAPMMAETQHFFLGLnirlyagyGLSETSGPHFMSSPY-NYRLY- 490
Cdd:cd17650 225 AQDFKTLAARFGQGMRII-------------NSYGVTEATIDSTYYEEGR--------DPLGDSANVPIGRPLpNTAMYv 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 491 --SSGKLVPgcrvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAIDE------EGWLHTGDAGRLDADGFLYITGRL 562
Cdd:cd17650 284 ldERLQPQP----------VGVAGELYIGGAGVARGYLNRPELTAERFVEnpfapgERMYRTGDLARWRADGNVELLGRV 353
|
330 340 350
....*....|....*....|....*....|....*...
gi 313747580 563 KELIITAGgenvppVPIE----EAVKMELPIISNAMLI 596
Cdd:cd17650 354 DHQVKIRG------FRIElgeiESQLARHPAIDEAVVA 385
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
489-597 |
5.32e-08 |
|
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: 55.80 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 489 LYSSGK-LVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRL 562
Cdd:cd05920 307 IHTQGRpMSPDDEIRVVDEEgnpvPPGeEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRI 386
|
90 100 110
....*....|....*....|....*....|....*
gi 313747580 563 KELiITAGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd05920 387 KDQ-INRGGEKIAAEEVENLL-LRHPAVHDAAVVA 419
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
262-596 |
6.37e-08 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 55.45 E-value: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 262 AIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAA--QIYDLWTGiq 339
Cdd:cd17649 86 GLLLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTP----GDRELQFASFNFDGAheQLLPPLIC-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 340 wGAQVCFAePDALKGSLVNTLREVEptsHMGV------PRVWEKIMERIQEVAAqsgfiRRKMLLWAMSVTLEQnltcpg 413
Cdd:cd17649 160 -GACVVLR-PDELWASADELAEMVR---ELGVtvldlpPAYLQQLAEEADRTGD-----GRPPSLRLYIFGGEA------ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 414 sdlkpfttrladyLVLAKVRQALGFAKcqknfygaapmmaetqhfflglniRLYAGYGLSET--SGPHFMSSPYNYRLYS 491
Cdd:cd17649 224 -------------LSPELLRRWLKAPV------------------------RLFNAYGPTEAtvTPLVWKCEAGAARAGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 492 S---GKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEAI-----DEEG--WLHTGDAGRLDADGFL 556
Cdd:cd17649 267 SmpiGRPLGGRSAYILDADLNpvpvgVTGELYIGGEGLARGYLGRPELTAERFvpdpfGAPGsrLYRTGDLARWRDDGVI 346
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 313747580 557 YITGRLKELiITAGGENVPPVPIEEAVkMELPIISNAMLI 596
Cdd:cd17649 347 EYLGRVDHQ-VKIRGFRIELGEIEAAL-LEHPGVREAAVV 384
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
493-582 |
6.85e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.54 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 493 GKLVPGCRVKLVNQDA------EGIGEICLWGRTIFMGYLNMEdktceAIDEEGWLHTGDAGRLDADGfLYITGRLKELI 566
Cdd:PRK05851 348 GNPIPGMEVRISPGDGaagvagREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGG-LVVCGRAKELI 421
|
90
....*....|....*.
gi 313747580 567 ITAgGENVPPVPIEEA 582
Cdd:PRK05851 422 TVA-GRNIFPTEIERV 436
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
118-599 |
7.55e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 55.42 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 118 DLIALGFKRQD-KW-EHISYSqyyllARRAAkgFLKQAHS------VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSP 189
Cdd:PRK13388 16 DTIAVRYGDRTwTWrEVLAEA-----AARAA--ALIALADpdrplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 190 EA-CQYIAY-DCcaNVIMVDTQ--KQLEKIlkiwkQLPHLKAVVIYKEPPPNKMAnvytmeefmELGNEVPEEALDAiiD 265
Cdd:PRK13388 89 AAlAADIRRaDC--QLLVTDAEhrPLLDGL-----DLPGVRVLDVDTPAYAELVA---------AAGALTPHREVDA--M 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 266 TQqpnqcCVLVYTSGTTGNPKGVMLSQDNITW-----TARYGSQAGDirpaevqqevvVSYL--PLSHIAAqIYDLWT-G 337
Cdd:PRK13388 151 DP-----FMLIFTSGTTGAPKAVRCSHGRLAFagralTERFGLTRDD-----------VCYVsmPLFHSNA-VMAGWApA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 338 IQWGAQVCfaepdalkgslvntlreveptshmgVPRVWekimeriqevaAQSGF---IRR----------KMLLWAMSvT 404
Cdd:PRK13388 214 VASGAAVA-------------------------LPAKF-----------SASGFlddVRRygatyfnyvgKPLAYILA-T 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 405 LEQnltcPGSDLKPfttrladylvlakVRQALGFAkcqknfygAAPM-MAETQHFFlglNIRLYAGYGLSETSG------ 477
Cdd:PRK13388 257 PER----PDDADNP-------------LRVAFGNE--------ASPRdIAEFSRRF---GCQVEDGYGSSEGAVivvrep 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 478 ---PHFMSSPY-NYRLYSSGKLVPgCRV-------KLVNQDaEGIGEIC-LWGRTIFMGYLNMEDKTCEAIdEEGWLHTG 545
