|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
6-537 |
0e+00 |
|
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: 1017.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 6 ILYGPEPFHPLADGTAGEQMFYALSRYADISGCIALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGL 85
Cdd:cd17642 1 IIVGPGPFYPLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 86 QFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNTFQKVLNVKSKLKYVETIIILDLNEDLGGYQCLNN 165
Cdd:cd17642 81 QFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 166 FISQNSDINLDVKKFKPNSFNRDDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTFGNAINPTTAILTVIPFHHG 245
Cdd:cd17642 161 FITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 246 FGMTTTLGYFTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEM 325
Cdd:cd17642 241 FGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 326 VKKRFKLNFVRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEE 405
Cdd:cd17642 321 VAKRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 406 ATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVV 485
Cdd:cd17642 401 ATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 41688574 486 VQTGKYLNEQIVQNFVSSQVSTAKWLRGGVKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:cd17642 481 LEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
40-529 |
0e+00 |
|
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: 553.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 40 ALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGI 119
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 120 VKPRIIFCSKNTFQKVLNVKSKLKYVETIIILDLNEDLGGYQC-LNNFISQNSDINLdvkkfKPNSFNRDDQVALVMFSS 198
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEdLLSPTLGEEDEDL-----PPPLKDGKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKNIVARFSHCKDPTFGNAINPTTaILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQSLQD 278
Cdd:cd05911 156 GTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDV-ILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 279 YKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLITPDTDVRP 358
Cdd:cd05911 235 YKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 359 GSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLK 438
Cdd:cd05911 315 GSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 439 SLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRGGVKFL 518
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFV 474
|
490
....*....|.
gi 41688574 519 DEIPKGSTGKI 529
Cdd:cd05911 475 DEIPKSASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
27-534 |
9.40e-151 |
|
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: 441.67 E-value: 9.40e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 27 YALSRYADISGCIALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSD 106
Cdd:cd05904 10 VSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 107 KYIERELIHSLGIVKPRIIFCSKNTFQKVLNvksklkYVETIIILDLNEDLGGYQCLNNFISQNSDinldvkkfKPNSFN 186
Cdd:cd05904 90 LSTPAEIAKQVKDSGAKLAFTTAELAEKLAS------LALPVVLLDSAEFDSLSFSDLLFEADEAE--------PPVVVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 187 RDDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHcKDPTFGNAINPTTAILTVIPFHHGFGMTT-TLGYFTCGFRVALMH 265
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQ-FVAGEGSNSDSEDVFLCVLPMFHIYGLSSfALGLLRLGATVVVMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 TFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETT 345
Cdd:cd05904 235 RFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 346 SAVLITPDTD---VRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDI 422
Cdd:cd05904 315 GVVAMCFAPEkdrAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 423 AYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVS 502
Cdd:cd05904 395 CYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVA 474
|
490 500 510
....*....|....*....|....*....|..
gi 41688574 503 SQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVL 534
Cdd:cd05904 475 KQVAPYKKVR-KVAFVDAIPKSPSGKILRKEL 505
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
52-541 |
1.59e-123 |
|
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: 370.29 E-value: 1.59e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCsknt 131
Cdd:COG0318 27 YAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqkvlnvksklkyvetiiildlnedlggyqclnnfisqnsdinldvkkfkpnsfnrddqvALVMFSSGTTGVSKGVMLTH 211
Cdd:COG0318 103 ------------------------------------------------------------ALILYTSGTTGRPKGVMLTH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVARFSHCKDpTFGnaINPTTAILTVIPFHHGFGMT-TTLGYFTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVPTL 290
Cdd:COG0318 123 RNLLANAAAIAA-ALG--LTPGDVVLVALPLFHVFGLTvGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 291 MAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAVLITPD--TDVRPGSTGKIVPFH 368
Cdd:COG0318 200 LARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIV-EGYGLTETSPVVTVNPEdpGERRPGSVGRPLPGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 369 AVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQV 448
Cdd:COG0318 279 EVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 449 APAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGK 528
Cdd:COG0318 357 YPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPR-RVEFVDELPRTASGK 435
|
490
....*....|...
gi 41688574 529 IDRKVLRQMFEKH 541
Cdd:COG0318 436 IDRRALRERYAAG 448
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
27-535 |
5.19e-113 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 346.20 E-value: 5.19e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 27 YALSRYADISGCIALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSD 106
Cdd:PLN02246 28 YCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 107 KYIERELIHSLGIVKPRIIFCSKNTFQKVlnvkSKLKYVETIIILDLNEDLGGyqCLN-NFISQNSDINLDVKKFKPnsf 185
Cdd:PLN02246 108 FYTPAEIAKQAKASGAKLIITQSCYVDKL----KGLAEDDGVTVVTIDDPPEG--CLHfSELTQADENELPEVEISP--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 186 nrDDQVALVmFSSGTTGVSKGVMLTHKNIVARFSHCKD---PTFGnaINPTTAILTVIPFHHGFGMTTTLgyfTCGFRVA 262
Cdd:PLN02246 179 --DDVVALP-YSSGTTGLPKGVMLTHKGLVTSVAQQVDgenPNLY--FHSDDVILCVLPMFHIYSLNSVL---LCGLRVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 263 ----LMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQG 338
Cdd:PLN02246 251 aailIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 YGLTETtSAVLI-------TPdTDVRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAII 411
Cdd:PLN02246 331 YGMTEA-GPVLAmclafakEP-FPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 412 NKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKY 491
Cdd:PLN02246 409 DKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSE 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 41688574 492 LNEQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PLN02246 489 ITEDEIKQFVAKQVVFYKRIH-KVFFVDSIPKAPSGKILRKDLR 531
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
52-535 |
4.85e-109 |
|
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: 333.38 E-value: 4.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKnT 131
Cdd:cd05936 27 YRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAV-S 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKYVETIiildlnedlggyqclnnfisqnsdinldvkkfkpnsfNRDDqVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd05936 106 FTDLLAAGAPLGERVAL-------------------------------------TPED-VAVLQYTSGTTGVPKGAMLTH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVARFSHCKDpTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTC-GFRVALMHTFEEKLFLQSLQDYKVESTLLVPTL 290
Cdd:cd05936 148 RNLVANALQIKA-WLEDLLEGDDVVLAALPLFHVFGLTVALLLPLAlGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 291 MAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTSAVLITPDTDVR-PGSTGKIVPFHA 369
Cdd:cd05936 227 YIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP-IVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 370 VKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVA 449
Cdd:cd05936 306 VKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 450 PAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKI 529
Cdd:cd05936 384 PREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR-QVEFRDELPKSAVGKI 462
|
....*.
gi 41688574 530 DRKVLR 535
Cdd:cd05936 463 LRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
190-530 |
1.78e-106 |
|
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: 322.31 E-value: 1.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 190 QVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTFgnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEE 269
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG---LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 270 KLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAVL 349
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLV-NGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 350 ITP--DTDVRPGSTGKIVPFHAVKVVDPTTGkILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDN 427
Cdd:cd04433 157 TGPpdDDARKPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-EDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 428 DGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVST 507
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|...
gi 41688574 508 AKWLRgGVKFLDEIPKGSTGKID 530
Cdd:cd04433 315 YKVPR-RVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
52-444 |
5.96e-97 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 300.77 E-value: 5.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKN- 130
Cdd:pfam00501 24 YRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDAl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TFQKVLNVKSKLKYVETIIILDLNEDLGgYQCLNNFISQNSDINLDVKKFKPnsfnrdDQVALVMFSSGTTGVSKGVMLT 210
Cdd:pfam00501 104 KLEELLEALGKLEVVKLVLVLDRDPVLK-EEPLPEEAKPADVPPPPPPPPDP------DDLAYIIYTSGTTGKPKGVMLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 211 HKNIVA-RFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTT-TLGYFTCGFRVALM---HTFEEKLFLQSLQDYKVESTL 285
Cdd:pfam00501 177 HRNLVAnVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPpgfPALDPAALLELIERYKVTVLY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 286 LVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKlNFVRQGYGLTETTSAVLITPDTD---VRPGSTG 362
Cdd:pfam00501 257 GVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTETTGVVTTPLPLDedlRSLGSVG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 363 KIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIK 442
Cdd:pfam00501 336 RPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
..
gi 41688574 443 YK 444
Cdd:pfam00501 416 LG 417
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
46-538 |
4.90e-94 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 296.33 E-value: 4.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 46 TKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRII 125
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 126 FCSKnTFQKVL-NVKSKLKYVETIIILD------LNEDLGGYQCLnnfISQNSDiNLDVKKFKPNSfnrddqVALVMFSS 198
Cdd:PRK06187 108 LVDS-EFVPLLaAILPQLPTVRTVIVEGdgpaapLAPEVGEYEEL---LAAASD-TFDFPDIDEND------AAAMLYTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKNIvarFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQSLQD 278
Cdd:PRK06187 177 GTTGHPKGVVLSHRNL---FLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIPRRFDPENLLDLIET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 279 YKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAVLITPDTD--- 355
Cdd:PRK06187 254 ERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLV-QGYGMTETSPVVSVLPPEDqlp 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 356 ---VRPGSTGKIVPFHAVKVVDPTtGKILGPN--ETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGH 430
Cdd:PRK06187 333 gqwTKRRSAGRPLPGVEARIVDDD-GDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 431 FYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVstAKW 510
Cdd:PRK06187 411 LYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRL--AKF 488
|
490 500
....*....|....*....|....*....
gi 41688574 511 -LRGGVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:PRK06187 489 kLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
32-543 |
4.79e-91 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 289.57 E-value: 4.79e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 32 YADIsgcIALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIER 111
Cdd:PLN02330 41 YADK---VAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALES 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 112 ELIHSLGIVKPRIIFCSKNTFQKVLNVKSKlkyvetIIILdlnedlgGYQCLNNFISQNSDINLDVK---KFKPNSFNRD 188
Cdd:PLN02330 118 EIKKQAEAAGAKLIVTNDTNYGKVKGLGLP------VIVL-------GEEKIEGAVNWKELLEAADRagdTSDNEEILQT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVmFSSGTTGVSKGVMLTHKNIVARFshCKDP-TFGNAINPTTAILTVIPFHHGFGMT-TTLGYFTCGFRVALMHT 266
Cdd:PLN02330 185 DLCALP-FSSGTTGISKGVMLTHRNLVANL--CSSLfSVGPEMIGQVVTLGLIPFFHIYGITgICCATLRNKGKVVVMSR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 FEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLK--EIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTET 344
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSAVLITPDTD-----VRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRS 419
Cdd:PLN02330 342 SCITLTHGDPEkghgiAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 420 GDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQN 499
Cdd:PLN02330 422 GDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILN 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 41688574 500 FVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR-QMFEKHKS 543
Cdd:PLN02330 502 FVAANVAHYKKVR-VVQFVDSIPKSLSGKIMRRLLKeKMLSINKA 545
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
37-538 |
4.75e-90 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 287.51 E-value: 4.75e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 37 GCIALTNAHTKENVLYEEFLKLSCRLAESFKKY-GLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDkyierelIH 115
Cdd:PLN02574 54 GDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP-------SS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 116 SLGIVKPRIIFCSKNTFQKVLNVKSKLKYVETIIIL-----DLNEDLGGYQCLNNFISQNSDinldvkkFKPNSFNRDDQ 190
Cdd:PLN02574 127 SLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGvpenyDFDSKRIEFPKFYELIKEDFD-------FVPKPVIKQDD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 191 VALVMFSSGTTGVSKGVMLTHKNIVA------RF--SHCKDPTFGNAInpttaiLTVIPFHHGFGMTT-TLGYFTCGFRV 261
Cdd:PLN02574 200 VAAIMYSSGTTGASKGVVLTHRNLIAmvelfvRFeaSQYEYPGSDNVY------LAALPMFHIYGLSLfVVGLLSLGSTI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 262 ALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSAL-VEKYDLSHLKEIASGGAPLS-KEIGEMVKKRFKLNFVrQGY 339
Cdd:PLN02574 274 VVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSgKFIQDFVQTLPHVDFI-QGY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 340 GLTETTSAVLITPDTD--VRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWL 417
Cdd:PLN02574 353 GMTESTAVGTRGFNTEklSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 418 RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIV 497
Cdd:PLN02574 433 RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAV 512
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 41688574 498 QNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:PLN02574 513 INYVAKQVAPYKKVR-KVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
189-531 |
2.49e-86 |
|
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: 273.72 E-value: 2.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVArfsHCKDPTFGNAINPTTAILTVIPFHHGFGM-TTTLGYFTCGFRVALMHTF 267
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLW---NAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 268 EEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKkRFKLNFVrQGYGLTETTSA 347
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFV-QGYGMTETSPG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 348 VLITP--DTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYY 425
Cdd:cd17631 253 VTFLSpeDHRRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 426 DNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQV 505
Cdd:cd17631 331 DEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERL 410
|
330 340
....*....|....*....|....*.
