|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
20-486 |
0e+00 |
|
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: 627.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLLAMPGqdvagapvvmsverkpgqsapnltdqdrlspllpnHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDY 179
Cdd:cd17652 81 ADARPALLLTTPD-----------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 180 VRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALAPLEEGGgLP 259
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD-LP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 260 PGLTLLVAGEACPAPVAKSWARDRVMINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGEL 339
Cdd:cd17652 205 DLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGEL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 340 YMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDG 419
Cdd:cd17652 285 YIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPG 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214003850 420 VAQAVVTEHD-----NRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALP 486
Cdd:cd17652 365 VAEAVVVVRDdrpgdKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
4-577 |
0e+00 |
|
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: 566.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 4 EASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAY 83
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 84 VPVDPDYPADRRRHMLDDTAAHCLLAMPGQDVA----GAPVVmSVERKPGQSAPnltDQDRLSPLLPNHPAYVIYTSGST 159
Cdd:COG1020 554 VPLDPAYPAERLAYMLEDAGARLVLTQSALAARlpelGVPVL-ALDALALAAEP---ATNPPVPVTPDDLAYVIYTSGST 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 160 GQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGI 239
Cdd:COG1020 630 GRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 240 THVTLPPSALAPL-EEGGGLPPGL-TLLVAGEACPAPVAKSWAR---DRVMINAYGPTEATVAVTA---SDPLTGEGTPP 311
Cdd:COG1020 710 TVLNLTPSLLRALlDAAPEALPSLrLVLVGGEALPPELVRRWRArlpGARLVNLYGPTETTVDSTYyevTPPDADGGSVP 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 312 IGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFV 391
Cdd:COG1020 790 IGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFL 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 392 GRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT-----EHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVV 466
Cdd:COG1020 870 GRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVaredaPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAV 949
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 467 VGLPRLPTSPNGKIDRAALPDPDREGAERvtsGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARI 546
Cdd:COG1020 950 VLLLPLPLTGNGKLDRLALPAPAAAAAAA---AAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARA 1026
|
570 580 590
....*....|....*....|....*....|.
gi 214003850 547 RQSLQVRLRVQAFFNAPTVAQLAKVLDGAPS 577
Cdd:COG1020 1027 ARLLLLLLLLLLLFLAAAAAAAAAAAAAAAA 1057
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
20-485 |
0e+00 |
|
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: 530.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLLampgqdvagapvvmsverkpgqsapnlTDqdrlspllPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDY 179
Cdd:cd05930 81 EDSGAKLVL---------------------------TD--------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 180 VRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALAPLEEGGGL- 258
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELa 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 259 -PPGL-TLLVAGEACPAPVAKSWAR---DRVMINAYGPTEATVAVTA---SDPLTGEGTPPIGRPITSVSTYILDDKLQP 330
Cdd:cd05930 206 aLPSLrLVLVGGEALPPDLVRRWREllpGARLVNLYGPTEATVDATYyrvPPDDEEDGRVPIGRPIPNTRVYVLDENLRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 331 VPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEV 410
Cdd:cd05930 286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF-GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 411 ESALLAVDGVAQAVVTEHDN-----RLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05930 365 EAALLAHPGVREAAVVAREDgdgekRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
10-573 |
1.22e-162 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 514.33 E-value: 1.22e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 10 ALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPD 89
Cdd:PRK12467 516 QLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 YPADRRRHMLDDTAAHCLLAMPGQdVAGAPVVMSVERKP-GQSAPNLTDQDRLSPLLPNHP---AYVIYTSGSTGQPKGV 165
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHL-LAQLPVPAGLRSLClDEPADLLCGYSGHNPEVALDPdnlAYVIYTSGSTGQPKGV 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 166 LVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLP 245
Cdd:PRK12467 675 AISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIV 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 246 PSALAPLEEGG---GLPPGLTLLVAGEACPAPVAKSWARDRV---MINAYGPTEATVAVTASdPLTGEGTP----PIGRP 315
Cdd:PRK12467 755 PSHLQALLQASrvaLPRPQRALVCGGEALQVDLLARVRALGPgarLINHYGPTETTVGVSTY-ELSDEERDfgnvPIGQP 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 316 ITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVD 395
Cdd:PRK12467 834 LANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGVIEYLGRMD 913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 396 DQLKVRGHRIEPGEVESALLAVDGVAQAVVT----EHDNRLIAYVVGTGGARVAA-----EDLLPPLRKRLPGYLVPDVV 466
Cdd:PRK12467 914 HQVKIRGFRIELGEIEARLLAQPGVREAVVLaqpgDAGLQLVAYLVPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHL 993
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 467 VGLPRLPTSPNGKIDRAALPDPDreGAERVTSGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARI 546
Cdd:PRK12467 994 LLLDSLPLTPNGKLDRKALPKPD--ASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRV 1071
|
570 580
....*....|....*....|....*..
gi 214003850 547 RQSLQVRLRVQAFFNAPTVAQLAKVLD 573
Cdd:PRK12467 1072 RQRLGIQVPLRTLFEHQTLAGFAQAVA 1098
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
10-485 |
1.95e-160 |
|
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: 466.68 E-value: 1.95e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 10 ALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPD 89
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 YPADRRRHMLDDTAAHCLL---AMPGQDVAGAPVVMSVERKPGQSAPNLtdqdrLSPLLPNHPAYVIYTSGSTGQPKGVL 166
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLtdrSLAGRAGGLEVAVVIDEALDAGPAGNP-----AVPVSPDDLAYVMYTSGSTGRPKGVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 VTHRGIPNLA--DDYVRrqnLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGIT--HV 242
Cdd:cd12117 156 VTHRGVVRLVknTNYVT---LGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTvlWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 243 TLP---------PSALAPLEEggglppgltLLVAGEACPAP----VAKSWARDRVmINAYGPTEATVAVTA---SDPLTG 306
Cdd:cd12117 233 TAAlfnqladedPECFAGLRE---------LLTGGEVVSPPhvrrVLAACPGLRL-VNGYGPTENTTFTTShvvTELDEV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 307 EGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDG 386
Cdd:cd12117 303 AGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF-GPGERLYRTGDLARWLPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 387 QLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEH-----DNRLIAYVVGTGGarVAAEDLLPPLRKRLPGYL 461
Cdd:cd12117 382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVRedaggDKRLVAYVVAEGA--LDAAELRAFLRERLPAYM 459
|
490 500
....*....|....*....|....
gi 214003850 462 VPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd12117 460 VPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
33-425 |
4.39e-156 |
|
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: 452.88 E-value: 4.39e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 33 SYAELNGEANLLARRLV-EHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLAMP 111
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 112 G----QDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVP 187
Cdd:TIGR01733 81 AlasrLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 188 DSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPL-ARLVRDQGITHVTLPPSALAPL-EEGGGLPPGL-TL 264
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVLNLTPSLLALLaAALPPALASLrLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 265 LVAGEACPAPVAKSWAR---DRVMINAYGPTEATVAVTA----SDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVG 337
Cdd:TIGR01733 241 ILGGEALTPALVDRWRArgpGARLINLYGPTETTVWSTAtlvdPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 338 ELYMTGPGLARGYLRRPAATAERFLPNPF-GGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLA 416
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400
|
....*....
gi 214003850 417 VDGVAQAVV 425
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
12-486 |
1.90e-155 |
|
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: 454.49 E-value: 1.90e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 12 FEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYP 91
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 92 ADRRRHMLDDTAAHCLLAMPGQDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRG 171
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 172 IPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALAP 251
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 252 LEE----GGGLPPGLT-LLVAGEACPA----PVAKSWARDRVMINAYGPTEATVA---VTASDPLTGEGTPPIGRPITSV 319
Cdd:cd17651 241 LAEhgrpLGVRLAALRyLLTGGEQLVLtedlREFCAGLPGLRLHNHYGPTETHVVtalSLPGDPAAWPAPPPIGRPIDNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 320 STYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLK 399
Cdd:cd17651 321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF-VPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 400 VRGHRIEPGEVESALLAVDGVAQAVVTEHDN-----RLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPT 474
Cdd:cd17651 400 IRGFRIELGEIEAALARHPGVREAVVLAREDrpgekRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
|
490
....*....|..
gi 214003850 475 SPNGKIDRAALP 486
Cdd:cd17651 480 TPNGKLDRRALP 491
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
11-489 |
1.14e-153 |
|
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: 449.86 E-value: 1.14e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLA----MPGQDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLlpnhpAYVIYTSGSTGQPKGVL 166
Cdd:cd17655 82 PEERIQYILEDSGADILLTqshlQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDL-----AYVIYTSGSTGKPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 VTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPP 246
Cdd:cd17655 157 IEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 247 SALAPLEEGGGLP--PGLTLLVAGEACPAPVAKSW----ARDRVMINAYGPTEATVAVTA--SDPLTGEGT-PPIGRPIT 317
Cdd:cd17655 237 AHLKLLDAADDSEglSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIyqYEPETDQQVsVPIGKPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 318 SVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQ 397
Cdd:cd17655 317 NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 398 LKVRGHRIEPGEVESALLAVDGVAQAVVT-----EHDNRLIAYVVGTggARVAAEDLLPPLRKRLPGYLVPDVVVGLPRL 472
Cdd:cd17655 396 VKIRGYRIELGEIEARLLQHPDIKEAVVIarkdeQGQNYLCAYIVSE--KELPVAQLREFLARELPDYMIPSYFIKLDEI 473
|
490
....*....|....*..
gi 214003850 473 PTSPNGKIDRAALPDPD 489
Cdd:cd17655 474 PLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
20-485 |
5.06e-153 |
|
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: 447.51 E-value: 5.06e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLL---AMPGQDVAGAPVVMSVERKPGQSAPNltdqdRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLA 176
Cdd:cd12116 81 EDAEPALVLtddALPDRLPAGLPVLLLALAAAAAAPAA-----PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 177 DDYVRRQNLVPDSRLLAFASPSFDAAVAE-FWPIWlAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALAPLEEG 255
Cdd:cd12116 156 HSMRERLGLGPGDRLLAVTTYAFDISLLElLLPLL-AGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 256 GGLP-PGLTLLVAGEACPAPVAKSW-ARDRVMINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPE 333
Cdd:cd12116 235 GWQGrAGLTALCGGEALPPDLAARLlSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 334 GDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESA 413
Cdd:cd12116 315 GVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 414 LLAVDGVAQAVVTEHDN----RLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd12116 395 LAAHPGVAQAAVVVREDggdrRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
5-576 |
5.34e-152 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 469.53 E-value: 5.34e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 5 ASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYV 84
Cdd:PRK10252 457 ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 85 PVDPDYPADRRRHMLDDTAAHCLLAMPGQD--VAGAPVVMSverkPGQSAPNLTDQDR-LSPLLPNHPAYVIYTSGSTGQ 161
Cdd:PRK10252 537 PLDTGYPDDRLKMMLEDARPSLLITTADQLprFADVPDLTS----LCYNAPLAPQGAApLQLSQPHHTAYIIFTSGSTGR 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 162 PKGVLVTHRGIPN----LADDYvrrqNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQ 237
Cdd:PRK10252 613 PKGVMVGQTAIVNrllwMQNHY----PLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEY 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 238 GITHVTLPPSAL----APLEEGGGLPPGLTL---LVAGEACPAPVAKSWARdRV---MINAYGPTEATVAVT-----ASD 302
Cdd:PRK10252 689 GVTTTHFVPSMLaafvASLTPEGARQSCASLrqvFCSGEALPADLCREWQQ-LTgapLHNLYGPTEAAVDVSwypafGEE 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 303 PLTGEGTP-PIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVW 381
Cdd:PRK10252 768 LAAVRGSSvPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVAR 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 382 AGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTE-----------HDNRLIAYVVGTGGARVAAEDLL 450
Cdd:PRK10252 847 WLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHAcvinqaaatggDARQLVGYLVSQSGLPLDTSALQ 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 451 PPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAervTSGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFF 530
Cdd:PRK10252 927 AQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQ---VPGRAPKTGTETIIAAAFSSLLGCDVVDADADFF 1003
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 214003850 531 DIGGHSLLATRLVARIRQSLQVRLRVQAFFNAPTVAQLAKVLDGAP 576
Cdd:PRK10252 1004 ALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEE 1049
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
11-572 |
1.40e-151 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 482.35 E-value: 1.40e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:PRK12467 3100 LIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY 3179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLAMpgqdvagAPVVMSVERKPGQSAPNLtDQDRLSPLLPNHP---------AYVIYTSGSTGQ 161
Cdd:PRK12467 3180 PRERLAYMIEDSGVKLLLTQ-------AHLLEQLPAPAGDTALTL-DRLDLNGYSENNPstrvmgenlAYVIYTSGSTGK 3251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 162 PKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAaSDLIPGEPLARLVRDQGITH 241
Cdd:PRK12467 3252 PKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRD-NDLWDPEELWQAIHAHRISI 3330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 242 VTLPPSAL---APLEEGGGLPPGLTLLVAGEACPA---PVAKSWARDRVMINAYGPTEATVAVTA----SDPLTGEGTPP 311
Cdd:PRK12467 3331 ACFPPAYLqqfAEDAGGADCASLDIYVFGGEAVPPaafEQVKRKLKPRGLTNGYGPTEAVVTVTLwkcgGDAVCEAPYAP 3410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 312 IGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFV 391
Cdd:PRK12467 3411 IGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYL 3490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 392 GRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDN----RLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVV 467
Cdd:PRK12467 3491 GRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGaggkQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLL 3570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 468 GLPRLPTSPNGKIDRAALPDPDREGAERVTsgrAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARIR 547
Cdd:PRK12467 3571 VLAAMPLGPNGKVDRKALPDPDAKGSREYV---APRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIR 3647
|
570 580
....*....|....*....|....*
gi 214003850 548 QSLQVRLRVQAFFNAPTVAQLAKVL 572
Cdd:PRK12467 3648 QSLGLKLSLRDLMSAPTIAELAGYS 3672
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-571 |
1.63e-149 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 476.37 E-value: 1.63e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLA----MPGQDVAGAPVVMSVERkPGQSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVL 166
Cdd:PRK12316 596 PAERLAYMLEDSGVQLLLSqshlGRKLPLAAGVQVLDLDR-PAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAG 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 VTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPP 246
Cdd:PRK12316 675 NRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVP 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 247 SALAPLEEGGGLPPGLTL---LVAGEACPAPV-----AKSWARDrvMINAYGPTEATVAVTASDPLT-GEGTPPIGRPIT 317
Cdd:PRK12316 755 SMLQAFLQDEDVASCTSLrriVCSGEALPADAqeqvfAKLPQAG--LYNLYGPTEAAIDVTHWTCVEeGGDSVPIGRPIA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 318 SVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGpGERMYRTGDRVWAGSDGQLVFVGRVDDQ 397
Cdd:PRK12316 833 NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQ 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 398 LKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNR-LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSP 476
Cdd:PRK12316 912 VKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKqLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTP 991
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 477 NGKIDRAALPDPDREGAERVTSgrAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARIRQSlQVRLRV 556
Cdd:PRK12316 992 NGKLDRKALPAPEASVAQQGYV--APRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSP 1068
|
570
....*....|....*
gi 214003850 557 QAFFNAPTVAQLAKV 571
Cdd:PRK12316 1069 RDLFQHQTIRSLALV 1083
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
20-486 |
5.75e-149 |
|
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: 436.41 E-value: 5.75e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLLAMPGQdvagapvvmsverkpgqsapnltdqdrlspllpnHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDY 179
Cdd:cd17649 81 EDSGAGLLLTHHPR----------------------------------QLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 180 VRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPS-----ALAPLEE 254
Cdd:cd17649 127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAylqqlAEEADRT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 255 GGGLPPGLTLLVA-GEACPAPVAKSWARDRV-MINAYGPTEATVAVTASDPLTGEG----TPPIGRPITSVSTYILDDKL 328
Cdd:cd17649 207 GDGRPPSLRLYIFgGEALSPELLRRWLKAPVrLFNAYGPTEATVTPLVWKCEAGAAragaSMPIGRPLGGRSAYILDADL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 329 QPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPG 408
Cdd:cd17649 287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 409 EVESALLAVDGVAQAVVTEHD----NRLIAYVVGTGGARVAA--EDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd17649 367 EIEAALLEHPGVREAAVVALDgaggKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDR 446
|
....
gi 214003850 483 AALP 486
Cdd:cd17649 447 KALP 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
9-485 |
7.69e-149 |
|
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: 437.48 E-value: 7.69e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDP 88
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 89 DYPADRRRHMLDDTAAHCLLAMPGQDVAGAPVVMSVERKPGQsAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVT 168
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA-LAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 169 HRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAE-FWPIwLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPS 247
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWElFWPL-VAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 248 ALAPL--EEGGGLPPGLTLLV-AGEACPAPVAKSWAR--DRVMINAYGPTEATVAVTA--SDPLTGEGTPPIGRPITSVS 320
Cdd:cd17646 239 MLRVFlaEPAAGSCASLRRVFcSGEALPPELAARFLAlpGAELHNLYGPTEAAIDVTHwpVRGPAETPSVPIGRPVPNTR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 321 TYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKV 400
Cdd:cd17646 319 LYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF-GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 401 RGHRIEPGEVESALLAVDGVAQAVVTEHDN-----RLIAYVVGT-GGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPT 474
Cdd:cd17646 398 RGFRVEPGEIEAALAAHPAVTHAVVVARAApagaaRLVGYVVPAaGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPL 477
|
490
....*....|.
gi 214003850 475 SPNGKIDRAAL 485
Cdd:cd17646 478 TANGKLDRAAL 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-577 |
2.09e-148 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 473.29 E-value: 2.09e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:PRK12316 4556 LVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLL----AMPGQDVAGAPVVMSVERKpgQSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVL 166
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLtqshLLQRLPIPDGLASLALDRD--EDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVA 4713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 VTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPgEPLARLVRDQGITHVTLPP 246
Cdd:PRK12316 4714 VSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDP-ERLYAEIHEHRVTVLVFPP 4792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 247 SALAPLEEG----GGLPPGLTLLVAGEACPAPVAKSW---ARDRVMINAYGPTEATVAVTASD----PLTGEGTPPIGRP 315
Cdd:PRK12316 4793 VYLQQLAEHaerdGEPPSLRVYCFGGEAVAQASYDLAwraLKPVYLFNGYGPTETTVTVLLWKardgDACGAAYMPIGTP 4872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 316 ITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVD 395
Cdd:PRK12316 4873 LGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLGRVD 4952
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 396 DQLKVRGHRIEPGEVESALLAVDGVAQAVVTE----HDNRLIAYVVGTGGARVAAED--------LLPPLRKRLPGYLVP 463
Cdd:PRK12316 4953 HQVKIRGFRIELGEIEARLREHPAVREAVVIAqegaVGKQLVGYVVPQDPALADADEaqaelrdeLKAALRERLPEYMVP 5032
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 464 DVVVGLPRLPTSPNGKIDRAALPDPDREGAERVTSgrAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLV 543
Cdd:PRK12316 5033 AHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYV--APRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVT 5110
|
570 580 590
....*....|....*....|....*....|....
gi 214003850 544 ARIRQSLQVRLRVQAFFNAPTVAQLAKVLDGAPS 577
Cdd:PRK12316 5111 SRIQLELGLELPLRELFQTPTLAAFVELAAAAGS 5144
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-574 |
8.30e-147 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 468.67 E-value: 8.30e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 10 ALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPD 89
Cdd:PRK12316 2007 QRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 YPADRRRHMLDDTAAHCLLAMPGQdVAGAPVVMSVERKPGQSAPNLTDQDRLSPLLPNHP---AYVIYTSGSTGQPKGVL 166
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLTQRHL-LERLPLPAGVARLPLDRDAEWADYPDTAPAVQLAGenlAYVIYTSGSTGLPKGVA 2165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 VTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEpLARLVRDQGITHVTLPP 246
Cdd:PRK12316 2166 VSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQ-LYDEMERHGVTILDFPP 2244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 247 S---ALAPLEEGGGLPPGL-TLLVAGEACPAPVAKSWARD---RVMINAYGPTEATVAVTA--SDPLTGEGT--PPIGRP 315
Cdd:PRK12316 2245 VylqQLAEHAERDGRPPAVrVYCFGGEAVPAASLRLAWEAlrpVYLFNGYGPTEAVVTPLLwkCRPQDPCGAayVPIGRA 2324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 316 ITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVD 395
Cdd:PRK12316 2325 LGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVEYLGRID 2404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 396 DQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDN----RLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPR 471
Cdd:PRK12316 2405 HQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGasgkQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLER 2484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 472 LPTSPNGKIDRAALPDPDREGAERvtSGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARIRQSLQ 551
Cdd:PRK12316 2485 LPLNPNGKLDRKALPKPDVSQLRQ--AYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLG 2562
|
570 580
....*....|....*....|...
gi 214003850 552 VRLRVQAFFNAPTVAQLAKVLDG 574
Cdd:PRK12316 2563 LEVPLRILFERPTLAAFAASLES 2585
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
20-485 |
5.06e-145 |
|
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: 426.34 E-value: 5.06e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLLampgqdvagapvvmsverkpgqsapnlTDqdrlspllPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDY 179
Cdd:cd17643 81 ADSGPSLLL---------------------------TD--------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 180 VRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALAPL----EEG 255
Cdd:cd17643 126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLveaaDRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 256 GGLPPGLTLLV-AGEACPAPVAKSWARDRV-----MINAYGPTEATVAVT-----ASDpLTGEGTPPIGRPITSVSTYIL 324
Cdd:cd17643 206 GRDPLALRYVIfGGEALEAAMLRPWAGRFGldrpqLVNMYGITETTVHVTfrpldAAD-LPAAAASPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 325 DDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHR 404
Cdd:cd17643 285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 405 IEPGEVESALLAVDGVAQAVVTEH-----DNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGK 479
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAVIVRedepgDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444
|
....*.
gi 214003850 480 IDRAAL 485
Cdd:cd17643 445 LDRAAL 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-571 |
5.98e-142 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 454.62 E-value: 5.98e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 5 ASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYV 84
Cdd:PRK12467 1573 ARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYV 1652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 85 PVDPDYPADRRRHMLDDTAAHCLLAMPG--QDVAGAPVVMSVERKPGQS-APNLTDQDRLSPLLPNHPAYVIYTSGSTGQ 161
Cdd:PRK12467 1653 PLDPEYPRERLAYMIEDSGIELLLTQSHlqARLPLPDGLRSLVLDQEDDwLEGYSDSNPAVNLAPQNLAYVIYTSGSTGR 1732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 162 PKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAE-FWPIwLAGGCLVLAAASDLIPGEPLARLVRDQGIT 240
Cdd:PRK12467 1733 PKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWElFWPL-INGARLVIAPPGAHRDPEQLIQLIERQQVT 1811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 241 HVTLPPSALAPLEEGGGL---PPGLTLLV-AGEACPAPVAKSWAR---DRVMINAYGPTEATVAVT----ASDPLTGEGT 309
Cdd:PRK12467 1812 TLHFVPSMLQQLLQMDEQvehPLSLRRVVcGGEALEVEALRPWLErlpDTGLFNLYGPTETAVDVThwtcRRKDLEGRDS 1891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 310 PPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLV 389
Cdd:PRK12467 1892 VPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGVIE 1971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 390 FVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNR----LIAYVVGTGGARVAAED--------LLPPLRKRL 457
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAngkqLVAYVVPTDPGLVDDDEaqvalraiLKNHLKASL 2051
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 458 PGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAERVTSgrAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSL 537
Cdd:PRK12467 2052 PEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYV--APQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSI 2129
|
570 580 590
....*....|....*....|....*....|....
gi 214003850 538 LATRLVARIRQSlQVRLRVQAFFNAPTVAQLAKV 571
Cdd:PRK12467 2130 ISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAV 2162
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
11-485 |
2.90e-141 |
|
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: 417.71 E-value: 2.90e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:cd05918 4 LIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTaahcllampgqdvaGAPVVmsverkpgqsapnLTDQdrlspllPNHPAYVIYTSGSTGQPKGVLVTHR 170
Cdd:cd05918 84 PLQRLQEILQDT--------------GAKVV-------------LTSS-------PSDAAYVIFTSGSTGKPKGVVIEHR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 171 GIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGepLARLVRDQGITHVTLPPSALA 250
Cdd:cd05918 130 ALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLND--LAGFINRLRVTWAFLTPSVAR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 251 PLEEggGLPPGL-TLLVAGEACPAPVAKSWARDRVMINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVsTYILD--DK 327
Cdd:cd05918 208 LLDP--EDVPSLrTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDpdNH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 328 LQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPF------GGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVR 401
Cdd:cd05918 285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 402 GHRIEPGEVESALLAVDGVAQAVVTE--------HDNRLIAYVVGTGG-----------------ARVAAEDLLPPLRKR 456
Cdd:cd05918 365 GQRVELGEIEHHLRQSLPGAKEVVVEvvkpkdgsSSPQLVAFVVLDGSssgsgdgdslflepsdeFRALVAELRSKLRQR 444
|
490 500
....*....|....*....|....*....
gi 214003850 457 LPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05918 445 LPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
11-485 |
1.39e-135 |
|
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: 402.08 E-value: 1.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDtaahcllampgqdvAGAPVVmsverkpgqsapnLTDqdrlspllPNHPAYVIYTSGSTGQPKGVLVTHR 170
Cdd:cd12115 84 PPERLRFILED--------------AQARLV-------------LTD--------PDDLAYVIYTSGSTGRPKGVAIEHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 171 GIPNLADDYvrRQNLVPD--SRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLArlvrdQGITHVTLPPSA 248
Cdd:cd12115 129 NAAAFLQWA--AAAFSAEelAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAA-----AEVTLINTVPSA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 249 LAPLEEGGGLPPGL-TLLVAGEACPAP-VAKSWARDRV--MINAYGPTEATVAVTASD-PLTGEGTPPIGRPITSVSTYI 323
Cdd:cd12115 202 AAELLRHDALPASVrVVNLAGEPLPRDlVQRLYARLQVerVVNLYGPSEDTTYSTVAPvPPGASGEVSIGRPLANTQAYV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 324 LDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGH 403
Cdd:cd12115 282 LDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF-GPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 404 RIEPGEVESALLAVDGVAQAVVTEH-----DNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNG 478
Cdd:cd12115 361 RIELGEIEAALRSIPGVREAVVVAIgdaagERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNG 440
|
....*..
gi 214003850 479 KIDRAAL 485
Cdd:cd12115 441 KIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-571 |
1.86e-131 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 424.37 E-value: 1.86e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLAMPGQDVAGAPVVMSVERKPGqsAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHR 170
Cdd:PRK12316 3142 PEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRG--DENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 171 GIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALA 250
Cdd:PRK12316 3220 ALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQ 3299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 251 PLEEGGGLPPGLTL---LVAGEACPAPVAKSWARDRVMINAYGPTEATVAVTASD-PLTGEGTPPIGRPITSVSTYILDD 326
Cdd:PRK12316 3300 AFLEEEDAHRCTSLkriVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQcVEEGKDAVPIGRPIANRACYILDG 3379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 327 KLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIE 406
Cdd:PRK12316 3380 SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIE 3458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 407 PGEVESALLAVDGVAQAVVTEHDNR-LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK12316 3459 LGEIEARLLEHPWVREAVVLAVDGRqLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 486 PDPDreGAERVTSGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARIRQsLQVRLRVQAFFNAPTV 565
Cdd:PRK12316 3539 PRPD--AALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQ-AGIRFTPKDLFQHQTI 3615
|
....*.
gi 214003850 566 AQLAKV 571
Cdd:PRK12316 3616 QGLARV 3621
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-562 |
7.51e-131 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 422.65 E-value: 7.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 1 MTGEASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAG 80
Cdd:PRK05691 1126 CAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 81 AAYVPVDPDYPADRRRHMLDDTAAHCLLAMPG--QDVAGAPVVMSV-------ERKPGQsAPNLTdqdrlspLLPNHPAY 151
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHllERLPQAEGVSAIaldslhlDSWPSQ-APGLH-------LHGDNLAY 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 152 VIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAE-FWPIwLAGGCLVLAAASDLIPGEPL 230
Cdd:PRK05691 1278 VIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWEcFWPL-ITGCRLVLAGPGEHRDPQRI 1356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 231 ARLVRDQGITHVTLPPSALAPL--EEGGGLPPGLTLLVAG-EACPAPVakswaRDRVMI--------NAYGPTEATVAVT 299
Cdd:PRK05691 1357 AELVQQYGVTTLHFVPPLLQLFidEPLAAACTSLRRLFSGgEALPAEL-----RNRVLQrlpqvqlhNRYGPTETAINVT 1431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 300 -----ASDpltGEGTPpIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMY 374
Cdd:PRK05691 1432 hwqcqAED---GERSP-IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLY 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 375 RTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDN----RLIAYVVGTGGARVAAEDLL 450
Cdd:PRK05691 1508 RTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGaagaQLVGYYTGEAGQEAEAERLK 1587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 451 PPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAERVtsgrAPSTPTEIHLAGLFAEVLGVSSVGVDDSFF 530
Cdd:PRK05691 1588 AALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHV----EPRTELQQQIAAIWREVLGLPRVGLRDDFF 1663
|
570 580 590
....*....|....*....|....*....|..
gi 214003850 531 DIGGHSLLATRLVARIRQSLQVRLRVQAFFNA 562
Cdd:PRK05691 1664 ALGGHSLLATQIVSRTRQACDVELPLRALFEA 1695
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
11-485 |
7.14e-129 |
|
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: 384.35 E-value: 7.14e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAhCLLampgqdvagapvvmsverkpgqsapnltdqdrLSPLLPNHPAYVIYTSGSTGQPKGVLVTHR 170
Cdd:cd17653 82 PSARIQAILRTSGA-TLL--------------------------------LTTDSPDDLAYIIFTSGSTGIPKGVMVPHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 171 GIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAasdliPGEPLARLVRDQGITHVTlpPSALA 250
Cdd:cd17653 129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD-----PSDPFAHVARTVDALMST--PSILS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 251 PLEEgGGLPPGLTLLVAGEACPAPVAKSWARDRVMINAYGPTEATVAVTASDPLTGEGTpPIGRPITSVSTYILDDKLQP 330
Cdd:cd17653 202 TLSP-QDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTCYILDADLQP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 331 VPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEV 410
Cdd:cd17653 280 VPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEI 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 411 ESALLAVDG-VAQAVVTEHDNRLIAYVVgtgGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd17653 359 EEVVLQSQPeVTQAAAIVVNGRLVAFVT---PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
11-486 |
3.46e-126 |
|
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: 378.70 E-value: 3.46e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:cd17644 5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLAMPgqdvagapvvmsverkpgqsaPNLtdqdrlspllpnhpAYVIYTSGSTGQPKGVLVTHR 170
Cdd:cd17644 85 PQERLTYILEDAQISVLLTQP---------------------ENL--------------AYVIYTSGSTGKPKGVMIEHQ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 171 GIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPS--- 247
Cdd:cd17644 130 SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAywh 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 248 --ALAPLEEGGGLPPGLTL-LVAGEACPAPVAKSWA---RDRV-MINAYGPTEATVAVTASDPLTGEGT----PPIGRPI 316
Cdd:cd17644 210 llVLELLLSTIDLPSSLRLvIVGGEAVQPELVRQWQknvGNFIqLINVYGPTEATIAATVCRLTQLTERnitsVPIGRPI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 317 TSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGG-PGERMYRTGDRVWAGSDGQLVFVGRVD 395
Cdd:cd17644 290 ANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSsESERLYKTGDLARYLPDGNIEYLGRID 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 396 DQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDN-----RLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLP 470
Cdd:cd17644 370 NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqpgnkRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLE 449
|
490
....*....|....*.
gi 214003850 471 RLPTSPNGKIDRAALP 486
Cdd:cd17644 450 ELPLTPNGKIDRRALP 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
11-571 |
3.77e-126 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 409.17 E-value: 3.77e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:PRK05691 2193 LFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLAMPGQDVAGAPVVMSVER------KPGQSAPNLTDQDRLSplLPNHPAYVIYTSGSTGQPKG 164
Cdd:PRK05691 2273 PLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARwcleddAAALAAYSDAPLPFLS--LPQHQAYLIYTSGSTGKPKG 2350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 165 VLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLiPGEPLARLVRDQGITHVTL 244
Cdd:PRK05691 2351 VVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQW-GAEEICQLIREQQVSILGF 2429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 245 PP---SALAP-LEEGGGLPPGLTLLVAGEACpapVAKSWARDR------VMINAYGPTEATV---AVTASDPL-TGEGTP 310
Cdd:PRK05691 2430 TPsygSQLAQwLAGQGEQLPVRMCITGGEAL---TGEHLQRIRqafapqLFFNAYGPTETVVmplACLAPEQLeEGAASV 2506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 311 PIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVF 390
Cdd:PRK05691 2507 PIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGGRLYRTGDLVRLRADGLVEY 2586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 391 VGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDN----RLIAYVVGTGGARVAA------EDLLPPLRKRLPGY 460
Cdd:PRK05691 2587 VGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTpsgkQLAGYLVSAVAGQDDEaqaalrEALKAHLKQQLPDY 2666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 461 LVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAERvtSGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLAT 540
Cdd:PRK05691 2667 MVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQ--AYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSI 2744
|
570 580 590
....*....|....*....|....*....|.
gi 214003850 541 RLVARIRQsLQVRLRVQAFFNAPTVAQLAKV 571
Cdd:PRK05691 2745 QVVSRARQ-LGIHFSPRDLFQHQTVQTLAAV 2774
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
20-485 |
2.15e-118 |
|
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: 357.93 E-value: 2.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDtaahcllampgqdvAGAPVVMsverkpgqsapnltdqdrlspLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDY 179
Cdd:cd17650 81 ED--------------SGAKLLL---------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 180 VRRQNLVPDS-RLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALAPL----EE 254
Cdd:cd17650 126 RREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVmayvYR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 255 GGGLPPGLTLLVAG-EACPAPVAKsWARDR-----VMINAYGPTEATVAVT----ASDPLTGEGTPPIGRPITSVSTYIL 324
Cdd:cd17650 206 NGLDLSAMRLLIVGsDGCKAQDFK-TLAARfgqgmRIINSYGVTEATIDSTyyeeGRDPLGDSANVPIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 325 DDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHR 404
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 405 IEPGEVESALLAVDGVAQAVVT-EHDNR----LIAYVVGTggARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGK 479
Cdd:cd17650 364 IELGEIESQLARHPAIDEAVVAvREDKGgearLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGK 441
|
....*.
gi 214003850 480 IDRAAL 485
Cdd:cd17650 442 VDRRAL 447
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
16-485 |
3.69e-112 |
|
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: 341.92 E-value: 3.69e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRR 95
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 96 RHMLDdtaahcllampgqdVAGAPVVMSVerkpgqsapnltdqdrlspllPNHPAYVIYTSGSTGQPKGVLVTHRGIPNL 175
Cdd:cd05945 81 REILD--------------AAKPALLIAD---------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 176 ADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVlAAASDLI--PGEPLARLvRDQGITHVTLPPSALAPLE 253
Cdd:cd05945 126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLV-PVPRDATadPKQLFRFL-AEHGITVWVSTPSFAAMCL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 254 EGGGLPPGL-----TLLVAGEACPAPVAKSWAR---DRVMINAYGPTEATVAVTA----SDPLTGEGTPPIGRPITSVST 321
Cdd:cd05945 204 LSPTFTPESlpslrHFLFCGEVLPHKTARALQQrfpDARIYNTYGPTEATVAVTYievtPEVLDGYDRLPIGYAKPGAKL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 322 YILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFlpnpFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVR 401
Cdd:cd05945 284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 402 GHRIEPGEVESALLAVDGVAQAVVT-----EHDNRLIAYVVGTGGA-RVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTS 475
Cdd:cd05945 360 GYRIELEEIEAALRQVPGVKEAVVVpkykgEKVTELIAFVVPKPGAeAGLTKAIKAELAERLPPYMIPRRFVYLDELPLN 439
|
490
....*....|
gi 214003850 476 PNGKIDRAAL 485
Cdd:cd05945 440 ANGKIDRKAL 449
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
11-486 |
3.05e-111 |
|
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: 339.53 E-value: 3.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLAMPGqdvagapvvmsverkpgqsapNLtdqdrlspllpnhpAYVIYTSGSTGQPKGVLVTHR 170
Cdd:cd17645 83 PGERIAYMLADSSAKILLTNPD---------------------DL--------------AYVIYTSGSTGLPKGVMIEHH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 171 GIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGIThVTLPPSALA 250
Cdd:cd17645 128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPTGAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 251 PLEEGGGLPPGLTLLVAGEACPAPVAKSWArdrvMINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQP 330
Cdd:cd17645 207 EQFMQLDNQSLRVLLTGGDKLKKIERKGYK----LVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 331 VPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEV 410
Cdd:cd17645 283 QPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 411 ESALLAVDGVAQAVVT-----EHDNRLIAYVvgTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd17645 362 EPFLMNHPLIELAAVLakedaDGRKYLVAYV--TAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
.