Cdd:PRK13388 309 gtpPGSIGRGApGVAIYNPETLTE-CAVarfdahgALLNAD-EAIGELVnTAGAGFFEGYYNNPEATAERM-RHGMYWSG 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313747580 546 DAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML-------IGDQ 599
Cdd:PRK13388 386 DLAYRDADGWIYFAGRTADW-MRVDGENLSAAPI-ERILLRHPAINRVAVyavpderVGDQ 444
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
250-562 |
8.03e-08 |
|
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: 55.38 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 250 ELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEvqQEVVVS--------- 320
Cdd:cd12116 106 LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGD--RLLAVTtyafdisll 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 321 --YLPLSHiaaqiydlwtgiqwGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWekimeRIqevAAQSGFIRRKm 396
Cdd:cd12116 184 elLLPLLA--------------GARVVIAPRETQRdpEALARLIEAHSITVMQATPATW-----RM---LLDAGWQGRA- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 397 llwamSVTleqnLTCPGSDLKPfttRLADYLvLAKVRQALgfakcqkNFYG---------AAPMMAETQHFFLGLNIrly 467
Cdd:cd12116 241 -----GLT----ALCGGEALPP---DLAARL-LSRVGSLW-------NLYGptettiwstAARVTAAAGPIPIGRPL--- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 468 agyglsetsgphfmsspYNYRLY---SSGKLVPgcrvklvnqdaEG-IGEICLWGRTIFMGYLNMEDKTCEAI-----DE 538
Cdd:cd12116 298 -----------------ANTQVYvldAALRPVP-----------PGvPGELYIGGDGVAQGYLGRPALTAERFvpdpfAG 349
|
330 340
....*....|....*....|....*.
gi 313747580 539 EG--WLHTGDAGRLDADGFLYITGRL 562
Cdd:cd12116 350 PGsrLYRTGDLVRRRADGRLEYLGRA 375
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
277-597 |
1.01e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.42 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 277 YTSGTTGNPKGVMLSQ-DNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGiqwGAQVCFAEPDALKGS 355
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHaDPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATG---GSAVINSAPVTPEAA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 356 LVNTLReVEPTSHMGVPRVWEKIMEriqevaaqsgfirrkmllwAMSVTLEQNLTCPGSDLKPFTTRLADYLVlakvrqa 435
Cdd:PRK06060 229 AILSAR-FGPSVLYGVPNFFARVID-------------------SCSPDSFRSLRCVVSAGEALELGLAERLM------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 436 lgfakcqkNFYGAAPMMAetqhfflglnirlyaGYGLSETsGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAEGIG-- 512
Cdd:PRK06060 282 --------EFFGGIPILD---------------GIGSTEV-GQTFVSNRVDeWRLGTLGRVLPPYEIRVVAPDGTTAGpg 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 513 -EICLW--GRTIFMGYLNMEDKTCEaidEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPI 589
Cdd:PRK06060 338 vEGDLWvrGPAIAKGYWNRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRADDTEVI-GGVNVDPREVERLI-IEDEA 412
|
....*...
gi 313747580 590 ISNAMLIG 597
Cdd:PRK06060 413 VAEAAVVA 420
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-313 |
1.01e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 55.94 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 86 ADGRVRLRIDPSCPQ---LPYTVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKQA----HSVAI 158
Cdd:PRK12467 492 AEERARELVRWNAPAteyAPDCVHQLIEAQARQHPERPALVFGEQ----VLSYAELNRQANRLAHVLIAAGvgpdVLVGI 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 159 LGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDccANVIMVDTQKQLEKILKIWKQLPHLkaVVIYKEPPPNK 238
Cdd:PRK12467 568 AVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD--SGVRLLLTQSHLLAQLPVPAGLRSL--CLDEPADLLCG 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313747580 239 MANVYtmeefmelgnevPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNIT----WTARYGSQAGDIRPAEV 313
Cdd:PRK12467 644 YSGHN------------PEVALD-------PDNLAYVIYTSGSTGQPKGVAISHGALAnyvcVIAERLQLAADDSMLMV 703
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
275-561 |
1.12e-07 |
|
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: 55.04 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 275 LVYTSGTTGNPKGVMLSQDNIT----WTARYGSQAGDIRpaevqqevVVSYLPLSHIAAQiYDLWTGIQWGAQVCFAEPD 350
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLAnlvaWQARASSLGPGAR--------TLQFAGLGFDVSV-QEIFSTLCAGATLVLPPEE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 351 ALkgslvntlreveptshMGVPRVWEKIME-RIQEVAAQSGFIRRkmllWAmsvtleqnltcpgSDLKPFTTRLADylvL 429