gi 41688574 506 STAKWLRgGVKFLDEIPKGSTGKIDR 531
Cdd:cd17631 411 ARYKIPK-SVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
40-536 |
3.20e-83 |
|
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: 267.64 E-value: 3.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 40 ALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGI 119
Cdd:cd05926 5 ALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 120 VKPRIIFCSKNTFQKVLNVKSKLKyvetIIILDLNEDLGGyqclNNFISQNSDINL---DVKKFKPNSFNRDDQVALVMF 196
Cdd:cd05926 85 LGSKLVLTPKGELGPASRAASKLG----LAILELALDVGV----LIRAPSAESLSNllaDKKNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 197 SSGTTGVSKGVMLTHKNIVARFSHCkdpTFGNAINPTTAILTVIPFHHGFG-MTTTLGYFTCGFRVALMHTFEEKLFLQS 275
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNI---TNTYKLTPDDRTLVVMPLFHVHGlVASLLSTLAAGGSVVLPPRFSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYKVESTLLVPTLMAF---FPKSALVEKYdlSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTSAVLITP 352
Cdd:cd05926 234 VRDYNATWYTAVPTIHQIllnRPEPNPESPP--PKLRFIRSCSASLPPAVLEALEATFGAP-VLEAYGMTEAAHQMTSNP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 353 -DTDVR-PGSTGKivPFHA-VKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDG 429
Cdd:cd05926 311 lPPGPRkPGSVGK--PVGVeVRILDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 430 HFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAK 509
Cdd:cd05926 388 YLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFK 467
|
490 500
....*....|....*....|....*..
gi 41688574 510 WLRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05926 468 VPK-KVYFVDELPKTATGKIQRRKVAE 493
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
52-534 |
1.50e-79 |
|
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: 255.87 E-value: 1.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLgivkpriifcsKNT 131
Cdd:cd05935 4 YLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYIL-----------NDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLkyvetiiildlnedlggyqclnnfisqnsdinldvkkfkpnsfnrdDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd05935 73 GAKVAVVGSEL----------------------------------------------DDLALIPYTSGTTGLPKGCMHTH 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVARFSHckdPTFGNAINPTTAILTVIPFHHGFGMTTTLGY-FTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVPTL 290
Cdd:cd05935 107 FSAAANALQ---SAVWTGLTPSDVILACLPLFHVTGFVGSLNTaVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 291 MAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAVLITPDtdVRPGSTGKIVPFHAV 370
Cdd:cd05935 184 LVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFV-EGYGLTETMSQTHTNPP--LRPKLQCLGIP*FGV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 371 --KVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEAT-KAIINKDG--WLRSGDIAYYDNDGHFYIVDRLKSLIKYKG 445
Cdd:cd05935 261 daRVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETeESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 446 YQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQ---TGKYLNEQIVQnFVSSQVSTAKWLRgGVKFLDEIP 522
Cdd:cd05935 341 FKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRpeyRGKVTEEDIIE-WAREQMAAYKYPR-EVEFVDELP 418
|
490
....*....|..
gi 41688574 523 KGSTGKIDRKVL 534
Cdd:cd05935 419 RSASGKILWRLL 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
48-537 |
8.97e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 253.67 E-value: 8.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 48 ENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFC 127
Cdd:PRK07656 29 QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 128 SKnTFQKVL-NVKSKLKYVETIIILDLNEDLGGYQCLNNFisqnSD-INLDVKKFKPNSFNRDDqVALVMFSSGTTGVSK 205
Cdd:PRK07656 109 LG-LFLGVDySATTRLPALEHVVICETEEDDPHTEKMKTF----TDfLAAGDPAERAPEVDPDD-VADILFTSGTTGRPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 206 GVMLTHKNI---VARFSHCKDptfgnaINPTTAILTVIPFHHGFGMTTtlGYFTCGFRVA--LMH-TFEEKLFLQSLQDY 279
Cdd:PRK07656 183 GAMLTHRQLlsnAADWAEYLG------LTEGDRYLAANPFFHVFGYKA--GVNAPLMRGAtiLPLpVFDPDEVFRLIETE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 280 KVesTLL--VPTLMAF---FPKSAlveKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLITPDT 354
Cdd:PRK07656 255 RI--TVLpgPPTMYNSllqHPDRS---AEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVTTFNRLD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 355 DVR---PGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHF 431
Cdd:PRK07656 330 DDRktvAGTIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 432 YIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWL 511
Cdd:PRK07656 409 YIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVP 488
|
490 500
....*....|....*....|....*.
gi 41688574 512 RgGVKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK07656 489 R-SIEFLDELPKNATGKVLKRALREK 513
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
52-539 |
2.94e-75 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 248.49 E-value: 2.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:COG0365 42 YAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQ--KVLNVKSK-------LKYVETIIILD---LNEDLGGYQCLNNFISQNSDinldvkKFKPNSFNRDDqVALVMFSSG 199
Cdd:COG0365 122 LRggKVIDLKEKvdealeeLPSLEHVIVVGrtgADVPMEGDLDWDELLAAASA------EFEPEPTDADD-PLFILYTSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 200 TTGVSKGVMLTHKNIVArfshckdptfgnainpttAILTVIPFHHGF------------GMTTTLGYFTCGfrvALMH-- 265
Cdd:COG0365 195 TTGKPKGVVHTHGGYLV------------------HAATTAKYVLDLkpgdvfwctadiGWATGHSYIVYG---PLLNga 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 ---TFEEKL-------FLQSLQDYKVESTLLVPT----LMAFFPKsaLVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFK 331
Cdd:COG0365 254 tvvLYEGRPdfpdpgrLWELIEKYGVTVFFTAPTairaLMKAGDE--PLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 332 LnFVRQGYGLTETTSAVL-ITPDTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDM--IMKSYYNNEEATK 408
Cdd:COG0365 332 V-PIVDGWGQTETGGIFIsNLPGLPVKPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVIKGPWpgMFRGYWNDPERYR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 409 AII--NKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVV 486
Cdd:COG0365 410 ETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVL 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 41688574 487 QTGKYLNEQIV---QNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMFE 539
Cdd:COG0365 490 KPGVEPSDELAkelQAHVREELGPYAYPR-EIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
47-534 |
4.19e-73 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 241.30 E-value: 4.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 47 KENVLYEEFLKLSCRLAESFK-KYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRII 125
Cdd:PRK06839 25 EEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 126 FCSKnTFQKVLNVKSKLKYVETIIILdlnEDLGGyqclnnfISQNSDINLDVKKfkpnsfnrDDQVALVMFSSGTTGVSK 205
Cdd:PRK06839 105 FVEK-TFQNMALSMQKVSYVQRVISI---TSLKE-------IEDRKIDNFVEKN--------ESASFIICYTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 206 GVMLTHKNIvarfshckdptFGNAINPTTAI--------LTVIPFHH--GFGMTTTLGYFTCGfRVALMHTFEEKLFLQS 275
Cdd:PRK06839 166 GAVLTQENM-----------FWNALNNTFAIdltmhdrsIVLLPLFHigGIGLFAFPTLFAGG-VIIVPRKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKE-IGEMVKKRFKLNfvrQGYGLTETTSAVLITPDT 354
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEElMREFIDRGFLFG---QGFGMTETSPTVFMLSEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 355 DVR--PGSTGKIVPFHAVKVVDPTTGKIlGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFY 432
Cdd:PRK06839 311 DARrkVGSIGKPVLFCDYELIDENKNKV-EVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 433 IVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLR 512
Cdd:PRK06839 389 IVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPK 468
|
490 500
....*....|....*....|..
gi 41688574 513 GGVkFLDEIPKGSTGKIDRKVL 534
Cdd:PRK06839 469 EIV-FLKELPKNATGKIQKAQL 489
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
6-542 |
1.03e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 236.47 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 6 ILYGPEPFHPLAdgtagEQMfyaLSRYADISGCIALtnahtKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGL 85
Cdd:PRK06710 19 ISYDIQPLHKYV-----EQM---ASRYPEKKALHFL-----GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 86 QFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNTFQKVLNVKSKLKyVETIIILDLNEDLGGYQCLNN 165
Cdd:PRK06710 86 QAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATK-IEHVIVTRIADFLPFPKNLLY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 166 FISQNSDINLDVKKFKP------NSFNRD------------DQVALVMFSSGTTGVSKGVMLTHKNIVArfshckDPTFG 227
Cdd:PRK06710 165 PFVQKKQSNLVVKVSESetihlwNSVEKEvntgvevpcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVS------NTLMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 228 -----NAINPTTAILTVIPFHHGFGMTTTLGY-FTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVE 301
Cdd:PRK06710 239 vqwlyNCKEGEEVVLGVLPFFHVYGMTAVMNLsIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 302 KYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAVLITPDTDVR-PGSTGKIVPFHAVKVVDPTTGKI 380
Cdd:PRK06710 319 EYDISSIRACISGSAPLPVEVQEKFETVTGGKLV-EGYGLTESSPVTHSNFLWEKRvPGSIGVPWPDTEAMIMSLETGEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 381 LGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQH 460
Cdd:PRK06710 398 LPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 461 PYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKwLRGGVKFLDEIPKGSTGKIDRKVLRQMFEK 540
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYK-VPKVYEFRDELPKTTVGKILRRVLIEEEKR 555
|
..
gi 41688574 541 HK 542
Cdd:PRK06710 556 KN 557
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
52-463 |
6.11e-68 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 229.99 E-value: 6.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCS-KN 130
Cdd:COG1022 43 WAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TFQKVLNVKSKLKYVETIIILDLNEDLGGYQCLN--NFISQNSDINLD------VKKFKPnsfnrdDQVALVMFSSGTTG 202
Cdd:COG1022 123 QLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLSldELLALGREVADPaelearRAAVKP------DDLATIIYTSGTTG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 203 VSKGVMLTHKNIVARFSHCKDPTfgnAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVAlmHTFEEKLFLQSLQDYKve 282
Cdd:COG1022 197 RPKGVMLTHRNLLSNARALLERL---PLGPGDRTLSFLPLAHVFERTVSYYALAAGATVA--FAESPDTLAEDLREVK-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 283 stllvPTLMAFFP--------------------KSALV-------EKYD------------------------LSHLKE- 310
Cdd:COG1022 270 -----PTFMLAVPrvwekvyagiqakaeeagglKRKLFrwalavgRRYArarlagkspslllrlkhaladklvFSKLREa 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 311 -------IASGGAPLSKEIGemvkkRFklnF------VRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVvdptt 377
Cdd:COG1022 345 lggrlrfAVSGGAALGPELA-----RF---FralgipVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI----- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 378 gkilgpNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLI-----KYkgyqVAPAE 452
Cdd:COG1022 412 ------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIvtsggKN----VAPQP 481
|
490
....*....|.