gi 214003850 486 P 486
Cdd:cd17645 440 P 440
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-495 |
1.21e-110 |
|
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: 338.32 E-value: 1.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDP 88
Cdd:COG0318 2 ADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 89 DYPADRRRHMLDDTAAHCLLAmpgqdvagapvvmsverkpgqsapnltdqdrlspllpnhpAYVIYTSGSTGQPKGVLVT 168
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVMLT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 169 HRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAA-VAEFWPIWLAGGCLVLAAASDLipgEPLARLVRDQGITHVTLPPS 247
Cdd:COG0318 122 HRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPRFDP---ERVLELIERERVTVLFGVPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 248 AL-----APLEEGGGLPPGLTLLVAGEACPAPVAKSWAR--DRVMINAYGPTEATVAVTASDPLTGEGTP-PIGRPITSV 319
Cdd:COG0318 199 MLarllrHPEFARYDLSSLRLVVSGGAPLPPELLERFEErfGVRIVEGYGLTETSPVVTVNPEDPGERRPgSVGRPLPGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 320 STYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFlpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLK 399
Cdd:COG0318 279 EVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--------RDGWLRTGDLGRLDEDGYLYIVGRKKDMII 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 400 VRGHRIEPGEVESALLAVDGVAQAVVT-----EHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPT 474
Cdd:COG0318 351 SGGENVYPAEVEEVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPR 430
|
490 500
....*....|....*....|.
gi 214003850 475 SPNGKIDRAALPDPDREGAER 495
Cdd:COG0318 431 TASGKIDRRALRERYAAGALE 451
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
20-486 |
7.30e-110 |
|
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: 337.14 E-value: 7.30e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLL------AMPGQDvaGAPVVMSVERKPGQSAPNLTDQDRlspllPNHPAYVIYTSGSTGQPKGVLVTHRGIP 173
Cdd:cd17656 82 LDSGVRVVLtqrhlkSKLSFN--KSTILLEDPSISQEDTSNIDYINN-----SDDLLYIIYTSGTTGKPKGVQLEHKNMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 174 NLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALAPLE 253
Cdd:cd17656 155 NLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 254 EGGGLPPGLT-----LLVAGE--ACPAPVAKSWARDRVMI-NAYGPTEATV--AVTASDPLTGEGTPPIGRPITSVSTYI 323
Cdd:cd17656 235 SEREFINRFPtcvkhIITAGEqlVITNEFKEMLHEHNVHLhNHYGPSETHVvtTYTINPEAEIPELPPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 324 LDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGH 403
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 404 RIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTggARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNG 478
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEAVVldkadDKGEKYLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNG 471
|
....*...
gi 214003850 479 KIDRAALP 486
Cdd:cd17656 472 KVDRKALP 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
20-486 |
1.33e-108 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 332.83 E-value: 1.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVG-PEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHM 98
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 99 LDDTAAHCLLAMPGQdvagapvvmsverkpgqsapnltdqdrlspllpnhPAYVIYTSGSTGQPKGVLVTHRGIPNLADD 178
Cdd:cd17648 81 LEDTGARVVITNSTD-----------------------------------LAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 179 YVRRQNLV--PDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALApLEEGG 256
Cdd:cd17648 126 LSERYFGRdnGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQ-QYDLA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 257 GLPPGLTLLVAGEACPAPVAKSwARDRV---MINAYGPTEATVAVTASDPLTGEG-TPPIGRPITSVSTYILDDKLQPVP 332
Cdd:cd17648 205 RLPHLKRVDAAGEEFTAPVFEK-LRSRFaglIINAYGPTETTVTNHKRFFPGDQRfDKSLGRPVRNTKCYVLNDAMKRVP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 333 EGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGE-------RMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRI 405
Cdd:cd17648 284 VGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 406 EPGEVESALLAVDGVAQAVV----------TEHDNRLIAYVVGTGGArVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTS 475
Cdd:cd17648 364 EPGEVEAALASYPGVRECAVvakedasqaqSRIQKYLVGYYLPEPGH-VPESDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
490
....*....|.
gi 214003850 476 PNGKIDRAALP 486
Cdd:cd17648 443 INGKLDVRALP 453
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
20-485 |
9.14e-108 |
|
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: 331.54 E-value: 9.14e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLL-----AMPGQDVAGAPVVMSVERKPGQSAPnltdqdrLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPN 174
Cdd:cd12114 81 ADAGARLVLtdgpdAQLDVAVFDVLILDLDALAAPAPPP-------PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 175 LADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPS----ALA 250
Cdd:cd12114 154 TILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAllemLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 251 PLEEGGGLPPGLTL-LVAGE----ACPAPVAKSWARDRVmINAYGPTEATVAVTA---SDPLTGEGTPPIGRPITSVSTY 322
Cdd:cd12114 234 VLEAAQALLPSLRLvLLSGDwiplDLPARLRALAPDARL-ISLGGATEASIWSIYhpiDEVPPDWRSIPYGRPLANQRYR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 323 ILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPfggPGERMYRTGD--RVWagSDGQLVFVGRVDDQLKV 400
Cdd:cd12114 313 VLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDlgRYR--PDGTLEFLGRRDGQVKV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 401 RGHRIEPGEVESALLAVDGVAQAVVT----EHDNRLIAYVV-GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTS 475
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARAVVVvlgdPGGKRLAAFVVpDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLT 467
|
490
....*....|
gi 214003850 476 PNGKIDRAAL 485
Cdd:cd12114 468 ANGKVDRAAL 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
10-574 |
1.01e-102 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 341.38 E-value: 1.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 10 ALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPD 89
Cdd:PRK05691 3724 RLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 YPADRRRHMLDDTAAHCLLAMPGQDVAGAPVVmsvERKPGQSAPNL----TDQDRLSPLL-------PNHPAYVIYTSGS 158
Cdd:PRK05691 3804 LPAQRLQRIIELSRTPVLVCSAACREQARALL---DELGCANRPRLlvweEVQAGEVASHnpgiysgPDNLAYVIYTSGS 3880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 159 TGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVL---AAASDliPGEPLArLVR 235
Cdd:PRK05691 3881 TGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIvpnAIAHD--PQGLLA-HVQ 3957
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 236 DQGITHVTLPPSALAPL--EEGGGLPPGLTLLVAGEACPAPVAKSWAR---DRVMINAYGPTEAT--VAVTASDPLTGEG 308
Cdd:PRK05691 3958 AQGITVLESVPSLIQGMlaEDRQALDGLRWMLPTGEAMPPELARQWLQrypQIGLVNAYGPAECSddVAFFRVDLASTRG 4037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 309 T-PPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQ 387
Cdd:PRK05691 4038 SyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGV 4117
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 388 LVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHD----NRLIAYVVGTGGARVAA---EDLLPPLRKRLPGY 460
Cdd:PRK05691 4118 LEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEgvngKHLVGYLVPHQTVLAQGallERIKQRLRAELPDY 4197
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 461 LVPDVVVGLPRLPTSPNGKIDRAALPDPDReGAERVTSGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLAT 540
Cdd:PRK05691 4198 MVPLHWLWLDRLPLNANGKLDRKALPALDI-GQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLAT 4276
|
570 580 590
....*....|....*....|....*....|....
gi 214003850 541 RLVARIRQSLQVRLRVQAFFNAPTVAQLAKVLDG 574
Cdd:PRK05691 4277 QIASRVQKALQRNVPLRAMFECSTVEELAEYIEG 4310
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
12-401 |
1.24e-100 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 311.17 E-value: 1.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 12 FEATAAAMPDRPAVAMGA-TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLAMPGQDVAGAPVVMSVERKPGQ------------------SAPNLTDQDRLSPLLPNHPAYV 152
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLvlvldrdpvlkeeplpeeAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 153 IYTSGSTGQPKGVLVTHRGIPNLADDYVRRQ----NLVPDSRLLAFASPSFDAAV-AEFWPIWLAGGCLVLAAASDLIPG 227
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 228 EPLARLVRDQGITHVTLPPSALAPLEEGGGLPPGL-----TLLVAGEACPAPVAKSWARD--RVMINAYGPTEATVAVTA 300
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALlsslrLVLSGGAPLPPELARRFRELfgGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 301 SDPLTGEGT--PPIGRPITSVSTYILDDK-LQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPnpfggpgERMYRTG 377
Cdd:pfam00501 321 PLPLDEDLRslGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-------DGWYRTG 393
|
410 420
....*....|....*....|....
gi 214003850 378 DRVWAGSDGQLVFVGRVDDQLKVR 401
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
16-485 |
1.90e-73 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 244.64 E-value: 1.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAV-----AMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:COG0365 19 AEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLAMPGQDVAGAPV------------------VMSVERKPGQSA-PNLTDQDRLS--------- 142
Cdd:COG0365 99 GAEALADRIEDAEAKVLITADGGLRGGKVIdlkekvdealeelpslehVIVVGRTGADVPmEGDLDWDELLaaasaefep 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 143 -PLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRR-QNLVPDSRLLAFASPSFdaAVAEFWPI---WLAGGCLV 217
Cdd:COG0365 179 ePTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTADIGW--ATGHSYIVygpLLNGATVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 218 LAAASDLIP-GEPLARLVRDQGITHVTLPPSALAPLEEGGGLPPG------LTLLV-AGEACPAPVAKsWARDRV---MI 286
Cdd:COG0365 257 LYEGRPDFPdPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkydlssLRLLGsAGEPLNPEVWE-WWYEAVgvpIV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 287 NAYGPTEATVAVTASDPltgeGTPP----IGRPITSVSTYILDDKLQPVPEGDVGELYMTG--PGLARGYLRRPAATAER 360
Cdd:COG0365 336 DGWGQTETGGIFISNLP----GLPVkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRET 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 361 FLpNPFGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT--EHDNRL---IAY 435
Cdd:COG0365 412 YF-GRFPG----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVgvPDEIRGqvvKAF 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 214003850 436 VVGTGGARVAAE---DLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:COG0365 487 VVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
148-481 |
8.83e-70 |
|
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: 228.32 E-value: 8.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 148 HPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDlipG 227
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 228 EPLARLVRDQGITHVTLPPSALA-----PLEEGGGLPPGLTLLVAGEACPAPVAKSWARDR--VMINAYGPTEATVAVTA 300
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLArllkaPESAGYDLSSLRALVSGGAPLPPELLERFEEAPgiKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 301 SDPLTGEGTPP-IGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFlpnpfggpGERMYRTGDR 379
Cdd:cd04433 158 GPPDDDARKPGsVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 380 VWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHD-----NRLIAYVVGTGGARVAAEDLLPPLR 454
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPdpewgERVVAVVVLRPGADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 214003850 455 KRLPGYLVPDVVVGLPRLPTSPNGKID 481
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
12-485 |
9.70e-68 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 227.86 E-value: 9.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 12 FEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYP 91
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 92 ADRrrhmlddtaahclLAMPgQDVAGAPVVMSVERKPGQ-------SAPNLTDQDRL-SPLLPNHP------AYVIYTSG 157
Cdd:PRK04813 88 AER-------------IEMI-IEVAKPSLIIATEELPLEilgipviTLDELKDIFATgNPYDFDHAvkgddnYYIIFTSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 158 STGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVlAAASDLI--PGEPLARLVR 235
Cdd:PRK04813 154 TTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLV-ALPKDMTanFKQLFETLPQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 236 dQGITHVTLPPS--ALAPLEEG--GGLPPGLT-LLVAGEACPAPVAKSwARDR----VMINAYGPTEATVAVTA------ 300
Cdd:PRK04813 233 -LPINVWVSTPSfaDMCLLDPSfnEEHLPNLThFLFCGEELPHKTAKK-LLERfpsaTIYNTYGPTEATVAVTSieitde 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 301 ----SDPLtgegtpPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFlpnpFGGPGERMYRT 376
Cdd:PRK04813 311 mldqYKRL------PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 377 GDrvwAGS--DGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT--EHDNR---LIAYVVGTGGARVAAEDL 449
Cdd:PRK04813 381 GD---AGYleDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVpyNKDHKvqyLIAYVVPKEEDFEREFEL 457
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 214003850 450 LPPLRK----RLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK04813 458 TKAIKKelkeRLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
11-573 |
7.97e-67 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 236.11 E-value: 7.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAV---------AMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGA 81
Cdd:TIGR03443 241 IFADNAEKHPDRTCVvetpsfldpSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 82 AYVPVDPDYPADRRRHMLDdtaahcllampgqdVAgAPVVMSVERKPGQSAPNLTD------------------------ 137
Cdd:TIGR03443 321 TFSVIDPAYPPARQTIYLS--------------VA-KPRALIVIEKAGTLDQLVRDyidkelelrteipalalqddgslv 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 138 --------QDRLSPLL------------PNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASP 197
Cdd:TIGR03443 386 ggsleggeTDVLAPYQalkdtptgvvvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGI 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 198 SFDAAVAE-FWPIWLaGGCLVLAAASDL-IPGEpLARLVRDQG--ITHVTlppsalapleeggglPPGLTLLVAGEACPA 273
Cdd:TIGR03443 466 AHDPIQRDmFTPLFL-GAQLLVPTADDIgTPGR-LAEWMAKYGatVTHLT---------------PAMGQLLSAQATTPI 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 274 PVAK------------------SWARDRVMINAYGPTEATVAVT-------ASDPL---TGEGTPPIGRPITSVSTYILD 325
Cdd:TIGR03443 529 PSLHhaffvgdiltkrdclrlqTLAENVCIVNMYGTTETQRAVSyfeipsrSSDSTflkNLKDVMPAGKGMKNVQLLVVN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 326 --DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFG---------------------GPGERMYRTGDRVWA 382
Cdd:TIGR03443 609 rnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVdpshwidldkennkperefwlGPRDRLYRTGDLGRY 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 383 GSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNR-----LIAYVV-------------------- 437
Cdd:TIGR03443 689 LPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKdeeptLVSYIVpqdksdeleefksevddees 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 438 ------GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAERVTSGRAPS------TP 505
Cdd:TIGR03443 769 sdpvvkGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASaadeefTE 848
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 506 TEIHLAGLFAEVL--GVSSVGVDDSFFDIGGHSLLATRLVARIRQSLQVRLRVQAFFNAPTVAQLAKVLD 573
Cdd:TIGR03443 849 TEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVD 918
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
11-485 |
5.10e-66 |
|
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: 223.89 E-value: 5.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:TIGR03098 5 LLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDDTAAHCLLA-------------------------MPGQDVAGAPVVMSVERKPGQSAPnltDQDRLSPLL 145
Cdd:TIGR03098 85 KAEQVAHILADCNVRLLVTsserldllhpalpgchdlrtliivgDPAHASEGHPGEEPASWPKLLALG---DADPPHPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 146 PNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLaaASDLI 225
Cdd:TIGR03098 162 DSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVL--HDYLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 226 PGEPLARLVRDQ--GITHV----------TLPPSALAPLE----EGGGLPPGLTllvageacpAPVAKSWARDRVMInAY 289
Cdd:TIGR03098 240 PRDVLKALEKHGitGLAAVpplwaqlaqlDWPESAAPSLRyltnSGGAMPRATL---------SRLRSFLPNARLFL-MY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 290 GPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNP--FG 367
Cdd:TIGR03098 310 GLTEAFRSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpfPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 368 GP--GERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTG 440
Cdd:TIGR03098 390 ELhlPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfgvpdPTLGQAIVLVVTPPG 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 214003850 441 GARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:TIGR03098 470 GEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
15-482 |
1.32e-61 |
|
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: 209.77 E-value: 1.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 15 TAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADR 94
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 95 RRHMLDDtaahcllampgqdvAGAPVVMSverkpgqsapnltdqdrlspllpnHPAYVIYTSGSTGQPKGVLVTHRGIPN 174
Cdd:cd17631 84 VAYILAD--------------SGAKVLFD------------------------DLALLMYTSGTTGRPKGAMLTHRNLLW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 175 LADDYVRRQNLVPDSRLLAFAsPSFDAAVAEFW--PIWLAGGCLVLAAASDliPGEPLArLVRDQGITHVTLPPSALAPL 252
Cdd:cd17631 126 NAVNALAALDLGPDDVLLVVA-PLFHIGGLGVFtlPTLLRGGTVVILRKFD--PETVLD-LIERHRVTSFFLVPTMIQAL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 253 EEGGGLP----PGL-TLLVAGEACPAPVAKSW-ARDRVMINAYGPTEATVAVTASDPLTGEGTP-PIGRPITSVSTYILD 325
Cdd:cd17631 202 LQHPRFAttdlSSLrAVIYGGAPMPERLLRALqARGVKFVQGYGMTETSPGVTFLSPEDHRRKLgSAGRPVFFVEVRIVD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 326 DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFlpnpFGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRI 405
Cdd:cd17631 282 PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF----RDG----WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 406 EPGEVESALLAVDGVAQ-AVVTEHDNR----LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKI 480
Cdd:cd17631 354 YPAEVEDVLYEHPAVAEvAVIGVPDEKwgeaVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKI 433
|
..
gi 214003850 481 DR 482
Cdd:cd17631 434 LK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
9-485 |
1.26e-57 |
|
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: 200.10 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDP 88
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 89 DYPADRRRHMLDDTAAHCL-LAMPGQDVAGAPvvmsverKPGQSAPNLTDQDrlspllpnhPAYVIYTSGSTGQPKGVLV 167
Cdd:cd05936 82 LYTPRELEHILNDSGAKALiVAVSFTDLLAAG-------APLGERVALTPED---------VAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 168 THRGIPNLADDYVRRQN--LVPDSRLLAfASPSFDA---AVAEFWPIwLAGGCLVlaaasdLIPG-EPLA--RLVRDQGI 239
Cdd:cd05936 146 THRNLVANALQIKAWLEdlLEGDDVVLA-ALPLFHVfglTVALLLPL-ALGATIV------LIPRfRPIGvlKEIRKHRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 240 THVTLPP---SALAPLEEGGGL-PPGLTLLVAGEA-CPAPVAKSWAR---DRVmINAYGPTEaTVAVTASDPLTGE---G 308
Cdd:cd05936 218 TIFPGVPtmyIALLNAPEFKKRdFSSLRLCISGGApLPVEVAERFEEltgVPI-VEGYGLTE-TSPVVAVNPLDGPrkpG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 309 TppIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLpnpfGGpgerMYRTGDRVWAGSDGQL 388
Cdd:cd05936 296 S--IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV----DG----WLRTGDIGYMDEDGYF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 389 VFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT-----EHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVP 463
Cdd:cd05936 366 FIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgvpdpYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVP 445
|
490 500
....*....|....*....|..
gi 214003850 464 DVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05936 446 RQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
20-485 |
2.42e-57 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 198.85 E-value: 2.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGA----TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRR 95
Cdd:cd17654 1 PDRPALIIDQttsdTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 96 RHMLDDTAAHCLLampgqdvagapvvmsVERKPGQSAPNLTDQDRLSPLLPNHP-AYVIYTSGSTGQPKGVLVTHRGI-P 173
Cdd:cd17654 81 LTVMKKCHVSYLL---------------QNKELDNAPLSFTPEHRHFNIRTDEClAYVIHTSGTTGTPKIVAVPHKCIlP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 174 NLAddYVRRQNLVPDSRLLAFASP-SFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLAR-LVRDQGITHVTLPPSALAP 251
Cdd:cd17654 146 NIQ--HFRSLFNITSEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 252 LEEGGGLPPGL-------TLLVAGEACPAPVA-KSWA----RDRVmINAYGPTEATVAVTASDPLTGEGTPPIGRPITSV 319
Cdd:cd17654 224 FGSQSIKSTVLsatsslrVLALGGEPFPSLVIlSSWRgkgnRTRI-FNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 320 STYILDdklQPVPEGDvGELYmtGPGLARGYlrrpaataerFLPNPFGGPGERMYRTGDRVWAgSDGQLVFVGRVDDQLK 399
Cdd:cd17654 303 VIEVRD---QNGSEGT-GQVF--LGGLNRVC----------ILDDEVTVPKGTMRATGDFVTV-KDGELFFLGRKDSQIK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 400 VRGHRIEPGEVESALLAVDGVAQAVVTEHDN-RLIAYVVGTG-GARVAAEdllppLRK-RLPGYLVPDVVVGLPRLPTSP 476
Cdd:cd17654 366 RRGKRINLDLIQQVIESCLGVESCAVTLSDQqRLIAFIVGESsSSRIHKE-----LQLtLLSSHAIPDTFVQIDKLPLTS 440
|
....*....
gi 214003850 477 NGKIDRAAL 485
Cdd:cd17654 441 HGKVDKSEL 449
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
2-485 |
4.90e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 193.97 E-value: 4.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 2 TGEASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGA 81
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 82 AYVPVDPDYPADRRRHMLDDTAAHCLLAMP---GQDVAGAPVVMSVERK--------PGQSAPNLTDQDRLSP------- 143
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLGlflGVDYSATTRLPALEHVviceteedDPHTEKMKTFTDFLAAgdpaera 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 144 --LLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAfASPSFDA---AVAefwpiWLA----GG 214
Cdd:PRK07656 161 peVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLA-ANPFFHVfgyKAG-----VNAplmrGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 215 CLVLAAASDliPGEPLaRLVRDQGIT--------------HVTLPPSALAPLEeggglppgltLLVAGEACPAPVAKSWA 280
Cdd:PRK07656 235 TILPLPVFD--PDEVF-RLIETERITvlpgpptmynsllqHPDRSAEDLSSLR----------LAVTGAASMPVALLERF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 281 RDR----VMINAYGPTEATVAVTAS----DPLTGEGTppIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLR 352
Cdd:PRK07656 302 ESElgvdIVLTGYGLSEASGVTTFNrlddDRKTVAGT--IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 353 RPAATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNR 431
Cdd:PRK07656 380 DPEATAAAIDADGW-------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEaAVIGVPDER 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 432 L----IAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK07656 453 LgevgKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
20-487 |
2.74e-52 |
|
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: 186.36 E-value: 2.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATT--LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRH 97
Cdd:cd05926 1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 98 MLDDT-----------------AAH---CLLAMPGQDVAGAPVVMSVERKPGQSAPNLTDQDRLSPlLPNHPAYVIYTSG 157
Cdd:cd05926 81 YLADLgsklvltpkgelgpasrAASklgLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVP-LPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 158 STGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAfASPSF--DAAVAEFWPIWLAGGCLVLAA---ASDLIPgeplar 232
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLV-VMPLFhvHGLVASLLSTLAAGGSVVLPPrfsASTFWP------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 233 LVRDQGITHVTLPPSALA-----PLEEGGGLPPGLTLLVAGEACPAPVAKSWARDRV---MINAYGPTEATVAVTaSDPL 304
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQillnrPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFgapVLEAYGMTEAAHQMT-SNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 305 TGEGTPP--IGRPiTSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWA 382
Cdd:cd05926 312 PPGPRKPgsVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 383 GSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV----TEHDNRLI-AYVVGTGGARVAAEDLLPPLRKRL 457
Cdd:cd05926 384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfgvpDEKYGEEVaAAVVLREGASVTEEELRAFCRKHL 463
|
490 500 510
....*....|....*....|....*....|
gi 214003850 458 PGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:cd05926 464 AAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
33-486 |
1.65e-51 |
|
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: 182.49 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 33 SYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLampg 112
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 113 qdvagapvvmsverkpgqsapnlTDqdrlspllpnhPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLL 192
Cdd:cd05934 81 -----------------------VD-----------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 193 AFAsPSF--DAAVAEFWPIWLAGGCLVLA---AASDLIpgeplaRLVRDQGITHVTLPPSALAPLEEGgglPPGLT---- 263
Cdd:cd05934 127 TVL-PLFhiNAQAVSVLAALSVGATLVLLprfSASRFW------SDVRRYGATVTNYLGAMLSYLLAQ---PPSPDdrah 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 264 -LLVAGEACPAPVAKSWARDR---VMINAYGPTEATVAVtASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGEL 339
Cdd:cd05934 197 rLRAAYGAPNPPELHEEFEERfgvRLLEGYGMTETIVGV-IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGEL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 340 YMT---GPGLARGYLRRPAATAERFLpnpfGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLA 416
Cdd:cd05934 276 VIRglrGWGFFKGYYNMPEATAEAMR----NG----WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 214003850 417 VDGVAQAVV-----TEHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALP 486
Cdd:cd05934 348 HPAVREAAVvavpdEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
8-485 |
4.71e-51 |
|
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: 183.34 E-value: 4.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 8 APALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVD 87
Cdd:cd05959 6 ATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 88 PDYPADRRRHMLDDTAAHCLLAMP------GQDVAGAP----VVMSVERKPGQSA--------PNLTDQDRLSPLLPNHP 149
Cdd:cd05959 86 TLLTPDDYAYYLEDSRARVVVVSGelapvlAAALTKSEhtlvVLIVSGGAGPEAGalllaelvAAEAEQLKPAATHADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 150 AYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRR-QNLVPDSRLLAFASPSFDAAV--AEFWPIWLAGGCLvlaaasdLIP 226
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLgnSLTFPLSVGATTV-------LMP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 227 GEPLARLVRDQGITH--------VTLPPSALAPLEEGGGLPPGLTLLV-AGEACPAPVAKSWaRDRV---MINAYGPTEA 294
Cdd:cd05959 239 ERPTPAAVFKRIRRYrptvffgvPTLYAAMLAAPNLPSRDLSSLRLCVsAGEALPAEVGERW-KARFgldILDGIGSTEM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 295 TVAVTASDPLTGE-GTPpiGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLpnpfggpGErM 373
Cdd:cd05959 318 LHIFLSNRPGRVRyGTT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GE-W 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 374 YRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT--EHDNRLI---AYVV---GTGGARVA 445
Cdd:cd05959 388 TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVgvEDEDGLTkpkAFVVlrpGYEDSEAL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 214003850 446 AEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05959 468 EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
21-485 |
5.47e-50 |
|
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: 178.64 E-value: 5.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 21 DRPAVAMGATTLSYAELNGEANLLARRLVEHG-VGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLLAmpgqdvagapvvmsverkpgqsapnltdqdrlspllpnhPAYVIYTSGSTGQPKGVLVTHRGIPNLADDY 179
Cdd:cd05941 81 TDSEPSLVLD---------------------------------------PALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 180 VRRQNLVPDSRLLaFASPSFDA---AVAEFWPIWLAGGCLVL----AAASDLIPGEPLA-----------RLVRDQGiTH 241
Cdd:cd05941 122 VDAWRWTEDDVLL-HVLPLHHVhglVNALLCPLFAGASVEFLpkfdPKEVAISRLMPSItvfmgvptiytRLLQYYE-AH 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 242 VTLPPSALAPLEEGgglppgLTLLVAGEAC-PAPVAKSWAR--DRVMINAYGPTEATVAvtASDPLTGE---GTppIGRP 315
Cdd:cd05941 200 FTDPQFARAAAAER------LRLMVSGSAAlPVPTLEEWEAitGHTLLERYGMTEIGMA--LSNPLDGErrpGT--VGMP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 316 ITSVSTYILDDK-LQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRV 394
Cdd:cd05941 270 LPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILGRS 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 395 -DDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDN----RLIAYVVGTGGAR-VAAEDLLPPLRKRLPGYLVPDVVV 467
Cdd:cd05941 343 sVDIIKSGGYKVSALEIERVLLAHPGVSEcAVIGVPDPdwgeRVVAVVVLRAGAAaLSLEELKEWAKQRLAPYKRPRRLI 422
|
490
....*....|....*...
gi 214003850 468 GLPRLPTSPNGKIDRAAL 485
Cdd:cd05941 423 LVDELPRNAMGKVNKKEL 440
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
30-480 |
1.07e-49 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 178.95 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 30 TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLA 109
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 110 MPGQ------DVAGAP-----VVMSVERKPGQSAPNLT---------DQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTH 169
Cdd:cd05911 89 DPDGlekvkeAAKELGpkdkiIVLDDKPDGVLSIEDLLsptlgeedeDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 170 RGI------PNLADDYvrrqNLVPDSRLLAFaSPSFdaavaefwpiWLAG-----GCLVLAAASDLIPG---EPLARLVR 235
Cdd:cd05911 169 RNLianlsqVQTFLYG----NDGSNDVILGF-LPLY----------HIYGlfttlASLLNGATVIIMPKfdsELFLDLIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 236 DQGITHVTLPPS---ALA--PLEEGGGLPPGLTLLVAGeacpAP--------VAKSWARDRVMiNAYGPTEATVAVTASd 302
Cdd:cd05911 234 KYKITFLYLVPPiaaALAksPLLDKYDLSSLRVILSGG----APlskelqelLAKRFPNATIK-QGYGMTETGGILTVN- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 303 PLTGEGTPPIGRPITSVSTYILDDKL-QPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVW 381
Cdd:cd05911 308 PDGDDKPGSVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 382 AGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV----TEHDNRL-IAYVVGTGGARVAAEDLLPPLRKR 456
Cdd:cd05911 381 FDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigipDEVSGELpRAYVVRKPGEKLTEKEVKDYVAKK 460
|
490 500
....*....|....*....|....*.
gi 214003850 457 LPGY--LVPDVVVgLPRLPTSPNGKI 480
Cdd:cd05911 461 VASYkqLRGGVVF-VDEIPKSASGKI 485
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-493 |
6.25e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 177.69 E-value: 6.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 1 MTGEASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAG 80
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 81 AAYVPVDPDYPADRRRHMLDDTAAHCLLAmpgqDVAGAPVVMSV-ERKPGQSAPNLTDQDRLSPLLPNHPAYV------- 152
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLV----DSEFVPLLAAIlPQLPTVRTVIVEGDGPAAPLAPEVGEYEellaaas 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 153 ----------------IYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFAsPSFDAAvAEFWPI--WLAGG 214
Cdd:PRK06187 157 dtfdfpdidendaaamLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIV-PMFHVH-AWGLPYlaLMAGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 215 CLVLAaasDLIPGEPLARLVRDQGITHVTLPPSAL-----APLEEGGGLpPGLTLLVAG-EACPAPVAKSW-ARDRV-MI 286
Cdd:PRK06187 235 KQVIP---RRFDPENLLDLIETERVTFFFAVPTIWqmllkAPRAYFVDF-SSLRLVIYGgAALPPALLREFkEKFGIdLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 287 NAYGPTEATVAVTASDP---LTGEGTPPI--GRPITSVSTYILDDKLQPVP--EGDVGELYMTGPGLARGYLRRPAATAE 359
Cdd:PRK06187 311 QGYGMTETSPVVSVLPPedqLPGQWTKRRsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 360 RFLpnpfGGpgerMYRTGDrvwAGS---DGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDN----R 431
Cdd:PRK06187 391 TID----GG----WLHTGD---VGYideDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEvAVIGVPDEkwgeR 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 214003850 432 LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVP---DVVVGLPRLPTspnGKIDRAALPDPDREGA 493
Cdd:PRK06187 460 PVAVVVLKPGATLDAKELRAFLRGRLAKFKLPkriAFVDELPRTSV---GKILKRVLREQYAEGK 521
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
7-485 |
8.74e-48 |
|
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: 174.56 E-value: 8.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAayVPV 86
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 87 DPdYPADRR---RHMLDDTAAHCLL-----------AMPGQDVAGAP----VVMSVERKPGQSAPNLTDQDRLSPLL--- 145
Cdd:COG1021 104 FA-LPAHRRaeiSHFAEQSEAVAYIipdrhrgfdyrALARELQAEVPslrhVLVVGDAGEFTSLDALLAAPADLSEPrpd 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 146 PNHPAYVIYTSGSTGQPKGVLVTHrgipnlaDDY---VRRQN----LVPDSRLLA---------FASPSFDAAvaefwpi 209
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPKLIPRTH-------DDYlysVRASAeicgLDADTVYLAalpaahnfpLSSPGVLGV------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 210 WLAGGCLVLAAASDliPGEPLArLVRDQGITHVTL-PPSALAPLEEGGGLPPGLT----LLVAGEACPAPVAKswardRV 284
Cdd:COG1021 249 LYAGGTVVLAPDPS--PDTAFP-LIERERVTVTALvPPLALLWLDAAERSRYDLSslrvLQVGGAKLSPELAR-----RV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 285 -------MINAYGPTEATVAVTA-SDPL-TGEGTppIGRPItsvSTY----ILDDKLQPVPEGDVGELYMTGPGLARGYL 351
Cdd:COG1021 321 rpalgctLQQVFGMAEGLVNYTRlDDPEeVILTT--QGRPI---SPDdevrIVDEDGNPVPPGEVGELLTRGPYTIRGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 352 RRPAATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDN 430
Cdd:COG1021 396 RAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDaAVVAMPDE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 431 RLI----AYVVGTgGARVAAEDLLPPLRKR-LPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:COG1021 469 YLGerscAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
31-480 |
1.72e-45 |
|
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: 166.40 E-value: 1.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLlam 110
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 111 pgqdvagapVVMSVERKPGQSApnltdqdrlsplLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSR 190
Cdd:cd05903 78 ---------VVPERFRQFDPAA------------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 191 LLAfASP--SFDAAVAEFWPIWLAGGCLVLAAASDLIPGeplARLVRDQGITHVTLPPSAL-----APLEEGGGLPPGLT 263
Cdd:cd05903 137 FLV-ASPmaHQTGFVYGFTLPLLLGAPVVLQDIWDPDKA---LALMREHGVTFMMGATPFLtdllnAVEEAGEPLSRLRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 264 LLVAGEACPAPVA-KSWARDRVMI-NAYGPTEATVAVTASDP-LTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELY 340
Cdd:cd05903 213 FVCGGATVPRSLArRAAELLGAKVcSAYGSTECPGAVTSITPaPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 341 MTGPGLARGYLRRPAATAERFlpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV 420
Cdd:cd05903 293 SRGPSVFLGYLDRPDLTADAA--------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGV 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 421 AQ-AVVTEHDNRL----IAYVVGTGGARVAAEDLLPPL-RKRLPGYLVPDVVVGLPRLPTSPNGKI 480
Cdd:cd05903 365 IEaAVVALPDERLgeraCAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
29-488 |
2.36e-45 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 167.69 E-value: 2.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 29 ATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLL 108
Cdd:cd17647 18 TRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 109 AMPGQDVAGAPvvmsverkpgQSAPNLTdqdrlspllpnhpayviYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPD 188
Cdd:cd17647 98 VIRAAGVVVGP----------DSNPTLS-----------------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 189 SRLLAFASPSFDAAVAE-FWPIWLaGGCLVLAAASDLIPGEPLARLVRDQG--ITHVTlppsalapleeggglPPGLTLL 265
Cdd:cd17647 151 DKFTMLSGIAHDPIQRDmFTPLFL-GAQLLVPTQDDIGTPGRLAEWMAKYGatVTHLT---------------PAMGQLL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 266 VAGEACPAPVAK------------------SWARDRVMINAYGPTEATVAVT-------ASDPLTGEGTP---PIGRPIT 317
Cdd:cd17647 215 TAQATTPFPKLHhaffvgdiltkrdclrlqTLAENVRIVNMYGTTETQRAVSyfevpsrSSDPTFLKNLKdvmPAGRGML 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 318 SVSTYILD--DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFG---------------------GPGERMY 374
Cdd:cd17647 295 NVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwlGPRDRLY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 375 RTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNR-----LIAYVV------------ 437
Cdd:cd17647 375 RTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKdeeptLVSYIVprfdkpddesfa 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 438 ---------------GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDP 488
Cdd:cd17647 455 qedvpkevstdpivkGLIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
32-487 |
6.76e-45 |
|
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: 164.43 E-value: 6.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLAmp 111
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 112 gqdvagapvvmsverkpgqsapnlTDQDrlspllpnhPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRL 191
Cdd:cd05972 79 ------------------------DAED---------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 192 LAFASPSF-DAAVAEFWPIWLAGGCLVLAAASDLIPgEPLARLVRDQGITHVTLPPSA---LAPLEEGGGLPPGLTLLV- 266
Cdd:cd05972 126 WNIADPGWaKGAWSSFFGPWLLGATVFVYEGPRFDA-ERILELLERYGVTSFCGPPTAyrmLIKQDLSSYKFSHLRLVVs 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 267 AGEACpAPVAKSWARDRVMI---NAYGPTEATVAVtaSDPLTGEGTP-PIGRPITSVSTYILDDKLQPVPEGDVGELYM- 341
Cdd:cd05972 205 AGEPL-NPEVIEWWRAATGLpirDGYGQTETGLTV--GNFPDMPVKPgSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIk 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 342 -TGPGLARGYLRRPAATAERFlpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV 420
Cdd:cd05972 282 lPPPGLFLGYVGDPEKTEASI--------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAV 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 214003850 421 AQAVVTEHDNRLI-----AYVVGTGGA---RVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:cd05972 354 AEAAVVGSPDPVRgevvkAFVVLTSGYepsEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
41-485 |
3.10e-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.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 160.68 E-value: 3.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 41 ANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAA----YVPVDPDYPADRRRHMLDDTAAHCLLAMPGQDVA 116
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 117 GAPVvMSVERKPGQSApnltDQDRLS---------PLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVP 187
Cdd:cd05922 83 LRDA-LPASPDPGTVL----DADGIRaarasapahEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 188 DSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAaaSDLIPGEPLARLVRDQGITHVTLPPSALAPLEEGG----GLPPGLT 263
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGfdpaKLPSLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 264 LLVAGEACPAPVAKSWA---RDRVMINAYGPTEATVAVTASDP-LTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGEL 339
Cdd:cd05922 236 LTQAGGRLPQETIARLRellPGAQVYVMYGQTEATRRMTYLPPeRILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 340 YMTGPGLARGYLRRPAATAERflpnpfGGPGERMYrTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDG 419
Cdd:cd05922 316 VHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 420 VAQAVVTEHDNRLIA--YVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05922 389 IIEAAAVGLPDPLGEklALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
16-485 |
7.34e-43 |
|
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: 160.19 E-value: 7.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYpadrR 95
Cdd:cd05920 25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSH----R 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 96 RHMLDDTAAHcllampgqdvaGAPVVMSVERKPGQSAPNLTDQDRLSPLlpNHPAYVIYTSGSTGQPKGVLVTHrgipnl 175
Cdd:cd05920 101 RSELSAFCAH-----------AEAVAYIVPDRHAGFDHRALARELAESI--PEVALFLLSGGTTGTPKLIPRTH------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 176 aDDY---VRRQ----NLVPDSRLLAFASPSFDAAVAEfwP----IWLAGGCLVLAAASDliPGEPLArLVRDQGITHVTL 244
Cdd:cd05920 162 -NDYaynVRASaevcGLDQDTVYLAVLPAAHNFPLAC--PgvlgTLLAGGRVVLAPDPS--PDAAFP-LIEREGVTVTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 245 -PPSALAPLEEGGGLPPGLTLL----VAGEACPAPVAkswARDRVMIN-----AYGPTEATVAVTASD--PLTGEGTPpi 312
Cdd:cd05920 236 vPALVSLWLDAAASRRADLSSLrllqVGGARLSPALA---RRVPPVLGctlqqVFGMAEGLLNYTRLDdpDEVIIHTQ-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 313 GRPITSV-STYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFV 391
Cdd:cd05920 311 GRPMSPDdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 392 GRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTgGARVAAEDLLPPLRKR-LPGYLVPDV 465
Cdd:cd05920 384 GRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVvampdELLGERSCAFVVLR-DPPPSAAQLRRFLRERgLAAYKLPDR 462
|
490 500
....*....|....*....|
gi 214003850 466 VVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05920 463 IEFVDSLPLTAVGKIDKKAL 482
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
22-485 |
2.69e-42 |
|
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: 157.62 E-value: 2.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 22 RPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDD 101
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 102 TAAHCLLampgqdvagapvvmsverkpgqsapnlTDQDRLspllpnhpAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVR 181
Cdd:cd05919 81 CEARLVV---------------------------TSADDI--------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 182 RQ-NLVPDSRLLAFASPSFDAAVAE--FWPIWLAGGCLVLAAASDliPGEPLARLVRDQGITHVTLPPSALAPLEEGGGL 258
Cdd:cd05919 126 EAlGLTPGDRVFSSAKMFFGYGLGNslWFPLAVGASAVLNPGWPT--AERVLATLARFRPTVLYGVPTFYANLLDSCAGS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 259 PPGLTLL----VAGEACPAPVAKSWARDRV--MINAYGPTEATVAVTASDPltGEGTP-PIGRPITSVSTYILDDKLQPV 331
Cdd:cd05919 204 PDALRSLrlcvSAGEALPRGLGERWMEHFGgpILDGIGATEVGHIFLSNRP--GAWRLgSTGRPVPGYEIRLVDEEGHTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 332 PEGDVGELYMTGPGLARGYLRRPAATAERFLpnpfggpgERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVE 411
Cdd:cd05919 282 PPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 412 SALLAVDGVAQAVV--TEHDNRLI---AYVVGTGGA---RVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRA 483
Cdd:cd05919 354 SLIIQHPAVAEAAVvaVPESTGLSrltAFVVLKSPAapqESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRF 433
|
..