Cdd:cd17651 212 VR----------------TDPPALAAWLDEqRISRVFLPTVALRA----LA-------------EHGRPLGVRLAA---L 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 430 AKVRQAlgfakcqknfyG-AAPMMAETQHFFLGL-NIRLYAGYGLSETsgpHFMSS------PYNYRLYSS-GKLVPGCR 500
Cdd:cd17651 256 RYLLTG-----------GeQLVLTEDLREFCAGLpGLRLHNHYGPTET---HVVTAlslpgdPAAWPAPPPiGRPIDNTR 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313747580 501 VKLVNQDAE----GI-GEICLWGRTIFMGYLNMEDKTCEAIDEEGWL------HTGDAGRLDADGFLYITGR 561
Cdd:cd17651 322 VYVLDAALRpvppGVpGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGR 393
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
274-597 |
1.61e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 54.45 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 274 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevvvsylplshiaaqiydLWtgiqwgaqvCFAEPD--- 350
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS--------------------FW---------NAADPGway 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 351 ----ALKGSLVNTLREVEPTSHMGVPRVWeKIMER--IQEVAAQSGFIRrkmLLWAMSVTLEQNLTcpgsdlkpfttrla 424
Cdd:cd05973 143 glyyAITGPLALGHPTILLEGGFSVESTW-RVIERlgVTNLAGSPTAYR---LLMAAGAEVPARPK-------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 425 dyLVLAKVRQAlgfakcqknfygAAPMMAETQHFF---LGLNIRLYagYGLSETSGP----HFMSSPYnyRLYSSGKLVP 497
Cdd:cd05973 205 --GRLRRVSSA------------GEPLTPEVIRWFdaaLGVPIHDH--YGQTELGMVlanhHALEHPV--HAGSAGRAMP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 498 GCRVKLVNQDAEGIGE-------------ICLWgrtiFMGYLNMEDKTCEAideeGWLHTGDAGRLDADGFLYITGRLKE 564
Cdd:cd05973 267 GWRVAVLDDDGDELGPgepgrlaidiansPLMW----FRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADD 338
|
330 340 350
....*....|....*....|....*....|...
gi 313747580 565 LIITAgGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd05973 339 VITMS-GYRIGPFDVESAL-IEHPAVAEAAVIG 369
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
461-596 |
4.47e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 52.96 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 461 GLNIRlyAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI--GEICL-WGRT----IFMGYLNMEDKTC 533
Cdd:cd05974 225 GLTIR--DGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPAteGEVALdLGDTrpvgLMKGYAGDPDKTA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313747580 534 EAIdEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISNAMLI 596
Cdd:cd05974 303 HAM-RGGYYRTGDIAMRDEDGYLTYVGRADD-VFKSSDYRISPFELESVL-IEHPAVAEAAVV 362
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
236-634 |
1.19e-06 |
|
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: 51.66 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 236 PNKMANVYTMEEFMELGNevPEEALDAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqq 315
Cdd:cd05915 124 VVMDEKAPEGYLAYEEAL--GEEADPVRVPERAA---CGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEK-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 316 EVVVSYLPLSHIAAQIYdLWTGIQWGAQ-VCFAEPDALKgSLVNTLREVEPTSHMGVPRVWEKIMERIQEVaaqsgfirR 394
Cdd:cd05915 197 DVVLPVVPMFHVNAWCL-PYAATLVGAKqVLPGPRLDPA-SLVELFDGEGVTFTAGVPTVWLALADYLEST--------G 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 395 KMLLWAMSVTleqnltcPGSDLKPFTTRLADYLVLAKVRQALGFAKCqknfYG---AAPMMAETQHFFLGLNIRLYAGYG 471
Cdd:cd05915 267 HRLKTLRRLV-------VGGSAAPRSLIARFERMGVEVRQGYGLTET----SPvvvQNFVKSHLESLSEEEKLTLKAKTG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 472 LS------ETSGPHFMSSPYnyrlyssgklvpgcrvklvnqDAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTG 545
Cdd:cd05915 336 LPiplvrlRVADEEGRPVPK---------------------DGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 546 DAGRLDADGFLYITGRLKElIITAGGENVPPVPIeEAVKMELPIISNAMLIG--DQRKFLSMLLTLKCTldpdtsdQTDN 623
Cdd:cd05915 395 DIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDL-ENALMGHPKVKEAAVVAipHPKWQERPLAVVVPR-------GEKP 465
|
410
....*....|.
gi 313747580 624 LTEQAMEFCQR 634
Cdd:cd05915 466 TPEELNEHLLK 476
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
511-575 |
1.46e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 51.65 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 511 IGEICLWGRTIFMGYLNMEDKTCEA--------IDE---EG------WLHTGDAGRLdADGFLYITGRLKELIITAGGEN 573
Cdd:PRK07769 418 IGEIWLHGNNIGTGYWGKPEETAATfqnilksrLSEshaEGapddalWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNH 496
|
..