gi 41688574 453 IEGILLQHPYI 463
Cdd:COG1022 482 IENALKASPLI 492
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
52-529 |
1.80e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 227.54 E-value: 1.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAeSF--KKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSK 129
Cdd:PRK08314 38 YRELLEEAERLA-GYlqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 130 NTFQKVLNVKSKLKyVETIIILDL-----------------------NEDLGGYQCLNNFISQNSdinldvkKFKPNSFN 186
Cdd:PRK08314 117 ELAPKVAPAVGNLR-LRHVIVAQYsdylpaepeiavpawlraepplqALAPGGVVAWKEALAAGL-------APPPHTAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 187 RDDqVALVMFSSGTTGVSKGVMLTHKNIVARfshckdpTFGNAI----NPTTAILTVIPFHHGFGMTTTL-GYFTCGFRV 261
Cdd:PRK08314 189 PDD-LAVLPYTSGTTGVPKGCMHTHRTVMAN-------AVGSVLwsnsTPESVVLAVLPLFHVTGMVHSMnAPIYAGATV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 262 ALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGL 341
Cdd:PRK08314 261 VLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYV-EGYGL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 342 TETTSAVLITPDTDVRPGSTGkiVPFHAV--KVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEAT-KAIINKDG--W 416
Cdd:PRK08314 340 TETMAQTHSNPPDRPKLQCLG--IPTFGVdaRVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATaEAFIEIDGkrF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 417 LRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVV---QTGKYLN 493
Cdd:PRK08314 418 FRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLrpeARGKTTE 497
|
490 500 510
....*....|....*....|....*....|....*.
gi 41688574 494 EQIVQnFVSSQVSTAKWLRgGVKFLDEIPKGSTGKI 529
Cdd:PRK08314 498 EEIIA-WAREHMAAYKYPR-IVEFVDSLPKSGSGKI 531
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
189-535 |
2.80e-66 |
|
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: 218.69 E-value: 2.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIV--ARFshckdptFGNAINPT--TAILTVIPFHHGFGMTttLGYFTCGFRVALM 264
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVnnGYF-------IGERLGLTeqDRLCIPVPLFHCFGSV--LGVLACLTHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 265 ----HTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYG 340
Cdd:cd05917 73 vfpsPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 341 LTETTSAVLITPDTD---VRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWL 417
Cdd:cd05917 153 MTETSPVSTQTRTDDsieKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 418 RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIV 497
Cdd:cd05917 233 HTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDI 312
|
330 340 350
....*....|....*....|....*....|....*...
gi 41688574 498 QNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd05917 313 KAYCKGKIAHYKVPR-YVFFVDEFPLTVSGKIQKFKLR 349
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
55-536 |
3.46e-65 |
|
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: 217.60 E-value: 3.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 55 FLKLSC---RLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELihslgivkpriifcsknT 131
Cdd:cd05912 4 FAELFEevsRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNEL-----------------A 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQkvlnvkskLKyvetiiildlnedlggyqclnnfisqnsdiNLDVKKfkpnsfnrdDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd05912 67 FQ--------LK------------------------------DSDVKL---------DDIATIMYTSGTTGKPKGVQQTF 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVARFSHCKDpTFGnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVPT-- 289
Cdd:cd05912 100 GNHWWSAIGSAL-NLG--LTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTml 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 290 --LMAFFPksalvEKYDlSHLKEIASGGAPLSKEIGEMVKKRfklNF-VRQGYGLTETTS-AVLITP-DTDVRPGSTGKI 364
Cdd:cd05912 177 qrLLEILG-----EGYP-NNLRCILLGGGPAPKPLLEQCKEK---GIpVYQSYGMTETCSqIVTLSPeDALNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 365 VPFHAVKVVDPTTGkilgPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYK 444
Cdd:cd05912 248 LFPVELKIEDDGQP----PYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 445 GYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQtgKYLNEQIVQNFVSSQVstAKWLR-GGVKFLDEIPK 523
Cdd:cd05912 323 GENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKL--AKYKVpKKIYFVDELPR 398
|
490
....*....|...
gi 41688574 524 GSTGKIDRKVLRQ 536
Cdd:cd05912 399 TASGKLLRHELKQ 411
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
52-535 |
6.22e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 221.18 E-value: 6.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKY-GLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKN 130
Cdd:PRK05677 52 YGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLAN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TFQKVLNV--KSKLKYVETIIILDLNEDLGGYqcLNNF-------------ISQNSDINlDV------KKFKPNSFNRDD 189
Cdd:PRK05677 132 MAHLAEKVlpKTGVKHVIVTEVADMLPPLKRL--LINAvvkhvkkmvpayhLPQAVKFN-DAlakgagQPVTEANPQADD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 190 qVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTttlgyFTCGfrvALMHTFEE 269
Cdd:PRK05677 209 -VAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIAPLPLYHIYAFT-----FHCM---AMMLIGNH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 270 KL----------FLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGY 339
Cdd:PRK05677 280 NIlisnprdlpaMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 340 GLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRS 419
Cdd:PRK05677 359 GMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 420 GDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQN 499
Cdd:PRK05677 438 GDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVME 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 41688574 500 FVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PRK05677 518 HMRANLTGYKVPK-AVEFRDELPTTNVGKILRRELR 552
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
52-535 |
1.20e-64 |
|
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: 216.82 E-value: 1.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSknt 131
Cdd:cd05972 3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqkvlnvksklkyvetiiildlnedlggyqclnnfisqnsdinldvkkfkpnsfnrDDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd05972 80 --------------------------------------------------------AEDPALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KnivARFSHCKDPTFGNAINPTTAILTVI--------------PFHHGfgmTTTLGYftcgfrvaLMHTFEEKLFLQSLQ 277
Cdd:cd05972 104 S---YPLGHIPTAAYWLGLRPDDIHWNIAdpgwakgawssffgPWLLG---ATVFVY--------EGPRFDAERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 278 DYKVESTLLVPTLMAFFPKsALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTSAVLITPDTDVR 357
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFPDMPVK 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 358 PGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFK-GDM-IMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVD 435
Cdd:cd05972 248 PGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKlPPPgLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 436 RLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIV---QNFVSSQVSTAKWLR 512
Cdd:cd05972 326 RADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAeelQGHVKKVLAPYKYPR 405
|
490 500
....*....|....*....|...
gi 41688574 513 gGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd05972 406 -EIEFVEELPKTISGKIRRVELR 427
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
10-535 |
1.26e-64 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 220.31 E-value: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 10 PEPFHPLADgtageqMF-YALSRYADISGCIALTNAHTkenvlyeeFLKLSCRlAESFKKY-----GLKQNDTIAVCSEN 83
Cdd:PRK08974 19 PDRYQSLVD------MFeQAVARYADQPAFINMGEVMT--------FRKLEER-SRAFAAYlqnglGLKKGDRVALMMPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 84 GLQFFLPLIASLYLGIIAAPVSDKYIERELIHSL------GIVkprIIFCSKNTFQKVLNvKSKLKYVetiIILDLNEDL 157
Cdd:PRK08974 84 LLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLndsgakAIV---IVSNFAHTLEKVVF-KTPVKHV---ILTRMGDQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 158 G-GYQCLNNFISQNsdinldVKKFKPN-------SF-----------------NRDDqVALVMFSSGTTGVSKGVMLTHK 212
Cdd:PRK08974 157 StAKGTLVNFVVKY------IKRLVPKyhlpdaiSFrsalhkgrrmqyvkpelVPED-LAFLQYTGGTTGVAKGAMLTHR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 213 NIVARFSHCKdPTFGNAINPTTA-ILTVIPFHHGFGMTTT-LGYFTCGFRvALMHTFEEKL--FLQSLQDYKVESTLLVP 288
Cdd:PRK08974 230 NMLANLEQAK-AAYGPLLHPGKElVVTALPLYHIFALTVNcLLFIELGGQ-NLLITNPRDIpgFVKELKKYPFTAITGVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 289 TLMaffpkSALV-----EKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAVLITP-DTDVRPGSTG 362
Cdd:PRK08974 308 TLF-----NALLnneefQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLL-EGYGLTECSPLVSVNPyDLDYYSGSIG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 363 KIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIK 442
Cdd:PRK08974 382 LPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMIL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 443 YKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFLDEIP 522
Cdd:PRK08974 460 VSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKI-FVVKKDPSLTEEELITHCRRHLTGYKVPK-LVEFRDELP 537
|
570
....*....|...
gi 41688574 523 KGSTGKIDRKVLR 535
Cdd:PRK08974 538 KSNVGKILRRELR 550
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
15-537 |
5.34e-64 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 218.49 E-value: 5.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 15 PLADGTAGEQMFYALSRYADISgciALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIAS 94
Cdd:PRK12583 14 PLLTQTIGDAFDATVARFPDRE---ALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 95 LYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSK--------NTFQKVL-NVKS---------KLKYVETIIILDLNED 156
Cdd:PRK12583 91 ARIGAILVNINPAYRASELEYALGQSGVRWVICADafktsdyhAMLQELLpGLAEgqpgalaceRLPELRGVVSLAPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 157 lGGYQCLNNFISQNSDINLDVKKFKPNSFNRDDQVALvMFSSGTTGVSKGVMLTHKNIV--ARFShckdptfGNAINPTT 234
Cdd:PRK12583 171 -PGFLAWHELQARGETVSREALAERQASLDRDDPINI-QYTSGTTGFPKGATLSHHNILnnGYFV-------AESLGLTE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 235 AILTVIP--FHHGFGMT-TTLGYFTCGFRVAL-MHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKE 310
Cdd:PRK12583 242 HDRLCVPvpLYHCFGMVlANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 311 IASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLITPDTD---VRPGSTGKIVPFHAVKVVDPTtGKILGPNETG 387
Cdd:PRK12583 322 GIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADdleRRVETVGRTQPHLEVKVVDPD-GATVPRGEIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 388 ELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAG 467
Cdd:PRK12583 401 ELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQ 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 468 VTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK12583 481 VFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPR-YFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-535 |
1.75e-63 |
|
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: 213.69 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:cd05934 6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDPAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQkvlnvksklkyvetiiildlnedlggyqclnnfisqnsdinldvkkfkpnsfnrddqvalvmFSSGTTGVSKGVMLTH 211
Cdd:cd05934 86 IL--------------------------------------------------------------YTSGTTGPPKGVVITH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNivARFShCKDPTFGNAINPTTAILTVIPFHHGFGMTTT-LGYFTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVPTL 290
Cdd:cd05934 104 AN--LTFA-GYYSARRFGLGEDDVYLTVLPLFHINAQAVSvLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 291 MAFFPKSALVEKyDLSHLKEIASGGAPLSKEIGEMvKKRFKLNFVrQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAV 370
Cdd:cd05934 181 LSYLLAQPPSPD-DRAHRLRAAYGAPNPPELHEEF-EERFGVRLL-EGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 371 KVVDPTtGKILGPNETGELYFK---GDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQ 447
Cdd:cd05934 258 RIVDDD-GQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGEN 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 448 VAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTG 527
Cdd:cd05934 336 ISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPR-YIRFVDDLPKTPTE 414
|
....*...