gi 214003850 484 AL 485
Cdd:cd05919 434 KL 435
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
20-495 |
7.83e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 157.84 E-value: 7.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLLAMPGQDVAGAPV----VMSVER----KPGQSAPNLTDQ-DRLSPL------LPNHPAYVIYTSGSTGQPKG 164
Cdd:PRK06188 106 EDAGISTLIVDPAPFVERALAllarVPSLKHvltlGPVPDGVDLLAAaAKFGPAplvaaaLPPDIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 165 VLVTHRGIPNLADDYVRRQNLVPDSRLLAfASPSFDAAVAEFWPIWLAGGCLVLAAASDliPGEPLaRLVRDQGITHVTL 244
Cdd:PRK06188 186 VMGTHRSIATMAQIQLAEWEWPADPRFLM-CTPLSHAGGAFFLPTLLRGGTVIVLAKFD--PAEVL-RAIEEQRITATFL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 245 PPSALAPLEEGGGLP----PGLTLLVAGEACPAPVAKSWARDR---VMINAYGPTEATVAVTASDPLTGEGTPP-----I 312
Cdd:PRK06188 262 VPTMIYALLDHPDLRtrdlSSLETVYYGASPMSPVRLAEAIERfgpIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltsC 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 313 GRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLpnpfGGpgerMYRTGDRVWAGSDGQLVFVG 392
Cdd:PRK06188 342 GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFR----DG----WLHTGDVAREDEDGFYYIVD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 393 RVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNR----LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVV 467
Cdd:PRK06188 414 RKKDMIVTGGFNVFPREVEDVLAEHPAVAQvAVIGVPDEKwgeaVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVD 493
|
490 500
....*....|....*....|....*...
gi 214003850 468 GLPRLPTSPNGKIDRAALPDPDREGAER 495
Cdd:PRK06188 494 FVDSLPLTALGKPDKKALRARYWEGRGR 521
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-485 |
2.27e-41 |
|
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: 154.90 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 33 SYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLampg 112
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 113 qdvagapvvmsverkpgqsapnlTDqdrlsplLPNHPAYVIYTSGSTGQPKGVLVTHRG-IPNLADDYVRRQNLVPDSRL 191
Cdd:cd05971 84 -----------------------TD-------GSDDPALIIYTSGTTGPPKGALHAHRVlLGHLPGVQFPFNLFPRDGDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 192 laFASPS--------FDAAVAefwpiWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPPSALAPLEEGG--GLPPG 261
Cdd:cd05971 134 --YWTPAdwawigglLDVLLP-----SLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGeqLKHAQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 262 LTL--LVAGEACPAPVAKSWARDR--VMIN-AYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDV 336
Cdd:cd05971 207 VKLraIATGGESLGEELLGWAREQfgVEVNeFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 337 GELYMTGPGLAR--GYLRRPAATAERFLPNPFggpgermyRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESAL 414
Cdd:cd05971 287 GEIAVELPDPVAflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 415 L--------AVDGVAQAVVTEhdnRLIAYVV---GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRA 483
Cdd:cd05971 359 LkhpavlmaAVVGIPDPIRGE---IVKAFVVlnpGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRR 435
|
..
gi 214003850 484 AL 485
Cdd:cd05971 436 EL 437
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
9-485 |
3.33e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 155.15 E-value: 3.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALFEATAAAMPDRP-AVAMGATTLSYAELNGEANLLARRlvehgVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVD 87
Cdd:PRK07787 2 ASLNPAAVAAAADIAdAVRIGGRVLSRSDLAGAATAVAER-----VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 88 PDYPADRRRHMLDDTAAHCLLAMPGQDVAGAPVVMSVERKPGQSAPNLTDqdrlspllPNHPAYVIYTSGSTGQPKGVLV 167
Cdd:PRK07787 77 PDSGVAERRHILADSGAQAWLGPAPDDPAGLPHVPVRLHARSWHRYPEPD--------PDAPALIVYTSGTTGPPKGVVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 168 THRGIPNLADdyvrrqnlvpdsrllafaspsfdaAVAEFWPiWLAGGCLV----LAAASDLIPGEpLARLVRDQGITHVT 243
Cdd:PRK07787 149 SRRAIAADLD------------------------ALAEAWQ-WTADDVLVhglpLFHVHGLVLGV-LGPLRIGNRFVHTG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 244 LP-PSALAPLEEGG-----GLPP----------------GLTLLVAGEAC-PAPVAKSWAR--DRVMINAYGPTEA--TV 296
Cdd:PRK07787 203 RPtPEAYAQALSEGgtlyfGVPTvwsriaadpeaaralrGARLLVSGSAAlPVPVFDRLAAltGHRPVERYGMTETliTL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 297 AVTASdpltGEGTPP-IGRPITSVSTYILDDKLQPVPEGD--VGELYMTGPGLARGYLRRPAATAERFLPNPFggpgerm 373
Cdd:PRK07787 283 STRAD----GERRPGwVGLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 374 YRTGDRVWAGSDGQLVFVGRVD-DQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDN----RLIAYVVgtGGARVAAE 447
Cdd:PRK07787 352 FRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREaAVVGVPDDdlgqRIVAYVV--GADDVAAD 429
|
490 500 510
....*....|....*....|....*....|....*...
gi 214003850 448 DLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK07787 430 ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
7-481 |
2.37e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 151.19 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV 86
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 87 DPDYPADRRRHMLDDTAAHCL---------LAMPGQDVAGAPVVMSVERKPGQSAPN--------LTDQDRLSPLLPNHP 149
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALvyerefaprVAEVLPRLPKLRTLVVVEDGSGNDLLPgavdyedaLAAGSPERDFGERSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 150 --AYVIYTSGSTGQPKGVLVTHR--------GIPNLADDYVRRQNLVPDSRLLAFASPSFDAA----VAEFWPIW---LA 212
Cdd:PRK07798 164 ddLYLLYTGGTTGMPKGVMWRQEdifrvllgGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPplmhGAGQWAAFaalFS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 213 GGCLVLAAASDLIPGEPLaRLVRDQGITHVTLPPSALA-PL-----EEGGGLPPGLTLLVAGEACPAPVAKS----WARD 282
Cdd:PRK07798 244 GQTVVLLPDVRFDADEVW-RTIEREKVNVITIVGDAMArPLldaleARGPYDLSSLFAIASGGALFSPSVKEalleLLPN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 283 RVMINAYGPTEA----TVAVTASDPLTGEGTPPIGRpitsvSTYILDDKLQPVP--EGDVGELYMTGPgLARGYLRRPAA 356
Cdd:PRK07798 323 VVLTDSIGSSETgfggSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEpgSGEIGWIARRGH-IPLGYYKDPEK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 357 TAERFlpnpFGGPGERMYRTGDRVWAGSDGQLVFVGRvdDQLKVR--GHRIEPGEVESALLAVDGVAQAVVTEHD----- 429
Cdd:PRK07798 397 TAETF----PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADALVVGVPderwg 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 214003850 430 NRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKID 481
Cdd:PRK07798 471 QEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
32-485 |
7.35e-39 |
|
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: 147.63 E-value: 7.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDtaahcllamp 111
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILND---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 112 gqdvAGAPVVMSverkpgqsapnLTDQDRLSpLLPnhpayviYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRL 191
Cdd:cd05935 72 ----SGAKVAVV-----------GSELDDLA-LIP-------YTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 192 LAFAsPSFDaaVAEFWPIWLA----GGCLVLAAASDlipGEPLARLVRDQGITHVTLPPSAL-----APLEEGGGLPPGL 262
Cdd:cd05935 129 LACL-PLFH--VTGFVGSLNTavyvGGTYVLMARWD---RETALELIEKYKVTFWTNIPTMLvdllaTPEFKTRDLSSLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 263 TLLVAGEACPAPVAKSwARDRVMIN---AYGPTEaTVAVTASDPLTGEGTPPIGRPITSVSTYILD-DKLQPVPEGDVGE 338
Cdd:cd05935 203 VLTGGGAPMPPAVAEK-LLKLTGLRfveGYGLTE-TMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 339 LYMTGPGLARGYLRRPAATAERFLPNPfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVD 418
Cdd:cd05935 281 IVVRGPQIFKGYWNRPEETEESFIEIK----GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHP 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 214003850 419 GVAQA-VVTEHDNRLI----AYVVGTGGAR--VAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05935 357 AI*EVcVISVPDERVGeevkAFIVLRPEYRgkVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
16-484 |
7.99e-38 |
|
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: 147.00 E-value: 7.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAM------GATTLSYAELNGEANLLARRLVEHGvGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPD 89
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 YP---ADRRRHMLDDTAAHCLLAMPGQDVA-----------GAPVVMSVERKPGQSApnltDQDRLSPLLPNHPAYVIYT 155
Cdd:cd05931 82 TPgrhAERLAAILADAGPRVVLTTAAALAAvrafaasrpaaGTPRLLVVDLLPDTSA----ADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 156 SGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPI-WLAGGCLVLAAASDLIpGEPL--AR 232
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTpLYSGGPSVLMSPAAFL-RRPLrwLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 233 LVRDQGITHVTLPPSAL------APLEEGGGLPPG--LTLLVAGEacpaPV------------AKSWARDRVMINAYGPT 292
Cdd:cd05931 237 LISRYRATISAAPNFAYdlcvrrVRDEDLEGLDLSswRVALNGAE----PVrpatlrrfaeafAPFGFRPEAFRPSYGLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 293 EATVAVTASDPLTG-------------------EGTPPI------GRPITSVSTYILD-DKLQPVPEGDVGELYMTGPGL 346
Cdd:cd05931 313 EATLFVSGGPPGTGpvvlrvdrdalagravavaADDPAArelvscGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 347 ARGYLRRPAATAERFLPNPfGGPGERMYRTGDRvwaG--SDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVD------ 418
Cdd:cd05931 393 ASGYWGRPEATAETFGALA-ATDEGGWLRTGDL---GflHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHpalrpg 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214003850 419 -GVAQAVVTEHDNRL-IAYVVGTGGARVAAEDLLPPLRKRLP---GyLVPDVVVGLPR--LPTSPNGKIDRAA 484
Cdd:cd05931 469 cVAAFSVPDDGEERLvVVAEVERGADPADLAAIAAAIRAAVArehG-VAPADVVLVRPgsIPRTSSGKIQRRA 540
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1-502 |
2.06e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 145.66 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 1 MTGEASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAG 80
Cdd:PRK06164 5 AAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 81 AAYVPVDPDYPADRRRHMLDDTAAHCLLAMPG----------QDVA-----GAPVVMSVERK---------------PGQ 130
Cdd:PRK06164 85 ATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidfaailAAVPpdalpPLRAIAVVDDAadatpapapgarvqlFAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 131 SAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAfASP-----SFDAAVAE 205
Cdd:PRK06164 165 PDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLA-ALPfcgvfGFSTLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 206 FwpiwLAGGCLVLAAASDlipGEPLARLVRDQGITHVTLPPSALAPL-EEGGGLPPGLTLLVAGEACPAPVAK---SWAR 281
Cdd:PRK06164 244 L----AGGAPLVCEPVFD---AARTARALRRHRVTHTFGNDEMLRRIlDTAGERADFPSARLFGFASFAPALGelaALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 282 DRVMINA--YGPTE--ATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQP--VPEGDVGELYMTGPGLARGYLRRPA 355
Cdd:PRK06164 317 ARGVPLTglYGSSEvqALVALQPATDPVSVRIEGGGRPASPEARVRARDPQDGalLPDGESGEIEIRAPSLMRGYLDNPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 356 ATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV--AQAVVTEHD--NR 431
Cdd:PRK06164 397 ATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVaaAQVVGATRDgkTV 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 214003850 432 LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPT--SPNG-KIDRAALpdpdREGAERVTSGRAP 502
Cdd:PRK06164 470 PVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVteSANGaKIQKHRL----REMAQARLAAERA 539
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
4-425 |
2.89e-37 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 146.01 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 4 EASTAPALFEATAAAMPDRPA----VAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKA 79
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVAlrekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 80 GAAYVPVDPDYPADRRRHMLDDTAAHCLLA------------------------MPGQDVAGAPVVMSVE--RKPGQSAP 133
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVedqeqldkllevrdelpslrhivvLDPRGLRDDPRLLSLDelLALGREVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 134 NLTD-QDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAF--ASPSFDAAVAEFwpiW 210
Cdd:COG1022 169 DPAElEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlpLAHVFERTVSYY---A 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 211 LAGGClVLAAASDLipgEPLARLVRDQGITHVTLPP--------SALAPLEEGGGL-----------------------P 259
Cdd:COG1022 246 LAAGA-TVAFAESP---DTLAEDLREVKPTFMLAVPrvwekvyaGIQAKAEEAGGLkrklfrwalavgrryararlagkS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 260 PGLTL---------LV-----------------AGEACPAPVAKS-WARDRVMINAYGPTEATVAVTASDPltGE---GT 309
Cdd:COG1022 322 PSLLLrlkhaladkLVfsklrealggrlrfavsGGAALGPELARFfRALGIPVLEGYGLTETSPVITVNRP--GDnriGT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 310 ppIGRPITSVSTYILDDklqpvpegdvGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAGSDGQLV 389
Cdd:COG1022 400 --VGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTGDIGELDEDGFLR 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 214003850 390 FVGRVDDQLKVR-GHRIEPGEVESALLAVDGVAQAVV 425
Cdd:COG1022 461 ITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
15-480 |
3.38e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 144.69 E-value: 3.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 15 TAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADR 94
Cdd:PRK08316 20 SARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 95 RRHMLDDTAAHCLLAMPG---------QDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLLPNH----------PAYVIYT 155
Cdd:PRK08316 100 LAYILDHSGARAFLVDPAlaptaeaalALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAepdveladddLAQILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 156 SGSTGQPKGVLVTHRGipnLADDYVR---RQNLVPDSRLLAfASPSFDAAVAE--FWPIWLAGGCLVLAAASDliPGEPL 230
Cdd:PRK08316 180 SGTESLPKGAMLTHRA---LIAEYVScivAGDMSADDIPLH-ALPLYHCAQLDvfLGPYLYVGATNVILDAPD--PELIL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 231 ARLVRDqGITHVTLPPS---ALA--PLEEggglPPGLTLLVAG----EACPAPVAKSwARDRV----MINAYGPTE---- 293
Cdd:PRK08316 254 RTIEAE-RITSFFAPPTvwiSLLrhPDFD----TRDLSSLRKGyygaSIMPVEVLKE-LRERLpglrFYNCYGQTEiapl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 294 ATVAvTASDPLTGEGTPpiGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLpnpfGGpgerM 373
Cdd:PRK08316 328 ATVL-GPEEHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR----GG----W 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 374 YRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNRLI----AYVVGTGGARVAAED 448
Cdd:PRK08316 397 FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEvAVIGLPDPKWIeavtAVVVPKAGATVTEDE 476
|
490 500 510
....*....|....*....|....*....|..
gi 214003850 449 LLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKI 480
Cdd:PRK08316 477 LIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
13-495 |
1.24e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 143.56 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 13 EATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLV-EHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYP 91
Cdd:PRK08314 17 EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 92 ADRRRHMLDDTAAHclLAMPGQDVAG--APVVMS--------------VERKPGQSAPNLTDQDRLSPLLPNH------- 148
Cdd:PRK08314 97 EEELAHYVTDSGAR--VAIVGSELAPkvAPAVGNlrlrhvivaqysdyLPAEPEIAVPAWLRAEPPLQALAPGgvvawke 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 --------PAYVI---------YTSGSTGQPKGVLVTHRGI-PNLADDYVRRqNLVPDSRLLAFAsPSFDaaVAEFW--- 207
Cdd:PRK08314 175 alaaglapPPHTAgpddlavlpYTSGTTGVPKGCMHTHRTVmANAVGSVLWS-NSTPESVVLAVL-PLFH--VTGMVhsm 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 208 --PIWlAGGCLVLAAASDLipgEPLARLVRDQGITHVTLPP-----------------SALAPLeeGGGlppgltllvaG 268
Cdd:PRK08314 251 naPIY-AGATVVLMPRWDR---EAAARLIERYRVTHWTNIPtmvvdflaspglaerdlSSLRYI--GGG----------G 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 269 EACPAPVAKSwARDRVMIN---AYGPTEaTVAVTASDPLTGEGTPPIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGP 344
Cdd:PRK08314 315 AAMPEAVAER-LKELTGLDyveGYGLTE-TMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 345 GLARGYLRRPAATAERFLpnPFGgpGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQA- 423
Cdd:PRK08314 393 QVFKGYWNRPEATAEAFI--EID--GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAc 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 424 VVTEHDNR----LIAYVVGTGGAR--VAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAER 495
Cdd:PRK08314 469 VIATPDPRrgetVKAVVVLRPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
16-487 |
1.87e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 142.25 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVA--MGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPAD 93
Cdd:PRK09088 5 ARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 94 RRRHMLDDtAAHCLLAMPGQDVAGAPVVMSVERKPgQSAPNLTDQDRlSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIP 173
Cdd:PRK09088 85 ELDALLQD-AEPRLLLGDDAVAAGRTDVEDLAAFI-ASADALEPADT-PSIPPERVSLILFTSGTSGQPKGVMLSERNLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 174 NLADDYVRRQNLVPDSRLLAFAsPSFD--AAVAEFWPIWLAGGCLVLAAASDliPGEPLARLVR-DQGITHVTLPPSALA 250
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDA-PMFHiiGLITSVRPVLAVGGSILVSNGFE--PKRTLGRLGDpALGITHYFCVPQMAQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 251 PLEEGGGLPPG----LTLLVAGEAC-PAPVAKSWARDRV-MINAYGPTEA-TVAVTASDP-LTGEGTPPIGRPITSVSTY 322
Cdd:PRK09088 239 AFRAQPGFDAAalrhLTALFTGGAPhAAEDILGWLDDGIpMVDGFGMSEAgTVFGMSVDCdVIRAKAGAAGIPTPTVQTR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 323 ILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFlpnpfggPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRG 402
Cdd:PRK09088 319 VVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 403 HRIEPGEVESALLAVDGVAQ-AVVTEHDNRL----IAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPN 477
Cdd:PRK09088 392 ENVYPAEIEAVLADHPGIREcAVVGMADAQWgevgYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTAS 471
|
490
....*....|
gi 214003850 478 GKIDRAALPD 487
Cdd:PRK09088 472 GKLQKARLRD 481
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
20-480 |
3.28e-35 |
|
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: 140.02 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAV------AMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPAD 93
Cdd:cd17634 67 GDRTAIiyegddTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 94 RRRHMLDDTAAHCLLAM-----PGQDVAGAPVVMSVERKPGQSAPNLTDQDRL--------------------------- 141
Cdd:cd17634 147 AVAGRIIDSSSRLLITAdggvrAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTgsdidwqegrdlwwrdliakaspehqp 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 142 SPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIP-NLADDYVRRQNLVPDSRLLAFASPSfdaavaefWPI---WLAGGCLV 217
Cdd:cd17634 227 EAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLvYAATTMKYVFDYGPGDIYWCTADVG--------WVTghsYLLYGPLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 218 LAAASDLIPGEP-------LARLVRDQGITHVTLPPSALAPLE-------EGGGLPPGLTLLVAGEACpAPVAKSWARDR 283
Cdd:cd17634 299 CGATTLLYEGVPnwptparMWQVVDKHGVNILYTAPTAIRALMaagddaiEGTDRSSLRILGSVGEPI-NPEAYEWYWKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 284 V------MINAYGPTEATVAVTAsdPLTGEGTPPIG---RPITSVSTYILDDKLQPVPEGDVGELYMTG--PGLARGYLR 352
Cdd:cd17634 378 IgkekcpVVDTWWQTETGGFMIT--PLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpwPGQTRTLFG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 353 RPaataERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT--EHD- 429
Cdd:cd17634 456 DH----ERFEQTYF-STFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgiPHAi 530
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 430 --NRLIAYVV---GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKI 480
Cdd:cd17634 531 kgQAPYAYVVlnhGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
31-485 |
2.05e-34 |
|
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: 134.78 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAhcllam 110
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 111 pgqdvagapvvmsverkpgqsapnltDQDRLspllpnhpAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSR 190
Cdd:cd05912 75 --------------------------KLDDI--------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 191 LLAfaspsfdaAVaefwPIWLAGGCLVLAAAsdLIPG-----------EPLARLVRDQGITHVTLPPSALAPLEE--GGG 257
Cdd:cd05912 121 WLC--------AL----PLFHISGLSILMRS--VIYGmtvylvdkfdaEQVLHLINSGKVTIISVVPTMLQRLLEilGEG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 258 LPPGL-TLLVAGEACPAPV-AKSWARDRVMINAYGPTEAT---VAVTASDPLTGEGTppIGRPITSVSTYILDDKlqpVP 332
Cdd:cd05912 187 YPNNLrCILLGGGPAPKPLlEQCKEKGIPVYQSYGMTETCsqiVTLSPEDALNKIGS--AGKPLFPVELKIEDDG---QP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 333 EGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermyRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVES 412
Cdd:cd05912 262 PYEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEE 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 413 ALLAVDGVAQAVVTEHDN-----RLIAYVVGTGgaRVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05912 334 VLLSHPAIKEAGVVGIPDdkwgqVPVAFVVSER--PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
9-485 |
3.49e-34 |
|
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: 135.71 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALFEA---TAAAMPDRPAVAM--GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAY 83
Cdd:cd05923 1 QTVFEMlrrAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 84 VPVDPDYPADRRRHMLDD----TAAHCLLAMPGQDVAGAPV-VMSVERKPGQSAP-NLTDQDRLSPLLPNHPAYVIYTSG 157
Cdd:cd05923 81 ALINPRLKAAELAELIERgemtAAVIAVDAQVMDAIFQSGVrVLALSDLVGLGEPeSAGPLIEDPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 158 STGQPKGVLVTHRGIP-----------NLADDYVRRQNLVPDSRLLAFASpSFDAAVAefwpiwlAGGCLVLAAASDliP 226
Cdd:cd05923 161 TTGLPKGAVIPQRAAEsrvlfmstqagLRHGRHNVVLGLMPLYHVIGFFA-VLVAALA-------LDGTYVVVEEFD--P 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 227 GEPLArLVRDQGITHVTLPPS---ALAPLEEGGG--LPPGLTLLVAGEACPAPVAKSWARDR--VMINAYGPTEATVAVT 299
Cdd:cd05923 231 ADALK-LIEQERVTSLFATPThldALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQHLpgEKVNIYGTTEAMNSLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 300 ASDPLTG-EGTPPIGRPITSVStyILDDKLQPVPEGDVGELYMTGPGLA--RGYLRRPAATAERFLpnpfggpgERMYRT 376
Cdd:cd05923 310 MRDARTGtEMRPGFFSEVRIVR--IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ--------DGWYRT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 377 GDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT----EHDNRLIAYVVGTGGARVAAEDLLPP 452
Cdd:cd05923 380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgvadERWGQSVTACVVPREGTLSADELDQF 459
|
490 500 510
....*....|....*....|....*....|....
gi 214003850 453 LR-KRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05923 460 CRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
32-485 |
1.34e-33 |
|
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: 133.01 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLAMP 111
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 112 gqdvagapvvmSVERKpgqsapnlTDqdrlspllPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRL 191
Cdd:cd05969 81 -----------ELYER--------TD--------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 192 LAFASPSFDA-AVAEFWPIWLaGGCLVLAAASDLIPgEPLARLVRDQGITHVTLPPSALAPLEEGGGLP------PGLTL 264
Cdd:cd05969 134 WCTADPGWVTgTVYGIWAPWL-NGVTNVVYEGRFDA-ESWYGIIERVKVTVWYTAPTAIRMLMKEGDELarkydlSSLRF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 265 LVAGEACPAPVAKSWARDRV---MINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYM 341
Cdd:cd05969 212 IHSVGEPLNPEAIRWGMEVFgvpIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 342 TG--PGLARGYLRRPAATAERFLpnpfGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDG 419
Cdd:cd05969 292 KPgwPSMFRGIWNDEERYKNSFI----DG----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPA 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 214003850 420 VAQA-VVTEHD----NRLIAYVVGTGGARVAAE---DLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05969 364 VAEAgVIGKPDplrgEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
16-511 |
1.44e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 134.52 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRR 95
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 96 RHMLDDTAAHCLLAMPG-QDVAGA-----PVVMSVERKPGQSAPNLTDQDRL--------SPL-LPNH-PAYVIYTSGST 159
Cdd:PRK07786 107 AFLVSDCGAHVVVTEAAlAPVATAvrdivPLLSTVVVAGGSSDDSVLGYEDLlaeagpahAPVdIPNDsPALIMYTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 160 GQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFD-AAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQG 238
Cdd:PRK07786 187 GRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 239 ITHVTLPPSALAPLEEGGGLPPGLTLLVAG-EACPAP--VAKSWAR---DRVMINAYGPTE---ATVAVTASDPLTGEGT 309
Cdd:PRK07786 267 TGIFLVPAQWQAVCAEQQARPRDLALRVLSwGAAPASdtLLRQMAAtfpEAQILAAFGQTEmspVTCMLLGEDAIRKLGS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 310 ppIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLpnpfGGpgerMYRTGDRVWAGSDGQLV 389
Cdd:PRK07786 347 --VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA----GG----WFHSGDLVRQDEEGYVW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 390 FVGRVDDQLKVRGHRIEPGEVESALLA-VDGVAQAVVTEHDNR-----LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVP 463
Cdd:PRK07786 417 VVDRKKDMIISGGENIYCAEVENVLAShPDIVEVAVIGRADEKwgevpVAVAAVRNDDAALTLEDLAEFLTDRLARYKHP 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 214003850 464 DVVVGLPRLPTSPNGKIDRAALpdPDREGAERVTSGRAPSTPTEIHLA 511
Cdd:PRK07786 497 KALEIVDALPRNPAGKVLKTEL--RERYGACVNVERRSASAGFTERRE 542
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
20-482 |
1.47e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 133.55 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLLAMPG---QDVAGAPVVMS-VERKPGQSAPNLTDqdrlSPLlpNHPAYVIYTSGSTGQPKGVLVTHR----- 170
Cdd:PRK03640 96 DDAEVKCLITDDDfeaKLIPGISVKFAeLMNGPKEEAEIQEE----FDL--DEVATIMYTSGTTGKPKGVIQTYGnhwws 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 171 ---GIPNLAddyvrrqnLVPDSRLLAfaspsfdaAVaefwPIWLAGGcLVLAAASdLIPGEPLA-----------RLVRD 236
Cdd:PRK03640 170 avgSALNLG--------LTEDDCWLA--------AV----PIFHISG-LSILMRS-VIYGMRVVlvekfdaekinKLLQT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 237 QGITHVTLPPSALAPLEE---GGGLPPGL--TLLVAGEACPAPVAKSWARDRVMINAYGPTEAT---VAVTASDPLTGEG 308
Cdd:PRK03640 228 GGVTIISVVSTMLQRLLErlgEGTYPSSFrcMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETAsqiVTLSPEDALTKLG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 309 TppIGRPITSVSTYILDDkLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermyRTGDRVWAGSDGQL 388
Cdd:PRK03640 308 S--AGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 389 VFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNRL-----IAYVVGTGGarVAAEDLLPPLRKRLPGYLVP 463
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwgqvpVAFVVKSGE--VTEEELRHFCEEKLAKYKVP 454
|
490
....*....|....*....
gi 214003850 464 DVVVGLPRLPTSPNGKIDR 482
Cdd:PRK03640 455 KRFYFVEELPRNASGKLLR 473
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
7-482 |
1.17e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 132.43 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV 86
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 87 DPDYPADRRRHMLDDTAA----------------------------HCLLAMP------------------GQDVAGAPV 120
Cdd:PRK05605 113 NPLYTAHELEHPFEDHGArvaivwdkvaptverlrrttpletivsvNMIAAMPllqrlalrlpipalrkarAALTGPAPG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 121 VMSVERKPGQSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRgipNLADDYVRRQNLVP-----DSRLLAfA 195
Cdd:PRK05605 193 TVPWETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHR---NLFANAAQGKAWVPglgdgPERVLA-A 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 196 SPSFDA----AVAEFWPiwLAGGCLVL--AAASDLI------------PGEP-----LARLVRDQGIT----------HV 242
Cdd:PRK05605 269 LPMFHAygltLCLTLAV--SIGGELVLlpAPDIDLIldamkkhpptwlPGVPplyekIAEAAEERGVDlsgvrnafsgAM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 243 TLPPSALAPLEE--GGglppgltLLVAGeacpapvakswardrvminaYGPTEaTVAVTASDPLTGEGTP-PIGRPITSV 319
Cdd:PRK05605 347 ALPVSTVELWEKltGG-------LLVEG--------------------YGLTE-TSPIIVGNPMSDDRRPgYVGVPFPDT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 320 STYILD--DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNpfggpgerMYRTGDRVWAGSDGQLVFVGRVDDQ 397
Cdd:PRK05605 399 EVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 398 LKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRL 472
Cdd:PRK05605 471 IITGGFNVYPAEVEEVLREHPGVEDAAVvglprEDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDEL 550
|
570
....*....|
gi 214003850 473 PTSPNGKIDR 482
Cdd:PRK05605 551 PRDQLGKVRR 560
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
30-437 |
1.18e-32 |
|
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: 130.41 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 30 TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLla 109
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 110 mpgqdVAGAPvvmsverkpgqsapnltdqdrlspllpNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDS 189
Cdd:cd05907 82 -----FVEDP---------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 190 RLLAF--ASPSFDAAVAEFWPIwLAGGCLVLAAASDLIPGEpLARlVRDQGITHVTL---PPSALAPLEEGGGLPPGLTL 264
Cdd:cd05907 130 RHLSFlpLAHVFERRAGLYVPL-LAGARIYFASSAETLLDD-LSE-VRPTVFLAVPRvweKVYAAIKVKAVPGLKRKLFD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 265 LVAGE----------ACPAPVAKSWARDRV-MINAYGPTEATVAVTASDPLTG-EGTppIGRPITSVSTYILDDklqpvp 332
Cdd:cd05907 207 LAVGGrlrfaasggaPLPAELLHFFRALGIpVYEGYGLTETSAVVTLNPPGDNrIGT--VGKPLPGVEVRIADD------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 333 egdvGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVR-GHRIEPGEVE 411
Cdd:cd05907 279 ----GEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIE 347
|
410 420
....*....|....*....|....*..
gi 214003850 412 SALLAVDGVAQAVVT-EHDNRLIAYVV 437
Cdd:cd05907 348 NALKASPLISQAVVIgDGRPFLVALIV 374
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
16-570 |
1.29e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 134.53 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAM------GATTLSYAELNGEANLLARRLVEHGVGPEKLVALaMPRSIEFVIAILAVHKAGAAYVPVDPd 89
Cdd:PRK05691 19 AAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAVLL-FPSGPDYVAAFFGCLYAGVIAVPAYP- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 yPADRRRH-------MLDDTAAHCLLAmpgqDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLL----------PNHPAYV 152
Cdd:PRK05691 97 -PESARRHhqerllsIIADAEPRLLLT----VADLRDSLLQMEELAAANAPELLCVDTLDPALaeawqepalqPDDIAFL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 153 IYTSGSTGQPKGVLVTHRGIpnLADDYVRRQ----NLVPDSRLLAFASPSFDAAV--AEFWPIWLAGGCLVLAaasdliP 226
Cdd:PRK05691 172 QYTSGSTALPKGVQVSHGNL--VANEQLIRHgfgiDLNPDDVIVSWLPLYHDMGLigGLLQPIFSGVPCVLMS------P 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 227 GEPLARLVR-DQGITHV-----------------TLPPSALAPLE-------EGGGLPPGLTLLvagEACPAPVAKSWAR 281
Cdd:PRK05691 244 AYFLERPLRwLEAISEYggtisggpdfayrlcseRVSESALERLDlsrwrvaYSGSEPIRQDSL---ERFAEKFAACGFD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 282 DRVMINAYGPTEATVAVTASDPltGEGTPPI----------------GRPITSVSTY-------ILD-DKLQPVPEGDVG 337
Cdd:PRK05691 321 PDSFFASYGLAEATLFVSGGRR--GQGIPALeldaealarnraepgtGSVLMSCGRSqpghavlIVDpQSLEVLGDNRVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 338 ELYMTGPGLARGYLRRPAATAERFLPNPfggpGERMYRTGDRVWAgSDGQLVFVGRVDDQLKVRGHRIEPGEVESAllav 417
Cdd:PRK05691 399 EIWASGPSIAHGYWRNPEASAKTFVEHD----GRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKT---- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 418 dgVAQAVVTEHDNRLIAYVV---GTGGARVAAE------DLLPP--LRKRLPGYL------VPDVVVGLP--RLPTSPNG 478
Cdd:PRK05691 470 --VEREVEVVRKGRVAAFAVnhqGEEGIGIAAEisrsvqKILPPqaLIKSIRQAVaeacqeAPSVVLLLNpgALPKTSSG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 479 KIDRAA----LPDPDRE------GAERVTSGRAPSTPTEI--HLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARI 546
Cdd:PRK05691 548 KLQRSAcrlrLADGSLDsyalfpALQAVEAAQTAASGDELqaRIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARL 627
|
650 660
....*....|....*....|....