gi 313747580 574 VP 575
Cdd:PRK07769 497 YP 498
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
250-571 |
1.59e-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: 51.31 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 250 ELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAA 329
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVD----LATFPLFALFG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 330 QIYDLWTGIQWGAQVCFAEPDALKgsLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvtleqnL 409
Cdd:cd05910 141 PALGLTSVIPDMDPTRPARADPQK--LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRR--------------V 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 410 TCPGSDLKPFttrladylVLAKVRQALGFAKCQKNFYGAapmmaeTQhfflGLNIRLYAGYGLSETSGPhfmsSPYNYRL 489
Cdd:cd05910 205 LSAGAPVPIA--------LAARLRKMLSDEAEILTPYGA------TE----ALPVSSIGSRELLATTTA----ATSGGAG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 490 YSSGKLVPGCRVKLVNQDAE--------------GIGEICLWGRTIFMGYLNMEDKTCEA-IDEEG---WLHTGDAGRLD 551
Cdd:cd05910 263 TCVGRPIPGVRVRIIEIDDEpiaewddtlelprgEIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLD 342
|
330 340
....*....|....*....|
gi 313747580 552 ADGFLYITGRLKELIITAGG 571
Cdd:cd05910 343 DEGRLWFCGRKAHRVITTGG 362
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
156-596 |
1.94e-06 |
|
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: 50.94 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 156 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILKIWKQLPHLKAVVIYKEPP 235
Cdd:cd17656 41 VAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL--TQRHLKSKLSFNKSTILLEDPSISQEDT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 236 PNkmanvytmeefmeLGNEVPEEALDAIIdtqqpnqccvlvYTSGTTGNPKGVMLSQDNITWTARYG-SQAGDIRPAEVQ 314
Cdd:cd17656 119 SN-------------IDYINNSDDLLYII------------YTSGTTGKPKGVQLEHKNMVNLLHFErEKTNINFSDKVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 315 QEVVVSYlplshiaaqiydlwtgiqwgaQVCFAEPDA--LKGSlvnTLREVEPTSHMGVPRVWEKI-MERIQEVAAQSGF 391
Cdd:cd17656 174 QFATCSF---------------------DVCYQEIFStlLSGG---TLYIIREETKRDVEQLFDLVkRHNIEVVFLPVAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 392 IRrkmllwamsvtleqnltcpgsdlkpfttrladylVLAKVRQALG-FAKCQKNFYGAAPMMAETQHF---FLGLNIRLY 467
Cdd:cd17656 230 LK----------------------------------FIFSEREFINrFPTCVKHIITAGEQLVITNEFkemLHEHNVHLH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 468 AGYGLSET---SGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEAI--- 536
Cdd:cd17656 276 NHYGPSEThvvTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQlqpqgIVGELYISGASVARGYLNRQELTAEKFfpd 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313747580 537 ---DEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAMLI 596
Cdd:cd17656 356 pfdPNERMYRTGDLARYLPDGNIEFLGRADHQ-VKIRGYRIELGEI-EAQLLNHPGVSEAVVL 416
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
510-590 |
2.12e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.90 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 510 GIGEICLWGRTIFMGYLNMEDKT------------------CEAIDEEGWLHTGDAGrLDADGFLYITGRLKELIITaGG 571
Cdd:PRK12476 428 EVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshaDGAADDGTWLRTGDLG-VYLDGELYITGRIADLIVI-DG 505
|
90
....*....|....*....
gi 313747580 572 ENVPPVPIEEAVKMELPII 590
Cdd:PRK12476 506 RNHYPQDIEATVAEASPMV 524
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
107-561 |
3.30e-06 |
|
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: 50.28 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 107 RMFYEALDKYGDLIALgfkrQDKWEHISYSQ---------YYLLARRAAKGFLkqahsVAILGFNSPEWFFSAVGTVFAG 177
Cdd:cd12117 1 ELFEEQAARTPDAVAV----VYGDRSLTYAElneranrlaRRLRAAGVGPGDV-----VGVLAERSPELVVALLAVLKAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 178 GIVTGIYTTSSPEACQYIAYDccANVIMVDTQKQLEKilkiwkQLPHLKAVVIYKEPPPnkmanvytmeefmelgnEVPE 257
Cdd:cd12117 72 AAYVPLDPELPAERLAFMLAD--AGAKVLLTDRSLAG------RAGGLEVAVVIDEALD-----------------AGPA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 258 EALDAIIDtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARyGSQAGDIRPaevqQEVVVSYLPLSHIAAqIYDLWTG 337
Cdd:cd12117 127 GNPAVPVS---PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK-NTNYVTLGP----DDRVLQTSPLAFDAS-TFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 338 IQWGAQVCFAEPDALKGslvntlreveptshmgvprvwekiMERIQEVAAQSGFirrkMLLWaMSVTLEQNLTcpgsDLK 417
Cdd:cd12117 198 LLNGARLVLAPKGTLLD------------------------PDALGALIAEEGV----TVLW-LTAALFNQLA----DED 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 418 PFTTRLADYLV-------LAKVRQALgfAKCQKnfygaapmmaetqhfflglnIRLYAGYGLSET---SGPHFMSSPYNY 487
Cdd:cd12117 245 PECFAGLRELLtggevvsPPHVRRVL--AACPG--------------------LRLVNGYGPTENttfTTSHVVTELDEV 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 488 RlySS---GKLVPGCRVKLVNQD----AEGI-GEICLWGRTIFMGYLNMEDKTCEAIDEEGWL------HTGDAGRLDAD 553
Cdd:cd12117 303 A--GSipiGRPIANTRVYVLDEDgrpvPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPD 380
|
....*...