gi 41688574 528 KIDRKVLR 535
Cdd:cd05934 415 KVAKAQLR 422
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
52-535 |
2.02e-63 |
|
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: 215.70 E-value: 2.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKN- 130
Cdd:cd05959 32 YAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGEl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 --TFQKVLNVKSKLKYveTIIILDLNEDLGGYQCLNNFISQNSDinldvkKFKPNSFNRDDqVALVMFSSGTTGVSKGVM 208
Cdd:cd05959 112 apVLAAALTKSEHTLV--VLIVSGGAGPEAGALLLAELVAAEAE------QLKPAATHADD-PAFWLYSSGSTGRPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 209 LTHKNIVARFSHCKDPTFGnaINPTTAILTV--IPFHHGFGMTTTLGyFTCGFRVALMHTF-EEKLFLQSLQDYKveSTL 285
Cdd:cd05959 183 HLHADIYWTAELYARNVLG--IREDDVCFSAakLFFAYGLGNSLTFP-LSVGATTVLMPERpTPAAVFKRIRRYR--PTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 286 L--VPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAVLITPDTDVRPGSTGK 363
Cdd:cd05959 258 FfgVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDIL-DGIGSTEMLHIFLSNRPGRVRYGTTGK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 364 IVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKY 443
Cdd:cd05959 337 PVPGYEVELRDED-GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 444 KGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQI---VQNFVSSQVSTAKWLRgGVKFLDE 520
Cdd:cd05959 415 SGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALeeeLKEFVKDRLAPYKYPR-WIVFVDE 493
|
490
....*....|....*
gi 41688574 521 IPKGSTGKIDRKVLR 535
Cdd:cd05959 494 LPKTATGKIQRFKLR 508
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
52-470 |
3.29e-60 |
|
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: 205.52 E-value: 3.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPvsdkyierelihslgivkpriIFCSKNT 131
Cdd:cd05907 8 WAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP---------------------IYPTSSA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKvlnvksklkyvetiiildlnedlggyqclnNFISQNSDINLdvkKFKPNSfnrdDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd05907 67 EQI------------------------------AYILNDSEAKA---LFVEDP----DDLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVarfSHCKdpTFGNAINPTT--AILTVIPFHHGFGMTTTLgYFTCGFRVALMHTFEEKLFLQSLQDYKvestllvPT 289
Cdd:cd05907 110 RNIL---SNAL--ALAERLPATEgdRHLSFLPLAHVFERRAGL-YVPLLAGARIYFASSAETLLDDLSEVR-------PT 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 290 LMAFFP------------------KSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKrfkLNF-VRQGYGLTETTSAVLI 350
Cdd:cd05907 177 VFLAVPrvwekvyaaikvkavpglKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRA---LGIpVYEGYGLTETSAVVTL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 351 TPDTDVRPGSTGKivpfhavkVVDPTTGKIlgpNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGH 430
Cdd:cd05907 254 NPPGDNRIGTVGK--------PLPGVEVRI---ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGF 322
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 41688574 431 FYIVDRLKSLIKY-KGYQVAPAEIEGILLQHPYIVDAGVTG 470
Cdd:cd05907 323 LHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
39-540 |
4.06e-60 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 206.35 E-value: 4.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 39 IALTNAHTKENvlYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLG 118
Cdd:PRK03640 19 TAIEFEEKKVT--FMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 119 IVKPRIIFCSKNtFQKVLNVKSKLKYvetiiildlnEDLggyqclnnfisqnsdINLDVKKFKPNSFNRDDQVALVMFSS 198
Cdd:PRK03640 97 DAEVKCLITDDD-FEAKLIPGISVKF----------AEL---------------MNGPKEEAEIQEEFDLDEVATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKNivarfsHCKDPTfGNAIN----PTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQ 274
Cdd:PRK03640 151 GTTGKPKGVIQTYGN------HWWSAV-GSALNlgltEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKINK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 275 SLQDYKVESTLLVPTLMaffpkSALVEKYDL----SHLKEIASGGAPLSKEIGEMVKKRfklNF-VRQGYGLTETTSAVL 349
Cdd:PRK03640 224 LLQTGGVTIISVVSTML-----QRLLERLGEgtypSSFRCMLLGGGPAPKPLLEQCKEK---GIpVYQSYGMTETASQIV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 350 ITPDTDVRP--GSTGKivP-FHA-VKVVDptTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYY 425
Cdd:PRK03640 296 TLSPEDALTklGSAGK--PlFPCeLKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 426 DNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVvqTGKYLNEQIVQNFVSSQV 505
Cdd:PRK03640 371 DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV--KSGEVTEEELRHFCEEKL 448
|
490 500 510
....*....|....*....|....*....|....*
gi 41688574 506 STAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMFEK 540
Cdd:PRK03640 449 AKYKVPK-RFYFVEELPRNASGKLLRHELKQLVEE 482
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
52-534 |
1.08e-59 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 203.83 E-value: 1.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKnt 131
Cdd:TIGR01923 2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqkvlnvKSKLKYVETIIILDLNedlggyqclnnfISQNSDINLdvkkfkpNSFNRDDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:TIGR01923 80 -------LLEEKDFQADSLDRIE------------AAGRYETSL-------SASFNMDQIATLMFTSGTTGKPKAVPHTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVARFSHCKDpTFGnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEklFLQSLQDYKVESTLLVPTLM 291
Cdd:TIGR01923 134 RNHYASAVGSKE-NLG--FTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 292 AFFPKSALVEkydlSHLKEIASGGAPLSKEigeMVKKRFKLNF-VRQGYGLTETTSAVL-ITPDTDVRPGSTGKIVPFHA 369
Cdd:TIGR01923 209 NRLLDEGGHN----ENLRKILLGGSAIPAP---LIEEAQQYGLpIYLSYGMTETCSQVTtATPEMLHARPDVGRPLAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 370 VKVVDPttgkilGPNETGELYFKGDMIMKSYYNNEEATKAIiNKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVA 449
Cdd:TIGR01923 282 IKIKVD------NKEGHGEIMVKGANLMKGYLYQGELTPAF-EQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 450 PAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgvVVQTGKYLNEQIVQNFVSSQVSTAKWlrgGVKF--LDEIPKGSTG 527
Cdd:TIGR01923 355 PEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVA--YIVSESDISQAKLIAYLTEKLAKYKV---PIAFekLDELPYNASG 429
|
....*..
gi 41688574 528 KIDRKVL 534
Cdd:TIGR01923 430 KILRNQL 436
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
52-540 |
1.19e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 207.16 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK05605 60 YAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKyVETIIILDLNEDLGGYQCL--------------------NNFIS----QNSDINLDVKKFKPNSFNR 187
Cdd:PRK05605 140 APTVERLRRTTP-LETIVSVNMIAAMPLLQRLalrlpipalrkaraaltgpaPGTVPwetlVDAAIGGDGSDVSHPRPTP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDqVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKD--PTFGNaiNPTTaILTVIPFHHGFGMT--TTLGYFtCGFRVAL 263
Cdd:PRK05605 219 DD-VALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvPGLGD--GPER-VLAALPMFHAYGLTlcLTLAVS-IGGELVL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 264 MHTFEEKLFLQSLQdyKVESTLL--VPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGL 341
Cdd:PRK05605 294 LPAPDIDLILDAMK--KHPPTWLpgVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLV-EGYGL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 342 TETTSAVLITP-DTDVRPGSTGkiVPFHA--VKVVDP-TTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINkDGWL 417
Cdd:PRK05605 371 TETSPIIVGNPmSDDRRPGYVG--VPFPDteVRIVDPeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-DGWF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 418 RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIV 497
Cdd:PRK05605 448 RTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGL 527
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 41688574 498 QNFVSSQVSTAKWLRGGVKFlDEIPKGSTGKIDRKVLRQMFEK 540
Cdd:PRK05605 528 RAYCREHLTRYKVPRRFYHV-DELPRDQLGKVRRREVREELLE 569
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
61-536 |
3.66e-59 |
|
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: 204.79 E-value: 3.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 61 RLAESFKKYGLKQNDTIAVCSENGLQFFlpliaSLYLGIIAA-----PVSDKYIERELIHSLGIVKPRIIFCSKNTFQKV 135
Cdd:cd12119 37 RLANALRRLGVKPGDRVATLAWNTHRHL-----ELYYAVPGMgavlhTINPRLFPEQIAYIINHAEDRVVFVDRDFLPLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 136 LNVKSKLKYVETIIILDLNED-----LGGYQCLNNFISQNSDiNLDVKKFKPNSfnrddqVALVMFSSGTTGVSKGVMLT 210
Cdd:cd12119 112 EAIAPRLPTVEHVVVMTDDAAmpepaGVGVLAYEELLAAESP-EYDWPDFDENT------AAAICYTSGTTGNPKGVVYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 211 HKNIVarfSHC-----KDptfGNAINPTTAILTVIP-FH-HGFGM--TTTLgyftCGFRVALMHTFEE-KLFLQSLQDYK 280
Cdd:cd12119 185 HRSLV---LHAmaallTD---GLGLSESDVVLPVVPmFHvNAWGLpyAAAM----VGAKLVLPGPYLDpASLAELIEREG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 281 VESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKlnFVRQGYGLTETTS-AVLITPDTDVRPG 359
Cdd:cd12119 255 VTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGV--RVIHAWGMTETSPlGTVARPPSEHSNL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 360 S----------TGKIVPFHAVKVVDPTTGKIlgP---NETGELYFKGDMIMKSYYNNEEATKAIiNKDGWLRSGDIAYYD 426
Cdd:cd12119 333 SedeqlalrakQGRPVPGVELRIVDDDGREL--PwdgKAVGELQVRGPWVTKSYYKNDEESEAL-TEDGWLRTGDVATID 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 427 NDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVs 506
Cdd:cd12119 410 EDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKV- 488
|
490 500 510
....*....|....*....|....*....|.
gi 41688574 507 tAKW-LRGGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd12119 489 -AKWwLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
196-537 |
4.31e-57 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 200.04 E-value: 4.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 196 FSSGTTGVSKGVMLTHKNIV--ARFShckdptfGNAINPTTA--ILTVIPFHHGFGMTT-TLGYFTCGfrvALM----HT 266
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILnnGYFI-------GEAMKLTEEdrLCIPVPLYHCFGMVLgNLACVTHG---ATMvypgEG 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 FEEKLFLQSLQDYKVESTLLVPTlMaF--------FPKsalvekYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQG 338
Cdd:PRK08315 276 FDPLATLAAVEEERCTALYGVPT-M-FiaeldhpdFAR------FDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 YGLTETtSAV----LITPDTDVRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKD 414
Cdd:PRK08315 348 YGMTET-SPVstqtRTDDPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 415 GWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNE 494
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE 506
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 41688574 495 QIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK08315 507 EDVRDFCRGKIAHYKIPR-YIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
29-536 |
2.08e-56 |
|
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: 197.72 E-value: 2.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 29 LSRYADISG---CIALTNAHTKENVL-YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPV 104
Cdd:cd05970 23 VDAMAKEYPdklALVWCDDAGEERIFtFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 105 SDKYIERELIHSLGIVKPRIIFC--SKNTFQKVLNVKSKLkYVETIIILDLNEDLGGYQCLNNFISQNSDInldvkkFKP 182
Cdd:cd05970 103 THQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPEC-PSKPKLVWVGDPVPEGWIDFRKLIKNASPD------FER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 183 ---NSFNRDDQVALVMFSSGTTGVSKgvMLTHKNIVArFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTL-GYFTCG 258
Cdd:cd05970 176 ptaNSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYP-LGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIyGQWIAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 259 FRVAL--MHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALvEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVR 336
Cdd:cd05970 253 AAVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK-LM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 337 QGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDM-----IMKSYYNNEEATKAII 411
Cdd:cd05970 331 EGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 412 nKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKY 491
Cdd:cd05970 410 -HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYE 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 41688574 492 LNEQI---VQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05970 489 PSEELkkeLQDHVKKVTAPYKYPR-IVEFVDELPKTISGKIRRVEIRE 535
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
45-536 |
2.19e-56 |
|
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: 195.34 E-value: 2.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 45 HTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLgivkpri 124
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRL------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 125 ifcsKNTFQKVlnvksklkyvetiIILDLNEDLggyqclnnfisqnsdinldvkkfkpnsfnrddqvALVMFSSGTTGVS 204
Cdd:cd05971 75 ----SNSGASA-------------LVTDGSDDP----------------------------------ALIIYTSGTTGPP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 205 KGVMLTHK-----NIVARFSHCKDPTFGNaINPTTA--------ILTVIPFHHgFGMTTtLGYftcgfrvaLMHTFEEKL 271
Cdd:cd05971 104 KGALHAHRvllghLPGVQFPFNLFPRDGD-LYWTPAdwawigglLDVLLPSLY-FGVPV-LAH--------RMTKFDPKA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 272 FLQSLQDYKVESTLLVPT---LMAFFPKSalVEKYDLShLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTSAV 348
Cdd:cd05971 173 ALDLMSRYGVTTAFLPPTalkMMRQQGEQ--LKHAQVK-LRAIATGGESLGEELLGWAREQFGVE-VNEFYGQTECNLVI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 349 LITPDT-DVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGD--MIMKSYYNNEEATKAIINKDgWLRSGDIAYY 425
Cdd:cd05971 249 GNCSALfPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPdpVAFLGYWNNPSATEKKMAGD-WLLTGDLGRK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 426 DNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQI---VQNFVS 502
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALareIQELVK 406
|
490 500 510
....*....|....*....|....*....|....