gi 214003850 547 RQSLQVRLRVQAFFNAPTVAQLAK 570
Cdd:PRK05691 628 RDELGIDLNLRQLFEAPTLAAFSA 651
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
15-485 |
1.47e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 131.79 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 15 TAAAMPDRPAVA--MGATtLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPA 92
Cdd:PRK06087 32 TARAMPDKIAVVdnHGAS-YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 93 DRRRHMLDDTAA-------------HCLLAMPGQDVAGA--PVVMSVERKPGQSAPNLT----DQDRLSPLLPNHP---A 150
Cdd:PRK06087 111 AELVWVLNKCQAkmffaptlfkqtrPVDLILPLQNQLPQlqQIVGVDKLAPATSSLSLSqiiaDYEPLTTAITTHGdelA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 151 YVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRL-----LAFASPSFDAAVAEFwpiwLAGGCLVLaaaSDLI 225
Cdd:PRK06087 191 AVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFmmpapLGHATGFLHGVTAPF----LIGARSVL---LDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 226 PGEPLARLVRDQGIT--HVTLP--PSALAPLEEGGGLPPGLTLLVAGEAcPAP---VAKSWARDRVMINAYGPTEAT--V 296
Cdd:PRK06087 264 TPDACLALLEQQRCTcmLGATPfiYDLLNLLEKQPADLSALRFFLCGGT-TIPkkvARECQQRGIKLLSVYGSTESSphA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 297 AVTASDPLTGEGTPPiGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAeRFLPNpfggpgERMYRT 376
Cdd:PRK06087 343 VVNLDDPLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RALDE------EGWYYS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 377 GDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV-AQAVVTEHDNRL----IAYVVGTGG-ARVAAEDLL 450
Cdd:PRK06087 415 GDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIhDACVVAMPDERLgersCAYVVLKAPhHSLTLEEVV 494
|
490 500 510
....*....|....*....|....*....|....*.
gi 214003850 451 PPL-RKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK06087 495 AFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
3-482 |
1.94e-32 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 131.84 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 3 GEASTAPALFEATAAAMPDRPAVAM----GAT-TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVH 77
Cdd:cd05968 58 GRMNIVEQLLDKWLADTRTRPALRWegedGTSrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 78 KAGAAYVPVDPDYPADRRRHMLDDTAAHCLLAMPG---------------QDVAGAPVV--MSVERKPGQSAPNLTDQDR 140
Cdd:cd05968 138 RIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnlkeeadKACAQCPTVekVVVVRHLGNDFTPAKGRDL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 141 LSPLL------------PNHPAYVIYTSGSTGQPKGVLVTHRGIP-NLADDYVRRQNLVPDSRLLAFASPSfdaavaefW 207
Cdd:cd05968 218 SYDEEketagdgaerteSEDPLMIIYTSGTTGKPKGTVHVHAGFPlKAAQDMYFQFDLKPGDLLTWFTDLG--------W 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 208 PI--WLAGGCLVLAAASDLIPGEP-------LARLVRDQGITHVTLPPSALAPLEEGGGLPPG----LTLLVAGEACPAP 274
Cdd:cd05968 290 MMgpWLIFGGLILGATMVLYDGAPdhpkadrLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNahdlSSLRVLGSTGEPW 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 275 VAKSW-------ARDRV-MINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEgDVGELYMTGP-- 344
Cdd:cd05968 370 NPEPWnwlfetvGKGRNpIINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPwp 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 345 GLARGYLRRPaataERFLpNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-- 422
Cdd:cd05968 449 GMTRGFWRDE----DRYL-ETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLEsa 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 423 AVVTEHD---NRLIAYVV---GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd05968 524 AIGVPHPvkgEAIVCFVVlkpGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
3-485 |
2.35e-32 |
|
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: 130.87 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 3 GEASTAPALFEATAAAMPDR----PAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHK 78
Cdd:cd05906 7 GAPRTLLELLLRAAERGPTKgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 79 AG--AAYVPVDPDY--PADRRRH------MLDDtaAHCL----LAMpgqDVAGAPVVMSVERKPGQSAPNLTDQDRLSPL 144
Cdd:cd05906 87 AGfvPAPLTVPPTYdePNARLRKlrhiwqLLGS--PVVLtdaeLVA---EFAGLETLSGLPGIRVLSIEELLDTAADHDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 145 L---PNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASpsFD--AAVAEF--WPIWLagGCLV 217
Cdd:cd05906 162 PqsrPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP--LDhvGGLVELhlRAVYL--GCQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 218 LAAASDLIPGEPLA--RLVRDQGITHVTLPPSALAPL----EEG----GGLPPGLTLLVAGEACPAPV--------AKSW 279
Cdd:cd05906 238 VHVPTEEILADPLRwlDLIDRYRVTITWAPNFAFALLndllEEIedgtWDLSSLRYLVNAGEAVVAKTirrllrllEPYG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 280 ARDRVMINAYGPTEATVAVTASDPLTGEGTPP------IGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRR 353
Cdd:cd05906 318 LPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQalefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 354 PAATAERFLPNPFggpgermYRTGDRVWAgSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV------AQAV--- 424
Cdd:cd05906 398 PEANAEAFTEDGW-------FRTGDLGFL-DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsftaAFAVrdp 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 214003850 425 --VTEHdnRLIAYVVgtggaRVAAEDLLPPLRKRLPGYLV------PDVVVGLPR--LPTSPNGKIDRAAL 485
Cdd:cd05906 470 gaETEE--LAIFFVP-----EYDLQDALSETLRAIRSVVSrevgvsPAYLIPLPKeeIPKTSLGKIQRSKL 533
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
12-493 |
2.87e-32 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 130.94 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 12 FEATAAAMPDRPAVA------MGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVP 85
Cdd:PRK13295 30 LDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 86 VDPDYPADRRRHMLD----------------DTAA-------------HCLLAMPGQDVAGAPVVMSVERKPGQSAPNLT 136
Cdd:PRK13295 110 LMPIFRERELSFMLKhaeskvlvvpktfrgfDHAAmarrlrpelpalrHVVVVGGDGADSFEALLITPAWEQEPDAPAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 137 DQDRLSPllpNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLaFASPSfdAAVAEF-----WPIWL 211
Cdd:PRK13295 190 ARLRPGP---DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVIL-MASPM--AHQTGFmyglmMPVML 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 212 aGGCLVLaaaSDLIPGEPLARLVRDQGITHVT-----LPPSALAPLEEGGGLPPGLTLLVAGEACPAPVAKSwARDR--- 283
Cdd:PRK13295 264 -GATAVL---QDIWDPARAAELIRTEGVTFTMastpfLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVER-ARAAlga 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 284 VMINAYGPTEaTVAVTA---SDPLTGEGTPPiGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAER 360
Cdd:PRK13295 339 KIVSAWGMTE-NGAVTLtklDDPDERASTTD-GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 361 FlpnpfggpgERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNRL----IAY 435
Cdd:PRK13295 417 A---------DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQvAIVAYPDERLgeraCAF 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 214003850 436 VVGTGGARVAAEDLLPPLR-KRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGA 493
Cdd:PRK13295 488 VVPRPGQSLDFEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGED 546
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-485 |
3.45e-32 |
|
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: 130.06 E-value: 3.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 28 GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCL 107
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 108 LAMP-----GQDVAGAP------VVM-SVERKPGQSAPNLTDQDRL----SPLLP------NHPAYVIYTSGSTGQPKGV 165
Cdd:cd12119 102 FVDRdflplLEAIAPRLptvehvVVMtDDAAMPEPAGVGVLAYEELlaaeSPEYDwpdfdeNTAAAICYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 166 LVTHRGI------PNLADDYVRRQN-----LVPDSRLLAFASPsFDAAvaefwpiwLAGGCLVLAAASDliPGEPLARLV 234
Cdd:cd12119 182 VYSHRSLvlhamaALLTDGLGLSESdvvlpVVPMFHVNAWGLP-YAAA--------MVGAKLVLPGPYL--DPASLAELI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 235 RDQGITHVTLPPSAL-----APLEEGGGLPPGLTLLVAGEACPAPVAKSWARDRV-MINAYGPTEATVAVTASDPLTGEG 308
Cdd:cd12119 251 EREGVTFAAGVPTVWqglldHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVrVIHAWGMTETSPLGTVARPPSEHS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 309 TPPI----------GRPITSVSTYILDDKLQPVPEGD--VGELYMTGPGLARGYLRRPAATaERFLPNPFggpgermYRT 376
Cdd:cd12119 331 NLSEdeqlalrakqGRPVPGVELRIVDDDGRELPWDGkaVGELQVRGPWVTKSYYKNDEES-EALTEDGW-------LRT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 377 GDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT--EH---DNRLIAYVVGTGGARVAAEDLLP 451
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIgvPHpkwGERPLAVVVLKEGATVTAEELLE 482
|
490 500 510
....*....|....*....|....*....|....
gi 214003850 452 PLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd12119 483 FLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
28-496 |
8.74e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 129.05 E-value: 8.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 28 GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCL 107
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 108 LA-------MPGQDVAGAPVVmSVERKPG-QSAPNLTDQDRLSP--------LLPNHPAY----------VIYTSGSTGQ 161
Cdd:PRK12406 88 IAhadllhgLASALPAGVTVL-SVPTPPEiAAAYRISPALLTPPagaidwegWLAQQEPYdgppvpqpqsMIYTSGTTGH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 162 PKGVLVTHrGIPNLADDYVRRQNLV----PDSRLLA-----FASP-SFDAAVAEFwpiwlaGGCLVLAAASDlipGEPLA 231
Cdd:PRK12406 167 PKGVRRAA-PTPEQAAAAEQMRALIyglkPGIRALLtgplyHSAPnAYGLRAGRL------GGVLVLQPRFD---PEELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 232 RLVRDQGITHVTLPPSALAPLEEgggLPP---------GLTLLVAGEA-CPAPVAKS----WArdRVMINAYGPTEATVA 297
Cdd:PRK12406 237 QLIERHRITHMHMVPTMFIRLLK---LPEevrakydvsSLRHVIHAAApCPADVKRAmiewWG--PVIYEYYGSTESGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 298 V--TASDPLTGEGTppIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLAR-GYLRRPAATAERflpnpfggpgER-- 372
Cdd:PRK12406 312 TfaTSEDALSHPGT--VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI----------DRgg 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 373 MYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTGGARVAAE 447
Cdd:PRK12406 380 FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVfgipdAEFGEALMAVVEPQPGATLDEA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 214003850 448 DLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAERV 496
Cdd:PRK12406 460 DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
32-485 |
1.33e-31 |
|
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: 127.25 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLlamp 111
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 112 gqdvagapvvmsverkpgqsapnLTDQDRLSPlLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLAdDYVRRQ-NLVPDSR 190
Cdd:cd05973 77 -----------------------VTDAANRHK-LDSDPFVMMFTSGTTGLPKGVPVPLRALAAFG-AYLRDAvDLRPEDS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 191 LLAFASPSFdaAVAEFWPIwlaGGCLVLAAASDLIPG----EPLARLVRDQGITHVTLPPSALAPLEEGG---GLPPGLT 263
Cdd:cd05973 132 FWNAADPGW--AYGLYYAI---TGPLALGHPTILLEGgfsvESTWRVIERLGVTNLAGSPTAYRLLMAAGaevPARPKGR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 264 LLVAGEACP--APVAKSWARDRVMI---NAYGPTEATVAVT----ASDPLTgEGTppIGRPITSVSTYILDDKLQPVPEG 334
Cdd:cd05973 207 LRRVSSAGEplTPEVIRWFDAALGVpihDHYGQTELGMVLAnhhaLEHPVH-AGS--AGRAMPGWRVAVLDDDGDELGPG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 335 DVGELYM---TGPGLA-RGYLRRPAATaerflpnpfggPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEV 410
Cdd:cd05973 284 EPGRLAIdiaNSPLMWfRGYQLPDTPA-----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 411 ESALLAVDGVAQAVVT-----EHDNRLIAYVV---GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd05973 353 ESALIEHPAVAEAAVIgvpdpERTEVVKAFVVlrgGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
...
gi 214003850 483 AAL 485
Cdd:cd05973 433 FLL 435
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
22-485 |
1.98e-31 |
|
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: 126.82 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 22 RPAVAMGATTLSYAELNGEANLLARRLV-EHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLD 100
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 101 DTA-AHCLLAmpgqdvagapvvmsverkpgqsaPNLTDQDRLSPLlpnhpayvIYTSGSTGQPKGVLVTHRGIPNLADDY 179
Cdd:cd05958 81 KARiTVALCA-----------------------HALTASDDICIL--------AFTSGTTGAPKATMHFHRDPLASADRY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 180 VRR-QNLVPDSRLLAFASPSFDAAVA--EFWPIWLAGGCLVLAAASdliPGEPLARLVRDQGITHVTLPPSALAPLEEGG 256
Cdd:cd05958 130 AVNvLRLREDDRFVGSPPLAFTFGLGgvLLFPFGVGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAMLAHPD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 257 GLPPGLTLLV----AGEACPAPVAKSW--ARDRVMINAYGPTEATVAVTASDPltGEGTP-PIGRPITSVSTYILDDKLQ 329
Cdd:cd05958 207 AAGPDLSSLRkcvsAGEALPAALHRAWkeATGIPIIDGIGSTEMFHIFISARP--GDARPgATGKPVPGYEAKVVDDEGN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 330 PVPEGDVGELYMTGPGLARGYLRRPAATAERflpnpfggpGERMYrTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGE 409
Cdd:cd05958 285 PVPDGTIGRLAVRGPTGCRYLADKRQRTYVQ---------GGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 410 VESALLAVDGVAQ-AVV-TEHDNRLI---AYVV---GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKID 481
Cdd:cd05958 355 VEDVLLQHPAVAEcAVVgHPDESRGVvvkAFVVlrpGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434
|
....
gi 214003850 482 RAAL 485
Cdd:cd05958 435 RFAL 438
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-485 |
5.58e-31 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 126.80 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV 86
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 87 DPDYPADRRRHMLDDTAAHCL-----------------LAMPGQDVAGAPVVMSVERKPGQSA-PNLTDQDRLSPLLPNH 148
Cdd:PRK06155 102 NTALRGPQLEHILRNSGARLLvveaallaaleaadpgdLPLPAVWLLDAPASVSVPAGWSTAPlPPLDAPAPAAAVQPGD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 PAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLA---AASDLI 225
Cdd:PRK06155 182 TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEprfSASGFW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 226 PGeplarlVRDQGIThVTLPPSALAPL---EEGGGLPPGLTLLVA-GEACPAPVAKSWaRDRV---MINAYGPTEATVAV 298
Cdd:PRK06155 262 PA------VRRHGAT-VTYLLGAMVSIllsQPARESDRAHRVRVAlGPGVPAALHAAF-RERFgvdLLDGYGSTETNFVI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 299 TASDPLTGEGTppIGRPITSVSTYILDDKLQPVPEGDVGELYMTG--PG-LARGYLRRPAATAE--RFLpnpfggpgerM 373
Cdd:PRK06155 334 AVTHGSQRPGS--MGRLAPGFEARVVDEHDQELPDGEPGELLLRAdePFaFATGYFGMPEKTVEawRNL----------W 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 374 YRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTGGARVAAED 448
Cdd:PRK06155 402 FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfpvpsELGEDEVMAAVVLRDGTALEPVA 481
|
490 500 510
....*....|....*....|....*....|....*..
gi 214003850 449 LLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK06155 482 LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
13-489 |
6.79e-31 |
|
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: 126.84 E-value: 6.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 13 EATAAAMPDRPAVAM-----GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV- 86
Cdd:cd05970 24 DAMAKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 87 ------DPDY---PADRRRHMLDD--------TAAHCLLAMPGQDVAGAPVVM----SVERKPGQSAPNLTDQDRLSPLL 145
Cdd:cd05970 104 hqltakDIVYrieSADIKMIVAIAednipeeiEKAAPECPSKPKLVWVGDPVPegwiDFRKLIKNASPDFERPTANSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 146 PNHPAYVIYTSGSTGQPKgvLVTHRGIPNLADDYVRR--QNLVPDSRLLAFASPSFDAAV-AEFWPIWLAGgCLVLAAAS 222
Cdd:cd05970 184 GEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKywQNVREGGLHLTVADTGWGKAVwGKIYGQWIAG-AAVFVYDY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 223 DLIPGEPLARLVRDQGITHVTLPPSA-------------LAPLEEGgglppgltlLVAGEACPAPVAKSW--ARDRVMIN 287
Cdd:cd05970 261 DKFDPKALLEKLSKYGVTTFCAPPTIyrfliredlsrydLSSLRYC---------TTAGEALNPEVFNTFkeKTGIKLME 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 288 AYGPTEATVAVtASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGEL---YMTGP--GLARGYLRRPAATAERFl 362
Cdd:cd05970 332 GFGQTETTLTI-ATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIvirTSKGKpvGLFGGYYKDAEKTAEVW- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 363 pnpFGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNRL-----IAYVV 437
Cdd:cd05970 410 ---HDG----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIrgqvvKATIV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 438 GTGGARvAAEDLLPPL----RKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPD 489
Cdd:cd05970 483 LAKGYE-PSEELKKELqdhvKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1-485 |
2.56e-30 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 125.00 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 1 MTGEASTAPA--------LFEATAAAMPDRPAVAMGA--TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFV 70
Cdd:PRK05852 3 FMGGAAPMASdfgpriadLVEVAATRLPEAPALVVTAdrIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 71 IAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLAM---PGQDVAGA----PVVMSVERKPGQSA----PNLTDQD 139
Cdd:PRK05852 83 VALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDadgPHDRAEPTtrwwPLTVNVGGDSGPSGgtlsVHLDAAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 140 RLSPL------LPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAG 213
Cdd:PRK05852 163 EPTPAtstpegLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 214 GCLVLAAASDLIPGEPLARLVRDQGITHVTLPPS------ALAPLEEGGGLPPGLTLLVAGEACPAPVAKSWARDRV--- 284
Cdd:PRK05852 243 GGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTihqillERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFaap 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 285 MINAYGPTEATVAVTAS---------DPltGEGTPPIGRPiTSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPA 355
Cdd:PRK05852 323 VVCAFGMTEATHQVTTTqiegigqteNP--VVSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 356 ATAERFLPNPFggpgermyRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNRLI-- 433
Cdd:PRK05852 400 ITAANFTDGWL--------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYge 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 214003850 434 ---AYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK05852 472 avaAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
16-485 |
2.66e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 125.15 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRR 95
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 96 RHMLDDTAAHCLLAmpgQDvAGAPVVMSVE-----------------------------RKPGQSAPNLTD--------- 137
Cdd:PRK06178 123 SYELNDAGAEVLLA---LD-QLAPVVEQVRaetslrhvivtsladvlpaeptlplpdslRAPRLAAAGAIDllpalract 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 138 -QDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRG-IPNLADDYVRRQNLVPDSRLLAFaspsfdaaVAEFW-------- 207
Cdd:PRK06178 199 aPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSF--------LPEFWiagenfgl 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 208 --PIWlAGGCLVLAAASDlipGEPLARLVRDQGITHVTLPPSALAPLEEGgglpPGL------TLLVAGeaCPAPVAKSW 279
Cdd:PRK06178 271 lfPLF-SGATLVLLARWD---AVAFMAAVERYRVTRTVMLVDNAVELMDH----PRFaeydlsSLRQVR--VVSFVKKLN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 280 ARDR---------VMINA-YGPTEATVAVTAS-----DPLTGEGTPP-IGRPITSVSTYILD-DKLQPVPEGDVGELYMT 342
Cdd:PRK06178 341 PDYRqrwraltgsVLAEAaWGMTETHTCDTFTagfqdDDFDLLSQPVfVGLPVPGTEFKICDfETGELLPLGAEGEIVVR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 343 GPGLARGYLRRPAATAERFLpnpfggpgERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALL---AVDG 419
Cdd:PRK06178 421 TPSLLKGYWNKPEATAEALR--------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGqhpAVLG 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 420 VaqAVVTEHDNR----LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVgLPRLPTSPNGKIDRAAL 485
Cdd:PRK06178 493 S--AVVGRPDPDkgqvPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
16-482 |
5.94e-30 |
|
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: 123.50 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGAT--TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPAD 93
Cdd:cd05904 15 ASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 94 RRRHMLDDTAAHCLLAMPgQDV-----AGAPVVMsVERKPGQSAPNLTDQDRLSPLLP-------NHPAYVIYTSGSTGQ 161
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTA-ELAeklasLALPVVL-LDSAEFDSLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 162 PKGVLVTHRGIPNLADDYVRRQNLV--PDSRLLAFAsPSFDaaVAEFWPIWLA----GGCLVLAAASDLipgEPLARLVR 235
Cdd:cd05904 173 SKGVMLTHRNLIAMVAQFVAGEGSNsdSEDVFLCVL-PMFH--IYGLSSFALGllrlGATVVVMPRFDL---EELLAAIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 236 DQGITHVTL-PPSALA----PLEEGGGLPPGLTLLVAGEACPAPVAKSWAR---DRVMINAYGPTEATvAVTASDPLTGE 307
Cdd:cd05904 247 RYKVTHLPVvPPIVLAlvksPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAkfpNVDLGQGYGMTEST-GVVAMCFAPEK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 308 GTPP---IGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPnpfggpgERMYRTGDRVWAG 383
Cdd:cd05904 326 DRAKygsVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK-------EGWLHTGDLCYID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 384 SDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNRL-----IAYVVGTGGARVAAEDLLPPLRKRLP 458
Cdd:cd05904 399 EDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEagevpMAFVVRKPGSSLTEDEIMDFVAKQVA 478
|
490 500
....*....|....*....|....
gi 214003850 459 GYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd05904 479 PYKKVRKVAFVDAIPKSPSGKILR 502
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
13-485 |
7.51e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 123.05 E-value: 7.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 13 EATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLV-EHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYP 91
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 92 ADRRRHMLDDTAAHCLLAMPGQDVAGAPV--VMSVERKPGQSAPNLTDQDRLSPLLP---NHPAYVIYTSGSTGQPKGVL 166
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALSMqkVSYVQRVISITSLKEIEDRKIDNFVEkneSASFIICYTSGTTGKPKGAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 VTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEF-WPIWLAGGCLVLAAASDliPGEPLaRLVRDQGITHVTLP 245
Cdd:PRK06839 169 LTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVPRKFE--PTKAL-SMIEKHKVTVVMGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 246 PS---AL--APLEEGGGLPPGLTLLVAGEACPAPVAKSWA-RDRVMINAYGPTEATVAV---TASDPLTGEGTppIGRPI 316
Cdd:PRK06839 246 PTihqALinCSKFETTNLQSVRWFYNGGAPCPEELMREFIdRGFLFGQGFGMTETSPTVfmlSEEDARRKVGS--IGKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 317 TSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermyRTGDRVWAGSDGQLVFVGRVDD 396
Cdd:PRK06839 324 LFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL--------CTGDLARVDEDGFVYIVGRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 397 QLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPR 471
Cdd:PRK06839 396 MIISGGENIYPLEVEQVINKLSDVYEVAVvgrqhVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKE 475
|
490
....*....|....
gi 214003850 472 LPTSPNGKIDRAAL 485
Cdd:PRK06839 476 LPKNATGKIQKAQL 489
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
7-487 |
1.65e-29 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 122.68 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMGATTLSYaelnGEANLLARRLVEHGVGPEKL-----VALAMPRSIEFVIAILAVHKAGA 81
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITY----READQLVEQFAAYLLGELQLkkgdrVALMMPNCLQYPIATFGVLRAGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 82 AYVPVDPDYPADRRRHMLDDTAAHCLLAMPG------QDVAGAPV--VMSVE---------------------------R 126
Cdd:PRK08751 102 TVVNVNPLYTPRELKHQLIDSGASVLVVIDNfgttvqQVIADTPVkqVITTGlgdmlgfpkaalvnfvvkyvkklvpeyR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 127 KPG----QSAPNLTDQDRLSPL--LPNHPAYVIYTSGSTGQPKGVLVTHRG-IPNL--ADDYVRRQN-LVPDSRLLAFAS 196
Cdd:PRK08751 182 INGairfREALALGRKHSMPTLqiEPDDIAFLQYTGGTTGVAKGAMLTHRNlVANMqqAHQWLAGTGkLEEGCEVVITAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 197 PSFD--AAVAEFWPIWLAGGCLVLAAASDLIPG--EPLARlVRDQGITHVTlppsalaPLEEGGGLPPGLT--------- 263
Cdd:PRK08751 262 PLYHifALTANGLVFMKIGGCNHLISNPRDMPGfvKELKK-TRFTAFTGVN-------TLFNGLLNTPGFDqidfsslkm 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 264 LLVAGEACPAPVAKSWAR--DRVMINAYGPTEATVAVTAsDPLT-GEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELY 340
Cdd:PRK08751 334 TLGGGMAVQRSVAERWKQvtGLTLVEAYGLTETSPAACI-NPLTlKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELC 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 341 MTGPGLARGYLRRPAATAERFlpnpfggPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV 420
Cdd:PRK08751 413 IKGPQVMKGYWKRPEETAKVM-------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 214003850 421 AQ----AVVTEHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PRK08751 486 LEvaavGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
23-495 |
1.95e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 121.93 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 23 PAVAMGAT--TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLD 100
Cdd:PRK08276 1 PAVIMAPSgeVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 101 DTAAHCLLAMPGQDVAGAPVVMSVERKPGQS---APNLTDQDRLSPLLPNHPAYVI----------YTSGSTGQPKGVLV 167
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELPAGVPLLlvvAGPVPGFRSYEEALAAQPDTPIadetagadmlYSSGTTGRPKGIKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 168 THRGIPNLADD------YVRRQNLVPDSRLLAfASPSFDAAVAEFWPIWLA-GGCLVLAAASDlipGEPLARLVRDQGIT 240
Cdd:PRK08276 161 PLPGLDPDEAPgmmlalLGFGMYGGPDSVYLS-PAPLYHTAPLRFGMSALAlGGTVVVMEKFD---AEEALALIERYRVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 241 HVTLPPSALAPLEEgggLPPGL-------TLLVAGEA---CPAPVakswarDRVMINAYGP--------TEA---TVAvT 299
Cdd:PRK08276 237 HSQLVPTMFVRMLK---LPEEVrarydvsSLRVAIHAaapCPVEV------KRAMIDWWGPiiheyyasSEGggvTVI-T 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 300 ASDPLTGEGTppIGRPITSVsTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPnpfggpgERMYRTGDR 379
Cdd:PRK08276 307 SEDWLAHPGS--VGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNP-------HGWVTVGDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 380 VWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAyVV----GTGGARVAAEDLL 450
Cdd:PRK08276 377 GYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVfgvpdEEMGERVKA-VVqpadGADAGDALAAELI 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 214003850 451 PPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAER 495
Cdd:PRK08276 456 AWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQR 500
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
15-485 |
3.21e-29 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 121.64 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 15 TAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAyvPVDPDYPADR 94
Cdd:PRK10946 32 TRHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 95 ------------------RRHML--DDTAAHCLLA-MPGQDV---AGAPVVMSVERKPGQSAPNLTDqdrlSPLLPNHPA 150
Cdd:PRK10946 110 selnayasqiepalliadRQHALfsDDDFLNTLVAeHSSLRVvllLNDDGEHSLDDAINHPAEDFTA----TPSPADEVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 151 YVIYTSGSTGQPKGVLVTHrgipnlaDDY---VRRQN----LVPDSRLL---------AFASPsfdAAVAEFwpiwLAGG 214
Cdd:PRK10946 186 FFQLSGGSTGTPKLIPRTH-------NDYyysVRRSVeicgFTPQTRYLcalpaahnyPMSSP---GALGVF----LAGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 215 CLVLAAASdlipgEPLA--RLVRDQGITHVTLPPSA----LAPLEEGGGLPP--GLTLL-VAGeacpAPVAKSWARdRV- 284
Cdd:PRK10946 252 TVVLAPDP-----SATLcfPLIEKHQVNVTALVPPAvslwLQAIAEGGSRAQlaSLKLLqVGG----ARLSETLAR-RIp 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 285 ------MINAYGPTEATVAVTASDP-----LTGEgtppiGRPITSV-STYILDDKLQPVPEGDVGELYMTGPGLARGYLR 352
Cdd:PRK10946 322 aelgcqLQQVFGMAEGLVNYTRLDDsderiFTTQ-----GRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 353 RPAATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNR 431
Cdd:PRK10946 397 SPQHNASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHaALVSMEDEL 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214003850 432 L----IAYVVGTGGARVAAedllppLRKRLPG-----YLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK10946 470 MgeksCAFLVVKEPLKAVQ------LRRFLREqgiaeFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
15-487 |
1.50e-28 |
|
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: 119.02 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 15 TAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPaDR 94
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 95 RRHMLDDtAAHCLLAMPGQDVAGAPVV-MSVERKPGQSAPNLTDQDRLspllpnhPAYVIYTSGSTGQPKGVLVTHRGIP 173
Cdd:cd05929 80 EACAIIE-IKAAALVCGLFTGGGALDGlEDYEAAEGGSPETPIEDEAA-------GWKMLYSGGTTGRPKGIKRGLPGGP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 174 NLADDYVRRQNLVP---DSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDliPGEPLaRLVRDQGITHVTLPP---S 247
Cdd:cd05929 152 PDNDTLMAAALGFGpgaDSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFD--PEEFL-RLIERYRVTFAQFVPtmfV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 248 ALAPLEEGGGLPPGLTLLV----AGEACPAPVAKSWAR--DRVMINAYGPTEAT--VAVTASDPLTGEGTppIGRPITSV 319
Cdd:cd05929 229 RLLKLPEAVRNAYDLSSLKrvihAAAPCPPWVKEQWIDwgGPIIWEYYGGTEGQglTIINGEEWLTHPGS--VGRAVLGK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 320 sTYILDDKLQPVPEGDVGELYMTGPGlARGYLRRPAATAERFlpnpfggpGERMYRT-GDRVWAGSDGQLVFVGRVDDQL 398
Cdd:cd05929 307 -VHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAAR--------NEGGWSTlGDVGYLDEDGYLYLTDRRSDMI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 399 KVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAyVVGTGGARVA----AEDLLPPLRKRLPGYLVPDVVVGL 469
Cdd:cd05929 377 ISGGVNIYPQEIENALIAHPKVLDAAVvgvpdEELGQRVHA-VVQPAPGADAgtalAEELIAFLRDRLSRYKCPRSIEFV 455
|
490
....*....|....*...
gi 214003850 470 PRLPTSPNGKIDRAALPD 487
Cdd:cd05929 456 AELPRDDTGKLYRRLLRD 473
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
16-487 |
3.49e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 114.98 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRR 95
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 96 RHMLDDTAAHCLL------AMPG----QDVAGAPVVMSVER--KPGQSAPnltdqdRLSPLLPNHPAYVIYTSGSTGQPK 163
Cdd:PRK06145 92 AYILGDAGAKLLLvdeefdAIVAletpKIVIDAAAQADSRRlaQGGLEIP------PQAAVAPTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 164 GVLVTHRGIPNLADDYVRRQNLVPDSRLLA----FASPSFD-AAVAEFWpiwlAGGclVLAAASDLIPGEPLARLVRDQg 238
Cdd:PRK06145 166 GVMHSYGNLHWKSIDHVIALGLTASERLLVvgplYHVGAFDlPGIAVLW----VGG--TLRIHREFDPEAVLAAIERHR- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 239 ITHVTLPPSALA-----PLEEGGGLPPGLTLLVAGEACPAPVAKSWAR---DRVMINAYGPTEATvavtASDPLTGEGTP 310
Cdd:PRK06145 239 LTCAWMAPVMLSrvltvPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRvftRARYIDAYGLTETC----SGDTLMEAGRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 311 -----PIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFlpnpFGGpgerMYRTGDRVWAGSD 385
Cdd:PRK06145 315 iekigSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF----YGD----WFRSGDVGYLDEE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 386 GQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHD----NRLIAYVVGTGGARVAAEDLLPPLRKRLPGY 460
Cdd:PRK06145 387 GFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEaAVIGVHDdrwgERITAVVVLNPGATLTLEALDRHCRQRLASF 466
|
490 500
....*....|....*....|....*..
gi 214003850 461 LVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PRK06145 467 KVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
15-480 |
4.39e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 115.14 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 15 TAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVD----PD- 89
Cdd:PRK07470 16 AARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNfrqtPDe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 --Y--PADRRRHML-----DDTAAHCLLAMP--------GQDVAGAPVVMSVERKPGQSAPNLT-DQDrlspllpnHPAY 151
Cdd:PRK07470 96 vaYlaEASGARAMIchadfPEHAAAVRAASPdlthvvaiGGARAGLDYEALVARHLGARVANAAvDHD--------DPCW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 152 VIYTSGSTGQPKGVLVTHRG----IPN-LADdyvrrqnLVPD----SRLLAFASPSFDAAVAEFwpIWLAGGclvlaAAS 222
Cdd:PRK07470 168 FFFTSGTTGRPKAAVLTHGQmafvITNhLAD-------LMPGtteqDASLVVAPLSHGAGIHQL--CQVARG-----AAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 223 DLIPGEPLA-----RLVRDQGITHVTLPPSALAPLEEGgglpPGLT---------LLVAGeacpAPVAKS---WARDR-- 283
Cdd:PRK07470 234 VLLPSERFDpaevwALVERHRVTNLFTVPTILKMLVEH----PAVDrydhsslryVIYAG----APMYRAdqkRALAKlg 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 284 -VMINAYGPTEATVAVT-------ASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPA 355
Cdd:PRK07470 306 kVLVQYFGLGEVTGNITvlppalhDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 356 ATAERFLPNPFggpgermyRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALL--------AVDGVAQAVVTE 427
Cdd:PRK07470 386 ANAKAFRDGWF--------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLthpavsevAVLGVPDPVWGE 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 214003850 428 HDnrlIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKI 480
Cdd:PRK07470 458 VG---VAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
9-480 |
7.42e-27 |
|
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: 113.93 E-value: 7.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALF-EATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVD 87
Cdd:cd12118 6 PLSFlERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 88 PDYPADRRRHMLDDTAAHCLLAmpGQDVAGAPVVMSVERKPGQSAPnltdQDRLSPLLPNhpayviYTSGSTGQPKGVLV 167
Cdd:cd12118 86 TRLDAEEIAFILRHSEAKVLFV--DREFEYEDLLAEGDPDFEWIPP----ADEWDPIALN------YTSGTTGRPKGVVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 168 THRGIPNLADDYVRRQNLVPDSRLLaFASPSFDAAVAEF-WPIWLAGG---CL--VLAAAsdlipgepLARLVRDQGITH 241
Cdd:cd12118 154 HHRGAYLNALANILEWEMKQHPVYL-WTLPMFHCNGWCFpWTVAAVGGtnvCLrkVDAKA--------IYDLIEKHKVTH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 242 VTLPPSAL-----APLEEGGGLPPGLTLLVAGEACPAPV-AKSWARDRVMINAYGPTEATVAVTA------SDPLTGE-- 307
Cdd:cd12118 225 FCGAPTVLnmlanAPPSDARPLPHRVHVMTAGAPPPAAVlAKMEELGFDVTHVYGLTETYGPATVcawkpeWDELPTEer 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 308 -------GTPPIGR-PITSVSTyildDKLQPVP-EGD-VGELYMTGPGLARGYLRRPAATAERFLpnpfGGpgerMYRTG 377
Cdd:cd12118 305 arlkarqGVRYVGLeEVDVLDP----ETMKPVPrDGKtIGEIVFRGNIVMKGYLKNPEATAEAFR----GG----WFHSG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 378 DRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV-AQAVVTEHDNRL----IAYVVGTGGARVAAEDLLPP 452
Cdd:cd12118 373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVlEAAVVARPDEKWgevpCAFVELKEGAKVTEEEIIAF 452
|
490 500
....*....|....*....|....*...