gi 313747580 554 GFLYITGR 561
Cdd:cd12117 381 GRLEFLGR 388
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
131-562 |
6.79e-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: 49.19 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAkGFLKQA-----HSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 205
Cdd:cd12114 11 GTLTYGELAERARRVA-GALKAAgvrpgDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 206 VDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKmanvytmeefmelgnevpeealdaiidtQQPNQCCVLVYTSGTTGNP 285
Cdd:cd12114 90 TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVD----------------------------VAPDDLAYVIFTSGSTGTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 286 KGVMLSQDN-----ITWTARYGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDalkgslvntl 360
Cdd:cd12114 142 KGVMISHRAalntiLDINRRFAVGPDD---------RVLALSSLSFDLS-VYDIFGALSAGATLVLPDEA---------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 361 REVEPTShmgvprvWEKIMERIQ-----EVAAQSgfirrKMLLWAmsvtLEQNLTCPGSdlkpftTRLA----DYLVL-- 429
Cdd:cd12114 202 RRRDPAH-------WAELIERHGvtlwnSVPALL-----EMLLDV----LEAAQALLPS------LRLVllsgDWIPLdl 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 430 -AKVRQALgfakcqknfygaapmmAETQHFFLGlnirlyagyGLSETS-----------GPHFMSSPYnyrlyssGKLVP 497
Cdd:cd12114 260 pARLRALA----------------PDARLISLG---------GATEASiwsiyhpidevPPDWRSIPY-------GRPLA 307
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313747580 498 GCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA----IDEEGWLHTGDAGRLDADGFLYITGRL 562
Cdd:cd12114 308 NQRYRVLDPRGRdcpdwVPGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLGRR 381
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
466-597 |
8.62e-06 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 49.00 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 466 LYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICLWGR-----TIFMGYLNMEDKTCEA 535
Cdd:cd05928 319 IYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLppgteGDIGIRVKpirpfGLFSGYVDNPEKTAAT 398
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313747580 536 IDEEGWLhTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:cd05928 399 IRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSS-GYRIGPFEVESAL-IEHPAVVESAVVS 457
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
74-597 |
1.50e-05 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 48.34 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 74 WDAPEEAL-WTTRADGRVRLRIDPSCPQ---LPYTVHRMFYEALDKY----GDLIALGFKRQD--KWEHISYSQYYLLAR 143
Cdd:cd17634 16 WGEAGKILdWITPYQKVKNTSFAPGAPSikwFEDATLNLAANALDRHlrenGDRTAIIYEGDDtsQSRTISYRELHREVC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 144 RAAKGFL----KQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM-----------VDT 208
Cdd:cd17634 96 RFAGTLLdlgvKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLItadggvragrsVPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 209 QKQLEKILKIwkQLPHLKAVVIYKepppnKMANVYTMEE-----FMELGNEVPEEALDAIIDTQQPnqcCVLVYTSGTTG 283
Cdd:cd17634 176 KKNVDDALNP--NVTSVEHVIVLK-----RTGSDIDWQEgrdlwWRDLIAKASPEHQPEAMNAEDP---LFILYTSGTTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 284 NPKGVMlsQDN------ITWTARYgsqAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAE--PDALKGS 355
Cdd:cd17634 246 KPKGVL--HTTggylvyAATTMKY---VFDYGPGDI----YWCTADVGWVTGHSYLLYGPLACGATTLLYEgvPNWPTPA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 356 LVNTLREVEPTSHMGV-PRVWEKIMeriqevAAQSGFIRRKmllwamSVTLEQNLTCPGSDLKPFTTRLAdylvlakvRQ 434
Cdd:cd17634 317 RMWQVVDKHGVNILYTaPTAIRALM------AAGDDAIEGT------DRSSLRILGSVGEPINPEAYEWY--------WK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 435 ALGFAKCqknfygaaPMMAEtqhfflglnirlyagYGLSETSGphFMSSP----YNYRLYSSGKLVPGCRVKLVnqDAEG 510
Cdd:cd17634 377 KIGKEKC--------PVVDT---------------WWQTETGG--FMITPlpgaIELKAGSATRPVFGVQPAVV--DNEG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 511 -------IGEICL---W-GRTifMGYLNMEDKTCEAIDE--EGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPV 577
Cdd:cd17634 430 hpqpggtEGNLVItdpWpGQT--RTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDD-VINVAGHRLGTA 506
|
570 580
....*....|....*....|
gi 313747580 578 PIEEAVKMElPIISNAMLIG 597
Cdd:cd17634 507 EIESVLVAH-PKVAEAAVVG 525
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
248-562 |
1.54e-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: 48.20 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 248 FMELGNEVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQD---NITWTARygSQAGDIRPAEVQQEV 317
Cdd:cd17644 77 YVPLDPNYPQERLTYILeDAQisvlltQPENLAYVIYTSGSTGKPKGVMIEHQslvNLSHGLI--KEYGITSSDRVLQFA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 318 VVSYlplSHIAAQIYDLWtgiqwgaqvcfaepdaLKG-SLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQsgfirrkM 396
Cdd:cd17644 155 SIAF---DVAAEEIYVTL----------------LSGaTLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAY-------W 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 397 LLWAMSVTLEqnlTCPGsdlkPFTTRLAdylvlakvrqALGFAKCQknfygaaPMMAETQHFFLGLNIRLYAGYGLSE-- 474
Cdd:cd17644 209 HLLVLELLLS---TIDL----PSSLRLV----------IVGGEAVQ-------PELVRQWQKNVGNFIQLINVYGPTEat 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 475 -TSGPHFMSSPYNYRLYSS--GKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCE-------AIDEE 539
Cdd:cd17644 265 iAATVCRLTQLTERNITSVpiGRPIANTQVYILDENLQPVpvgvpGELHIGGVGLARGYLNRPELTAEkfishpfNSSES 344
|
330 340
....*....|....*....|....