gi 41688574 503 SQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05971 407 TRLAAHEYPR-EIEFVNELPRTATGKIRRRELRA 439
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
52-537 |
2.11e-55 |
|
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: 193.70 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGlKQNDTIAVCSENGLQFFLPLIASLYLGIIaaPVSDKYI--ERELIHSLGIVKPRIIFCSK 129
Cdd:cd05909 10 YRKLLTGAIALARKLAKMT-KEGENVGVMLPPSAGGALANFALALSGKV--PVMLNYTagLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 130 nTFQKVLNVKsKLKYVET---IIIL-DLNEDLGGYQCLNNFI-----SQNSDINLDVKKFKPnsfnrdDQVALVMFSSGT 200
Cdd:cd05909 87 -QFIEKLKLH-HLFDVEYdarIVYLeDLRAKISKADKCKAFLagkfpPKWLLRIFGVAPVQP------DDPAVILFTSGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 201 TGVSKGVMLTHKNIVARFSHCKdptfgNAINPTT--AILTVIPFHHGFGMTTTLGY-FTCGFRVALM-HTFEEKLFLQSL 276
Cdd:cd05909 159 EGLPKGVVLSHKNLLANVEQIT-----AIFDPNPedVVFGALPFFHSFGLTGCLWLpLLSGIKVVFHpNPLDYKKIPELI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 277 QDYKVESTLLVPTLMAFFPKSAlvEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTSAVLI-TPDTD 355
Cdd:cd05909 234 YDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECSPVISVnTPQSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 356 VRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVD 435
Cdd:cd05909 311 NKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 436 RLKSLIKYKGYQVAPAEIEGILLQH-PYIVDAGVTGIPDEAAGElpaAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRGG 514
Cdd:cd05909 390 RLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE---KIVLLTTTTDTDPSSLNDILKNAGISNLAKPSY 466
|
490 500
....*....|....*....|...
gi 41688574 515 VKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:cd05909 467 IHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
52-535 |
2.01e-53 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 189.85 E-value: 2.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKN- 130
Cdd:PRK07059 51 YGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 --TFQKVLNvKSKLKYVetiIILDLNEDLGGYQCLNNFISQNsdinldVKK------------------------FKPNS 184
Cdd:PRK07059 131 atTVQQVLA-KTAVKHV---VVASMGDLLGFKGHIVNFVVRR------VKKmvpawslpghvrfndalaegarqtFKPVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 185 FNRDDqVALVMFSSGTTGVSKGVMLTHKNIVA---RFSHCKDPTFGNAINPTT-AILTVIPFHHGFGMTTT--LGYFTCG 258
Cdd:PRK07059 201 LGPDD-VAFLQYTGGTTGVSKGATLLHRNIVAnvlQMEAWLQPAFEKKPRPDQlNFVCALPLYHIFALTVCglLGMRTGG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 259 FRVALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLnFVRQG 338
Cdd:PRK07059 280 RNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGC-PITEG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 YGLTETTSAVLITP-DTDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWL 417
Cdd:PRK07059 359 YGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 418 RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgVVVQTGKYLNEQIV 497
Cdd:PRK07059 438 RTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKL-FVVKKDPALTEEDV 516
|
490 500 510
....*....|....*....|....*....|....*...
gi 41688574 498 QNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PRK07059 517 KAFCKERLTNYKRPK-FVEFRTELPKTNVGKILRRELR 553
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
10-538 |
5.18e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 188.27 E-value: 5.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 10 PEPFHPL-ADGTAGEQMFYALSRYAD----ISGCIALTnahtkenvlYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENG 84
Cdd:PRK06188 2 ATMADLLhSGATYGHLLVSALKRYPDrpalVLGDTRLT---------YGQLADRISRYIQAFEALGLGTGDAVALLSLNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 85 LQFFLPLIASLYLGI-------IAAPVSDKYIERELIHSLGIVKPriifcskNTFQK----VLNVKSKLKYVETIIILDL 153
Cdd:PRK06188 73 PEVLMAIGAAQLAGLrrtalhpLGSLDDHAYVLEDAGISTLIVDP-------APFVEralaLLARVPSLKHVLTLGPVPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 154 NEDLGGyqclnnfisqnsdinlDVKKFKPN---SFNRDDQVALVMFSSGTTGVSKGVMLTHKNIV-------ARFSHCKD 223
Cdd:PRK06188 146 GVDLLA----------------AAAKFGPAplvAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIAtmaqiqlAEWEWPAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 224 PTFgnainpttaiLTVIPFHHGFGMTTTLGYFTCGFrVALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKY 303
Cdd:PRK06188 210 PRF----------LMCTPLSHAGGAFFLPTLLRGGT-VIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 304 DLSHLKEIASGGAPLS----KEIGEmvkkRFKLNFVrQGYGLTETTSAVLI------TPDTDVRPGSTGKIVPFHAVKVV 373
Cdd:PRK06188 279 DLSSLETVYYGASPMSpvrlAEAIE----RFGPIFA-QYYGQTEAPMVITYlrkrdhDPDDPKRLTSCGRPTPGLRVALL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 374 DPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEI 453
Cdd:PRK06188 354 DED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 454 EGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQ---VSTAKwlrgGVKFLDEIPKGSTGKID 530
Cdd:PRK06188 432 EDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERkgsVHAPK----QVDFVDSLPLTALGKPD 507
|
....*...
gi 41688574 531 RKVLRQMF 538
Cdd:PRK06188 508 KKALRARY 515
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
52-536 |
6.68e-53 |
|
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: 185.96 E-value: 6.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESF-KKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIfcskn 130
Cdd:cd05941 14 YADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 tfqkvlnvksklkyvetiiiLDLnedlggyqclnnfisqnsdinldvkkfkpnsfnrddqvALVMFSSGTTGVSKGVMLT 210
Cdd:cd05941 89 --------------------LDP--------------------------------------ALILYTSGTTGRPKGVVLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 211 HKNIVA---------RFShckdptfgnainPTTAILTVIPFHHGFGMTTTL-GYFTCGFRVALMHTFEEKLFLQSlqDYK 280
Cdd:cd05941 111 HANLAAnvralvdawRWT------------EDDVLLHVLPLHHVHGLVNALlCPLFAGASVEFLPKFDPKEVAIS--RLM 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 281 VESTLL--VPT----LMAF----FPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKlNFVRQGYGLTETTSAvLI 350
Cdd:cd05941 177 PSITVFmgVPTiytrLLQYyeahFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITG-HTLLERYGMTEIGMA-LS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 351 TP-DTDVRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDG 429
Cdd:cd05941 255 NPlDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 430 HFYIVDRLKS-LIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKY-LNEQIVQNFVSSQVST 507
Cdd:cd05941 335 YYWILGRSSVdIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAaLSLEELKEWAKQRLAP 414
|
490 500
....*....|....*....|....*....
gi 41688574 508 AKWLRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05941 415 YKRPR-RLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
34-531 |
1.19e-52 |
|
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: 185.72 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 34 DISGCIALTnahtkenvlYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIEREL 113
Cdd:cd05914 1 LYYGGEPLT---------YKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 114 IHSLGIVKPRIIFCSKNtfqkvlnvksklkyvetiiildlnedlggyqclnnfisqnsdinldvkkfkpnsfnrdDQVAL 193
Cdd:cd05914 72 HHILNHSEAKAIFVSDE----------------------------------------------------------DDVAL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 194 VMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTFgnaINPTTAILTVIPFHHGFGMTTTLGY-FTCGFRVALMHTFEEKLf 272
Cdd:cd05914 94 INYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL---LGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAK- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 273 LQSLQDYKVESTLLVPTL--------MAFFPKSALVE-KYDLS----------------------HLKEIASGGAPLSKE 321
Cdd:cd05914 170 IIALAFAQVTPTLGVPVPlviekifkMDIIPKLTLKKfKFKLAkkinnrkirklafkkvheafggNIKEFVIGGAKINPD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 322 IGEMVKkrfKLNF-VRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTTgkilgPNETGELYFKGDMIMKSY 400
Cdd:cd05914 250 VEEFLR---TIGFpYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDP-----ATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 401 YNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLI-KYKGYQVAPAEIEGILLQHPYIVDAGV---------TG 470
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVvvqekklvaLA 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41688574 471 IPDEAAGELPAAGVVVQTGKYLNEQIVQnfVSSQVSTAKWLRGGVKFLDEIPKGSTGKIDR 531
Cdd:cd05914 402 YIDPDFLDVKALKQRNIIDAIKWEVRDK--VNQKVPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
14-535 |
6.34e-52 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 187.47 E-value: 6.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 14 HPLADGTAGEQMFYALSRYADISG-CIALT------NAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQ 86
Cdd:PRK07529 16 VPLAARDLPASTYELLSRAAARHPdAPALSflldadPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 87 FFLPLIASLYLGIiAAPVSdKYIERELIHS-LGIVKPRIIFCSK-----NTFQKVLNVKSKLKYVETIIILDLNEDLGGY 160
Cdd:PRK07529 96 THFALWGGEAAGI-ANPIN-PLLEPEQIAElLRAAGAKVLVTLGpfpgtDIWQKVAEVLAALPELRTVVEVDLARYLPGP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 161 QCL-------------NNF---ISQNSDINLdvkkFKPNSFNRDDqVALVMFSSGTTGVSKGVMLTHKNIVArfshckdp 224
Cdd:PRK07529 174 KRLavplirrkahariLDFdaeLARQPGDRL----FSGRPIGPDD-VAAYFHTGGTTGMPKLAQHTHGNEVA-------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 225 tfgNA--------INPTTAILTVIPFHHGFG-MTTTLGYFTCGFRVALM--HTFEEKLFLQSL----QDYKVESTLLVPT 289
Cdd:PRK07529 241 ---NAwlgalllgLGPGDTVFCGLPLFHVNAlLVTGLAPLARGAHVVLAtpQGYRGPGVIANFwkivERYRINFLSGVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 290 LMAffpksAL----VEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTSAVLITP-DTDVRPGSTGKI 364
Cdd:PRK07529 318 VYA-----ALlqvpVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVR-IVEGYGLTEATCVSSVNPpDGERRIGSVGLR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 365 VPFHAVKVV--DPTtGKIL---GPNETGELYFKGDMIMKSYYNnEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKS 439
Cdd:PRK07529 392 LPYQRVRVVilDDA-GRYLrdcAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKD 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 440 LIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRGGVKFLD 519
Cdd:PRK07529 470 LIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAVPKHVRILD 549
|
570
....*....|....*.
gi 41688574 520 EIPKGSTGKIDRKVLR 535
Cdd:PRK07529 550 ALPKTAVGKIFKPALR 565
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
52-536 |
1.02e-51 |
|
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: 182.58 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKnt 131
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqkvlnvksklkyvetiiildlnedlggyqclnnfisqnsdinldvkKFKPNSFNRD-DQVALVMFSSGTTGVSKGVMLT 210
Cdd:cd05903 82 -----------------------------------------------RFRQFDPAAMpDAVALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 211 HKNIVARFS-HCKDPTFGnainPTTAILTVIPFHHGFGMtttLGYFTC----GFRVALMHTFEEKLFLQSLQDYKVESTL 285
Cdd:cd05903 115 HNTLSASIRqYAERLGLG----PGDVFLVASPMAHQTGF---VYGFTLplllGAPVVLQDIWDPDKALALMREHGVTFMM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 286 LVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLnFVRQGYGLTETTSAVLITPDTDV--RPGSTGK 363
Cdd:cd05903 188 GATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTECPGAVTSITPAPEdrRLYTDGR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 364 IVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINkDGWLRSGDIAYYDNDGHFYIVDRLKSLIKY 443
Cdd:cd05903 267 PLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 444 KGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLN-EQIVQNFVSSQVSTAKWLRgGVKFLDEIP 522
Cdd:cd05903 345 GGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTfDELVAYLDRQGVAKQYWPE-RLVHVDDLP 423
|
490
....*....|....