gi 214003850 453 LRKRLPGYLVPDVVVGLPrLPTSPNGKI 480
Cdd:cd12118 453 CREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
29-485 |
1.01e-26 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 114.01 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 29 ATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLL 108
Cdd:PRK08008 35 VRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 109 AMPG--------QDVAGAPV---------------VMSVERKPGQSAPNLTDQdrlSPLLPNHPAYVIYTSGSTGQPKGV 165
Cdd:PRK08008 115 TSAQfypmyrqiQQEDATPLrhicltrvalpaddgVSSFTQLKAQQPATLCYA---PPLSTDDTAEILFTSGTTSRPKGV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 166 LVTHRgipNL--ADDYVRRQ-NLVPDSRLLAFAsPSF------DAAVAEFwpiwLAGGCLVLAAASDlipgeplARLVRD 236
Cdd:PRK08008 192 VITHY---NLrfAGYYSAWQcALRDDDVYLTVM-PAFhidcqcTAAMAAF----SAGATFVLLEKYS-------ARAFWG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 237 Q------GITHV------TLPPSALAPLEEGGGLPPGLTLLVAGEAcpapvAKSWARDRV---MINAYGPTEATVAVTAS 301
Cdd:PRK08008 257 QvckyraTITECipmmirTLMVQPPSANDRQHCLREVMFYLNLSDQ-----EKDAFEERFgvrLLTSYGMTETIVGIIGD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 302 DPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTG-PG--LARGYLRRPAATAERFLPNPFggpgermYRTGD 378
Cdd:PRK08008 332 RPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYYLDPKATAKVLEADGW-------LHTGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 379 RVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTE-----HDNRLIAYVVGTGGARVAAEDLLPPL 453
Cdd:PRK08008 405 TGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGikdsiRDEAIKAFVVLNEGETLSEEEFFAFC 484
|
490 500 510
....*....|....*....|....*....|..
gi 214003850 454 RKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK08008 485 EQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
7-482 |
1.08e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 114.10 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMG--ATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYV 84
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 85 PVDPDYPADRRRHMLDDTAAHCLLAMP--------------------GQDVAGAP---------VVMSVERKPG------ 129
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADafktsdyhamlqellpglaeGQPGALACerlpelrgvVSLAPAPPPGflawhe 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 130 -QSAPN-LTDQD---RLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAfASPSFDAava 204
Cdd:PRK12583 179 lQARGEtVSREAlaeRQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCV-PVPLYHC--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 205 eFWPIWLAGGCLVLAAASdLIPGE---PLARL--VRDQGITHVT-LPPSALAPLEEGG----GLPPGLTLLVAGEACPAP 274
Cdd:PRK12583 255 -FGMVLANLGCMTVGACL-VYPNEafdPLATLqaVEEERCTALYgVPTMFIAELDHPQrgnfDLSSLRTGIMAGAPCPIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 275 VAKSWARDRVMIN---AYGPTEA---TVAVTASDPLTGEgTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLAR 348
Cdd:PRK12583 333 VMRRVMDEMHMAEvqiAYGMTETspvSLQTTAADDLERR-VETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 349 GYLRRPAATAERFLPNPFggpgerMYrTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV--- 425
Cdd:PRK12583 412 GYWNNPEATAESIDEDGW------MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVfgv 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 214003850 426 --TEHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:PRK12583 485 pdEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
7-489 |
4.42e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 112.33 E-value: 4.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV 86
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 87 DPDYPADR-----RRHML-----DDTAAHCLLAMPgQDVAGAPVVMSVERKPGQSAPNLTDQDRL--------SPLLPNH 148
Cdd:PRK07788 130 NTGFSGPQlaevaAREGVkalvyDDEFTDLLSALP-PDLGRLRAWGGNPDDDEPSGSTDETLDDLiagsstapLPKPPKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 PAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRqnlVPDSR--LLAFASPSFDAAVAEFWPIWLAGGC-LVLAAASDli 225
Cdd:PRK07788 209 GGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSR---VPFRAgeTTLLPAPMFHATGWAHLTLAMALGStVVLRRRFD-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 226 PGEPLARLVRDQGITHVTLPPSALAPLEEGGGLPPGLTL------LVAGEACPAPVAKSwARDR---VMINAYGPTEATV 296
Cdd:PRK07788 284 PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTsslkiiFVSGSALSPELATR-ALEAfgpVLYNLYGSTEVAF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 297 AVTAS--DPLTGEGTppIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYlrrpaaTAerflpnpfGGPGER-- 372
Cdd:PRK07788 363 ATIATpeDLAEAPGT--VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TD--------GRDKQIid 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 373 -MYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT-----EHDNRLIAYVVGTGGARVAA 446
Cdd:PRK07788 427 gLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgvddeEFGQRLRAFVVKAPGAALDE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 214003850 447 EDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPD 489
Cdd:PRK07788 507 DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
149-485 |
8.36e-26 |
|
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: 108.19 E-value: 8.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 PAYVIYTSGSTGQPKGVLVTHRgipNLADDYVRRQNLVP----DSRLLAfaSPSFDaaVAEFWPIWLaggclVLAAASDL 224
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAA---NLLASAAGLHSRLGfgggDSWLLS--LPLYH--VGGLAILVR-----SLLAGAEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 225 IPGEPLARLVRD---QGITHVTLPPSALAPLEEGGGLPPGLT----LLVAGEACPAPVAKSWARDRV-MINAYGPTEATV 296
Cdd:cd17630 70 VLLERNQALAEDlapPGVTHVSLVPTQLQRLLDSGQGPAALKslraVLLGGAPIPPELLERAADRGIpLYTTYGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 297 AVTASDPLtGEGTPPIGRPITSVSTYILDDklqpvpegdvGELYMTGPGLARGYLRRPaataerfLPNPFGGPGerMYRT 376
Cdd:cd17630 150 QVATKRPD-GFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEFNEDG--WFTT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 377 GDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTGGARVAaeDLLP 451
Cdd:cd17630 210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVvgvpdEELGQRPVAVIVGRGPADPA--ELRA 287
|
330 340 350
....*....|....*....|....*....|....
gi 214003850 452 PLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
32-485 |
3.02e-25 |
|
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: 108.42 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDdtaahcllamp 111
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 112 gqdvAGAPVVMSVERKPGQSAPNLtdqdrlspllpnhpayVIYTSGSTGQPKGVLVTHRGIP--NLADDYvrRQNLVPDS 189
Cdd:cd05974 70 ----RGGAVYAAVDENTHADDPML----------------LYFTSGTTSKPKLVEHTHRSYPvgHLSTMY--WIGLKPGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 190 RLLAFASPSF-DAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRdQGITHVTLPPSALAPL--EEGGGLPPGLTLLV 266
Cdd:cd05974 128 VHWNISSPGWaKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVR-YGVTTLCAPPTVWRMLiqQDLASFDVKLREVV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 267 -AGEACPAP----VAKSWARdrVMINAYGPTEATVAVTASdPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVG-ELY 340
Cdd:cd05974 207 gAGEPLNPEvieqVRRAWGL--TIRDGYGQTETTALVGNS-PGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVAlDLG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 341 MTGP-GLARGYLRRPAATAerflpnpfGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDG 419
Cdd:cd05974 284 DTRPvGLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPA 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 214003850 420 VAQAVV--TEHDNRLI---AYVVGTGGA---RVAAEDLLPPLRKRLPGY-LVPDVVVGlpRLPTSPNGKIDRAAL 485
Cdd:cd05974 356 VAEAAVvpSPDPVRLSvpkAFIVLRAGYepsPETALEIFRFSRERLAPYkRIRRLEFA--ELPKTISGKIRRVEL 428
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
4-487 |
3.44e-25 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 109.72 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 4 EASTAPALFEATAAAMPDRPA-VAMGaTTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAA 82
Cdd:PRK07059 21 QYPSLADLLEESFRQYADRPAfICMG-KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 83 YVPVDPDYPADRRRHMLDDTAA-----------------------HCLLAMPGqDVAGA--PVVMSVERK-----PGQSA 132
Cdd:PRK07059 100 VVNVNPLYTPRELEHQLKDSGAeaivvlenfattvqqvlaktavkHVVVASMG-DLLGFkgHIVNFVVRRvkkmvPAWSL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 133 PN-------LTDQDRLS----PLLPNHPAYVIYTSGSTGQPKGVLVTHRGIpnLAD--------DYVRRQNLVPDSRLLA 193
Cdd:PRK07059 179 PGhvrfndaLAEGARQTfkpvKLGPDDVAFLQYTGGTTGVSKGATLLHRNI--VANvlqmeawlQPAFEKKPRPDQLNFV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 194 FASPSFD--AAVAEFWPIWLAGGCLVLAAASDLIPGeplarLVRDQGITHVTLPPsALAPLEEGGGLPPGLT------LL 265
Cdd:PRK07059 257 CALPLYHifALTVCGLLGMRTGGRNILIPNPRDIPG-----FIKELKKYQVHIFP-AVNTLYNALLNNPDFDkldfskLI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 266 VA---GEACPAPVAKSWARDR--VMINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELY 340
Cdd:PRK07059 331 VAnggGMAVQRPVAERWLEMTgcPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEIC 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 341 MTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV 420
Cdd:PRK07059 411 IRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214003850 421 ----AQAVVTEHDNRLI-AYVVGTGGArVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PRK07059 484 levaAVGVPDEHSGEAVkLFVVKKDPA-LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
30-485 |
1.08e-24 |
|
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: 108.56 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 30 TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLA 109
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 110 M-----PGQDVAGAPVV-----MSVERKP-------GQSAPNLTDQDR---------------LSPLLPNHPAYVIYTSG 157
Cdd:cd05967 161 AscgiePGKVVPYKPLLdkaleLSGHKPHhvlvlnrPQVPADLTKPGRdldwsellakaepvdCVPVAATDPLYILYTSG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 158 STGQPKGVL-----------VTHRGIPNLADDYVrrqnlvpdsrllafaspsfdaavaeFWPI----WLAG------GCL 216
Cdd:cd05967 241 TTGKPKGVVrdngghavalnWSMRNIYGIKPGDV-------------------------WWAAsdvgWVVGhsyivyGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 217 VLAAASDLIPGEPLA--------RLVRDQGITHVTLPPSAL-----APLEEGGGLPPGL----TLLVAGEACPAPVaKSW 279
Cdd:cd05967 296 LHGATTVLYEGKPVGtpdpgafwRVIEKYQVNALFTAPTAIrairkEDPDGKYIKKYDLsslrTLFLAGERLDPPT-LEW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 280 AR---DRVMINAYGPTEATVAVTASdpLTGEGTPPI-----GRPITSVSTYILDDKLQPVPEGDVGELYMTGPgLARGYL 351
Cdd:cd05967 375 AEntlGVPVIDHWWQTETGWPITAN--PVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCL 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 352 RRPAATAERFLPNPFGG-PGerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHD 429
Cdd:cd05967 452 LTLWKNDERFKKLYLSKfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEcAVVGVRD 529
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 214003850 430 ----NRLIAYVVGTGGARVAAEDLLPPL----RKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05967 530 elkgQVPLGLVVLKEGVKITAEELEKELvalvREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1-488 |
1.56e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 107.54 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 1 MTGEASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAG 80
Cdd:PRK13382 38 MRREGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 81 AAYVPVDPDYPADRRRHMLDDTAAHCL------LAMPGQDVAGAPVVMSVERKPGQSAPNLTDQDRLSPL------LPNH 148
Cdd:PRK13382 118 ADILLLNTSFAGPALAEVVTREGVDTViydeefSATVDRALADCPQATRIVAWTDEDHDLTVEVLIAAHAgqrpepTGRK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 PAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDsRLLAFASPSFDAavaefWPIwlagGCLVLAA--ASDLI- 225
Cdd:PRK13382 198 GRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAE-EPTVIVAPMFHA-----WGF----SQLVLAAslACTIVt 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 226 -----PGEPLArLVRDQGITHVTLPPSALAPLEEgggLPP-------GLTLLVA---GEACPAPVAKSWaRDR---VMIN 287
Cdd:PRK13382 268 rrrfdPEATLD-LIDRHRATGLAVVPVMFDRIMD---LPAevrnrysGRSLRFAaasGSRMRPDVVIAF-MDQfgdVIYN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 288 AYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYlrRPAATAERFlpnpfg 367
Cdd:PRK13382 343 NYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFH------ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 368 gpgERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTGGA 442
Cdd:PRK13382 415 ---DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVigvddEQYGQRLAAFVVLKPGA 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 214003850 443 RVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDP 488
Cdd:PRK13382 492 SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
149-481 |
2.64e-24 |
|
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: 103.92 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 PAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAfASPSFDAAVAEF-WPIWLAGGCLVLAAASDlipG 227
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLN-SGPLFHIGTLMFtLATFHAGGTNVFVRRVD---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 228 EPLARLVRDQGITHVTLPPSALAPLEE-GGGLPPGLTLLVAGEACP---APVAKSWARDRVMINAYGPTEATVAVTASdP 303
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPPTIDQIVElNADGLYDLSSLRSSPAAPewnDMATVDTSPWGRKPGGYGQTEVMGLATFA-A 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 304 LTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLpnpFGGpgermYRTGDRVWAG 383
Cdd:cd17636 157 LGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR---GGW-----HHTNDLGRRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 384 SDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNRLI----AYVVGTGGARVAAEDLLPPLRKRLP 458
Cdd:cd17636 229 PDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADaAVIGVPDPRWAqsvkAIVVLKPGASVTEAELIEHCRARIA 308
|
330 340
....*....|....*....|...
gi 214003850 459 GYLVPDVVVGLPRLPTSPNGKID 481
Cdd:cd17636 309 SYKKPKSVEFADALPRTAGGADD 331
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
30-426 |
4.51e-24 |
|
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: 105.88 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 30 TTLSYAELNGEANLLARRLvEHGVGPEKLVALAMPRSIEFVIAILAVHKAGaaYVPVDPDYPADRR--RHMLDDTAAHCL 107
Cdd:cd05909 6 TSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGLRelRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 108 LA----------MPGQDVAGAPVVMSVERKPGQ---------------SAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQP 162
Cdd:cd05909 83 LTskqfieklklHHLFDVEYDARIVYLEDLRAKiskadkckaflagkfPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 163 KGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASP--SFDAAVAEFWPIwLAGGCLVLAaaSDLIPGEPLARLVRDQGIT 240
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTGCLWLPL-LSGIKVVFH--PNPLDYKKIPELIYDKKAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 241 HVTLPPSAL------APLEEggglPPGLTLLVAG-EACPAPVAKSWAR--DRVMINAYGPTEATVAVTASDPLTG--EGT 309
Cdd:cd05909 240 ILLGTPTFLrgyaraAHPED----FSSLRLVVAGaEKLKDTLRQEFQEkfGIRILEGYGTTECSPVISVNTPQSPnkEGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 310 ppIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFlpnpfggpGERMYRTGDRVWAGSDGQL 388
Cdd:cd05909 316 --VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF--------GDGWYDTGDIGKIDGEGFL 385
|
410 420 430
....*....|....*....|....*....|....*...
gi 214003850 389 VFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT 426
Cdd:cd05909 386 TITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAV 423
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
3-487 |
5.25e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.00 E-value: 5.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 3 GEASTAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEH-GVGPEKLVALAMPRSIEFVIAILAVHKAGA 81
Cdd:PRK05677 21 DEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 82 AYVPVDPDYPADRRRHMLDDTAAH---CLLAMPGQDVAGAP--------------------------VVMSVERK-PGQS 131
Cdd:PRK05677 101 IVVNTNPLYTAREMEHQFNDSGAKalvCLANMAHLAEKVLPktgvkhvivtevadmlpplkrllinaVVKHVKKMvPAYH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 132 APN---LTD---QDRLSPLLPNHP-----AYVIYTSGSTGQPKGVLVTHRgipNLADDYVRRQNLV-------------- 186
Cdd:PRK05677 181 LPQavkFNDalaKGAGQPVTEANPqaddvAVLQYTGGTTGVAKGAMLTHR---NLVANMLQCRALMgsnlnegceiliap 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 187 -PDSRLLAFaspSFDAAVaefwpIWLAGGCLVLAAASDLIPGeplarLVRD------QGITHVTLPPSALAPLEEGGGLP 259
Cdd:PRK05677 258 lPLYHIYAF---TFHCMA-----MMLIGNHNILISNPRDLPA-----MVKElgkwkfSGFVGLNTLFVALCNNEAFRKLD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 260 -PGLTL-LVAGEACPAPVAKSWARDR--VMINAYGPTEaTVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGD 335
Cdd:PRK05677 325 fSALKLtLSGGMALQLATAERWKEVTgcAICEGYGMTE-TSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 336 VGELYMTGPGLARGYLRRPAATAERFlpnpfggPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALL 415
Cdd:PRK05677 404 VGELCVKGPQVMKGYWQRPEATDEIL-------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLA 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214003850 416 AVDGVAQ-AVVTEHDNR----LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PRK05677 477 ALPGVLQcAAIGVPDEKsgeaIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
11-488 |
6.15e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 105.67 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEH-GVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPD 89
Cdd:PRK12492 29 VFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 YPADRRRHMLDDTAAHCL--LAMPGQDV----AGAPVVMSVERKPGQSAPNL------TDQDRLSPLLPNHP-------- 149
Cdd:PRK12492 109 YTAREMRHQFKDSGARALvyLNMFGKLVqevlPDTGIEYLIEAKMGDLLPAAkgwlvnTVVDKVKKMVPAYHlpqavpfk 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 150 ---------------------AYVIYTSGSTGQPKGVLVTHRG-IPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFW 207
Cdd:PRK12492 189 qalrqgrglslkpvpvglddiAVLQYTGGTTGLAKGAMLTHGNlVANMLQVRACLSQLGPDGQPLMKEGQEVMIAPLPLY 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 208 PIWLAGG---CLVLAAASDLIPGEP--LARLVRDQGITHVtlppSALAPLEeggglppglTLLVA--------------- 267
Cdd:PRK12492 269 HIYAFTAncmCMMVSGNHNVLITNPrdIPGFIKELGKWRF----SALLGLN---------TLFVAlmdhpgfkdldfsal 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 268 ------GEACPAPVAKSWARDR--VMINAYGPTEaTVAVTASDP---LTGEGTppIGRPITSVSTYILDDKLQPVPEGDV 336
Cdd:PRK12492 336 kltnsgGTALVKATAERWEQLTgcTIVEGYGLTE-TSPVASTNPygeLARLGT--VGIPVPGTALKVIDDDGNELPLGER 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 337 GELYMTGPGLARGYLRRPAATAERFlpnpfggPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLA 416
Cdd:PRK12492 413 GELCIKGPQVMKGYWQQPEATAEAL-------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMA 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214003850 417 VDGVAQ-AVVTEHDNR----LIAYVVGTGGArVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDP 488
Cdd:PRK12492 486 HPKVANcAAIGVPDERsgeaVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
16-425 |
7.14e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 105.75 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGAT----------TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVP 85
Cdd:PRK09274 16 AQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 86 VDPDYPADRRRHMLDDTAAHCLLAMPGQDVA-----------------------GAPVVMSVERKPGQSAPNLTDqdrls 142
Cdd:PRK09274 96 VDPGMGIKNLKQCLAEAQPDAFIGIPKAHLArrlfgwgkpsvrrlvtvggrllwGGTTLATLLRDGAAAPFPMAD----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 143 pLLPNHPAYVIYTSGSTGQPKGVLVTHRG----IPNLADDYvrrqNLVPDSRLLA----FASpsFDAAvaefwpiwlAGG 214
Cdd:PRK09274 171 -LAPDDMAAILFTSGSTGTPKGVVYTHGMfeaqIEALREDY----GIEPGEIDLPtfplFAL--FGPA---------LGM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 215 CLVLaaaSDLIPGEPL----ARLV---RDQGITHVTLPPSALAPLEEGG---GLP-PGL-TLLVAGeacpAPV-AKSWAR 281
Cdd:PRK09274 235 TSVI---PDMDPTRPAtvdpAKLFaaiERYGVTNLFGSPALLERLGRYGeanGIKlPSLrRVISAG----APVpIAVIER 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 282 DRVMINA-------YGPTEAT-VAVTASDPL---------TGEGTPpIGRPITSVSTYI--LDDKLQP-------VPEGD 335
Cdd:PRK09274 308 FRAMLPPdaeiltpYGATEALpISSIESREIlfatraatdNGAGIC-VGRPVDGVEVRIiaISDAPIPewddalrLATGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 336 VGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMyrtGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVE---- 411
Cdd:PRK09274 387 IGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRM---GDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCErifn 463
|
490 500
....*....|....*....|.
gi 214003850 412 -------SALLAVdGVAQAVV 425
Cdd:PRK09274 464 thpgvkrSALVGV-GVPGAQR 483
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
11-487 |
8.04e-24 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 105.52 E-value: 8.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPA-VAMGATtLSYAELNGEANLLARRLvEHGVGPEK--LVALAMPRSIEFVIAILAVHKAGAAYVPVD 87
Cdd:PRK08974 28 MFEQAVARYADQPAfINMGEV-MTFRKLEERSRAFAAYL-QNGLGLKKgdRVALMMPNLLQYPIALFGILRAGMIVVNVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 88 PDYPADRRRHMLDDTAA-----------------------HCLLAMPGQDVAGAP------VVMSVERK-PGQSAPN-LT 136
Cdd:PRK08974 106 PLYTPRELEHQLNDSGAkaivivsnfahtlekvvfktpvkHVILTRMGDQLSTAKgtlvnfVVKYIKRLvPKYHLPDaIS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 137 DQDRLS---------P-LLPNHPAYVIYTSGSTGQPKGVLVTHRG-IPNLAD-DYVRRQNLVPDSRLLAFASP---SFDA 201
Cdd:PRK08974 186 FRSALHkgrrmqyvkPeLVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQaKAAYGPLLHPGKELVVTALPlyhIFAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 202 AVAEFWPIWLAGGCLVLAAASDlIPG--EPLARlVRDQGITHVTLPPSALAPLEEGGGLP-PGLTLLVAG-EACPAPVAK 277
Cdd:PRK08974 266 TVNCLLFIELGGQNLLITNPRD-IPGfvKELKK-YPFTAITGVNTLFNALLNNEEFQELDfSSLKLSVGGgMAVQQAVAE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 278 SWAR--DRVMINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPA 355
Cdd:PRK08974 344 RWVKltGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 356 ATAErFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ--AVVTEHDN--R 431
Cdd:PRK08974 424 ATDE-VIKDGW-------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEvaAVGVPSEVsgE 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 432 LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PRK08974 496 AVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
16-488 |
2.74e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 103.62 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGAT--TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPAD 93
Cdd:PRK13391 7 AQTTPDKPAVIMASTgeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 94 RRRHMLDDTAAHCLLAMPGQ-DVAGApvvmSVERKPGQSAPNLTDQD-------RLSPLLPNHPAYVI----------YT 155
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKlDVARA----LLKQCPGVRHRLVLDGDgelegfvGYAEAVAGLPATPIadeslgtdmlYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 156 SGSTGQPKGVL--VTHRGI---PNLADDYVRRQNLVPDSRLLAFAsPSFDAAVAEFWPIWLA-GGCLVLAAASDlipGEP 229
Cdd:PRK13391 163 SGTTGRPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRSDMVYLSPA-PLYHSAPQRAVMLVIRlGGTVIVMEHFD---AEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 230 LARLVRDQGITHVTLPPSALAPLEEgggLPPGL-------TLLVAGEA---CPAPVAKSwardrvMINAYGP-------- 291
Cdd:PRK13391 239 YLALIEEYGVTHTQLVPTMFSRMLK---LPEEVrdkydlsSLEVAIHAaapCPPQVKEQ------MIDWWGPiiheyyaa 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 292 TEA--TVAVTASDPLTGEGTppIGRPITSVsTYILDDKLQPVPEGDVGELYMTGpGLARGYLRRPAATAERFLPNPfggp 369
Cdd:PRK13391 310 TEGlgFTACDSEEWLAHPGT--VGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG---- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 370 geRMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALL--------AVDGVAQAVVTEHDNRLIAYVVGTGG 441
Cdd:PRK13391 382 --TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLIthpkvadaAVFGVPNEDLGEEVKAVVQPVDGVDP 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 214003850 442 ARVAAEDLLPPLRKRLPGYLVP---DVVVGLPRLPTspnGKIDRAALPDP 488
Cdd:PRK13391 460 GPALAAELIAFCRQRLSRQKCPrsiDFEDELPRLPT---GKLYKRLLRDR 506
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
31-482 |
4.74e-23 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 103.48 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV----DPDYPADR------------ 94
Cdd:TIGR02188 88 KITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVfggfSAEALADRindagaklvita 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 95 -------RRHMLDDTAAHCLlAMPGQDV--------AGAPVVMSVE-----------RKPGQSAPnltdqdrlSPLLPNH 148
Cdd:TIGR02188 168 deglrggKVIPLKAIVDEAL-EKCPVSVehvlvvrrTGNPVVPWVEgrdvwwhdlmaKASAYCEP--------EPMDSED 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 PAYVIYTSGSTGQPKGVL-----------VTHRGIPNLADDYVrrqnlvpdsrllafaspsfdaavaeFWPI----WLAG 213
Cdd:TIGR02188 239 PLFILYTSGSTGKPKGVLhttggyllyaaMTMKYVFDIKDGDI-------------------------FWCTadvgWITG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 214 ------GCLVLAAASDLIPGEP-------LARLVRDQGITHVTLPPSALAPLEEGGGLPP------GLTLL-VAGEacP- 272
Cdd:TIGR02188 294 hsyivyGPLANGATTVMFEGVPtypdpgrFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVkkhdlsSLRLLgSVGE--Pi 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 273 APVAKSWARDRV------MINAYGPTEATVAVTASDPltgeGTPPI-----GRPITSVSTYILDDKLQPVP-EGDVGELY 340
Cdd:TIGR02188 372 NPEAWMWYYKVVgkercpIVDTWWQTETGGIMITPLP----GATPTkpgsaTLPFFGIEPAVVDEEGNPVEgPGEGGYLV 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 341 MTG--PGLARGYLRRPaataERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVD 418
Cdd:TIGR02188 448 IKQpwPGMLRTIYGDH----ERFVDTYF-SPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHP 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214003850 419 GVAQ-AVVTEHD----NRLIAYVV---GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:TIGR02188 523 AVAEaAVVGIPDdikgQAIYAFVTlkdGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMR 594
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-482 |
7.12e-23 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 102.64 E-value: 7.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV----DPDYPADRrrhMLD------ 100
Cdd:cd05966 84 TITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfagfSAESLADR---INDaqcklv 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 101 -------------------DTAA-------HCLLAMpgqdVAGAPVVMSVER-------KPGQSAPNLTDqdrlsPLLPN 147
Cdd:cd05966 161 itadggyrggkviplkeivDEALekcpsveKVLVVK----RTGGEVPMTEGRdlwwhdlMAKQSPECEPE-----WMDSE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 148 HPAYVIYTSGSTGQPKGVLVTHRGI---PNLADDYVRrqNLVPDSRllafaspsfdaavaeFW----PIWLAG------G 214
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYllyAATTFKYVF--DYHPDDI---------------YWctadIGWITGhsyivyG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 215 CLVLAAASDLIPGEPL----AR---LVRDQGITHVTLPPSALAPLEEGGGLPP------GLTLL--VaGEacP-APVAKS 278
Cdd:cd05966 295 PLANGATTVMFEGTPTypdpGRywdIVEKHKVTIFYTAPTAIRALMKFGDEWVkkhdlsSLRVLgsV-GE--PiNPEAWM 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 279 WARDRV------MINAYGPTE-ATVAVTasdPLTGEgTP--P--IGRPITSVSTYILDDKLQPVPEGDVGELYMTG--PG 345
Cdd:cd05966 372 WYYEVIgkercpIVDTWWQTEtGGIMIT---PLPGA-TPlkPgsATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRpwPG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 346 LARGYLRRPaataERFLP---NPFGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ 422
Cdd:cd05966 448 MARTIYGDH----ERYEDtyfSKFPG----YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAE 519
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 423 -AVVTEHD----NRLIAYVV---GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd05966 520 aAVVGRPHdikgEAIYAFVTlkdGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
7-569 |
8.42e-23 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 103.24 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV 86
Cdd:COG3319 5 AAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 87 DPDYPADRRRHMLDDTAAHCLLAMPGQDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVL 166
Cdd:COG3319 85 ALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 VTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQGITHVTLPP 246
Cdd:COG3319 165 VLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 247 SA---------LAPLEEGGGLPPGLTLLVAGEACPAPVAKSWARDRVMINAYGPTEATVAVTASDPLTGEGTPPIGRPIT 317
Cdd:COG3319 245 AAlllllalalLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 318 SVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQ 397
Cdd:COG3319 325 LVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 398 LKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNRLIAYVVGTGGARVAAEDLLPPLRK-RLPGYLVPDVVVGLPRLPTSP 476
Cdd:COG3319 405 RLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLlLLLLLPPPLPPALLLLLLLLL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 477 NGKIDRAALPDPDREGAERVTSGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARIRQSLQVRLRV 556
Cdd:COG3319 485 LLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLL 564
|
570
....*....|...
gi 214003850 557 QAFFNAPTVAQLA 569
Cdd:COG3319 565 LALLLAPTLAALA 577
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
11-487 |
8.86e-23 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 101.88 E-value: 8.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAM---GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVD 87
Cdd:PRK07514 5 LFDALRAAFADRDAPFIetpDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 88 PDYPADRRRHMLDDTAAHCLLAMPGQ--------DVAGAPVVMSVERKPGQSapnLTDQDR-LSPLLPNHP------AYV 152
Cdd:PRK07514 85 TAYTLAELDYFIGDAEPALVVCDPANfawlskiaAAAGAPHVETLDADGTGS---LLEAAAaAPDDFETVPrgaddlAAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 153 IYTSGSTGQPKGVLVTHRgipNLAD------DYVRRQnlvPDSRLLaFASPSFDAAvaefwPIWLAGGCLVLAAASDLIp 226
Cdd:PRK07514 162 LYTSGTTGRSKGAMLSHG---NLLSnaltlvDYWRFT---PDDVLI-HALPIFHTH-----GLFVATNVALLAGASMIF- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 227 gepLARLVRDQGIThvtLPPSALAPLeeggGLP---------PGLT--------LLVAGEAcP--APVAKSWaRDR---V 284
Cdd:PRK07514 229 ---LPKFDPDAVLA---LMPRATVMM----GVPtfytrllqePRLTreaaahmrLFISGSA-PllAETHREF-QERtghA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 285 MINAYGPTEaTVAVTaSDPLTGE---GTppIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAER 360
Cdd:PRK07514 297 ILERYGMTE-TNMNT-SNPYDGErraGT--VGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 361 FLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVV-TEHDN---RLIAY 435
Cdd:PRK07514 373 FRADGF-------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVEsAVIgVPHPDfgeGVTAV 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 214003850 436 VVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PRK07514 446 VVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
16-485 |
8.97e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 102.01 E-value: 8.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGAT--TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPAD 93
Cdd:PRK13390 7 AQIAPDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 94 RRRHMLDDTAAHCLLAMPGQD----VAGAPVVM------------SVERKPGQSAPNLTDQdrlsPLlpnhPAYVIYTSG 157
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDglaaKVGADLPLrlsfggeidgfgSFEAALAGAGPRLTEQ----PC----GAVMLYSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 158 STGQPKGVLvthrgiPNLADDYVRRqnlvPDSRLLAFASPSFDAAVAEFW----PIWLA------------GGCLVLAAA 221
Cdd:PRK13390 159 TTGFPKGIQ------PDLPGRDVDA----PGDPIVAIARAFYDISESDIYyssaPIYHAaplrwcsmvhalGGTVVLAKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 222 SDlipGEPLARLVRDQGITHVTLPPSAL-------APLEEGGGLPPGLTLLVAGEACPAPVAKSwardrvMINAYGP--- 291
Cdd:PRK13390 229 FD---AQATLGHVERYRITVTQMVPTMFvrllkldADVRTRYDVSSLRAVIHAAAPCPVDVKHA------MIDWLGPivy 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 292 -----TEA--TVAVTASDPLTGEGTppIGRPITSvSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLP- 363
Cdd:PRK13390 300 eyyssTEAhgMTFIDSPDWLAHPGS--VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPa 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 364 NPFggpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESAL--------LAVDGVAQAVVTEHDNRLIAY 435
Cdd:PRK13390 377 HPF------WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALtmhpavhdVAVIGVPDPEMGEQVKAVIQL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 214003850 436 VVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK13390 451 VEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
12-463 |
2.07e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 101.10 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 12 FEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDpdyp 91
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 92 adrrRHMLDDTAAHCL-LAMP----------------GQDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLLP-------- 146
Cdd:PRK08279 119 ----TQQRGAVLAHSLnLVDAkhlivgeelveafeeaRADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPttnpasrs 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 147 ----NHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAF--------ASPSFDAAVAefwpiwlAGG 214
Cdd:PRK08279 195 gvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCClplyhntgGTVAWSSVLA-------AGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 215 CLVLA---AASDLIPGeplarlVRDQGITHVTL-----------PPSalaPLEE--------GGGLPPGLtllvageacp 272
Cdd:PRK08279 268 TLALRrkfSASRFWDD------VRRYRATAFQYigelcryllnqPPK---PTDRdhrlrlmiGNGLRPDI---------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 273 apvaksWAR-------DRVMiNAYGPTEATVAVTASDPLtgEGTppIGR-PITSVSTYIL--------------DDKLQP 330
Cdd:PRK08279 329 ------WDEfqqrfgiPRIL-EFYAASEGNVGFINVFNF--DGT--VGRvPLWLAHPYAIvkydvdtgepvrdaDGRCIK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 331 VPEGDVGELymtgpgLAR--------GYlRRPAATAERFLPNPFgGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRG 402
Cdd:PRK08279 398 VKPGEVGLL------IGRitdrgpfdGY-TDPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKG 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214003850 403 HRIEPGEVESALLAVDGVAQAVV-----TEHDNRL-IAYVVGTGGARVAAEDLLPPLRKRLPGYLVP 463
Cdd:PRK08279 470 ENVATTEVENALSGFPGVEEAVVygvevPGTDGRAgMAAIVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
149-482 |
2.19e-22 |
|
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: 98.49 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 PAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQ-NLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAasDLIPG 227
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGG--ENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 228 EPLARLVRDQGITHVTLPPSALAPL----EEGGGLPPGLTLLVAGEACPAPVAKS---WARDRVMINAYGPTEATVAVTA 300
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLvselKSANATVPSLRLIGYGGSRAIAADVRfieATGLTNTAQVYGLSETGTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 301 SdplTGEGTPPI---GRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLpnpfggpgERMYRTG 377
Cdd:cd17635 161 P---TDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI--------DGWVNTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 378 DRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTE-HDNRL----IAYVVGTG-GARVAAEDLLP 451
Cdd:cd17635 230 DLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEiSDEEFgelvGLAVVASAeLDENAIRALKH 309
|
330 340 350
....*....|....*....|....*....|.
gi 214003850 452 PLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd17635 310 TIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
152-480 |
2.63e-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: 97.96 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 152 VIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFaSPSFDAavaefwpIWLAGGCLV-LAAASDLIPG--- 227
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLII-NPFFHT-------FGYKAGIVAcLLTGATVVPVavf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 228 EPLA--RLVRDQGITHVTLPPSALAPLEEGGGLPPG----LTLLVAGEACPAPVAKSWARDRVMIN----AYGPTEATVA 297
Cdd:cd17638 77 DVDAilEAIERERITVLPGPPTLFQSLLDHPGRKKFdlssLRAAVTGAATVPVELVRRMRSELGFEtvltAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 298 V---TASDPLTGEGTppIGRPITSVSTYILDDklqpvpegdvGELYMTGPGLARGYLRRPAATAERFlpnpfggPGERMY 374
Cdd:cd17638 157 TmcrPGDDAETVATT--CGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI-------DADGWL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 375 RTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNRL----IAYVVGTGGARVAAEDL 449
Cdd:cd17638 218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQvAVIGVPDERMgevgKAFVVARPGVTLTEEDV 297
|
330 340 350
....*....|....*....|....*....|.