gi 313747580 540 GWLH-TGDAGRLDADGFLYITGRL 562
Cdd:cd17644 345 ERLYkTGDLARYLPDGNIEYLGRI 368
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
268-562 |
1.78e-05 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 48.04 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 268 QPNQCCVLVYTSGTTGNPKGVMLSQDNI-----TWTARYGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGA 342
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHAGIvnrllWMQDEYPLGPGD---------RVLQKTPLSFDVS-VWELFWPLVAGA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 343 QVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEkimERIQEVAAQSGfirrkmllwamsVTLEQnLTCPGSDLKPft 420
Cdd:cd17646 206 RLVVARPGGHRdpAYLAALIREHGVTTCHFVPSMLR---VFLAEPAAGSC------------ASLRR-VFCSGEALPP-- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 421 tRLADylvlakvrqalgfakcqknfygaapmmaetqHFFLGLNIRLYAGYGLSETS--GPHFMSSPYNYRLYSS-GKLVP 497
Cdd:cd17646 268 -ELAA-------------------------------RFLALPGAELHNLYGPTEAAidVTHWPVRGPAETPSVPiGRPVP 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313747580 498 GCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAI-----DEEGWLH-TGDAGRLDADGFLYITGRL 562
Cdd:cd17646 316 NTRLYVL--DDALrpvpvgvPGELYLGGVQLARGYLGRPALTAERFvpdpfGPGSRMYrTGDLARWRPDGALEFLGRS 391
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
203-597 |
3.19e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.08 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 203 VIMVDtQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMA-------NVYTMEEFMElGN-------EVPEEALDAIidtqq 268
Cdd:PRK05620 114 VIVAD-PRLAEQLGEILKECPCVRAVVFIGPSDADSAAahmpegiKVYSYEALLD-GRstvydwpELDETTAAAI----- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 269 pnqcCvlvYTSGTTGNPKGVMLSQDNItWTARYGSQAGD---IRPAEvqqevvvSYL---PLSHIAAqiydlW----TGI 338
Cdd:PRK05620 187 ----C---YSTGTTGAPKGVVYSHRSL-YLQSLSLRTTDslaVTHGE-------SFLccvPIYHVLS-----WgvplAAF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 339 QWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqSGFIR---RKMLLwamsvtleQNLTCPGSD 415
Cdd:PRK05620 247 MSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLM---------VHYLKnppERMSL--------QEIYVGGSA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 416 LKPfttrladylVLAKVRQALgfakcqknfYGaapmmaetqhfflglnIRLYAGYGLSETSGPHFMSSP---------YN 486
Cdd:PRK05620 310 VPP---------ILIKAWEER---------YG----------------VDVVHVWGMTETSPVGTVARPpsgvsgearWA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 487 YRlYSSGKLVPGCRVKLVNqDAEGI-------GEICLWGRTIFMGYLNME----------------DKTCEAIDEEGWLH 543
Cdd:PRK05620 356 YR-VSQGRFPASLEYRIVN-DGQVMestdrneGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLR 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 313747580 544 TGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISNAMLIG 597
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARD-VIRSGGEWIYSAQLENYI-MAAPEVVECAVIG 485
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
465-616 |
9.13e-05 |
|
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: 45.62 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 465 RLYAGYGLSE-----TSGPhfMSSPYNYrlYSSGKLVPGCRVKLVNQD----AEGI-GEICLWGRTIFMGYLNMEDKTCE 534
Cdd:cd17645 236 KLVNNYGPTEntvvaTSFE--IDKPYAN--IPIGKPIDNTRVYILDEAlqlqPIGVaGELCIAGEGLARGYLNRPELTAE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 535 A------IDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEAVkMELPIISNAMLI----GDQRKFLS 604
Cdd:cd17645 312 KfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ-VKIRGYRIEPGEIEPFL-MNHPLIELAAVLakedADGRKYLV 389
|
170
....*....|..