gi 41688574 523 KGSTGKIDRKVLRQ 536
Cdd:cd05903 424 RTPSGKVQKFRLRE 437
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
62-535 |
1.69e-51 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 184.70 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 62 LAESFKKY-----GLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSL---GIVKPRII--FCSknT 131
Cdd:PRK08751 59 LVEQFAAYllgelQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLidsGASVLVVIdnFGT--T 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLnVKSKLKYVETIIILDLnedLG-------------------GYQcLNNFISQNSDINLDVKKFKPNSFNRDDQVA 192
Cdd:PRK08751 137 VQQVI-ADTPVKQVITTGLGDM---LGfpkaalvnfvvkyvkklvpEYR-INGAIRFREALALGRKHSMPTLQIEPDDIA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 193 LVMFSSGTTGVSKGVMLTHKNIVARF--SHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFT--CGFRVALMHTFE 268
Cdd:PRK08751 212 FLQYTGGTTGVAKGAMLTHRNLVANMqqAHQWLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMkiGGCNHLISNPRD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 269 EKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAV 348
Cdd:PRK08751 292 MPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLV-EAYGLTETSPAA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 349 LITP-DTDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDN 427
Cdd:PRK08751 371 CINPlTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 428 DGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgVVVQTGKYLNEQIVQNFVSSQVST 507
Cdd:PRK08751 450 QGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKV-VIVKKDPALTAEDVKAHARANLTG 528
|
490 500
....*....|....*....|....*...
gi 41688574 508 AKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PRK08751 529 YKQPR-IIEFRKELPKTNVGKILRRELR 555
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
191-529 |
6.00e-51 |
|
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: 177.69 E-value: 6.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 191 VALVMFSSGTTGVSKGVMLTHKNIV---ARFSHCKDPTFGNAInpttaiLTVIPFHHGFGMTTtlGYFTC---GFRVALM 264
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLraaAAWADCADLTEDDRY------LIINPFFHTFGYKA--GIVAClltGATVVPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 265 HTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTET 344
Cdd:cd17638 74 AVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSAVLITPDTDVRPGST--GKIVPFHAVKVVDPttgkilgpnetGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDI 422
Cdd:cd17638 154 GVATMCRPGDDAETVATtcGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 423 AYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVS 502
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCR 302
|
330 340
....*....|....*....|....*..
gi 41688574 503 SQVSTAKWLRgGVKFLDEIPKGSTGKI 529
Cdd:cd17638 303 ERLANYKVPR-FVRFLDELPRNASGKV 328
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
52-539 |
1.40e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 181.67 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK08316 39 YAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKYVETI--IILDLNEDLGGYQCLNNFISQNSDINLDVkkfkpnsFNRDDQVALVMFSSGTTGVSKGVML 209
Cdd:PRK08316 119 APTAEAALALLPVDTLIlsLVLGGREAPGGWLDFADWAEAGSVAEPDV-------ELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 210 THKNIVARFSHCkdpTFGNAINPTTAILTVIPFHHGFGMTTTLG-YFTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVP 288
Cdd:PRK08316 192 THRALIAEYVSC---IVAGDMSADDIPLHALPLYHCAQLDVFLGpYLYVGATNVILDAPDPELILRTIEAERITSFFAPP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 289 TLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRF-KL---NFvrqgYGLTET--TSAVLITPDTDVRPGSTG 362
Cdd:PRK08316 269 TVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLpGLrfyNC----YGQTEIapLATVLGPEEHLRRPGSAG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 363 KIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIK 442
Cdd:PRK08316 345 RPVLNVETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIK 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 443 YKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKwLRGGVKFLDEIP 522
Cdd:PRK08316 423 TGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFK-VPKRVIFVDELP 501
|
490
....*....|....*..
gi 41688574 523 KGSTGKIDRKVLRQMFE 539
Cdd:PRK08316 502 RNPSGKILKRELRERYA 518
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
52-535 |
1.98e-50 |
|
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: 179.24 E-value: 1.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIErelihslGIVKPRIifcsKNT 131
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGP-------EAIRDRL----ENS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKyvetiiildlnedlggyqclnnfisqnsdinldvKKFKPNSfnrddqVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd05969 72 EAKVLITTEELY----------------------------------ERTDPED------PTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVAR---------------FSHCKDPtfGNAINPTTAILTviPFHHGFGMTTTLGyftcgfrvalmhTFEEKLFLQSL 276
Cdd:cd05969 112 DAMIFYyftgkyvldlhpddiYWCTADP--GWVTGTVYGIWA--PWLNGVTNVVYEG------------RFDAESWYGII 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 277 QDYKVESTLLVPTLMAFFPKS--ALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFvRQGYGLTETTSAVLIT-PD 353
Cdd:cd05969 176 ERVKVTVWYTAPTAIRMLMKEgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPI-HDTWWQTETGSIMIANyPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 354 TDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDM--IMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHF 431
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTKGILALKPGWpsMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 432 YIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG----KYLNEQIVqNFVSSQVST 507
Cdd:cd05969 333 WFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfepsDELKEEII-NFVRQKLGA 411
|
490 500
....*....|....*....|....*...
gi 41688574 508 AKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd05969 412 HVAPR-EIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
52-537 |
3.46e-49 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 178.48 E-value: 3.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKY-GLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIfCSKN 130
Cdd:PRK12492 52 YAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAL-VYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TF----QKVLNvKSKLKYVETIIILDLNEDLGGYqCLNNFISQnsdinldVKKFKPN-------SFNRD----------- 188
Cdd:PRK12492 131 MFgklvQEVLP-DTGIEYLIEAKMGDLLPAAKGW-LVNTVVDK-------VKKMVPAyhlpqavPFKQAlrqgrglslkp 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 -----DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCK------DPTFGNAINPTTAILTV-IPFHHGFGMTTTLG--Y 254
Cdd:PRK12492 202 vpvglDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRaclsqlGPDGQPLMKEGQEVMIApLPLYHIYAFTANCMcmM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 255 FTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNF 334
Cdd:PRK12492 282 VSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 335 VrQGYGLTETTSAVLITP-DTDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINK 413
Cdd:PRK12492 362 V-EGYGLTETSPVASTNPyGELARLGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 414 DGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLN 493
Cdd:PRK12492 440 EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSV 519
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 41688574 494 EQI----VQNFVSSQVSTAKWLRggvkflDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK12492 520 EELkaycKENFTGYKVPKHIVLR------DSLPMTPVGKILRRELRDI 561
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
189-535 |
4.37e-49 |
|
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: 173.44 E-value: 4.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVArfshckDPTFGNAI---NPTTAILTVIPFHHGFG-MTTTLGYFTCGFRVALM 264
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVY------NAWMLALNslfDPDDVLLCGLPLFHVNGsVVTLLTPLASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 265 --------HTFEEklFLQSLQDYKVESTLLVPTLMAffpksALVEK---YDLSHLKEIASGGAPLSKEIGEMVKKRFKLN 333
Cdd:cd05944 76 gpagyrnpGLFDN--FWKLVERYRITSLSTVPTVYA-----ALLQVpvnADISSLRFAMSGAAPLPVELRARFEDATGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 334 FVrQGYGLTETTSAVLIT-PDTDVRPGSTGKIVPFHAVKVV--DPTTGKIL--GPNETGELYFKGDMIMKSYYNNEEAtK 408
Cdd:cd05944 149 VV-EGYGLTEATCLVAVNpPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLRdcAPDEVGEICVAGPGVFGGYLYTEGN-K 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 409 AIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQT 488
Cdd:cd05944 227 NAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 41688574 489 GKYLNEQIVQNFVSSQVSTAKWLRGGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd05944 307 GAVVEEEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
39-535 |
4.94e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 177.02 E-value: 4.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 39 IALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLG 118
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 119 IVKPRIIFCSKNTFQKVLNVKSKLKYVETIIILDlNEDLGGYQCLNNFISQNSDINLDvkkfkpnsfnrdDQVA--LVMF 196
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELPAGVPLLLVV-AGPVPGFRSYEEALAAQPDTPIA------------DETAgaDMLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 197 SSGTTGVSKGVM--LTHKNI-VARFSHCKDPTFGNAINPTTAILTVIPFHHG----FGMTTTlgyfTCGFRVALMHTFEE 269
Cdd:PRK08276 148 SSGTTGRPKGIKrpLPGLDPdEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrFGMSAL----ALGGTVVVMEKFDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 270 KLFLQSLQDYKVESTLLVPTL---MAFFPKsALVEKYDLSHLKEIASGGAPLSKEIgemvkKRFKLNF----VRQGYGLT 342
Cdd:PRK08276 224 EEALALIERYRVTHSQLVPTMfvrMLKLPE-EVRARYDVSSLRVAIHAAAPCPVEV-----KRAMIDWwgpiIHEYYASS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 343 ETTSAVLITP-DTDVRPGSTGKivPFHA-VKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSG 420
Cdd:PRK08276 298 EGGGVTVITSeDWLAHPGSVGK--AVLGeVRILDED-GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 421 DIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgvVVQT------GKYLNE 494
Cdd:PRK08276 375 DVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPadgadaGDALAA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 41688574 495 QIVQnFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PRK08276 453 ELIA-WLRGRLAHYKCPR-SIDFEDELPRTPTGKLYKRRLR 491
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
61-535 |
8.60e-49 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 176.41 E-value: 8.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 61 RLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKN---TFQKVLN 137
Cdd:PRK08008 49 RTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQfypMYRQIQQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 138 VKSKLkyVETIIILDlnEDLGGYQCLNNFISQNSDINLDVKKFKPNSfnrDDQVALVMFSSGTTGVSKGVMLTHKNIvaR 217
Cdd:PRK08008 129 EDATP--LRHICLTR--VALPADDGVSSFTQLKAQQPATLCYAPPLS---TDDTAEILFTSGTTSRPKGVVITHYNL--R 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 218 FS-HCKDptFGNAINPTTAILTVIP-FHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVP----TLM 291
Cdd:PRK08008 200 FAgYYSA--WQCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPmmirTLM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 292 AFfPKSAlvekYDLSH-LKEIASGgAPLSKEIGEMVKKRFKlnfVR--QGYGLTETTSAVLITPDTDVR--PgSTGKIVP 366
Cdd:PRK08008 278 VQ-PPSA----NDRQHcLREVMFY-LNLSDQEKDAFEERFG---VRllTSYGMTETIVGIIGDRPGDKRrwP-SIGRPGF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 367 FHAVKVVDpTTGKILGPNETGELYFKG---DMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKY 443
Cdd:PRK08008 348 CYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 444 KGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKwLRGGVKFLDEIPK 523
Cdd:PRK08008 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFK-VPSYLEIRKDLPR 505
|
490
....*....|..