gi 214003850 450 LPPLRKRLPGYLVPDVVVGLPRLPTSPNGKI 480
Cdd:cd17638 298 IAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
6-487 |
4.66e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 96.83 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 6 STAPALFeaTAAAMPDRPAVAMGAT--TLSYAELNGEANLLARRLVEH-GVGPEKLVALAMPRSIEFVIAILAVHKAGAA 82
Cdd:PLN02574 41 DAVSFIF--SHHNHNGDTALIDSSTgfSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 83 YVPVDP-DYPADRRRHMLDDTAA--------HCLLAMPGQDVAGAPVVMSVERKPGQSAPN----LTDQDRL-SPLLPNH 148
Cdd:PLN02574 119 VTTMNPsSSLGEIKKRVVDCSVGlaftspenVEKLSPLGVPVIGVPENYDFDSKRIEFPKFyeliKEDFDFVpKPVIKQD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 149 P-AYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNlvpdSRLLAFASPSFDAAVAEFWPIW----LAGGCLVLAA--- 220
Cdd:PLN02574 199 DvAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEA----SQYEYPGSDNVYLAALPMFHIYglslFVVGLLSLGStiv 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 221 ------ASDLIpgeplaRLVRDQGITHVTLPPSALAPL----EEGGGLPPGLTLLVAGEAcpAPVAKSWARDRV------ 284
Cdd:PLN02574 275 vmrrfdASDMV------KVIDRFKVTHFPVVPPILMALtkkaKGVCGEVLKSLKQVSCGA--APLSGKFIQDFVqtlphv 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 285 -MINAYGPTEATVAVTA---SDPLT-----GEGTPPIGRPITSVSTYILddklqpVPEGDVGELYMTGPGLARGYLRRPA 355
Cdd:PLN02574 347 dFIQGYGMTESTAVGTRgfnTEKLSkyssvGLLAPNMQAKVVDWSTGCL------LPPGNCGELWIQGPGVMKGYLNNPK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 356 ATAERFLPnpfggpgERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNR---- 431
Cdd:PLN02574 421 ATQSTIDK-------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKecge 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 214003850 432 -LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PLN02574 494 iPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
30-438 |
5.86e-21 |
|
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: 95.89 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 30 TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAahclla 109
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 110 mpgqdvagaPVVMSVErkpgqsapnltdqdrlspllpNHP---AYVIYTSGSTGQPKGVLVTHRGIpnladdyvrrqnLV 186
Cdd:cd17640 78 ---------SVALVVE---------------------NDSddlATIIYTSGTTGNPKGVMLTHANL------------LH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 187 PDSRLLAFASPSFDAAVAEFWPIW-----------LAGGCL-----VLAAASDLIPGEP-----LARL-----------V 234
Cdd:cd17640 116 QIRSLSDIVPPQPGDRFLSILPIWhsyersaeyfiFACGCSqaytsIRTLKDDLKRVKPhyivsVPRLweslysgiqkqV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 235 RDQGITHVTLPPSAL------APLEEGGGLPPGLTLLVagEACPAPVakswardrvmINAYGPTEATVAVTA---SDPLT 305
Cdd:cd17640 196 SKSSPIKQFLFLFFLsggifkFGISGGGALPPHVDTFF--EAIGIEV----------LNGYGLTETSPVVSArrlKCNVR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 306 GEgtppIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAGS 384
Cdd:cd17640 264 GS----VGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTC 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 385 DGQLVFVGRVDDQLKVR-GHRIEPGEVESALLAVDGVAQAVVTEHDNR-LIAYVVG 438
Cdd:cd17640 333 GGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKrLGALIVP 388
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
12-495 |
9.75e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 95.62 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 12 FEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPeKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYP 91
Cdd:PRK07638 7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 92 ADRRRHMLDDTAAHCLLA-----MPGQDVAGaPVVMSVERKPGQSApnltDQDRLSPL--LPNHPAYVIYTSGSTGQPKG 164
Cdd:PRK07638 86 QDELKERLAISNADMIVTeryklNDLPDEEG-RVIEIDEWKRMIEK----YLPTYAPIenVQNAPFYMGFTSGSTGKPKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 165 VLVTHRG-----IPNLADDYVRRQN--LVPDSrllAFASPSFDAAVAEFWpiwlAGGCLVLaaASDLIPGEPLARLVRDQ 237
Cdd:PRK07638 161 FLRAQQSwlhsfDCNVHDFHMKREDsvLIAGT---LVHSLFLYGAISTLY----VGQTVHL--MRKFIPNQVLDKLETEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 238 GITHVTLPPSALAPLEEGGGLPPGLTLLVAGEACPAPvAKSWARDRV----MINAYGPTEATVaVTASDPLTGEGTP-PI 312
Cdd:PRK07638 232 ISVMYTVPTMLESLYKENRVIENKMKIISSGAKWEAE-AKEKIKNIFpyakLYEFYGASELSF-VTALVDEESERRPnSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 313 GRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAErflPNPFGgpgermYRT-GDRVWAGSDGQLVFV 391
Cdd:PRK07638 310 GRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE---LNADG------WMTvRDVGYEDEEGFIYIV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 392 GRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV--TEHD---NRLIAYVVGTGGARvaaeDLLPPLRKRLPGYLVPDVV 466
Cdd:PRK07638 381 GREKNMILFGGINIFPEEIESVLHEHPAVDEIVVigVPDSywgEKPVAIIKGSATKQ----QLKSFCLQRLSSFKIPKEW 456
|
490 500
....*....|....*....|....*....
gi 214003850 467 VGLPRLPTSPNGKIDRAALPDPDREGAER 495
Cdd:PRK07638 457 HFVDEIPYTNSGKIARMEAKSWIENQEKI 485
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
20-425 |
9.85e-21 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 95.32 E-value: 9.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHML 99
Cdd:PRK09029 17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 100 DDTAAHCLLAMPGQDVAGAPVVMSVERKPGQSAPNLtDQDRLspllpnhpAYVIYTSGSTGQPKGVLVTHRGIPNLADDY 179
Cdd:PRK09029 97 PSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAW-QPQRL--------ATMTLTSGSTGLPKAAVHTAQAHLASAEGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 180 VrrqNLVP----DSRLLAFasPSFD-AAVAEFWPiWL-AGGCLVLAAasdlipGEPLARLVrdQGITHVTLPPSALAPLE 253
Cdd:PRK09029 168 L---SLMPftaqDSWLLSL--PLFHvSGQGIVWR-WLyAGATLVVRD------KQPLEQAL--AGCTHASLVPTQLWRLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 254 EGGGLPPGLT-LLVAGEACPAPVA--------KSWArdrvminAYGPTEATVAVTA--SDPLTGEGTPPIGRPITSVSty 322
Cdd:PRK09029 234 DNRSEPLSLKaVLLGGAAIPVELTeqaeqqgiRCWC-------GYGLTEMASTVCAkrADGLAGVGSPLPGREVKLVD-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 323 ilddklqpvpegdvGELYMTGPGLARGYLR----RPAATAERFlpnpfggpgermYRTGDR-VWAGsdGQLVFVGRVDDQ 397
Cdd:PRK09029 305 --------------GEIWLRGASLALGYWRqgqlVPLVNDEGW------------FATRDRgEWQN--GELTILGRLDNL 356
|
410 420
....*....|....*....|....*...
gi 214003850 398 LKVRGHRIEPGEVESALLAVDGVAQAVV 425
Cdd:PRK09029 357 FFSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
11-486 |
1.15e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 95.45 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 11 LFEATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:PRK13383 40 LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 PADRRRHMLDdtaAHCLLAMPGQD-----VAGAPVVMSVERKPGQSAPNLTDQDRLSPllpnHPAYVIYTSGSTGQPKGV 165
Cdd:PRK13383 120 RSDALAAALR---AHHISTVVADNefaerIAGADDAVAVIDPATAGAEESGGRPAVAA----PGRIVLLTSGTTGKPKGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 166 --LVTHRGIPNLADDYVRRQNLVPDSRLlAFASPSFDAAVAEFWPIWLA-GGCLVLAAASDLIPGEPLARLVRDQGITHV 242
Cdd:PRK13383 193 prAPQLRSAVGVWVTILDRTRLRTGSRI-SVAMPMFHGLGLGMLMLTIAlGGTVLTHRHFDAEAALAQASLHRADAFTAV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 243 --------TLPPSALAPleegGGLPPGLTLLVAGEACPAPVAKSW--ARDRVMINAYGPTEATVAVTASDPLTGEGTPPI 312
Cdd:PRK13383 272 pvvlarilELPPRVRAR----NPLPQLRVVMSSGDRLDPTLGQRFmdTYGDILYNGYGSTEVGIGALATPADLRDAPETV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 313 GRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLrrpaataerflpnpfGGPGER----MYRTGDRVWAGSDGQL 388
Cdd:PRK13383 348 GKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYT---------------DGGGKAvvdgMTSTGDMGYLDNAGRL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 389 VFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHD----NRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVP 463
Cdd:PRK13383 413 FIVGREDDMIISGGENVYPRAVENALAAHPAVADnAVIGVPDerfgHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQP 492
|
490 500
....*....|....*....|...
gi 214003850 464 DVVVGLPRLPTSPNGKIDRAALP 486
Cdd:PRK13383 493 RDINIVSSIPRNPTGKVLRKELP 515
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
28-437 |
1.35e-20 |
|
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: 94.82 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 28 GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCL 107
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 108 LampgqdvagapvvmsverkpgqsapnLTDQDRLspllpnhpAYVIYTSGSTGQPKGVLVTHRGIpnLAD-DYVRRQNLV 186
Cdd:cd05914 84 F--------------------------VSDEDDV--------ALINYTSGTTGNSKGVMLTYRNI--VSNvDGVKEVVLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 187 -PDSRLLAF-----------------------------ASPSFDA-AVAEFWPIwlAGGCLVLA----AASDLIPGEPLA 231
Cdd:cd05914 128 gKGDKILSIlplhhiypltftlllpllngahvvfldkiPSAKIIAlAFAQVTPT--LGVPVPLViekiFKMDIIPKLTLK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 232 RL-------VRDQGITHVTLPpsalAPLEEGGGlppGLTLLVAGEAcpaPVAKSWARDRVMIN-----AYGPTEaTVAVT 299
Cdd:cd05914 206 KFkfklakkINNRKIRKLAFK----KVHEAFGG---NIKEFVIGGA---KINPDVEEFLRTIGfpytiGYGMTE-TAPII 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 300 ASDPLTGEGTPPIGRPITSVSTYILDdklqPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDR 379
Cdd:cd05914 275 SYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW-------FHTGDL 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 214003850 380 VWAGSDGQLVFVGRVDDQLKV-RGHRIEPGEVESALLAVDGVAQAVVTEHDNRLIAYVV 437
Cdd:cd05914 344 GKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAY 402
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
151-481 |
2.48e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 92.83 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 151 YVIYTSGSTGQPKGVLVTH--------------RGIPNLADDYVRRQNLVPDSRLLAfASPSFDAAVAEFWPIWLAGGCL 216
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifrmlmggadfgTGEFTPSEDAHKAAAAAAGTVMFP-APPLMHGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 217 VLAAASDLIPGEPLaRLVRDQGITHVTLPPSALA-----PLEEGGGLP-PGLTLLVAGEACPAPVAKS----WARDRVMI 286
Cdd:cd05924 86 VVLPDDRFDPEEVW-RTIEKHKVTSMTIVGDAMArplidALRDAGPYDlSSLFAISSGGALLSPEVKQglleLVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 287 NAYGPTEA----TVAVTASDPLTGEGTPPIGRpitsvsTYILDDKLQPVPEGDVGELYMTGPGL-ARGYLRRPAATAERF 361
Cdd:cd05924 165 DAFGSSETgftgSGHSAGSGPETGPFTRANPD------TVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 362 lpnpFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYV 436
Cdd:cd05924 239 ----PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVvgrpdERWGQEVVAVV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 214003850 437 VGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKID 481
Cdd:cd05924 315 QLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
152-482 |
7.43e-20 |
|
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: 90.79 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 152 VIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLA----FASPSFDAAVAEFwpiwLAGGCLVLAAASDliPG 227
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNmlplFHIAGLNLALATF----HAGGANVVMEKFD--PA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 228 EpLARLVRDQGITH-VTLPPSALAPLEEGGGLPPGLTLL--VAGEACPAPV--------AKSWArdrvminAYGPTEATV 296
Cdd:cd17637 79 E-ALELIEEEKVTLmGSFPPILSNLLDAAEKSGVDLSSLrhVLGLDAPETIqrfeettgATFWS-------LYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 297 AVTASDPLTGEGTppIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLpnpfGGpgerMYRT 376
Cdd:cd17637 151 LVTLSPYRERPGS--AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR----NG----WHHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 377 GDRVWAGSDGQLVFVGRV--DDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRLIAYVVGTGGARVAAEDL 449
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVigvpdPKWGEGIKAVCVLKPGATLTADEL 300
|
330 340 350
....*....|....*....|....*....|...
gi 214003850 450 LPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd17637 301 IEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
132-485 |
2.34e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 91.28 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 132 APNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLaFASPSF-DAAVAEFWPIW 210
Cdd:PRK07867 137 AAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCY-VSMPLFhSNAVMAGWAVA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 211 LAGGC-LVLAA---ASDLIPGeplarlVRDQGITH---VTLPPS-ALAPLEEGGGLPPGLTLLVAGEACPAPVAKSWAR- 281
Cdd:PRK07867 216 LAAGAsIALRRkfsASGFLPD------VRRYGATYanyVGKPLSyVLATPERPDDADNPLRIVYGNEGAPGDIARFARRf 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 282 DRVMINAYGPTEATVAVTASdpltgEGTPP--IGRPITSVStyILD-DKLQPVPEGD------------VGELY-MTGPG 345
Cdd:PRK07867 290 GCVVVDGFGSTEGGVAITRT-----PDTPPgaLGPLPPGVA--IVDpDTGTECPPAEdadgrllnadeaIGELVnTAGPG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 346 LARGYLRRPAATAERFLpnpfGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV 425
Cdd:PRK07867 363 GFEGYYNDPEADAERMR----GG----VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAV 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 214003850 426 -----TEHDNRLIAYVVGTGGAR----------VAAEDLLPplrKRLPGYlvpdvVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK07867 435 yavpdPVVGDQVMAALVLAPGAKfdpdafaeflAAQPDLGP---KQWPSY-----VRVCAELPRTATFKVLKRQL 501
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-482 |
3.03e-19 |
|
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: 89.26 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 154 YTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRL-------------------------LAFASPSFDAAVaefwp 208
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplfhcfgsvlgvlaclthgatMVFPSPSFDPLA----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 209 iwlaggclVLAAASD----LIPGEPlarlvrDQGITHVTLPPSALAPLeegGGLPPGLTllvAGEACPAPVAKSWARDRV 284
Cdd:cd05917 84 --------VLEAIEKekctALHGVP------TMFIAELEHPDFDKFDL---SSLRTGIM---AGAPCPPELMKRVIEVMN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 285 MIN---AYGPTEATVAVTASDPltgEGTPP-----IGRPITSVSTYILDDKLQPVPE-GDVGELYMTGPGLARGYLRRPA 355
Cdd:cd05917 144 MKDvtiAYGMTETSPVSTQTRT---DDSIEkrvntVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 356 ATAERFLpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLkVRG-HRIEPGEVESALLAVDGVAQA-VVTEHDNRL- 432
Cdd:cd05917 221 KTAEAID-------GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVqVVGVPDERYg 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 214003850 433 ---IAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd05917 293 eevCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
148-482 |
5.88e-19 |
|
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: 87.85 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 148 HPAYVIYTSGSTGQPKGVLVTHRG-----IPNLADDYVRRQN--LVPDSrlLAFaSPSFDAAVAEFWpiwlAGGCLVLAa 220
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSwiesfVCNEDLFNISGEDaiLAPGP--LSH-SLFLYGAISALY----LGGTFIGQ- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 221 aSDLIPGEpLARLVRDQGITHVTLPPSALAPL-EEGGGLPPGLTLLVAGEACPAPVAKSWAR---DRVMINAYGPTEATV 296
Cdd:cd17633 73 -RKFNPKS-WIRKINQYNATVIYLVPTMLQALaRTLEPESKIKSIFSSGQKLFESTKKKLKNifpKANLIEFYGTSELSF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 297 aVTASDPLTGEGTPPIGRPITSVSTYILDDKlqpvpEGDVGELYMTGPGLARGYLRRPAATAERFlpnpfggpgermYRT 376
Cdd:cd17633 151 -ITYNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------MSV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 377 GDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNR-----LIAYVVGTGgarVAAEDLLP 451
Cdd:cd17633 213 GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDArfgeiAVALYSGDK---LTYKQLKR 289
|
330 340 350
....*....|....*....|....*....|.
gi 214003850 452 PLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:cd17633 290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
32-426 |
5.96e-19 |
|
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: 90.22 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDT-AAHCLLAM 110
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSeSKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 111 PGQDVAGAPVVM-SVERKPGQSAPNLTDQDRLSPLLPNHP-------------AYVIYTSGSTGQPKGVLVTHRGIPNLA 176
Cdd:cd05932 87 LDDWKAMAPGVPeGLISISLPPPSAANCQYQWDDLIAQHPpleerptrfpeqlATLIYTSGTTGQPKGVMLTFGSFAWAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 177 DDYVRRQNLVPDSRLLAFASPsfdAAVAEFWPI---WLAGGCLVLAAAS------DLIPGEP-----LARL-VRDQGITH 241
Cdd:cd05932 167 QAGIEHIGTEENDRMLSYLPL---AHVTERVFVeggSLYGGVLVAFAESldtfveDVQRARPtlffsVPRLwTKFQQGVQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 242 VTLPPSALAPLEE--------GGGLPPGLTL----LVAGEACPAPVAK-SWARdRVMIN---AYGPTEATVAVTASDPLT 305
Cdd:cd05932 244 DKIPQQKLNLLLKipvvnslvKRKVLKGLGLdqcrLAGCGSAPVPPALlEWYR-SLGLNileAYGMTENFAYSHLNYPGR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 306 G-EGTppIGRPITSVSTYILDDklqpvpegdvGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAGS 384
Cdd:cd05932 323 DkIGT--VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF-------LRTGDKGELDA 383
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 214003850 385 DGQLVFVGRVDDQLKV-RGHRIEPGEVESALLAVDGVAQAVVT 426
Cdd:cd05932 384 DGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
31-482 |
8.07e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 89.95 E-value: 8.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV----DPDYPADR------------ 94
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDRledseakvlitt 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 95 ----RRHMLDDTAA--HCLLAmpGQDVAGAPVVMSVERKPGQSAPNLTdqdrLSPLLPNHPAYVIYTSGSTGQPKGVL-- 166
Cdd:PRK04319 153 pallERKPADDLPSlkHVLLV--GEDVEEGPGTLDFNALMEQASDEFD----IEWTDREDGAILHYTSGSTGKPKGVLhv 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 ----VTHRgipnLADDYVrrQNLVPDSRLLAFASPSFDAAVAE--FWPiWLAGGCLVLAAAsDLIPgEPLARLVRDQGIT 240
Cdd:PRK04319 227 hnamLQHY----QTGKYV--LDLHEDDVYWCTADPGWVTGTSYgiFAP-WLNGATNVIDGG-RFSP-ERWYRILEDYKVT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 241 HVTLPPSALAPLEEGGG-------LPPGLTLLVAGEACpAPVAKSWARD----RVMINaYGPTEATVAVTASDPltgegT 309
Cdd:PRK04319 298 VWYTAPTAIRMLMGAGDdlvkkydLSSLRHILSVGEPL-NPEVVRWGMKvfglPIHDN-WWMTETGGIMIANYP-----A 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 310 PPI-----GRPITSVSTYILDDKLQPVPEGDVGELYM-TG-PGLARGYLRRPAATAERFLPNpfggpgerMYRTGDRVWA 382
Cdd:PRK04319 371 MDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGwPSMMRGIWNNPEKYESYFAGD--------WYVSGDSAYM 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 383 GSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQA-VVTEHD----NRLIAYVV---GTGGARVAAEDLLPPLR 454
Cdd:PRK04319 443 DEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAgVIGKPDpvrgEIIKAFVAlrpGYEPSEELKEEIRGFVK 522
|
490 500
....*....|....*....|....*...
gi 214003850 455 KRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:PRK04319 523 KGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
31-487 |
1.05e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 89.06 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPdypADRRRHMlddtaAHCLLAM 110
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP---GMGRKNL-----KQCLQEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 111 PGQDVAGAPvvmsverkpgqsapnltdqdrlsplLPNHPAYVIYTSGSTGQPKGVLVTHRG----IPNLADDYvrrqNLV 186
Cdd:cd05910 74 EPDAFIGIP-------------------------KADEPAAILFTSGSTGTPKGVVYRHGTfaaqIDALRQLY----GIR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 187 PDSRLLafaspsfdaavAEFWPIWLAGGCL-VLAAASDLIPGEP-------LARLVRDQGITHVTLPPSALAPLEEGGG- 257
Cdd:cd05910 125 PGEVDL-----------ATFPLFALFGPALgLTSVIPDMDPTRParadpqkLVGAIRQYGVSIVFGSPALLERVARYCAq 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 258 ----LPPGLTLLVAGEACPAPVAKSWAR----DRVMINAYGPTEA-TVAVTASDPLTGEGTPP--------IGRPITSVS 320
Cdd:cd05910 194 hgitLPSLRRVLSAGAPVPIALAARLRKmlsdEAEILTPYGATEAlPVSSIGSRELLATTTAAtsggagtcVGRPIPGVR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 321 TYILD---------DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMyrtGDRVWAGSDGQLVFV 391
Cdd:cd05910 274 VRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRM---GDLGYLDDEGRLWFC 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 392 GRVDDQLKVRGHRIEPGEVESALLAVDGVAQAV-------VTEHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPD 464
Cdd:cd05910 351 GRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAlvgvgkpGCQLPVLCVEPLPGTITPRARLEQELRALAKDYPHTQRIG 430
|
490 500
....*....|....*....|....*
gi 214003850 465 VVVGLPRLPTSP--NGKIDRAALPD 487
Cdd:cd05910 431 RFLIHPSFPVDIrhNAKIFREKLAV 455
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
10-485 |
1.96e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 88.86 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 10 ALFEATAAAMPDRPAV--------AMGATTLSYAELNGE----ANLLARRlvehGVGPEKLVALAMPRSIEFVIAILAVH 77
Cdd:PRK07529 29 ELLSRAAARHPDAPALsflldadpLDRPETWTYAELLADvtrtANLLHSL----GVGPGDVVAFLLPNLPETHFALWGGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 78 KAGAAyVPVDPDYPADRRRHMLDDTAAHCLLA---MPGQD--------VAGAPVVMSV--------------------ER 126
Cdd:PRK07529 105 AAGIA-NPINPLLEPEQIAELLRAAGAKVLVTlgpFPGTDiwqkvaevLAALPELRTVvevdlarylpgpkrlavpliRR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 127 KPGQSAPNLTDQ------DRL---SPLLPNHPAYVIYTSGSTGQPKGVLVTHRGipNLADDYVRRQNL--VPDSRLLAfA 195
Cdd:PRK07529 184 KAHARILDFDAElarqpgDRLfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN--EVANAWLGALLLglGPGDTVFC-G 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 196 SPSF--DAAVAEFWPIWLAGGCLVLAAAS-----DLIPGepLARLVRDQGITHVTLPPSALAPLEEgggLPPG------L 262
Cdd:PRK07529 261 LPLFhvNALLVTGLAPLARGAHVVLATPQgyrgpGVIAN--FWKIVERYRINFLSGVPTVYAALLQ---VPVDghdissL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 263 TLLVAGEAcPAPVA---KSWARDRVMI-NAYGPTEATVAVTASdPLTGEGTP-PIGRPI--TSVSTYILDDK---LQPVP 332
Cdd:PRK07529 336 RYALCGAA-PLPVEvfrRFEAATGVRIvEGYGLTEATCVSSVN-PPDGERRIgSVGLRLpyQRVRVVILDDAgryLRDCA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 333 EGDVGELYMTGPGLARGYLrRPAATAERFLpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDqLKVR-GHRIEPGEVE 411
Cdd:PRK07529 414 VDEVGVLCIAGPNVFSGYL-EAAHNKGLWL-------EDGWLNTGDLGRIDADGYFWLTGRAKD-LIIRgGHNIDPAAIE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 412 SALLAVDGVAQAVVT----EHDNRL-IAYVVGTGGARVAAEDLLPPLRKRLPG-YLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK07529 485 EALLRHPAVALAAAVgrpdAHAGELpVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
293-576 |
2.51e-18 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 85.57 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 293 EATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGER 372
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 373 MYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTE-----HDNRLIAYVVGTGGARVAAE 447
Cdd:COG3433 81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAAlrgagVGLLLIVGAVAALDGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 448 DLLPpLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAERVTSGRAPSTPTEIH--LAGLFAEVLGVS--SV 523
Cdd:COG3433 161 ALAA-LDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEeeLRADVAELLGVDpeEI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 214003850 524 GVDDSFFDIGGHSLLATRLVARIRQsLQVRLRVQAFFNAPTVAQLAKVLDGAP 576
Cdd:COG3433 240 DPDDNLFDLGLDSIRLMQLVERWRK-AGLDVSFADLAEHPTLAAWWALLAAAQ 291
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
13-499 |
3.99e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 87.78 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 13 EATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPA 92
Cdd:PRK06710 31 EQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 93 DRRRHMLDDTAAHCLLAM------------------------------------PGQDVAGAPVVMSVERKPGQSAPNLT 136
Cdd:PRK06710 111 RELEYQLHDSGAKVILCLdlvfprvtnvqsatkiehvivtriadflpfpknllyPFVQKKQSNLVVKVSESETIHLWNSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 137 DQDRLSPL-LPNHP----AYVIYTSGSTGQPKGVLVTHRG-IPNLADDYVRRQNLVPDSRLLAFASPSFD--AAVAEFWP 208
Cdd:PRK06710 191 EKEVNTGVeVPCDPendlALLQYTGGTTGFPKGVMLTHKNlVSNTLMGVQWLYNCKEGEEVVLGVLPFFHvyGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 209 IWLAGGCLVLAAASDLipgeplaRLVRDQGITH-VTLPPSAL--------APLEEGGGLPpGLTLLVAGEAcPAPVAKSW 279
Cdd:PRK06710 271 SIMQGYKMVLIPKFDM-------KMVFEAIKKHkVTLFPGAPtiyiallnSPLLKEYDIS-SIRACISGSA-PLPVEVQE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 280 ARDRV----MINAYGPTEATvAVTASDPLTGEGTP-PIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPGLARGYLRR 353
Cdd:PRK06710 342 KFETVtggkLVEGYGLTESS-PVTHSNFLWEKRVPgSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 354 PAATAERFlpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT-----EH 428
Cdd:PRK06710 421 PEETAAVL--------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIgvpdpYR 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 214003850 429 DNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPDPDREGAERVTSG 499
Cdd:PRK06710 493 GETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNEDEQTG 563
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
6-484 |
6.42e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 87.31 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 6 STAPALFEATAAAMPDRPA---------VAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAmPRSIEFVIAILAV 76
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAftfidyeqdPAGVAETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 77 HKAGAAYVPVDPDYPA---DRRRHMLDDTAAHCLLAMPGqdVAGApVVMSVERKPGQSAP--------NLTDQDRLSPLL 145
Cdd:PRK05850 80 LQAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSA--VVDD-VTEYVAPQPGQSAPpvievdllDLDSPRGSDARP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 146 PNHP--AYVIYTSGSTGQPKGVLVTHRG-IPN---LADDYVRRQNLVpdsrllafasPSFDAAVAEFWPIWLAGGcLVLA 219
Cdd:PRK05850 157 RDLPstAYLQYTSGSTRTPAGVMVSHRNvIANfeqLMSDYFGDTGGV----------PPPDTTVVSWLPFYHDMG-LVLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 220 AASDLIPG------EPLARLVRD----QGITHVTLPPSAlAPL------------EEGGGLPPG--LTLLVAGEACPAPV 275
Cdd:PRK05850 226 VCAPILGGcpavltSPVAFLQRParwmQLLASNPHAFSA-APNfafelavrktsdDDMAGLDLGgvLGIISGSERVHPAT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 276 AKSWA--------RDRVMINAYGPTEATVAVTASDP----------------------LTGEGTPPI--GRPiTSVSTYI 323
Cdd:PRK05850 305 LKRFAdrfapfnlRETAIRPSYGLAEATVYVATREPgqppesvrfdyeklsaghakrcETGGGTPLVsyGSP-RSPTVRI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 324 LD-DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERF---LPNPFGG-PGERMYRTGDrvwAG--SDGQLVFVGRVDD 396
Cdd:PRK05850 384 VDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPGtPEGPWLRTGD---LGfiSEGELFIVGRIKD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 397 QLKVRGHRIEPGEVESALLAVDG---VAQAVVTEHDNRL--IAYVVGTGGARVAAEDLLPPLRK-------RLPGYLVPD 464
Cdd:PRK05850 461 LLIVDGRNHYPDDIEATIQEITGgrvAAISVPDDGTEKLvaIIELKKRGDSDEEAMDRLRTVKRevtsaisKSHGLSVAD 540
|
570 580
....*....|....*....|.
gi 214003850 465 VVVGLP-RLPTSPNGKIDRAA 484
Cdd:PRK05850 541 LVLVAPgSIPITTSGKIRRAA 561
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
13-485 |
7.09e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 86.92 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 13 EATAAAMPDRPAVAMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPA 92
Cdd:PRK08162 25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 93 DRRRHMLD--------------DTAAHCLLAMPGQDvagaPVVMSVERKPGQSAPNLTDQDRLSPLLPNHPAYVI----- 153
Cdd:PRK08162 105 ASIAFMLRhgeakvlivdtefaEVAREALALLPGPK----PLVIDVDDPEYPGGRFIGALDYEAFLASGDPDFAWtlpad 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 154 --------YTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLaFASPSFDAAVAEF-WPIWLAGGCLVLAAASDl 224
Cdd:PRK08162 181 ewdaialnYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYL-WTLPMFHCNGWCFpWTVAARAGTNVCLRKVD- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 225 ipGEPLARLVRDQGITHVTLPP---SAL--APLEEGGGLPPGLTLLVAGEACPAPV-AKSWARDRVMINAYGPTE--ATV 296
Cdd:PRK08162 259 --PKLIFDLIREHGVTHYCGAPivlSALinAPAEWRAGIDHPVHAMVAGAAPPAAViAKMEEIGFDLTHVYGLTEtyGPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 297 AVTASDPltGEGTPPIGR------------PITSVSTYILDDKLQPVP-EGD-VGELYMTGPGLARGYLRRPAATAERFL 362
Cdd:PRK08162 337 TVCAWQP--EWDALPLDEraqlkarqgvryPLQEGVTVLDPDTMQPVPaDGEtIGEIMFRGNIVMKGYLKNPKATEEAFA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 363 pnpfGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALL---AVdgVAQAVVTEHDNRL----IAY 435
Cdd:PRK08162 415 ----GG----WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYrhpAV--LVAAVVAKPDPKWgevpCAF 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 214003850 436 VVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPrLPTSPNGKIDRAAL 485
Cdd:PRK08162 485 VELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVL 533
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
31-487 |
1.32e-17 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 85.56 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLV-EHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAyvpvdpdyPADRRRHMLDDTAAHCLla 109
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PAFINYNLSGDPLIHCL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 110 mpgqDVAGAPVVMSVerkpgqsapnltdqdrlspllPNHPAYVIYTSGSTGQPKGVLVTHRgiPNLADDYVRRQ--NLVP 187
Cdd:cd05937 75 ----KLSGSRFVIVD---------------------PDDPAILIYTSGTTGLPKAAAISWR--RTLVTSNLLSHdlNLKN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 188 DSRL-----LAFASPSFDAAVAefwpIWLAGGCLVLA---AASDLIPGeplarlVRDQGITHV-----------TLPPSa 248
Cdd:cd05937 128 GDRTytcmpLYHGTAAFLGACN----CLMSGGTLALSrkfSASQFWKD------VRDSGATIIqyvgelcryllSTPPS- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 249 laPLEE--------GGGLPPGL--------TLLVAGE--ACPAPVAKSWARDRV-----MINAYGPT-----EATVAVTA 300
Cdd:cd05937 197 --PYDRdhkvrvawGNGLRPDIwerfrerfNVPEIGEfyAATEGVFALTNHNVGdfgagAIGHHGLIrrwkfENQVVLVK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 301 SDPLTGEgtpPIGRPITSVStyilddklQPVPEGDVGELYMTGP----GLARGYLRRPAATAERFLPNPFGgPGERMYRT 376
Cdd:cd05937 275 MDPETDD---PIRDPKTGFC--------VRAPVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRDVFR-KGDIYFRT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 377 GDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-----TEHDNRliayvVGTGGARVAAEDLLP 451
Cdd:cd05937 343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygvkvPGHDGR-----AGCAAITLEESSAVP 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 214003850 452 P----------LRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:cd05937 418 TeftksllaslARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
7-480 |
4.19e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 84.48 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVAMGATTL--SYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYV 84
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 85 PVDPDYpadrRRH---------------------------MLDDTAAHCLLAMPGQ-DVAGAP-----VVMSVERKPG-- 129
Cdd:PRK08315 97 TINPAY----RLSeleyalnqsgckaliaadgfkdsdyvaMLYELAPELATCEPGQlQSARLPelrrvIFLGDEKHPGml 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 130 ---------QSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLaFASPSFD 200
Cdd:PRK08315 173 nfdellalgRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLC-IPVPLYH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 201 ---------AAVAefwpiwlAGGCLVlaaasdlIPGE---PLARL--VRDQGITHV-TLPPSALAPLEEggglpPGL--- 262
Cdd:PRK08315 252 cfgmvlgnlACVT-------HGATMV-------YPGEgfdPLATLaaVEEERCTALyGVPTMFIAELDH-----PDFarf 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 263 ------TLLVAGEACPAPVAKswardRVM---------InAYGPTEATVAVTAS---DPL-----TgegtppIGRPITSV 319
Cdd:PRK08315 313 dlsslrTGIMAGSPCPIEVMK-----RVIdkmhmsevtI-AYGMTETSPVSTQTrtdDPLekrvtT------VGRALPHL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 320 STYILD-DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAE-----RFLpnpfggpgermyRTGDRVWAGSDGQLVFVGR 393
Cdd:PRK08315 381 EVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEaidadGWM------------HTGDLAVMDEEGYVNIVGR 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 394 VDDQLkVR-GHRIEPGEVESALLAVDGVAQA-VVTEHDNR----LIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVV 467
Cdd:PRK08315 449 IKDMI-IRgGENIYPREIEEFLYTHPKIQDVqVVGVPDEKygeeVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIR 527
|
570
....*....|...