gi 313747580 605 MLLTLKCTLDPD 616
Cdd:cd17645 390 AYVTAPEEIPHE 401
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
497-562 |
9.80e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 45.66 E-value: 9.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313747580 497 PGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDaDGFLYITGRL 562
Cdd:PRK04813 325 PDSPLLIIDEEGTklpdgEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYLE-DGLLFYQGRI 397
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
256-624 |
9.88e-05 |
|
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: 45.39 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 256 PEEALDAIIDTQQ-------PNQCCVLVYTSGTTGNPKGVMLSQDN----ITWtarygsqAGDIRPAEVQQEVVVSY--- 321
Cdd:cd12115 84 PPERLRFILEDAQarlvltdPDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQW-------AAAAFSAEELAGVLASTsic 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 322 LPLShiaaqIYDLWTGIQWGAQVCFAE--------PDALKGSLVNTlreveptshmgVPRVwekimerIQEVAAQSGFIR 393
Cdd:cd12115 157 FDLS-----VFELFGPLATGGKVVLADnvlalpdlPAAAEVTLINT-----------VPSA-------AAELLRHDALPA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 394 rkmllwAMSVTleqNLTcpGsdlKPFTTRLADYLvlakvrqalgfakcqknfYGAAPMmaetqhfflglnIRLYAGYGLS 473
Cdd:cd12115 214 ------SVRVV---NLA--G---EPLPRDLVQRL------------------YARLQV------------ERVVNLYGPS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 474 ET---SGPHFMsSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWL- 542
Cdd:cd12115 250 EDttySTVAPV-PPGASGEVSIGRPLANTQAYVL--DRALqpvplgvPGELYIGGAGVARGYLGRPGLTAERFLPDPFGp 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 543 -----HTGDAGRLDADGFLYITGRLKELIITAGgenvppVPIE----EAVKMELPIISNA--MLIGDQ--RKFLSMLLTL 609
Cdd:cd12115 327 garlyRTGDLVRWRPDGLLEFLGRADNQVKVRG------FRIElgeiEAALRSIPGVREAvvVAIGDAagERRLVAYIVA 400
|
410
....*....|....*
gi 313747580 610 KCTLDPDTSDQTDNL 624
Cdd:cd12115 401 EPGAAGLVEDLRRHL 415
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
131-344 |
1.26e-04 |
|
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: 45.36 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 131 EHISYSQYYLLARRAAKGF-----LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYiAYDCC-ANVI 204
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALlahagLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLH-CFRCCgAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 205 MVDT--QKQLEKILkiwkqlPHLKA--VVIY---KEPPPNKMANVytMEEFMELGNEVPEEALDAIIDTQQPnqcCVLVY 277
Cdd:cd05938 83 VVAPelQEAVEEVL------PALRAdgVSVWylsHTSNTEGVISL--LDKVDAASDEPVPASLRAHVTIKSP---ALYIY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 278 TSGTTGNPKGVMLSQDNItWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 344
Cdd:cd05938 152 TSGTTGLPKAARISHLRV-LQCSGFLSLCGVT----ADDVIYITLPLYHSSGFLLGIGGCIELGATC 213
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
256-296 |
1.36e-04 |
|
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: 44.99 E-value: 1.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 313747580 256 PEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNIT 296
Cdd:cd17643 72 PVERIAFILaDSGpsllltDPDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
264-574 |
1.37e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.19 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 264 IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDirPAEvqQEVVVSYLPLSHiaaqiydlwtgiQWGAQ 343
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS--PKE--DDVMMSFLPPFH------------AYGFN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 344 VCfaepdalkgSLVNTLreveptshMGVPRVW-------EKIMERIQEVAAqsgfirrkmllwamsvtleqnlTCPGSdl 416
Cdd:PRK06334 241 SC---------TLFPLL--------SGVPVVFaynplypKKIVEMIDEAKV----------------------TFLGS-- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 417 kpfTTRLADYLVLAKVRQ-----ALGFAKCQKNFYGAApMMAETQHFFLglNIRLYAGYGLSETSgP----HFMSSPYNY 487
Cdd:PRK06334 280 ---TPVFFDYILKTAKKQesclpSLRFVVIGGDAFKDS-LYQEALKTFP--HIQLRQGYGTTECS-PvitiNTVNSPKHE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 488 RLYssGKLVPGCRVKLVNQDAEG------IGEICLWGRTIFMGYLNmEDKTCEAI--DEEGWLHTGDAGRLDADGFLYIT 559
Cdd:PRK06334 353 SCV--GMPIRGMDVLIVSEETKVpvssgeTGLVLTRGTSLFSGYLG-EDFGQGFVelGGETWYVTGDLGYVDRHGELFLK 429
|
330
....*....|....*
gi 313747580 560 GRLKELiITAGGENV 574
Cdd:PRK06334 430 GRLSRF-VKIGAEMV 443
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
511-584 |
1.57e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 44.93 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 511 IGEICLWGRTIFMGYLNMEDKT-----------CEAIDEEGWLHTGDAGRLDaDGFLYITGRLKELIITAgGENVPPVPI 579
Cdd:PRK05850 397 VGEIWVHGDNVAAGYWQKPEETertfgatlvdpSPGTPEGPWLRTGDLGFIS-EGELFIVGRIKDLLIVD-GRNHYPDDI 474
|
....*
gi 313747580 580 EEAVK 584
Cdd:PRK05850 475 EATIQ 479
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-562 |
2.21e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.95 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 105 VHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKQAHS----VAILGFNSPEWFFSAVGTVFAGGIV 180
Cdd:PRK12316 3059 VHRLFEEQVERTPDAVALAFGEQ----RLSYAELNRRANRLAHRLIERGVGpdvlVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 181 TGIYTTSSPEACQYIAYDCCANVIMvdTQKQLekilkiwkQLPHLKAV-VIYKEPPPNkmanvytmeefmELGNEVPEEA 259