gi 41688574 524 GSTGKIDRKVLR 535
Cdd:PRK08008 506 NCSGKIIKKNLK 517
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
19-537 |
1.48e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 176.66 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 19 GTAGEQMFYALSRYADIsgcIALTNAHtkENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLG 98
Cdd:PRK07788 49 GPFAGLVAHAARRAPDR---AALIDER--GTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 99 --II------AAPVSDKYIERE----LIHSlgivkpriifcskNTFQKVLN-VKSKLKYVETIIILDLNEDLGGYQC--L 163
Cdd:PRK07788 124 arIIllntgfSGPQLAEVAAREgvkaLVYD-------------DEFTDLLSaLPPDLGRLRAWGGNPDDDEPSGSTDetL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 164 NNFISQNSDINLdVKKFKPNSFnrddqvalVMFSSGTTGVSKGVMLTHKNIVArfshckdptfgnainPTTAILTVIPFH 243
Cdd:PRK07788 191 DDLIAGSSTAPL-PKPPKPGGI--------VILTSGTTGTPKGAPRPEPSPLA---------------PLAGLLSRVPFR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 244 HGfgMTT--------TLGYFTC------GFRVALMHTFEEKLFLQSLQDYKVESTLLVPT----LMAFFPKsaLVEKYDL 305
Cdd:PRK07788 247 AG--ETTllpapmfhATGWAHLtlamalGSTVVLRRRFDPEATLEDIAKHKATALVVVPVmlsrILDLGPE--VLAKYDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 306 SHLKEIASGGAPLSKEIGEMVKKRFK---LNFvrqgYGLTETTSAVLITPDtDVR--PGSTGKIVPFHAVKVVDPTtGKI 380
Cdd:PRK07788 323 SSLKIIFVSGSALSPELATRALEAFGpvlYNL----YGSTEVAFATIATPE-DLAeaPGTVGRPPKGVTVKILDEN-GNE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 381 LGPNETGELYFKGDMIMKSYYNNeeATKAIInkDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQH 460
Cdd:PRK07788 397 VPRGVVGRIFVGNGFPFEGYTDG--RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGH 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688574 461 PYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK07788 473 PDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPR-DVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
52-536 |
2.83e-47 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 173.01 E-value: 2.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFC---- 127
Cdd:PRK06087 52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlf 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 128 SKNTFQK-VLNVKSKLKYVETIIILD----LNEDLGGYQCLNNFISQNSDINLDvkkfkpnsfnrDDQVALVMFSSGTTG 202
Cdd:PRK06087 132 KQTRPVDlILPLQNQLPQLQQIVGVDklapATSSLSLSQIIADYEPLTTAITTH-----------GDELAAVLFTSGTEG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 203 VSKGVMLTHKNIVA-RFSHCKdptfGNAINPTTAILTVIPFHH--GF--GMTTTlgyFTCGFRVALMHTFEEKLFLQSLQ 277
Cdd:PRK06087 201 LPKGVMLTHNNILAsERAYCA----RLNLTWQDVFMMPAPLGHatGFlhGVTAP---FLIGARSVLLDIFTPDACLALLE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 278 DYKVE----STLLVPTLMAFFPKSalveKYDLSHLKEIASGGAPLSKEIGEMVKKR-FKLNFVrqgYGLTETTSAVLITP 352
Cdd:PRK06087 274 QQRCTcmlgATPFIYDLLNLLEKQ----PADLSALRFFLCGGTTIPKKVARECQQRgIKLLSV---YGSTESSPHAVVNL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 353 DTDV-RPGST-GKIVPFHAVKVVDPTTgKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGH 430
Cdd:PRK06087 347 DDPLsRFMHTdGYAAAGVEIKVVDEAR-KTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 431 FYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgVVVQTGKYLN---EQIVQNFVSSQVST 507
Cdd:PRK06087 426 IKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCA-YVVLKAPHHSltlEEVVAFFSRKRVAK 504
|
490 500
....*....|....*....|....*....
gi 41688574 508 AKWLRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:PRK06087 505 YKYPE-HIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
40-535 |
3.23e-47 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 172.18 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 40 ALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGI 119
Cdd:PRK13391 15 AVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 120 VKPRIIFCSKNTFQKVLNVKSKLKYVETIIILDLNEDLGGYQCLNNFISQNSDINLDvkkfkpnsfnrdDQV--ALVMFS 197
Cdd:PRK13391 95 SGARALITSAAKLDVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAGLPATPIA------------DESlgTDMLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 198 SGTTGVSKGVM--LTHKNIVAR---FSHCKdPTFGnaINPTTAILTVIPFHHG----FGMTTTlgyfTCGFRVALMHTFE 268
Cdd:PRK13391 163 SGTTGRPKGIKrpLPEQPPDTPlplTAFLQ-RLWG--FRSDMVYLSPAPLYHSapqrAVMLVI----RLGGTVIVMEHFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 269 EKLFLQSLQDYKVESTLLVPTL---MAFFPKsALVEKYDLSHLKEIASGGAPLSKEIGE-MVKkrFKLNFVRQGYGLTET 344
Cdd:PRK13391 236 AEQYLALIEEYGVTHTQLVPTMfsrMLKLPE-EVRDKYDLSSLEVAIHAAAPCPPQVKEqMID--WWGPIIHEYYAATEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSAVLI-TPDTDVRPGSTGKIVpFHAVKVVDPTtGKILGPNETGELYFKGDMiMKSYYNNEEATKAIINKDG-WLRSGDI 422
Cdd:PRK13391 313 LGFTACdSEEWLAHPGTVGRAM-FGDLHILDDD-GAELPPGEPGTIWFEGGR-PFEYLNDPAKTAEARHPDGtWSTVGDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 423 AYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGElpAAGVVVQT------GKYLNEQI 496
Cdd:PRK13391 390 GYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGE--EVKAVVQPvdgvdpGPALAAEL 467
|
490 500 510
....*....|....*....|....*....|....*....
gi 41688574 497 VQnFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PRK13391 468 IA-FCRQRLSRQKCPR-SIDFEDELPRLPTGKLYKRLLR 504
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
58-535 |
1.61e-46 |
|
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: 169.16 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 58 LSCRLAESFKKYGLKQNDTIAVCSENGLQF----FLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSK---N 130
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYielsFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAgaaD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TFQKVLNVksklkYVETIIILDLnEDLGGyqclnnfisqnsdinldVKKFKPNSFNRDDQVALVMFSSGTTGVSKGVMLT 210
Cdd:cd05922 82 RLRDALPA-----SPDPGTVLDA-DGIRA-----------------ARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 211 HKNIVArfshckdptfgNA--------INPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFE-EKLFLQSLQDYKV 281
Cdd:cd05922 139 HQNLLA-----------NArsiaeylgITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 282 ESTLLVPTLMAFFPKSALvEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLITPDTDV--RPG 359
Cdd:cd05922 208 TGLAGVPSTYAMLTRLGF-DPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERIleKPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 360 STGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKS 439
Cdd:cd05922 287 SIGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 440 LIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEaAGELPAAGVVVQTGKYLNEqiVQNFVSSQVSTAKwLRGGVKFLD 519
Cdd:cd05922 366 MIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDKIDPKD--VLRSLAERLPPYK-VPATVRVVD 441
|
490
....*....|....*.
gi 41688574 520 EIPKGSTGKIDRKVLR 535
Cdd:cd05922 442 ELPLTASGKVDYAALR 457
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
189-535 |
2.70e-46 |
|
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: 168.04 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFShckdpTFGNAI---NPTTAILTVIPFHHGFGMTTTLGY-FTCGFRVALM 264
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASAD-----RYAVNVlrlREDDRFVGSPPLAFTFGLGGVLLFpFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 265 HTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTET 344
Cdd:cd05958 172 EEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPII-DGIGSTEM 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSAVLITPDTDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMImksYYNNEEATKAIINKDGWLRSGDIAY 424
Cdd:cd05958 251 FHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGPTG---CRYLADKRQRTYVQGGWNITGDTYS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 425 YDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIV---QNFV 501
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLArelQDHA 406
|
330 340 350
....*....|....*....|....*....|....
gi 41688574 502 SSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd05958 407 KAHIAPYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
45-540 |
2.88e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 169.19 E-value: 2.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 45 HTKENVL-YEEFLKLSCRLAESFKKYGlKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPR 123
Cdd:PRK07638 21 KENDRVLtYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 124 IIFCSKNTFQKVLNVKSKlkyvetIIILDlnedlggyQClNNFISQNSDINLDVKKFKPNSFnrddqvaLVMFSSGTTGV 203
Cdd:PRK07638 100 MIVTERYKLNDLPDEEGR------VIEID--------EW-KRMIEKYLPTYAPIENVQNAPF-------YMGFTSGSTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 204 SKGVMLTHKNIVARFShCKDPTFGnaINPTTAIL---TVIPFHHGFGMTTTLgYFtcGFRVALMHTFEEKLFLQSLQDYK 280
Cdd:PRK07638 158 PKAFLRAQQSWLHSFD-CNVHDFH--MKREDSVLiagTLVHSLFLYGAISTL-YV--GQTVHLMRKFIPNQVLDKLETEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 281 VESTLLVPTLM-AFFPKSALVEKYDLshlkeIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLITP-DTDVRP 358
Cdd:PRK07638 232 ISVMYTVPTMLeSLYKENRVIENKMK-----IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDeESERRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 359 GSTGKivPFHAVKV-VDPTTGKILGPNETGELYFKGDMIMkSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRL 437
Cdd:PRK07638 307 NSVGR--PFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFF-MGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGRE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 438 KSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTgkylNEQIVQNFVSSQVSTAK----WLrg 513
Cdd:PRK07638 384 KNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSA----TKQQLKSFCLQRLSSFKipkeWH-- 457
|
490 500
....*....|....*....|....*..
gi 41688574 514 gvkFLDEIPKGSTGKIDRKVLRQMFEK 540
Cdd:PRK07638 458 ---FVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
52-539 |
4.31e-46 |
|
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: 169.56 E-value: 4.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGII--AAPVSDKyiERELIHSLGIVKPRIIFCSK 129
Cdd:COG1021 53 YAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvFALPAHR--RAEISHFAEQSEAVAYIIPD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 130 NT----FQKVLN-VKSKLKYVETIIILDlneDLGGYQCLNNFISQNSDinldVKKFKPNSfnrdDQVALVMFSSGTTGVS 204
Cdd:COG1021 131 RHrgfdYRALAReLQAEVPSLRHVLVVG---DAGEFTSLDALLAAPAD----LSEPRPDP----DDVAFFQLSGGTTGLP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 205 KGVMLTHK----NIVARFSHCkdptfgnAINPTTAILTVIPFHHGFGMT--TTLGYFTCGFRVALMHTFEEKLFLQSLQD 278
Cdd:COG1021 200 KLIPRTHDdylySVRASAEIC-------GLDADTVYLAALPAAHNFPLSspGVLGVLYAGGTVVLAPDPSPDTAFPLIER 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 279 YKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLnFVRQGYGLTEttSAVLITP---DTD 355
Cdd:COG1021 273 ERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGC-TLQQVFGMAE--GLVNYTRlddPEE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 356 VRPGSTGK-IVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIV 434
Cdd:COG1021 350 VILTTQGRpISPDDEVRIVDED-GNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 435 DRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgVVVQTGKYLNEQIVQNFVSSQ-VSTAKWL-R 512
Cdd:COG1021 429 GRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCA-FVVPRGEPLTLAELRRFLRERgLAAFKLPdR 507
|
490 500
....*....|....*....|....*..