gi 214003850 468 GLPRLPTSPNGKI 480
Cdd:PRK08315 528 FVDEFPMTVTGKI 540
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
31-463 |
1.80e-16 |
|
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: 82.02 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAyvpvdpdyPADRRRHMLDDTAAHCLlam 110
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--------AALINYNLRGESLAHCL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 111 pgqDVAGAPVVMsVERkpgqsapnltdqdrlspllpnhpAYVIYTSGSTGQPKGVLVTHR-----------GIPNLADD- 178
Cdd:cd05940 72 ---NVSSAKHLV-VDA-----------------------ALYIYTSGTTGLPKAAIISHRrawrggaffagSGGALPSDv 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 179 -------YVRRQNLV-PDSRLLAFAS----PSFDAAvaEFWPIWLAGGCLVLAAASDLI------PGEPLARLVRDQGIT 240
Cdd:cd05940 125 lytclplYHSTALIVgWSACLASGATlvirKKFSAS--NFWDDIRKYQATIFQYIGELCryllnqPPKPTERKHKVRMIF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 241 HVTLPPSALAPLEEGGGLPPGLTLLVAGEAcpapVAKSWARDRV-----MINAYGPTEATVAVTASDPLTGEgtpPIGRP 315
Cdd:cd05940 203 GNGLRPDIWEEFKERFGVPRIAEFYAATEG----NSGFINFFGKpgaigRNPSLLRKVAPLALVKYDLESGE---PIRDA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 316 itsvstyilDDKLQPVPEGDVGELYMTGPGLAR--GYLRrPAATAERFLPNPFGgPGERMYRTGDRVWAGSDGQLVFVGR 393
Cdd:cd05940 276 ---------EGRCIKVPRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVFK-KGDAWFNTGDLMRLDGEGFWYFVDR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 394 VDDQLKVRGHRIEPGEVESALLAVDGVAQAVVtehdnrliaYVV---GTGG-ARVAAEDLLPP-----------LRKRLP 458
Cdd:cd05940 345 LGDTFRWKGENVSTTEVAAVLGAFPGVEEANV---------YGVqvpGTDGrAGMAAIVLQPNeefdlsalaahLEKNLP 415
|
....*
gi 214003850 459 GYLVP 463
Cdd:cd05940 416 GYARP 420
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
20-480 |
2.87e-16 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 81.93 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPAVAMGATT-----LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPA-- 92
Cdd:cd05943 82 ADDPAAIYAAEDgerteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVpg 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 93 --DR-------------------RRHMLDDTAAHCLLAMPG---------------QDVAGAPVVMSVER--KPGQSAPn 134
Cdd:cd05943 162 vlDRfgqiepkvlfavdaytyngKRHDVREKVAELVKGLPSllavvvvpytvaagqPDLSKIAKALTLEDflATGAAGE- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 135 ltdqDRLSPLLPNHPAYVIYTSGSTGQPK-------GVLVTHRGIPNLADDyvrrqnLVPDSRLLAFASPSfdaavaefW 207
Cdd:cd05943 241 ----LEFEPLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILHCD------LRPGDRLFYYTTCG--------W 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 208 PIW------LAGGC-LVLAAASDLIP-GEPLARLVRDQGITHVTLPPSALAPLEEgGGLPPGL--------TLLVAGeac 271
Cdd:cd05943 303 MMWnwlvsgLAVGAtIVLYDGSPFYPdTNALWDLADEEGITVFGTSAKYLDALEK-AGLKPAEthdlsslrTILSTG--- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 272 pAPVAKS---WARD----RVMINAY-GPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQPVPeGDVGELYMTG 343
Cdd:cd05943 379 -SPLKPEsfdYVYDhikpDVLLASIsGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVW-GEKGELVCTK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 344 PGLAR--GYLRRP------AATAERFlpnpfggPGerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALL 415
Cdd:cd05943 457 PFPSMpvGFWNDPdgsryrAAYFAKY-------PG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVE 527
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 416 AVDGVAQAVVTEHDN-----RLIAYVVGTGGARvaaedLLPPLRKRLPGYL--------VPDVVVGLPRLPTSPNGKI 480
Cdd:cd05943 528 KIPEVEDSLVVGQEWkdgdeRVILFVKLREGVE-----LDDELRKRIRSTIrsalsprhVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
21-425 |
1.21e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 80.07 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 21 DRPAVAMGATTLSYAELNGEANL---LARRLVEHGvGPEKlVALAMPRSIEFVIAILAVHKAGAAYVPVDP-----DYPA 92
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAAraaALIALADPD-RPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLNTtrrgaALAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 93 DRRRH----MLDDTAAHCLLAmpGQDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVT 168
Cdd:PRK13388 94 DIRRAdcqlLVTDAEHRPLLD--GLDLPGVRVLDVDTPAYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 169 HRGIPNLADDYVRRQNLVPDSrLLAFASPSF--DAAVAEFWPIWLAGGCLVLAA---ASDLIPGeplarlVRDQGITHVT 243
Cdd:PRK13388 172 HGRLAFAGRALTERFGLTRDD-VCYVSMPLFhsNAVMAGWAPAVASGAAVALPAkfsASGFLDD------VRRYGATYFN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 244 LPPSALAPLEEGGGLPPG----LTLLVAGEACPAPVAKSWARDRV-MINAYGPTEATVAVTASDpltgeGTPP--IGRPI 316
Cdd:PRK13388 245 YVGKPLAYILATPERPDDadnpLRVAFGNEASPRDIAEFSRRFGCqVEDGYGSSEGAVIVVREP-----GTPPgsIGRGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 317 TSVSTYILDD-KLQPVPEGD-----------VGELYMT-GPGLARGYLRRPAATAERFlpnpfggpGERMYRTGDRVWAG 383
Cdd:PRK13388 320 PGVAIYNPETlTECAVARFDahgallnadeaIGELVNTaGAGFFEGYYNNPEATAERM--------RHGMYWSGDLAYRD 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 214003850 384 SDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV 425
Cdd:PRK13388 392 ADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAV 433
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
154-491 |
5.02e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.96 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 154 YTSGSTGQPKGVLVTHRG--IPNLADDYVRRqnlVPDSRLLAFASPSFDAAVAEF-WPIWLAGG---CLVLAAASDLIPG 227
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGayLMALSNALIWG---MNEGAVYLWTLPMFHCNGWCFtWTLAALCGtniCLRQVTAKAIYSA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 228 eplarlVRDQGITHVTLPPSAL-----APLEEG-GGLPPGLTLLVAGEACPAPVAKSWARD--RV-----MINAYGPTea 294
Cdd:PLN02479 279 ------IANYGVTHFCAAPVVLntivnAPKSETiLPLPRVVHVMTAGAAPPPSVLFAMSEKgfRVthtygLSETYGPS-- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 295 tvAVTASDPlTGEGTPPIGRP-------ITSVSTYILD----DKLQPVPE--GDVGELYMTGPGLARGYLRRPAATAERF 361
Cdd:PLN02479 351 --TVCAWKP-EWDSLPPEEQArlnarqgVRYIGLEGLDvvdtKTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 362 LpnpfGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQA-VVTEHDNRL----IAYV 436
Cdd:PLN02479 428 A----NG----WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAsVVARPDERWgespCAFV 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 437 VGTGGA-----RVAAEDLLPPLRKRLPGYLVPDVVVGLPrLPTSPNGKIDRAALPDPDRE 491
Cdd:PLN02479 500 TLKPGVdksdeAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAKE 558
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
501-575 |
5.69e-15 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 69.88 E-value: 5.69e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 501 APSTPTEIHLAGLFAEVLGV--SSVGVDDSFF-DIGGHSLLATRLVARIRQSLQVRLRVQAFFNAPTVAQLAKVLDGA 575
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
32-484 |
1.38e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 76.58 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAayVPVDPDYPA---------DRRRHMLDDT 102
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGL--VPVPLPLPMgfggresyiAQLRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 103 AAHCLLAMPG-QDVAGApvvmSVERKPGQSAPNLTDQDR-------LSPLLPNHPAYVIYTSGSTGQPKGVLVTHR-GIP 173
Cdd:PRK09192 128 QPAAIITPDElLPWVNE----ATHGNPLLHVLSHAWFKAlpeadvaLPRPTPDDIAYLQYSSGSTRFPRGVIITHRaLMA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 174 NLADDYVRRQNLVPDSRLLAfaspsfdaavaefwpiWLA-----G--GCLVLAAAS----DLIPGE-----PL------- 230
Cdd:PRK09192 204 NLRAISHDGLKVRPGDRCVS----------------WLPfyhdmGlvGFLLTPVATqlsvDYLPTRdfarrPLqwldlis 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 231 -----------------ARLVRDQGITHVTLPPSALApleeGGGlppgltllvaGEACPAPVAKSWA--------RDRVM 285
Cdd:PRK09192 268 rnrgtisysppfgyelcARRVNSKDLAELDLSCWRVA----GIG----------ADMIRPDVLHQFAeafapagfDDKAF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 286 INAYGPTEATVAVTASDPLTG-----------EGTP---PIGRPITSVSTY-------------ILDDKLQPVPEGDVGE 338
Cdd:PRK09192 334 MPSYGLAEATLAVSFSPLGSGivveevdrdrlEYQGkavAPGAETRRVRTFvncgkalpgheieIRNEAGMPLPERVVGH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 339 LYMTGPGLARGYLRRPAAT----AERFLpnpfggpgermyRTGDRVWAgSDGQLVFVGRVDDQLKVRGHRIEPGEVESAL 414
Cdd:PRK09192 414 ICVRGPSLMSGYFRDEESQdvlaADGWL------------DTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 415 LAVDG-----VAQAVVTEHDNRLIAYVVgtgGARVAAEDLLPPLRKRLPGYL-----VPDVVVGLP--RLPTSPNGKIDR 482
Cdd:PRK09192 481 EQEPElrsgdAAAFSIAQENGEKIVLLV---QCRISDEERRGQLIHALAALVrsefgVEAAVELVPphSLPRTSSGKLSR 557
|
..
gi 214003850 483 AA 484
Cdd:PRK09192 558 AK 559
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
13-485 |
1.54e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 76.61 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 13 EATAAAMPDRPAVaMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPA 92
Cdd:PRK06060 13 QASEAGWYDRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 93 DRRRHMLDDTAAHCLLAM-PGQDVAGAPVVMsverkpgQSAPNLTDQDRLSP-----LLPNHPAYVIYTSGSTGQPKGVL 166
Cdd:PRK06060 92 DDHALAARNTEPALVVTSdALRDRFQPSRVA-------EAAELMSEAARVAPggyepMGGDALAYATYTSGTTGPPKAAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 167 VTHRGIPNLADDYVRRQ-NLVPDSRLLAFASPSFDAAVA-EFWPIWLAGGCLVLAAASdlIPGEPLARLvrdqgitHVTL 244
Cdd:PRK06060 165 HRHADPLTFVDAMCRKAlRLTPEDTGLCSARMYFAYGLGnSVWFPLATGGSAVINSAP--VTPEAAAIL-------SARF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 245 PPSALApleeggGLPPGLTLLVagEACPApvaKSWARDRVMINAYGPTEATVAVTASD-----P-LTGEGTPPIGRPITS 318
Cdd:PRK06060 236 GPSVLY------GVPNFFARVI--DSCSP---DSFRSLRCVVSAGEALELGLAERLMEffggiPiLDGIGSTEVGQTFVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 319 VStyiLDD-------KLQP-------VPEGDV------GELYMTGPGLARGYLRRPaataERFLPNpfggpgERMYRTGD 378
Cdd:PRK06060 305 NR---VDEwrlgtlgRVLPpyeirvvAPDGTTagpgveGDLWVRGPAIAKGYWNRP----DSPVAN------EGWLDTRD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 379 RVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT-----EHDNRLIAYVVGTGGARV---AAEDLL 450
Cdd:PRK06060 372 RVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVavresTGASTLQAFLVATSGATIdgsVMRDLH 451
|
490 500 510
....*....|....*....|....*....|....*
gi 214003850 451 PPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK06060 452 RGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
125-487 |
2.45e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.83 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 125 ERKPGQSAPNLTDQDRLSPLLPNhpayviYTSGSTGQPKGVLVTHRG--IPNLADDYVRRQNLVPdsrLLAFASPSFDAA 202
Cdd:PLN03102 170 EPTPSLVARMFRIQDEHDPISLN------YTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCP---VYLWTLPMFHCN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 203 VAEF-WPIWLAGG---CLVLAAASDLIpgeplaRLVRDQGITHVTLPPSALAPLEEGGGL-----PPGLTLLVAGEACPA 273
Cdd:PLN03102 241 GWTFtWGTAARGGtsvCMRHVTAPEIY------KNIEMHNVTHMCCVPTVFNILLKGNSLdlsprSGPVHVLTGGSPPPA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 274 PVAKSWAR--DRVMiNAYGPTEATVAVTASDPLTGEGTPPIGRPI-----TSVSTYILDD-------KLQPVPEG--DVG 337
Cdd:PLN03102 315 ALVKKVQRlgFQVM-HAYGLTEATGPVLFCEWQDEWNRLPENQQMelkarQGVSILGLADvdvknkeTQESVPRDgkTMG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 338 ELYMTGPGLARGYLRRPAATAERFlpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAV 417
Cdd:PLN03102 394 EIVIKGSSIMKGYLKNPKATSEAF--------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKY 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 418 DGVAQAVVTEHDNRL-----IAYVVGTGGARVAAE----------DLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDR 482
Cdd:PLN03102 466 PKVLETAVVAMPHPTwgetpCAFVVLEKGETTKEDrvdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILK 545
|
....*
gi 214003850 483 AALPD 487
Cdd:PLN03102 546 PKLRD 550
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
370-486 |
4.30e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 74.30 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 370 GERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-TEHDN----RLIAYVVGTGGarV 444
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVyRGKDPvageRVKAKVISHEE--I 366
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 214003850 445 AAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALP 486
Cdd:PRK08308 367 DPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
150-485 |
4.33e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 74.05 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 150 AYVIYTSGSTGQPKGVLVTHRGIpnLADDYVRRQNLVPDSR-LLAFASPSF--DAAVAEFWPIWLAGGCLVLAAASDLI- 225
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNE--VYNAWMLALNSLFDPDdVLLCGLPLFhvNGSVVTLLTPLASGAHVVLAGPAGYRn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 226 PG--EPLARLVRDQGITHVTLPPSALAPL-EEGGGLPPGLTLLVAGEACPAPVA-KSWARDRV---MINAYGPTEATVAV 298
Cdd:cd05944 83 PGlfDNFWKLVERYRITSLSTVPTVYAALlQVPVNADISSLRFAMSGAAPLPVElRARFEDATglpVVEGYGLTEATCLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 299 TASDPLTGEGTPPIGRPI--TSVSTYILD---DKLQPVPEGDVGELYMTGPGLARGYLRRPAATaerflpNPFGGPGerM 373
Cdd:cd05944 163 AVNPPDGPKRPGSVGLRLpyARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNK------NAFVADG--W 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 374 YRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVA-QAVVTEHDNRL----IAYVVGTGGARVAAED 448
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAfAGAVGQPDAHAgelpVAYVQLKPGAVVEEEE 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 214003850 449 LLPPLRKRLPGY-LVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd05944 315 LLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
150-485 |
9.19e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 72.77 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 150 AYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRR-------------------QNLVpdSRLLAFASPSFDAAVAEFWPIW 210
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRlggpgqwllalpahhiaglQVLV--RSVIAGSEPVELDVSAGFDPTA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 211 LAggclvlAAASDLIPGEPLARLVRDQGITHVTLPPS--ALAPLEeggglppglTLLVAGEACPAPVAKSWARDRVMI-N 287
Cdd:PRK07824 116 LP------RAVAELGGGRRYTSLVPMQLAKALDDPAAtaALAELD---------AVLVGGGPAPAPVLDAAAAAGINVvR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 288 AYGPTEatvavtasdplTGEGTPPIGRPITSVSTYILDdklqpvpegdvGELYMTGPGLARGYLRRPAataerflPNPFG 367
Cdd:PRK07824 181 TYGMSE-----------TSGGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 368 GPGerMYRTGDrVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNRL----IAYVVGTGGA 442
Cdd:PRK07824 232 EPG--WFRTDD-LGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADcAVFGLPDDRLgqrvVAAVVGDGGP 308
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 214003850 443 RVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK07824 309 APTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
510-567 |
2.09e-13 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 64.89 E-value: 2.09e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 510 LAGLFAEVLGVS--SVGVDDSFFDIGGHSLLATRLVARIRQSLQVRLRVQAFFNAPTVAQ 567
Cdd:pfam00550 3 LRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
16-485 |
2.38e-13 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 72.71 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGAT--TLSYAELNgeanLLARR----LVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPD 89
Cdd:PLN02246 33 LSEFSDRPCLIDGATgrVYTYADVE----LLSRRvaagLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 90 Y-PADRRRHM------LDDTAAHCLLAMPGQDVAGAPVVMSVERKPG---------QSAPNLTDQDRLSPllpNHPAYVI 153
Cdd:PLN02246 109 YtPAEIAKQAkasgakLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEgclhfseltQADENELPEVEISP---DDVVALP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 154 YTSGSTGQPKGVLVTHRGI------------PNLaddyvrrqNLVPDSRLLAFAsPSFDaaVAEFWPIWLAGgcLVLAAA 221
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHKGLvtsvaqqvdgenPNL--------YFHSDDVILCVL-PMFH--IYSLNSVLLCG--LRVGAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 222 SDLIPGEPLAR---LVRDQGITHVTL-PPSALA----PLEEGGGLPpGLTLLVAGeacPAPVAKSWA---RDR----VMI 286
Cdd:PLN02246 253 ILIMPKFEIGAlleLIQRHKVTIAPFvPPIVLAiaksPVVEKYDLS-SIRMVLSG---AAPLGKELEdafRAKlpnaVLG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 287 NAYGPTEATVAVTASDPLTGEGTP----PIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPGLARGYLRRPAATA--- 358
Cdd:PLN02246 329 QGYGMTEAGPVLAMCLAFAKEPFPvksgSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATAnti 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 359 --ERFLpnpfggpgermyRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHDNRL--- 432
Cdd:PLN02246 409 dkDGWL------------HTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADaAVVPMKDEVAgev 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 214003850 433 -IAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PLN02246 477 pVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
28-492 |
4.70e-13 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 71.74 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 28 GATTLSYAELNGEANLLARRLV-EHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHC 106
Cdd:PRK05620 35 EQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 107 LLAMP------GQDVAGAPVVMSV--------ERKPGQSAPNLTDQDRLS-----------PLLPNH-PAYVIYTSGSTG 160
Cdd:PRK05620 115 IVADPrlaeqlGEILKECPCVRAVvfigpsdaDSAAAHMPEGIKVYSYEAlldgrstvydwPELDETtAAAICYSTGTTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 161 QPKGVLVTHRGIpnladdYVRRQNLVPDSRLLAFASPSFDAAVAEF----W--PI--WLAGGCLVLAAASdlIPGEPLAR 232
Cdd:PRK05620 195 APKGVVYSHRSL------YLQSLSLRTTDSLAVTHGESFLCCVPIYhvlsWgvPLaaFMSGTPLVFPGPD--LSAPTLAK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 233 LVRD--------------QGITHVTLPPSALAPLEEggglppgltLLVAGEACPAPVAKSW-ARDRV-MINAYGPTEATV 296
Cdd:PRK05620 267 IIATamprvahgvptlwiQLMVHYLKNPPERMSLQE---------IYVGGSAVPPILIKAWeERYGVdVVHVWGMTETSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 297 AVTASDPLTG------------EGTPPIGRPITSVStyilDDKLQPVPEGDVGELYMTGPGLARGYLRRPAAT----AER 360
Cdd:PRK05620 338 VGTVARPPSGvsgearwayrvsQGRFPASLEYRIVN----DGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaAST 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 361 FLPNPFGGPGERM-----YRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDN----- 430
Cdd:PRK05620 414 FRGEDVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDdkwge 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 214003850 431 RLIAYVV---GTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRA--------------ALPDPDREG 492
Cdd:PRK05620 494 RPLAVTVlapGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKdlrqhladgdfeiiKLKGPGESG 572
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
31-485 |
4.91e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 71.85 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLL-- 108
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVItc 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 109 --------AMPGQDVAGAPVVMSV--------------------ERKPGQSAPNLTDQDrlspLLPNHPA---------- 150
Cdd:PLN02654 200 navkrgpkTINLKDIVDAALDESAkngvsvgicltyenqlamkrEDTKWQEGRDVWWQD----VVPNYPTkcevewvdae 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 151 ---YVIYTSGSTGQPKGVLVTHRGIpnladdyvrrqnLVPDSRLLAFAspsFDAAVAE-FWPI----WLAGGCLV----- 217
Cdd:PLN02654 276 dplFLLYTSGSTGKPKGVLHTTGGY------------MVYTATTFKYA---FDYKPTDvYWCTadcgWITGHSYVtygpm 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 218 LAAASDLI----PGEPLA----RLVRDQGITHVTLPPSALAPLEEGGGLP----PGLTLLVAGEACPAPVAKSWardRVM 285
Cdd:PLN02654 341 LNGATVLVfegaPNYPDSgrcwDIVDKYKVTIFYTAPTLVRSLMRDGDEYvtrhSRKSLRVLGSVGEPINPSAW---RWF 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 286 INAYGPTEATVAVTASDPLTGEG--TPPIGR----------PITSVSTYILDDKLQPVpEGDV-GELYMTG--PGLARGy 350
Cdd:PLN02654 418 FNVVGDSRCPISDTWWQTETGGFmiTPLPGAwpqkpgsatfPFFGVQPVIVDEKGKEI-EGECsGYLCVKKswPGAFRT- 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 351 LRRPAATAERFLPNPFGGpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT--EH 428
Cdd:PLN02654 496 LYGDHERYETTYFKPFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVgiEH 571
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 214003850 429 DNR---LIAYVVGTGGARVAAE---DLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PLN02654 572 EVKgqgIYAFVTLVEGVPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
28-484 |
5.46e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 71.57 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 28 GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAhcL 107
Cdd:PRK07768 26 APVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLR--V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 108 LAMPGQD--VAGAPVVMSVE--RKPGQSAPNLTDQDRLSPLLP-----NHPAYVIYTSGSTGQPKGVLVTHRGIPNLADD 178
Cdd:PRK07768 104 IGMIGAKavVVGEPFLAAAPvlEEKGIRVLTVADLLAADPIDPvetgeDDLALMQLTSGSTGSPKAVQITHGNLYANAEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 179 YVRRQNLVPDSRLLAFASPSF-DAAVAEFWPIWLAGGC-LVLAAASDLIpGEPL--ARLVRDQGIThVTLPP----SALA 250
Cdd:PRK07768 184 MFVAAEFDVETDVMVSWLPLFhDMGMVGFLTVPMYFGAeLVKVTPMDFL-RDPLlwAELISKYRGT-MTAAPnfayALLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 251 PLEEGGGLPPGLTL------LVAGEAC-PAPV-------AKSWARDRVMINAYGPTEATVAVTASDPLTG---------- 306
Cdd:PRK07768 262 RRLRRQAKPGAFDLsslrfaLNGAEPIdPADVedlldagARFGLRPEAILPAYGMAEATLAVSFSPCGAGlvvdevdadl 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 307 -----EGTPP----------IGRPITSVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLrrpaaTAERFLP--NPFGgp 369
Cdd:PRK07768 342 laalrRAVPAtkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL-----TMDGFIPaqDADG-- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 370 gerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGV----AQAVVTEHDNRL--IAYVVGTGGAR 443
Cdd:PRK07768 415 ---WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrpgnAVAVRLDAGHSRegFAVAVESNAFE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 214003850 444 VAAEdlLPPLRKRLPGYLV------PDVVVGLP--RLPTSPNGKIDRAA 484
Cdd:PRK07768 492 DPAE--VRRIRHQVAHEVVaevgvrPRNVVVLGpgSIPKTPSGKLRRAN 538
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
7-481 |
7.05e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 71.88 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPAVA-MGATTLSYAELNGEANLLARRLvEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAayVP 85
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALARLL-KRELKDEENVGILLPPSVAGALANLALLLAGK--VP 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 86 VDPDYPADrrrhmlDDTAAHCLLAMPGQDV----------AGAPVVMSVERKPG-----QSAPNLTDQDRLSPLL----- 145
Cdd:PRK08633 693 VNLNYTAS------EAALKSAIEQAQIKTVitsrkfleklKNKGFDLELPENVKviyleDLKAKISKVDKLTALLaarll 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 146 --------------PNHPAYVIYTSGSTGQPKGVLVTHRGI-PNL--ADDYVRRQNlvpDSRLLAfASP---SFDAAVAE 205
Cdd:PRK08633 767 parllkrlygptfkPDDTATIIFSSGSEGEPKGVMLSHHNIlSNIeqISDVFNLRN---DDVILS-SLPffhSFGLTVTL 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 206 FWPiwLAGGCLVLAAASDLiPGEPLARLVRDQGITHVTLPPSALAPLEEGGGLPP----GLTLLVAG-EACPAPVAKSWa 280
Cdd:PRK08633 843 WLP--LLEGIKVVYHPDPT-DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPlmfaSLRLVVAGaEKLKPEVADAF- 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 281 RDRVMIN---AYGPTEATVAVTASDP---------LTG--EGTppIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPG 345
Cdd:PRK08633 919 EEKFGIRileGYGATETSPVASVNLPdvlaadfkrQTGskEGS--VGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQ 996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 346 LARGYLRRPAATAE--RFLpnpfggPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAV--DGVA 421
Cdd:PRK08633 997 VMKGYLGDPEKTAEviKDI------DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEV 1070
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214003850 422 QAVVTEHDN-----RLIayVVGTGGA-------RVAAEDLLPPLRKrlPGYLVpdVVVGLPRLPTspnGKID 481
Cdd:PRK08633 1071 VFAVTAVPDekkgeKLV--VLHTCGAedveelkRAIKESGLPNLWK--PSRYF--KVEALPLLGS---GKLD 1133
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
59-487 |
8.29e-13 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 70.96 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 59 VALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLAmpgqDVAGAPVVMSVERKpgqsAPNLTDQ 138
Cdd:cd05928 70 VAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT----SDELAPEVDSVASE----CPSLKTK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 139 DRLSP-----------LL----PNH---------PAYVIYTSGSTGQPKGVLVTHR--GIPnladdyvrrqnLVPDSRLL 192
Cdd:cd05928 142 LLVSEksrdgwlnfkeLLneasTEHhcvetgsqePMAIYFTSGTTGSPKMAEHSHSslGLG-----------LKVNGRYW 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 193 AFASPS-----------FDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRdQGITHVTLPPSALAPLeegggLPPG 261
Cdd:cd05928 211 LDLTASdimwntsdtgwIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSS-YPITTFCGAPTVYRML-----VQQD 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 262 LT---------LLVAGEACPAPVAKSW-ARDRVMI-NAYGPTEaTVAVTASdpLTGEGTPP--IGRPITSVSTYILDDK- 327
Cdd:cd05928 285 LSsykfpslqhCVTGGEPLNPEVLEKWkAQTGLDIyEGYGQTE-TGLICAN--FKGMKIKPgsMGKASPPYDVQIIDDNg 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 328 --LQPVPEGDVG-ELYMTGP-GLARGYLRRPAATAERFLPNpfggpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGH 403
Cdd:cd05928 362 nvLPPGTEGDIGiRVKPIRPfGLFSGYVDNPEKTAATIRGD--------FYLTGDRGIMDEDGYFWFMGRADDVINSSGY 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 404 RIEPGEVESALLAVDGVAQ-AVVTEHD----NRLIAYVVGTGGARV-AAEDLLPPLRKRLPG----YLVPDVVVGLPRLP 473
Cdd:cd05928 434 RIGPFEVESALIEHPAVVEsAVVSSPDpirgEVVKAFVVLAPQFLShDPEQLTKELQQHVKSvtapYKYPRKVEFVQELP 513
|
490
....*....|....
gi 214003850 474 TSPNGKIDRAALPD 487
Cdd:cd05928 514 KTVTGKIQRNELRD 527
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
9-448 |
8.95e-13 |
|
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: 70.95 E-value: 8.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALFEATAAAMPDRPAVAMGAT--------------------TLSYAELNGEANLLARRL-VEHGVGPEKLVALAMPRSI 67
Cdd:cd17632 25 AQIIATVMTGYADRPALGQRATelvtdpatgrttlrllprfeTITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 68 EFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDT--------AAHCLLAMPGQDVAGAPVVMSV--------------- 124
Cdd:cd17632 105 DYATVDLALTRLGAVSVPLQAGASAAQLAPILAETeprllavsAEHLDLAVEAVLEGGTPPRLVVfdhrpevdahraale 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 125 ---ERKPGQSAPNLT-----DQDRLSPLLP--------NHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVP- 187
Cdd:cd17632 185 sarERLAAVGIPVTTltliaVRGRDLPPAPlfrpepddDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPp 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 188 DSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASD-----------------LIP----------GEPLARLVRdQGIT 240
Cdd:cd17632 265 ASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDmstlfddlalvrptelfLVPrvcdmlfqryQAELDRRSV-AGAD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 241 HVTLPPSALAPLEE---GGglppGLTLLVAGEACPAPVAKSWAR---DRVMINAYGPTEATVAVtasdpLTGEgtppIGR 314
Cdd:cd17632 344 AETLAERVKAELRErvlGG----RLLAAVCGSAPLSAEMKAFMEsllDLDLHDGYGSTEAGAVI-----LDGV----IVR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 315 PItsvstyILDDKLQPVPEGDV---------GELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAGSD 385
Cdd:cd17632 411 PP------VLDYKLVDVPELGYfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDVMAELGP 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 386 GQLVFVGRVDDQLKV-RGHRIEPGEVESALLAVDGVAQAVVTEHDNR--LIAYVVGTGGARVAAED 448
Cdd:cd17632 478 DRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGNSERayLLAVVVPTQDALAGEDT 543
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
9-485 |
1.28e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALFEATAAAMPDRP-AVAM----GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAY 83
Cdd:PRK05857 14 STVLDRVFEQARQQPeAIALrrcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 84 VPVDPDYPA---DRRRHMLDDTAahcLLAMPGQDVAGAPVVMSVERKP----------GQSAPNLtDQDRLSPLL---PN 147
Cdd:PRK05857 94 VMADGNLPIaaiERFCQITDPAA---ALVAPGSKMASSAVPEALHSIPviavdiaavtRESEHSL-DAASLAGNAdqgSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 148 HPAYVIYTSGSTGQPKGVLVTHR---GIPnladDYVRRQNLvpdsRLLAFA------SPSFDAAVAEFWpiWLAGGclVL 218
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKAVLLANRtffAVP----DILQKEGL----NWVTWVvgettySPLPATHIGGLW--WILTC--LM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 219 AAASDLIPGE---PLARLVRDQGITHVTLPPSALA----PLEEGGGLPPGLTLLVAG--EACPAPVAKSWARDRVMINAY 289
Cdd:PRK05857 238 HGGLCVTGGEnttSLLEILTTNAVATTCLVPTLLSklvsELKSANATVPSLRLVGYGgsRAIAADVRFIEATGVRTAQVY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 290 GPTE----ATVAVTASDPLTGEGTPPIGRPITSVSTYILDDK------LQPVPEGDVGELYMTGPGLARGYLRRPAATAE 359
Cdd:PRK05857 318 GLSEtgctALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 360 RFLpnpfggpgERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNRLIAYVVGT 439
Cdd:PRK05857 398 VLI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGL 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 440 ggARVAAEDL----LPPLRKRLPGYL--------VPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK05857 470 --AVVASAELdesaARALKHTIAARFrresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
16-170 |
2.23e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 69.91 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAM-----GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDY 90
Cdd:PRK08180 49 AQEAPDRVFLAErgadgGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 91 ---PAD--RRRHMLD---------DTAAHCLLAMPGQDVAGAPVVMSVERKPGQSAPNLTD----------QDRLSPLLP 146
Cdd:PRK08180 129 slvSQDfgKLRHVLElltpglvfaDDGAAFARALAAVVPADVEVVAVRGAVPGRAATPFAAllatpptaavDAAHAAVGP 208
|
170 180
....*....|....*....|....
gi 214003850 147 NHPAYVIYTSGSTGQPKGVLVTHR 170
Cdd:PRK08180 209 DTIAKFLFTSGSTGLPKAVINTHR 232
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
31-437 |
7.68e-12 |
|
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: 67.63 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLam 110
Cdd:cd17639 5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 111 pgqdvagapvvmsverkpgqsapnlTDQDrlspllPNHPAYVIYTSGSTGQPKGVLVTHR----GIPNLADDYVrrQNLV 186
Cdd:cd17639 83 -------------------------TDGK------PDDLACIMYTSGSTGNPKGVMLTHGnlvaGIAGLGDRVP--ELLG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 187 PDSRLLA------------------------FASPS--FDAAVA-------EFWPIWLAGGCLVL-----AAASDLIPGE 228
Cdd:cd17639 130 PDDRYLAylplahifelaaenvclyrggtigYGSPRtlTDKSKRgckgdltEFKPTLMVGVPAIWdtirkGVLAKLNPMG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 229 PLARLVRDQGIThvtlppSALAPLEEGGGLP----------PGLT------LLVAGeacpAPVAKSWAR-----DRVMIN 287
Cdd:cd17639 210 GLKRTLFWTAYQ------SKLKALKEGPGTPlldelvfkkvRAALggrlryMLSGG----APLSADTQEflnivLCPVIQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 288 AYGPTEaTVAVTAS----DPLTGEgtppIGRPITSVstyilDDKLQPVPEGDV--------GELYMTGPGLARGYLRRPA 355
Cdd:cd17639 280 GYGLTE-TCAGGTVqdpgDLETGR----VGPPLPCC-----EIKLVDWEEGGYstdkppprGEILIRGPNVFKGYYKNPE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 356 ATAERFLpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVR-GHRIEPGEVESALL---AVDGVAqAVVTEHDNR 431
Cdd:cd17639 350 KTKEAFD-------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRsnpLVNNIC-VYADPDKSY 421
|
....*.
gi 214003850 432 LIAYVV 437
Cdd:cd17639 422 PVAIVV 427
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
145-499 |
1.18e-11 |
|
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: 67.13 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 145 LPNHPAYVIYTSGSTGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWpiwLAggCLVLAAASDL 224
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFH---LA--PLIAGMNQYL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 225 IPGEPLARL-------VRDQGITHVTLPPSA----LAPLEEGGGLPPGLTLL---------VAGEACPA---PVAKSWAR 281
Cdd:cd05908 179 MPTRLFIRRpilwlkkASEHKATIVSSPNFGykyfLKTLKPEKANDWDLSSIrmilngaepIDYELCHEfldHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 282 DRVMINAYGPTEATVAVTASD---PLT-----------GEGTPPI-------------GRPITSVSTYILDDKLQPVPEG 334
Cdd:cd05908 259 RNAILPVYGLAEASVGASLPKaqsPFKtitlgrrhvthGEPEPEVdkkdsecltfvevGKPIDETDIRICDEDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 335 DVGELYMTGPGLARGYLRRPAATAERFLPNPFggpgermYRTGDRVWAgSDGQLVFVGRVDDQLKVRGHRIEPGEVESAL 414
Cdd:cd05908 339 YIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 415 LAVDGVAQ---AVVTEHD-----NRLIAYVVgtggARVAAEDLLpPLRKRLPGYLVP------DVVVGLPRLPTSPNGKI 480
Cdd:cd05908 411 EELEGVELgrvVACGVNNsntrnEEIFCFIE----HRKSEDDFY-PLGKKIKKHLNKrggwqiNEVLPIRRIPKTTSGKV 485
|
410
....*....|....*....
gi 214003850 481 DRAALpdpdregAERVTSG 499
Cdd:cd05908 486 KRYEL-------AQRYQSG 497
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
17-485 |
1.60e-11 |
|
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: 66.78 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 17 AAMPDRPAV--AMGATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADR 94
Cdd:cd17642 28 ASVPGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 95 RRHMLDDTAAHCLLAMPG--QDVAGA----PVV---------------MSVERKPGQSAPNLTDQDRLSPLLPNHP---A 150
Cdd:cd17642 108 LDHSLNISKPTIVFCSKKglQKVLNVqkklKIIktiiildskedykgyQCLYTFITQNLPPGFNEYDFKPPSFDRDeqvA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 151 YVIYTSGSTGQPKGVLVTHRGIpnladdyVRRQNLVPDSRLLAFASPsfDAAVAEFWPIWLAGGCLVLAAAsdLIPG--- 227
Cdd:cd17642 188 LIMNSSGSTGLPKGVQLTHKNI-------VARFSHARDPIFGNQIIP--DTAILTVIPFHHGFGMFTTLGY--LICGfrv 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 228 --------EPLARLVRDQGITHVTLPPSALA-----PLEEGGGLPPGLTLLVAGeacpAPVAKS---WARDRVMIN---- 287
Cdd:cd17642 257 vlmykfeeELFLRSLQDYKVQSALLVPTLFAffaksTLVDKYDLSNLHEIASGG----APLSKEvgeAVAKRFKLPgirq 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 288 AYGPTEATVAVTASdPLTGEGTPPIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAErfLPNPF 366
Cdd:cd17642 333 GYGLTETTSAILIT-PEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKA--LIDKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 367 GgpgerMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT----EHDNRL-IAYVVGTGG 441
Cdd:cd17642 410 G-----WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAgipdEDAGELpAAVVVLEAG 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 214003850 442 ARVAAEDLLPPLR------KRLPGYlvpdvVVGLPRLPTSPNGKIDRAAL 485
Cdd:cd17642 485 KTMTEKEVMDYVAsqvstaKRLRGG-----VKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
30-482 |
3.21e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 65.93 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 30 TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV----DPDYPADR----------- 94
Cdd:PRK00174 97 RKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADRiidagaklvit 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 95 --------RRHML----DDTAAHCL--------------LAM-PGQD------VAGA-----PVVMSVErkpgqsapnlt 136
Cdd:PRK00174 177 adegvrggKPIPLkanvDEALANCPsvekvivvrrtggdVDWvEGRDlwwhelVAGAsdecePEPMDAE----------- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 137 dqdrlspllpnHPAYVIYTSGSTGQPKGVL-----------VTHRGIPNLADDYVrrqnlvpdsrllafaspsfdaavae 205
Cdd:PRK00174 246 -----------DPLFILYTSGSTGKPKGVLhttggylvyaaMTMKYVFDYKDGDV------------------------- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 206 FWPI----WLAG------GCLVLAAASDLIPGEP-------LARLVRDQGITHVTLPPSAL-APLEEGGGLPPG-----L 262
Cdd:PRK00174 290 YWCTadvgWVTGhsyivyGPLANGATTLMFEGVPnypdpgrFWEVIDKHKVTIFYTAPTAIrALMKEGDEHPKKydlssL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 263 TLL------------------VAGEACPapVAKSWARdrvminaygpTEaTVAVTASdPLTGeGTP--P--IGRPITSVS 320
Cdd:PRK00174 370 RLLgsvgepinpeawewyykvVGGERCP--IVDTWWQ----------TE-TGGIMIT-PLPG-ATPlkPgsATRPLPGIQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 321 TYILDDKLQPVPEGDVGELYMTG--PGLARGYLRRPaataERFLPNPFGG-PGerMYRTGDRVWAGSDGQLVFVGRVDDQ 397
Cdd:PRK00174 435 PAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDH----ERFVKTYFSTfKG--MYFTGDGARRDEDGYYWITGRVDDV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 398 LKVRGHRIEPGEVESALLAVDGVAQAVV--TEHD---NRLIAYVVGTGGARVAAEdllppLRKRLPGYLV--------PD 464
Cdd:PRK00174 509 LNVSGHRLGTAEIESALVAHPKVAEAAVvgRPDDikgQGIYAFVTLKGGEEPSDE-----LRKELRNWVRkeigpiakPD 583
|
570
....*....|....*...