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLL--SQSHL--------RLPLAQGVqVLDLDRGDE------------NYAEANPAIR 3192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 260 LDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAqIYDLWTGIQ 339
Cdd:PRK12316 3193 TM-------PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGL----GVGDRVLQFTTFSFDVF-VEELFWPLM 3260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 340 WGAQVCFAEPDalKGSLVNTLREVEPTSHMGVPR-VWEKIMERIQEVAAQSGFIRRKMLlwamsvtleqnltCPGSDLKP 418
Cdd:PRK12316 3261 SGARVVLAGPE--DWRDPALLVELINSEGVDVLHaYPSMLQAFLEEEDAHRCTSLKRIV-------------CGGEALPA 3325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 419 fttrladylvlaKVRQALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSetsgphfMSSPYNYRLYSSGKLVPg 498
Cdd:PRK12316 3326 ------------DLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRP-------IANRACYILDGSLEPVP- 3385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 499 crvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAI------DEEGWLHTGDAGRLDADGFLYITGRL 562
Cdd:PRK12316 3386 ---------VGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLARYRADGVIEYIGRV 3446
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
256-352 |
2.28e-04 |
|
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: 44.17 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 256 PEEALDAIIDTQQPnqCCVL---------VYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqEVVVSYLPLSH 326
Cdd:cd17652 72 PAERIAYMLADARP--ALLLttpdnlayvIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPG----SRVLQFASPSF 145
|
90 100
....*....|....*....|....*.
gi 313747580 327 IAAqIYDLWTGIQWGAQVCFAEPDAL 352
Cdd:cd17652 146 DAS-VWELLMALLAGATLVLAPAEEL 170
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
493-571 |
2.80e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 44.12 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 493 GKLVPGCRVKLVNQDAE--------------GIGEICLWGRTIFMGYLNMEDKTCEA--IDEEG--WLHTGDAGRLDADG 554
Cdd:PRK09274 355 GRPVDGVEVRIIAISDApipewddalrlatgEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQG 434
|
90
....*....|....*..
gi 313747580 555 FLYITGRLKELIITAGG 571
Cdd:PRK09274 435 RLWFCGRKAHRVETAGG 451
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-307 |
2.87e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.56 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 72 AQWDAPEEALwttradgrvrlridPSCPQlpytVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLK 151
Cdd:PRK12316 1990 ADWDRTPEAY--------------PRGPG----VHQRIAEQAARAPEAIAVVFGDQ----HLSYAELDSRANRLAHRLRA 2047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 152 QA----HSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILkiwkqlphlka 227
Cdd:PRK12316 2048 RGvgpeVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL--TQRHLLERL----------- 2114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 228 vviykePPPNKMAN--VYTMEEFMELGNEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQ----DNITWT-AR 300
Cdd:PRK12316 2115 ------PLPAGVARlpLDRDAEWADYPDTAPAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHgalvAHCQAAgER 2181
|
....*..
gi 313747580 301 YGSQAGD 307
Cdd:PRK12316 2182 YELSPAD 2188
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
258-344 |
3.47e-04 |
|
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: 43.57 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 258 EALDAIIDTQQPNQCCV-------LVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQ 330
Cdd:cd05939 85 DPLLTQSSTEPPSQDDVnfrdklfYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRP----EDVVYDCLPLYHSAGG 160
|
90
....*....|....
gi 313747580 331 IYDLWTGIQWGAQV 344
Cdd:cd05939 161 IMGVGQALLHGSTV 174
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
276-294 |
6.31e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 42.96 E-value: 6.31e-04
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
273-344 |
9.08e-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: 42.34 E-value: 9.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313747580 273 CVLVYTSGTTGNPKGVMLSQDNItWTARYGSQAGDIRpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 344
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGA---LPSDVLYTCLPLYHSTALIVGWSACLASGATL 151
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
268-351 |
9.69e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.72 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313747580 268 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT----WT-ARYGSQAGDI----RPAEVQQEVVVSYLPLshIAaqiydlwtgi 338
Cdd:PRK10252 596 QPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllWMqNHYPLTADDVvlqkTPCSFDVSVWEFFWPF--IA---------- 663
|
90
....*....|...
gi 313747580 339 qwGAQVCFAEPDA 351
Cdd:PRK10252 664 --GAKLVMAEPEA 674
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
275-326 |
1.49e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 41.85 E-value: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 313747580 275 LVYTSGTTGNPKGVMLSQDNITWT-----ARYGSQAGDIRPAEVqqeVVVSYLPLSH 326
Cdd:PRK05850 165 LQYTSGSTRTPAGVMVSHRNVIANfeqlmSDYFGDTGGVPPPDT---TVVSWLPFYH 218
|
|
| |