gi 214003850 465 VVVGLPRLPTSPNGKIDR 482
Cdd:PRK00174 584 VIQFAPGLPKTRSGKIMR 601
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
146-482 |
5.85e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 65.21 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 146 PNHPAYVIYTSGSTGQPKGVLVTHRG--IPNLA----------DDYVRRQNLV-------PDSRLLAFAS----PSFDAA 202
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSAliVQSLAkiaivgygedDVYLHTAPLChigglssALAMLMVGAChvllPKFDAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 203 VAeFWPIWLAG-GCL--VLAAASDLIpgeplaRLVRDQGITHVTlpPSALAPLEEGGGLPpglTLLVAGEACPAPVAKsw 279
Cdd:PLN02860 251 AA-LQAIKQHNvTSMitVPAMMADLI------SLTRKSMTWKVF--PSVRKILNGGGSLS---SRLLPDAKKLFPNAK-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 280 ardrvMINAYGPTEATVAVT------------------ASDPLTGEGTPP----IGRPITSVSTYILDDKLQPVpegdvG 337
Cdd:PLN02860 317 -----LFSAYGMTEACSSLTfmtlhdptlespkqtlqtVNQTKSSSVHQPqgvcVGKPAPHVELKIGLDESSRV-----G 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 338 ELYMTGPGLARGYLRRPAATAERfLPNpfggpgERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAV 417
Cdd:PLN02860 387 RILTRGPHVMLGYWGQNSETASV-LSN------DGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQH 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 418 DGVAQAVVTE-HDNRLIAYVVG------------------TGGARVAAEDLLPPLR-KRLPGYLVPD-VVVGLPRLPTSP 476
Cdd:PLN02860 460 PGVASVVVVGvPDSRLTEMVVAcvrlrdgwiwsdnekenaKKNLTLSSETLRHHCReKNLSRFKIPKlFVQWRKPFPLTT 539
|
....*.
gi 214003850 477 NGKIDR 482
Cdd:PLN02860 540 TGKIRR 545
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4-487 |
1.37e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 63.84 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 4 EASTAPALFEATAAAMPDRPAVAMGAT--TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGA 81
Cdd:PLN02330 26 DKLTLPDFVLQDAELYADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 82 AYVPVDPD----------YPADRRRHMLDDTAAHCLLAMpgqdvaGAPVVMSVERKpGQSAPNLTD----QDRLSPLLPN 147
Cdd:PLN02330 106 VFSGANPTaleseikkqaEAAGAKLIVTNDTNYGKVKGL------GLPVIVLGEEK-IEGAVNWKElleaADRAGDTSDN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 148 HPAY------VIYTSGSTGQPKGVLVTHRgipnladdyvrrqNLVPD--SRLLAFASPSFDAAVA----EFWPIW-LAGG 214
Cdd:PLN02330 179 EEILqtdlcaLPFSSGTTGISKGVMLTHR-------------NLVANlcSSLFSVGPEMIGQVVTlgliPFFHIYgITGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 215 C---------LVLAAASDLipgeplaRLVRDQGITH-VT----LPPSALA----PLEEGGGLPPGLTLLVAGEACP-AP- 274
Cdd:PLN02330 246 CcatlrnkgkVVVMSRFEL-------RTFLNALITQeVSfapiVPPIILNlvknPIVEEFDLSKLKLQAIMTAAAPlAPe 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 275 ----VAKSWARDRVMiNAYGPTE-ATVAVTASDPLTGEGTP---PIGRPITSVSTYILD-DKLQPVPEGDVGELYMTGPG 345
Cdd:PLN02330 319 lltaFEAKFPGVQVQ-EAYGLTEhSCITLTHGDPEKGHGIAkknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQC 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 346 LARGYLRRPAATAERFlpnpfggPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV 425
Cdd:PLN02330 398 VMQGYYNNKEETDRTI-------DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214003850 426 T-----EHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PLN02330 471 VplpdeEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
147-485 |
1.58e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 63.57 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 147 NHPAYVIYTSGSTGQPKGVLVTHRgipnladdyvrrqnlvpDSRLLAFASPSFDA----AVAEFWPI--------W---- 210
Cdd:PRK07008 176 NQASSLCYTSGTTGNPKGALYSHR-----------------STVLHAYGAALPDAmglsARDAVLPVvpmfhvnaWglpy 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 211 ---LAGGCLVLAAASdlIPGEPLARLVRDQGITHVTLPPSALAPL-----EEGGGLPPGLTLLVAGEACPAPVAKSWARD 282
Cdd:PRK07008 239 sapLTGAKLVLPGPD--LDGKSLYELIEAERVTFSAGVPTVWLGLlnhmrEAGLRFSTLRRTVIGGSACPPAMIRTFEDE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 283 R--VMINAYGPTEATVAVTASDPLTGEGTPPI----------GRPITSVSTYILDDKLQPVPEGDV--GELYMTGPGLAR 348
Cdd:PRK07008 317 YgvEVIHAWGMTEMSPLGTLCKLKWKHSQLPLdeqrkllekqGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVID 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 349 GYLRRPAATAERflpnpfggpgeRMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQA--VVT 426
Cdd:PRK07008 397 RYFRGDASPLVD-----------GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAacIAC 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 214003850 427 EH---DNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK07008 466 AHpkwDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
147-487 |
3.46e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.46 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 147 NHPAYVIYTSGSTGQPKGVLVTHRG------IPNLADDYVRRQN-----LVP----DSRLLAFASPSfdaavaefwpiwl 211
Cdd:PRK06018 177 NTAAGMCYTSGTTGDPKGVLYSHRSnvlhalMANNGDALGTSAAdtmlpVVPlfhaNSWGIAFSAPS------------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 212 AGGCLVLAAASdlIPGEPLARLVRDQGITHVTLPPSALAPL-----EEGGGLPPGLTLLVAGEACPAPVAKSWARDRV-M 285
Cdd:PRK06018 244 MGTKLVMPGAK--LDGASVYELLDTEKVTFTAGVPTVWLMLlqymeKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVeV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 286 INAYGPTEATVAVTAS------DPLTGEGTPPI----GRPITSVSTYILDDKLQPVP-EGDV-GELYMTGPGLARGYLRr 353
Cdd:PRK06018 322 RHAWGMTEMSPLGTLAalkppfSKLPGDARLDVlqkqGYPPFGVEMKITDDAGKELPwDGKTfGRLKVRGPAVAAAYYR- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 354 paATAERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVT-----EH 428
Cdd:PRK06018 401 --VDGEILDDDGF-------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIgvyhpKW 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 214003850 429 DNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PRK06018 472 DERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
9-170 |
6.09e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 61.99 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 9 PALFEATAAAMPDRPAVAM------GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAA 82
Cdd:PRK12582 52 PHLLAKWAAEAPDRPWLAQrepghgQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 83 YVPVDPDY----------------------------PADRRRHMLDDTAAHCLL---------AMPGQDVAGAPVVMSVE 125
Cdd:PRK12582 132 AAPVSPAYslmshdhaklkhlfdlvkprvvfaqsgaPFARALAALDLLDVTVVHvtgpgegiaSIAFADLAATPPTAAVA 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 214003850 126 rkpgQSAPNLTdqdrlspllPNHPAYVIYTSGSTGQPKGVLVTHR 170
Cdd:PRK12582 212 ----AAIAAIT---------PDTVAKYLFTSGSTGMPKAVINTQR 243
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
13-429 |
1.87e-09 |
|
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: 60.14 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 13 EATAAAMPDRPAVAM-----GATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVD 87
Cdd:cd05921 2 AHWARQAPDRTWLAEregngGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 88 PDYPA-----DRRRHMLD---------DTAAHCLLAMPGQDVAGAPVVMSVERKPGQSA---------PNLTDQDRLSPL 144
Cdd:cd05921 82 PAYSLmsqdlAKLKHLFEllkpglvfaQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAisfaelaatPPTAAVDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 145 L-PNHPAYVIYTSGSTGQPKGVLVTHRGI----PNLADDYVRRQNLVPDSRLLAFASPSFdAAVAEFWPIWLAGGCLVLA 219
Cdd:cd05921 162 VgPDTVAKFLFTSGSTGLPKAVINTQRMLcanqAMLEQTYPFFGEEPPVLVDWLPWNHTF-GGNHNFNLVLYNGGTLYID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 220 AASDLiPG---EPLARLVRDQGITHVTLPP--SALAPLEE-------------------GGGLPPGLTllvagEACPAPV 275
Cdd:cd05921 241 DGKPM-PGgfeETLRNLREISPTVYFNVPAgwEMLVAALEkdealrrrffkrlklmfyaGAGLSQDVW-----DRLQALA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 276 AKSWARDRVMINAYGPTEATVAVTAS-DPLTGEGTppIGRPITSVstyilddKLQPVPEGDVGELYMTGPGLARGYLRRP 354
Cdd:cd05921 315 VATVGERIPMMAGLGATETAPTATFThWPTERSGL--IGLPAPGT-------ELKLVPSGGKYEVRVKGPNVTPGYWRQP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 355 AATAERFLPNPFggpgermYRTGDRVWAGSDGQ----LVFVGRVDDQLKVR-GHRIEPGEVESALLAVDG--VAQAVVTE 427
Cdd:cd05921 386 ELTAQAFDEEGF-------YCLGDAAKLADPDDpakgLVFDGRVAEDFKLAsGTWVSVGPLRARAVAACAplVHDAVVAG 458
|
..
gi 214003850 428 HD 429
Cdd:cd05921 459 ED 460
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
16-485 |
3.08e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 59.58 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 16 AAAMPDRPAVAMGAT------TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV--- 86
Cdd:PRK10524 63 LAKRPEQLALIAVSTetdeerTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVfgg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 87 ----------DPDYP-----AD---------RRRHMLDD-------TAAHCLLA----MPGQDVAGAPVVMSVERkpgqs 131
Cdd:PRK10524 143 fashslaariDDAKPvlivsADagsrggkvvPYKPLLDEaialaqhKPRHVLLVdrglAPMARVAGRDVDYATLR----- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 132 APNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVlvtHRGIPNLAddyvrrqnlvpdsrlLAFASPS---FDAAVAE-FW 207
Cdd:PRK10524 218 AQHLGARVPVEWLESNEPSYILYTSGTTGKPKGV---QRDTGGYA---------------VALATSMdtiFGGKAGEtFF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 208 PI----WLAG------GCLVLAAASDLIPGEPLA-------RLVRDQGITHVTLPPSALAPLEEgggLPPGL-------- 262
Cdd:PRK10524 280 CAsdigWVVGhsyivyAPLLAGMATIMYEGLPTRpdagiwwRIVEKYKVNRMFSAPTAIRVLKK---QDPALlrkhdlss 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 263 --TLLVAGEACPAPVAkSWARDRV---MINAYGPTEA-----TVAVTASDPLTGEGTPpiGRPITSVSTYILDDKL-QPV 331
Cdd:PRK10524 357 lrALFLAGEPLDEPTA-SWISEALgvpVIDNYWQTETgwpilAIARGVEDRPTRLGSP--GVPMYGYNVKLLNEVTgEPC 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 332 PEGDVGELYMTGPgLARGYLRRPAATAERFLPNPFGGPGERMYRTGDrvWA--GSDGQLVFVGRVDDQLKVRGHRIEPGE 409
Cdd:PRK10524 434 GPNEKGVLVIEGP-LPPGCMQTVWGDDDRFVKTYWSLFGRQVYSTFD--WGirDADGYYFILGRTDDVINVAGHRLGTRE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 410 VESALLAVDGVAQ-AVVTEHDN----RLIAYVVGTGGARVAAEDLLPPLR--------KRLPGYLVPDVVVGLPRLPTSP 476
Cdd:PRK10524 511 IEESISSHPAVAEvAVVGVKDAlkgqVAVAFVVPKDSDSLADREARLALEkeimalvdSQLGAVARPARVWFVSALPKTR 590
|
....*....
gi 214003850 477 NGKIDRAAL 485
Cdd:PRK10524 591 SGKLLRRAI 599
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
409-479 |
4.67e-09 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 52.93 E-value: 4.67e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 214003850 409 EVESALLAVDGVAQ-AVVTEHD----NRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGK 479
Cdd:pfam13193 1 EVESALVSHPAVAEaAVVGVPDelkgEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
20-241 |
8.19e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 58.27 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 20 PDRPA-VAMG----ATTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPA-- 92
Cdd:PRK03584 98 DDRPAiIFRGedgpRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVqg 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 93 --DR-------------------RRHMLDDTAAHCLLAMPG----------QDVAGAPVVMSVERKPGQSAPNLTDQDRL 141
Cdd:PRK03584 178 vlDRfgqiepkvliavdgyryggKAFDRRAKVAELRAALPSlehvvvvpylGPAAAAAALPGALLWEDFLAPAEAAELEF 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 142 SPLLPNHPAYVIYTSGSTGQPK-------GVLVTHRGIPNLADDyvrrqnLVPDSRLLAFASPSfdaavaefWPIW---- 210
Cdd:PRK03584 258 EPVPFDHPLWILYSSGTTGLPKcivhghgGILLEHLKELGLHCD------LGPGDRFFWYTTCG--------WMMWnwlv 323
|
250 260 270
....*....|....*....|....*....|....*
gi 214003850 211 ---LAGGCLVLAAASDLIP-GEPLARLVRDQGITH 241
Cdd:PRK03584 324 sglLVGATLVLYDGSPFYPdPNVLWDLAAEEGVTV 358
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
509-574 |
9.73e-09 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 52.64 E-value: 9.73e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 214003850 509 HLAGLFAEVLGVSS---VGVDDSFFDIGGHSLLATRLVARIRQSLQVRLRVQAFFNAPTVAQLAKVLDG 574
Cdd:smart00823 16 LVREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
32-437 |
1.17e-08 |
|
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: 57.61 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGV--GPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLA 109
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 110 MPGQDVAGAPVVMSVERKpgqsapnltDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGIPNL---ADDYVRRQNLV 186
Cdd:cd05927 86 DAGVKVYSLEEFEKLGKK---------NKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNvagVFKILEILNKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 187 -PDSRLLAFASPS--FDAAVaefwpIWLA---GGCL-------------VLAAASDLIPGEP------------------ 229
Cdd:cd05927 157 nPTDVYISYLPLAhiFERVV-----EALFlyhGAKIgfysgdirlllddIKALKPTVFPGVPrvlnriydkifnkvqakg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 230 -LARLVRDQGITHvtlppsALAPLEEGG-----------------GLPPGLTLLVAGEACPAPVAKSWAR---DRVMINA 288
Cdd:cd05927 232 pLKRKLFNFALNY------KLAELRSGVvraspfwdklvfnkikqALGGNVRLMLTGSAPLSPEVLEFLRvalGCPVLEG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 289 YGPTEATVAVTASDP---LTGEgtppIGRPITSVstyilDDKLQPVPE------GDV--GELYMTGPGLARGYLRRPAAT 357
Cdd:cd05927 306 YGQTECTAGATLTLPgdtSVGH----VGGPLPCA-----EVKLVDVPEmnydakDPNprGEVCIRGPNVFSGYYKDPEKT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 358 AERFLPNPFggpgermYRTGDRVWAGSDGQLVFVGRVDDQLK-VRGHRIEPGEVESALLAVDGVAQAVVT--EHDNRLIA 434
Cdd:cd05927 377 AEALDEDGW-------LHTGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPFVAQIFVYgdSLKSFLVA 449
|
...
gi 214003850 435 YVV 437
Cdd:cd05927 450 IVV 452
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
29-411 |
3.21e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 56.28 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 29 ATTLSYAELNGEANLLARRLvEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPV-DPDYP--ADRRRHMLDDTAAH 105
Cdd:PRK07769 53 ARDLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 106 CLLAMPGqdvAGAPVVMSVERKPGQSAPNLTDQDRL--------SPLLPNHP--AYVIYTSGSTGQPKGVLVTHRGIP-N 174
Cdd:PRK07769 132 AILTTTD---SAEGVRKFFRARPAKERPRVIAVDAVpdevgatwVPPEANEDtiAYLQYTSGSTRIPAGVQITHLNLPtN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 175 L--------ADDYVRRQNLVP---DSRLL------------AFASPSFDAAVAEFWPIWLA----GGCLVLAAASDL--- 224
Cdd:PRK07769 209 VlqvidaleGQEGDRGVSWLPffhDMGLItvllpallghyiTFMSPAAFVRRPGRWIRELArkpgGTGGTFSAAPNFafe 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 225 ------IP--GEPLARLVRDQGITHVTLPPS---------ALAPLeeggGLPP-------GL---TLLVAgeACPA-PVA 276
Cdd:PRK07769 289 haaargLPkdGEPPLDLSNVKGLLNGSEPVSpasmrkfneAFAPY----GLPPtaikpsyGMaeaTLFVS--TTPMdEEP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 277 KSWARDRVMINAygptEATVAVTASDPltgEGTPPIGRPITSVSTY--ILD-DKLQPVPEGDVGELYMTGPGLARGYLRR 353
Cdd:PRK07769 363 TVIYVDRDELNA----GRFVEVPADAP---NAVAQVSAGKVGVSEWavIVDpETASELPDGQIGEIWLHGNNIGTGYWGK 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 214003850 354 PAATAERF---LPNPF------GGPGERMY-RTGDR-VWAgsDGQLVFVGRVDDQLKVRGHRIEPGEVE 411
Cdd:PRK07769 436 PEETAATFqniLKSRLseshaeGAPDDALWvRTGDYgVYF--DGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
333-487 |
2.43e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.46 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 333 EGDVGELYMTGPGLARGYLrrPAataerFLPNPfggpgeRMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVES 412
Cdd:PRK07445 298 ANQTGNITIQAQSLALGYY--PQ-----ILDSQ------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEA 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 413 ALLAVDGVAQAVV-----TEHDNRLIAYVVGTGGArVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALPD 487
Cdd:PRK07445 365 AILATGLVQDVCVlglpdPHWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
28-170 |
2.45e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 53.45 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 28 GATTLSYAELNGEANLLARRLVEH-GVGPEKLVALAMPRSIEFVIAILAVHKAG--AAYVP------------------- 85
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 86 ----------VDPDYPAdrrrhmLDDTAAHCLLAMPGQDVAGapvVMSVERKPGQSAPNLTDQDRLSPLLPNHPAYVIYT 155
Cdd:cd05938 82 lvvapelqeaVEEVLPA------LRADGVSVWYLSHTSNTEG---VISLLDKVDAASDEPVPASLRAHVTIKSPALYIYT 152
|
170
....*....|....*
gi 214003850 156 SGSTGQPKGVLVTHR 170
Cdd:cd05938 153 SGTTGLPKAARISHL 167
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
31-429 |
3.83e-07 |
|
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: 52.81 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 31 TLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLDDTAAHCLLAM 110
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 111 PGQDVAG----APVVMSVE------------------------RKPGQSA----PNLTDQdRLSPLLPNHPAYVIYTSGS 158
Cdd:cd17641 91 DEEQVDKlleiADRIPSVRyviycdprgmrkyddprlisfedvVALGRALdrrdPGLYER-EVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 159 TGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPsfdAAVAEFwpIWLAGGCLVLAAASDLiPGEPLARL--VRD 236
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPL---PWIGEQ--MYSVGQALVCGFIVNF-PEEPETMMedLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 237 QGITHVTLPP------------------------------SALAPLEEG-GGLPPGLTLLVAgeacpapvakSWARDRVM 285
Cdd:cd17641 244 IGPTFVLLPPrvwegiaadvrarmmdatpfkrfmfelgmkLGLRALDRGkRGRPVSLWLRLA----------SWLADALL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 286 INAY----GPTEATVAVTASDPLtGEGT----PPIGRPITSV---------STYILDDKLQP----VPEGD-------VG 337
Cdd:cd17641 314 FRPLrdrlGFSRLRSAATGGAAL-GPDTfrffHAIGVPLKQLygqtelagaYTVHRDGDVDPdtvgVPFPGtevrideVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 338 ELYMTGPGLARGYLRRPAATAERFLpnpfggpGERMYRTGDRVWAGSDGQLVFVGRVDDQLKV-RGHRIEPGEVESALLA 416
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFD-------EDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKF 465
|
490
....*....|...
gi 214003850 417 VDGVAQAVVTEHD 429
Cdd:cd17641 466 SPYIAEAVVLGAG 478
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
134-444 |
7.96e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 51.74 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 134 NLTDQDrlspllPNHPAYVIYTSGSTGQPKGVLVTHRgipnladdyvrrqNLVPDSR-LLAFASPSFDAAVAEFWPIWLA 212
Cdd:PRK06334 176 GVSDKD------PEDVAVILFTSGTEKLPKGVPLTHA-------------NLLANQRaCLKFFSPKEDDVMMSFLPPFHA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 213 GG---CL---VLAAASDLIPGEPL--ARLVRDQGITHVTLPPSA-------LAPLEEGGGLPPGLTLLVAGeacpAPVAK 277
Cdd:PRK06334 237 YGfnsCTlfpLLSGVPVVFAYNPLypKKIVEMIDEAKVTFLGSTpvffdyiLKTAKKQESCLPSLRFVVIG----GDAFK 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 278 SWARDRV--------MINAYGPTEATVAVTASDPLTGEGTPPIGRPITSVSTYILDDKLQ-PVPEGDVGELYMTGPGLAR 348
Cdd:PRK06334 313 DSLYQEAlktfphiqLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFS 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 349 GYLrrpaatAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAvvtEH 428
Cdd:PRK06334 393 GYL------GEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA---DH 463
|
330
....*....|....*.
gi 214003850 429 DNRLIayVVGTGGARV 444
Cdd:PRK06334 464 AGPLV--VCGLPGEKV 477
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
146-485 |
1.89e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.12 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 146 PNHPAYVIYTSGSTGQPKGVLVTHRGIpnLADDY--VRRQNLVPDSRLLAfASPSFDAavaefwpIWLAGGcLVLAAASD 223
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNL--LANRAqvAARIDFSPEDKVFN-ALPVFHS-------FGLTGG-LVLPLLSG 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 224 ----LIPgEPL-----ARLVRDQGITHVTLPPSALApleeggglppG------------LTLLVAG-EACPAPVAKSWAR 281
Cdd:PRK06814 861 vkvfLYP-SPLhyriiPELIYDTNATILFGTDTFLN----------GyaryahpydfrsLRYVFAGaEKVKEETRQTWME 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 282 D---RVMiNAYGPTEATVAVTASDPLTGE-GTppIGRPITSVstyilDDKLQPVP---EGdvGELYMTGPGLARGYLRrp 354
Cdd:PRK06814 930 KfgiRIL-EGYGVTETAPVIALNTPMHNKaGT--VGRLLPGI-----EYRLEPVPgidEG--GRLFVRGPNVMLGYLR-- 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 355 aatAERflPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVD-GVAQAVVTEHD---- 429
Cdd:PRK06814 998 ---AEN--PGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWpDALHAAVSIPDarkg 1072
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 214003850 430 NRLIAYVVGTGGARvaaEDLLPPLRKR-LPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK06814 1073 ERIILLTTASDATR---AAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAV 1126
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
323-431 |
2.10e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.15 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 323 ILD-DKLQPVPEGDVGELYMTGpgLAR-GY--LRrpaataerflpnpfggpgermYRTGD--RVWAG--SDG----QLVF 390
Cdd:COG1541 265 IIDpETGEPVPEGEEGELVVTT--LTKeAMplIR---------------------YRTGDltRLLPEpcPCGrthpRIGR 321
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 214003850 391 V-GRVDDQLKVRGHRIEPGEVESALLAVDGVA---QAVVTEHDNR 431
Cdd:COG1541 322 IlGRADDMLIIRGVNVFPSQIEEVLLRIPEVGpeyQIVVDREGGL 366
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
323-431 |
2.73e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 49.93 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 323 ILDDK-LQPVPEGDVGELYMTgpglargylrrpaataerfLPNPFGGPGERmYRTGDRVwagsdgQLVF----------- 390
Cdd:cd05913 261 IIDPEtGEPVPPGEVGELVFT-------------------TLTKEAMPLIR-YRTRDIT------RLLPgpcpcgrthrr 314
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 214003850 391 ----VGRVDDQLKVRGHRIEPGEVESALLAVDGV---AQAVVTEHDNR 431
Cdd:cd05913 315 idriTGRSDDMLIIRGVNVFPSQIEDVLLKIPGLgphYQLILTRQEHL 362
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
120-394 |
2.84e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 50.36 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 120 VVMSVERKPGQSAPNL-TDQDRLspllpnhpAYVIYTSGSTGQPKGVLVTHR----GIPNLADD---------------- 178
Cdd:PTZ00216 244 VVAKGHSAGSHHPLNIpENNDDL--------ALIMYTSGTTGDPKGVMHTHGsltaGILALEDRlndligppeedetycs 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 179 ---------------YVRRQNLV----PDSRLLAFASPSFDaaVAEFWPIWLAGGCLVL-----AAASDLIPGEPLARLV 234
Cdd:PTZ00216 316 ylplahimefgvtniFLARGALIgfgsPRTLTDTFARPHGD--LTEFRPVFLIGVPRIFdtikkAVEAKLPPVGSLKRRV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 235 RDQGIThvtlppSALAPLEEG------------------GGlppGLTLLVAGEACPAPVAKSWARdrV----MINAYGPT 292
Cdd:PTZ00216 394 FDHAYQ------SRLRALKEGkdtpywnekvfsapravlGG---RVRAMLSGGGPLSAATQEFVN--VvfgmVIQGWGLT 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 293 EaTVAVtASDPLTGEGTP-PIGRPITSVSTYILD-------DKlqPVPEGdvgELYMTGPGLARGYLRRPAATAERFLPn 364
Cdd:PTZ00216 463 E-TVCC-GGIQRTGDLEPnAVGQLLKGVEMKLLDteeykhtDT--PEPRG---EILLRGPFLFKGYYKQEELTREVLDE- 534
|
330 340 350
....*....|....*....|....*....|
gi 214003850 365 pfGGpgerMYRTGDRVWAGSDGQLVFVGRV 394
Cdd:PTZ00216 535 --DG----WFHTGDVGSIAANGTLRIIGRV 558
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
7-412 |
4.70e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 49.35 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 7 TAPALFEATAAAMPDRPA---------VAMGATTLSYAELNGEANLLARRLVEHgVGPEKLVALAMPRSIEFVIAILAVH 77
Cdd:PRK12476 35 TLISLIERNIANVGDTVAyryldhshsAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 78 KAGAAYVPV-DPDYP--ADRRRHMLDD---------TAA-----HCLLAMPGqdvAGAPVVMSVERKPGQSAPNLTDqdr 140
Cdd:PRK12476 114 KAGTIAVPLfAPELPghAERLDTALRDaeptvvlttTAAaeaveGFLRNLPR---LRRPRVIAIDAIPDSAGESFVP--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 141 lSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGI-PNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLA 219
Cdd:PRK12476 188 -VELDTDDVSHLQYTSGSTRPPVGVEITHRAVgTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLM 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 220 AASDLI--PGeplaRLVRDQGITHVTLPPSALAP-----LEEGGGLPPG--------LTLLVAGEacpaPVAKSWAR--- 281
Cdd:PRK12476 267 SPTAFVrrPQ----RWIKALSEGSRTGRVVTAAPnfayeWAAQRGLPAEgddidlsnVVLIIGSE----PVSIDAVTtfn 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 282 ---------DRVMINAYGPTEATVAVTASDP--------------------LTGEGTP------PIGRPITSVSTYILD- 325
Cdd:PRK12476 339 kafapyglpRTAFKPSYGIAEATLFVATIAPdaepsvvyldreqlgagravRVAADAPnavahvSCGQVARSQWAVIVDp 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 326 DKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERF-----LPNPFGG------PGERMYRTGDrVWAGSDGQLVFVGRV 394
Cdd:PRK12476 419 DTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqSRLAEGShadgaaDDGTWLRTGD-LGVYLDGELYITGRI 497
|
490
....*....|....*...
gi 214003850 395 DDQLKVRGHRIEPGEVES 412
Cdd:PRK12476 498 ADLIVIDGRNHYPQDIEA 515
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
288-447 |
6.00e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.99 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 288 AYGPTEATVAVTASDPLTG----EGTPP----------IGRPITSVSTYIL-DDKLQPVPEGDVGELYMTGPGLARGYLR 352
Cdd:PRK05851 309 SYGLAESTCAVTVPVPGIGlrvdEVTTDdgsgarrhavLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSGYLG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 353 RPAATAERFLPnpfggpgermyrTGDRVWAGsDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVVtehdnrl 432
Cdd:PRK05851 389 QAPIDPDDWFP------------TGDLGYLV-DGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAV------- 448
|
170
....*....|....*....
gi 214003850 433 IAYVVGTGGAR----VAAE 447
Cdd:PRK05851 449 VAVGTGEGSARpglvIAAE 467
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
140-172 |
1.23e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 48.19 E-value: 1.23e-05
10 20 30
....*....|....*....|....*....|....*...
gi 214003850 140 RLSPLLPNHP-----AYVIYTSGSTGQPKGVLVTHRGI 172
Cdd:PLN02387 238 KENPVDPDLPspndiAVIMYTSGSTGLPKGVMMTHGNI 275
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
79-575 |
5.06e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.40 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 79 AGAAYVPVD-PDYPADRRrhmldDTAAHCLLAMPGQDVAGAPVVMSVERKPGQSAPNLTDQDRLSPLLPNHPAYVIYTSG 157
Cdd:COG3321 854 PGRGRRRVPlPTYPFQRE-----DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 158 STGQPKGVLVTHRGIPNLADDYVRRQNLVPDSRLLAFASPSFDAAVAEFWPIWLAGGCLVLAAASDLIPGEPLARLVRDQ 237
Cdd:COG3321 929 LLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAA 1008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 238 GITHVTLPPSALAPLEEGGGLPPGLTLLVAGEACPAPVAKSWARDRVMINAYGPTEATVAVTASDPLTGEGTPPIGRPIT 317
Cdd:COG3321 1009 ALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAA 1088
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 318 SVSTYILDDKLQPVPEGDVGELYMTGPGLARGYLRRPAATAERFLPNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQ 397
Cdd:COG3321 1089 ALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALL 1168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 398 LKVRGHRIEPGEVESALLAVDGVAQAVVTEHDNRLIAYVVGTGGARVAAEDLLPPLRKRLPGYLVPDVVVGLPRLPTSPN 477
Cdd:COG3321 1169 AAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAAL 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 478 GKIDRAALPDPDREGAERVTSGRAPSTPTEIHLAGLFAEVLGVSSVGVDDSFFDIGGHSLLATRLVARIRQSLQVRLRVQ 557
Cdd:COG3321 1249 AAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAA 1328
|
490
....*....|....*...
gi 214003850 558 AFFNAPTVAQLAKVLDGA 575
Cdd:COG3321 1329 ALAALAAAVAAALALAAA 1346
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
129-172 |
1.68e-04 |
|
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: 44.66 E-value: 1.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 214003850 129 GQSAPNLTDQDRLSPLLPNHPAYVIYTSGSTGQPKGVLVTHRGI 172
Cdd:cd05933 132 GRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNI 175
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
146-485 |
3.76e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 43.55 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 146 PNHPAYVIYTSGSTGQPKGVLVTHRG-------IPNLADdyvrrqnLVPDSRLLAfASPSFDA---AVAEFWPiwlaggc 215
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSllanveqIKTIAD-------FTPNDRFMS-ALPLFHSfglTVGLFTP------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 216 LVLAAASDLIPgEPL-----ARLVRDQGITHVTLPPSALA-------PLEEGGglppgLTLLVAGEACPAPVAKSWARDR 283
Cdd:PRK08043 429 LLTGAEVFLYP-SPLhyrivPELVYDRNCTVLFGTSTFLGnyarfanPYDFAR-----LRYVVAGAEKLQESTKQLWQDK 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 284 VMI---NAYGPTEATVAVTASDPLTGE-GTppIGRPITSvstyiLDDKLQPVP---EGdvGELYMTGPGLARGYLR--RP 354
Cdd:PRK08043 503 FGLrilEGYGVTECAPVVSINVPMAAKpGT--VGRILPG-----MDARLLSVPgieQG--GRLQLKGPNIMNGYLRveKP 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 355 ----AATAErflpNPFGGPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQ-AVVTEHD 429
Cdd:PRK08043 574 gvleVPTAE----NARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQhATAIKSD 649
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 214003850 430 -NRLIAYVVGTGGARVAAEDLLPPLRKR-LPGYLVPDVVVGLPRLPTSPNGKIDRAAL 485
Cdd:PRK08043 650 aSKGEALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTL 707
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
30-492 |
1.71e-03 |
|
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: 41.26 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 30 TTLSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAayvpVDPDYPADRRRHMLddtaAHCLla 109
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGV----ETALINSNLRLESL----LHCI-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 110 mpgqDVAGA---------PVVMSVERKPgQSAPNLTDQDRLspllpnhpaYVIYTSGSTGQPKGVLVTHRGIPNLA---- 176
Cdd:cd05939 72 ----TVSKAkalifnlldPLLTQSSTEP-PSQDDVNFRDKL---------FYIYTSGTTGLPKAAVIVHSRYYRIAagay 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 177 -------DD--------YVRRQNLVPDSRLLAFAS-----PSFDAAvaEFWPIWLAGGCLVlaaaSDLIpGEpLARLVRD 236
Cdd:cd05939 138 yafgmrpEDvvydclplYHSAGGIMGVGQALLHGStvvirKKFSAS--NFWDDCVKYNCTI----VQYI-GE-ICRYLLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 237 QgithvtlPPSalaPLEE--------GGGLPPGLtllvageacpapvaksWAR--DRVMINA----YGPTEATVAVTASD 302
Cdd:cd05939 210 Q-------PPS---EEEQkhnvrlavGNGLRPQI----------------WEQfvRRFGIPQigefYGATEGNSSLVNID 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 303 PLTGEG--TPPIGRPITSVSTYILDDKL-----------QPVPEGDVGElyMTGPGLARGYLRR------PAATAERFLP 363
Cdd:cd05939 264 NHVGACgfNSRILPSVYPIRLIKVDEDTgelirdsdglcIPCQPGEPGL--LVGKIIQNDPLRRfdgyvnEGATNKKIAR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 364 NPFGgPGERMYRTGDRVWAGSDGQLVFVGRVDDQLKVRGHRIEPGEVESALLAVDGVAQAVV-------TEHDNRLIAYV 436
Cdd:cd05939 342 DVFK-KGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygvevpgVEGRAGMAAIV 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 214003850 437 VGTGG---ARVAAEdllppLRKRLPGYLVPDVVVGLPRLPTSPNGKIDRAALpdpDREG 492
Cdd:cd05939 421 DPERKvdlDRFSAV-----LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL---QKEG 471
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
32-176 |
4.00e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 40.08 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 32 LSYAELNGEANLLARRLVEHGVGPEKLVALAMPRSIEFVIAILAVHKAGAAYVPVDPDYPADRRRHMLD----------- 100
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNhaevaaifcvp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214003850 101 ---DTAAHCLLAMPGQD----VAGAPVVM-SVERKPG---QSAPNLTDQDRLSPLLPNHP-----AYVIYTSGSTGQPKG 164
Cdd:PLN02736 159 qtlNTLLSCLSEIPSVRlivvVGGADEPLpSLPSGTGveiVTYSKLLAQGRSSPQPFRPPkpedvATICYTSGTTGTPKG 238
|
170
....*....|...
gi 214003850 165 VLVTHRG-IPNLA 176
Cdd:PLN02736 239 VVLTHGNlIANVA 251
|
|
| |