gi 41688574 513 ggVKFLDEIPKGSTGKIDRKVLRQMFE 539
Cdd:COG1021 508 --LEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
52-538 |
1.08e-45 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 167.95 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQ----------KVLNVKSKlkyVETIIILDLNEDL----GGYQCLNNFISQnsdinldvkkFKPNSFNRDDQVALVMFS 197
Cdd:PRK12406 94 LHglasalpagvTVLSVPTP---PEIAAAYRISPALltppAGAIDWEGWLAQ----------QEPYDGPPVPQPQSMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 198 SGTTGVSKGVmlthknivARFShckdPTFGNAIN------------PTTAILTVIPFHH----GFGMTTtlgyFTCGFRV 261
Cdd:PRK12406 161 SGTTGHPKGV--------RRAA----PTPEQAAAaeqmraliyglkPGIRALLTGPLYHsapnAYGLRA----GRLGGVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 262 ALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPK--SALVEKYDLSHLKEIASGGAPLSKEIgemvkKRFKLNF----V 335
Cdd:PRK12406 225 VLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADV-----KRAMIEWwgpvI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 336 RQGYGLTETTSAVLITP-DTDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKD 414
Cdd:PRK12406 300 YEYYGSTESGAVTFATSeDALSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 415 GWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNE 494
Cdd:PRK12406 379 GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 41688574 495 QIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPK-HIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
196-535 |
2.14e-45 |
|
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: 166.71 E-value: 2.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 196 FSSGTTGVSKGVMLTHK--------NIVArfshckdptfgNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTF 267
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRgaylnalaNILE-----------WEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 268 EEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSkeiGEMVKKRFKLNF-VRQGYGLTETTS 346
Cdd:cd12118 209 DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPP---AAVLAKMEELGFdVTHVYGLTETYG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 347 AVLI---TPDTDVRPGS--------TGkiVPFH---AVKVVDPTTGK-ILGPNET-GELYFKGDMIMKSYYNNEEATKAI 410
Cdd:cd12118 286 PATVcawKPEWDELPTEerarlkarQG--VRYVgleEVDVLDPETMKpVPRDGKTiGEIVFRGNIVMKGYLKNPEATAEA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 411 InKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGK 490
Cdd:cd12118 364 F-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 41688574 491 YLNEQIVQNFVSSQVSTAKWLRgGVKFlDEIPKGSTGKIDRKVLR 535
Cdd:cd12118 443 KVTEEEIIAFCREHLAGFMVPK-TVVF-GELPKTSTGKIQKFVLR 485
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
189-536 |
7.95e-44 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 167.02 E-value: 7.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDptfgnAINPTT--AILTVIPFHHGFGMTTTLGYFTC-GFRVAlMH 265
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISD-----VFNLRNddVILSSLPFFHSFGLTVTLWLPLLeGIKVV-YH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 T--FEEKLFLQSLQDYKVesTLLV--PTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGL 341
Cdd:PRK08633 856 PdpTDALGIAKLVAKHRA--TILLgtPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRIL-EGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 342 TETTS-AVLITPD---------TDVRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAII 411
Cdd:PRK08633 933 TETSPvASVNLPDvlaadfkrqTGSKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVI 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 412 ---NKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQhpyIVDAG-----VTGIPDEAAGElpaAG 483
Cdd:PRK08633 1013 kdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK---ALGGEevvfaVTAVPDEKKGE---KL 1086
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41688574 484 VVVQTGKYLNEQIVQNFVSSQVSTAKWLRGGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:PRK08633 1087 VVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
195-535 |
9.56e-44 |
|
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: 161.78 E-value: 9.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 195 MFSSGTTGVSKGVMLTHKNIVARFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQ 274
Cdd:cd05929 131 LYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 275 SLQDYKVESTLLVPTLMAFFPK--SALVEKYDLSHLKEIASGGAPLSKEIGE-MVK----KRFKLnfvrqgYGLTETTSA 347
Cdd:cd05929 211 LIERYRVTFAQFVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEqWIDwggpIIWEY------YGGTEGQGL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 348 VLITPDTDVR-PGSTGKIVpFHAVKVVDpTTGKILGPNETGELYFKGDMiMKSYYNNEEATKAIINKDGWLRSGDIAYYD 426
Cdd:cd05929 285 TIINGEEWLThPGSVGRAV-LGKVHILD-EDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVGYLD 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 427 NDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgvVVQTGKYLNEQIV-----QNFV 501
Cdd:cd05929 362 EDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTAlaeelIAFL 439
|
330 340 350
....*....|....*....|....*....|....
gi 41688574 502 SSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd05929 440 RDRLSRYKCPR-SIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
17-535 |
1.03e-43 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 163.53 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 17 ADGTAGEQMfyALsRYADisgcialtnAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVcsenglqfFLPLIASLY 96
Cdd:PRK04319 53 ADGGRKDKV--AL-RYLD---------ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFI--------FMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 97 ---LGI-----IAAPVSDKYIERELIHSLGIVKPRIIFCSKNTFQKVlnVKSKLKYVETIIILDLNEDLG-GYQCLNNFI 167
Cdd:PRK04319 113 falLGAlkngaIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEEGpGTLDFNALM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 168 SQNSDinldvkKFKPNSFNRDDQvALVMFSSGTTGVSKGVMLTHKNIVARFSHCK---------------DPTF--Gnai 230
Cdd:PRK04319 191 EQASD------EFDIEWTDREDG-AILHYTSGSTGKPKGVLHVHNAMLQHYQTGKyvldlheddvywctaDPGWvtG--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 231 nptTAILTVIPFHHGFGMTTTLGYFTCGFrvalmhtfeeklFLQSLQDYKVESTLLVPT----LMaffpkSA---LVEKY 303
Cdd:PRK04319 261 ---TSYGIFAPWLNGATNVIDGGRFSPER------------WYRILEDYKVTVWYTAPTairmLM-----GAgddLVKKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 304 DLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETtSAVLI--TPDTDVRPGSTGKIVPFHAVKVVDPTtGKIL 381
Cdd:PRK04319 321 DLSSLRHILSVGEPLNPEVVRWGMKVFGLP-IHDNWWMTET-GGIMIanYPAMDIKPGSMGKPLPGIEAAIVDDQ-GNEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 382 GPNETGELYFKG---DMiMKSYYNNEEATKAIINkDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILL 458
Cdd:PRK04319 398 PPNRMGNLAIKKgwpSM-MRGIWNNPEKYESYFA-GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 459 QHPYIVDAGVTGIPDEAAGELPAAGVVVQTGkY-----LNEQIVQnFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKV 533
Cdd:PRK04319 476 EHPAVAEAGVIGKPDPVRGEIIKAFVALRPG-YepseeLKEEIRG-FVKKGLGAHAAPR-EIEFKDKLPKTRSGKIMRRV 552
|
..
gi 41688574 534 LR 535
Cdd:PRK04319 553 LK 554
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
52-535 |
1.72e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 161.51 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIfcsknt 131
Cdd:PRK09088 25 YAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqkvlnVKSKLKYVETIIILDLNEdlggyqclnnFISQNSDINLDVKKFKPNsfnrdDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:PRK09088 99 ------LGDDAVAAGRTDVEDLAA----------FIASADALEPADTPSIPP-----ERVSLILFTSGTSGQPKGVMLSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIvarfshckdptFGNAIN--------PTTAILTVIPFHHGFGMTTTLgyftcgfRVALMHT--------FEEKLFLQS 275
Cdd:PRK09088 158 RNL-----------QQTAHNfgvlgrvdAHSSFLCDAPMFHIIGLITSV-------RPVLAVGgsilvsngFEPKRTLGR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYKVEST--LLVPTLMAFFPKSALVEKYDLSHLKEIASGGAP-LSKEIGEMVKKRFKlnfVRQGYGLTETTSAVLITP 352
Cdd:PRK09088 220 LGDPALGIThyFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILGWLDDGIP---MVDGFGMSEAGTVFGMSV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 353 DTDV---RPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDG 429
Cdd:PRK09088 297 DCDViraKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 430 HFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAK 509
Cdd:PRK09088 376 FFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYK 455
|
490 500
....*....|....*....|....*.
gi 41688574 510 wLRGGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PRK09088 456 -VPKHLRLVDALPRTASGKLQKARLR 480
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
194-531 |
2.59e-43 |
|
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: 157.05 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 194 VMFSSGTTGVSKGVMLTHKNIVARFSHCkDPTFGnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFL 273
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQL-IHAMG--LTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 274 QSLQDYKVestllvpTLMAFFPK--SALVEK-----YDLSHLKEIASGGAPlskeigEMVKKRFKLNFVR--QGYGLTET 344
Cdd:cd17637 82 ELIEEEKV-------TLMGSFPPilSNLLDAaeksgVDLSSLRHVLGLDAP------ETIQRFEETTGATfwSLYGQTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSAVLITPDTDvRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAY 424
Cdd:cd17637 149 SGLVTLSPYRE-RPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 425 YDNDGHFYIVDRL--KSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVS 502
Cdd:cd17637 226 FDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVG 305
|
330 340
....*....|....*....|....*....
gi 41688574 503 SQVSTAKWLRgGVKFLDEIPKGSTGKIDR 531
Cdd:cd17637 306 SRIARYKKPR-YVVFVEALPKTADGSIDR 333
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
52-542 |
6.56e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 161.36 E-value: 6.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK06178 61 YAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKyVETIIILDLNEDL-------------------GGYQCLNNFISqnsdinlDVKKFKPNSFNRDDQVA 192
Cdd:PRK06178 141 APVVEQVRAETS-LRHVIVTSLADVLpaeptlplpdslraprlaaAGAIDLLPALR-------ACTAPVPLPPPALDALA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 193 LVMFSSGTTGVSKGVMLTHKNIV---ARFShckdpTFGNAINPTTAILTVIPFH----HGFGMTTTLgyfTCGFRVALMH 265
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEHTQRDMVytaAAAY-----AVAVVGGEDSVFLSFLPEFwiagENFGLLFPL---FSGATLVLLA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 TFEEKLFLQSLQDYKVESTLLV----PTLMAFfPKSAlveKYDLSHLKEIasGGAPLSKEIGEMVKKRFKL---NFVRQG 338
Cdd:PRK06178 285 RWDAVAFMAAVERYRVTRTVMLvdnaVELMDH-PRFA---EYDLSSLRQV--RVVSFVKKLNPDYRQRWRAltgSVLAEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 -YGLTETTSAVLITP-----DTDVR--PGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAI 410
Cdd:PRK06178 359 aWGMTETHTCDTFTAgfqddDFDLLsqPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 411 InKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGK 490
Cdd:PRK06178 439 L-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGA 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 41688574 491 YLNEQIVQNFVSSQVSTAKWLRggVKFLDEIPKGSTGKIDRKVLRQMFEKHK 542
Cdd:PRK06178 518 DLTAAALQAWCRENMAVYKVPE--IRIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
61-540 |
1.22e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 159.82 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 61 RLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERE---LIHSLGivkPRIIFCSKNTFQKVLN 137
Cdd:PRK07470 44 ALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEvayLAEASG---ARAMICHADFPEHAAA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 138 VKSKLKYVETIIILDLNEDLGGYQCLnnfISQNSDinldvKKFKPNSFNRDDQvALVMFSSGTTGVSKGVMLTHKN---I 214
Cdd:PRK07470 121 VRAASPDLTHVVAIGGARAGLDYEAL---VARHLG-----ARVANAAVDHDDP-CWFFFTSGTTGRPKAAVLTHGQmafV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 215 VArfSHCKDPTFGnainpTT---AILTVIPFHHGFGmTTTLGYFTCGFRVALMHT--FEEKLFLQSLQDYKVESTLLVPT 289
Cdd:PRK07470 192 IT--NHLADLMPG-----TTeqdASLVVAPLSHGAG-IHQLCQVARGAATVLLPSerFDPAEVWALVERHRVTNLFTVPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 290 LMAFFPKSALVEKYDLSHLKEIASGGAPLSKEigEMVKKRFKLNFVR-QGYGLTETTSAVLITP--------DTDVRPGS 360
Cdd:PRK07470 264 ILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRA--DQKRALAKLGKVLvQYFGLGEVTGNITVLPpalhdaedGPDARIGT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 361 TGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEAT-KAIinKDGWLRSGDIAYYDNDGHFYIVDRLKS 439
Cdd:PRK07470 342 CGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANaKAF--RDGWFRTGDLGHLDARGFLYITGRASD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 440 LIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFLD 519
Cdd:PRK07470 419 MYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPK-RFFFWD 497
|
490 500
....*....|....*....|.
gi 41688574 520 EIPKGSTGKIDRKVLRQMFEK 540
Cdd:PRK07470 498 ALPKSGYGKITKKMVREELEE 518
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
188-538 |
3.55e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 158.79 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDpTFGNAINPTTAILTViPFHHGFGMTTTLGYFTCGFRVAL--MH 265
Cdd:PRK07786 173 NDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLR-TNGADINSDVGFVGV-PLFHIAGIGSMLPGLLLGAPTVIypLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 TFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLShLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETT 345
Cdd:PRK07786 251 AFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 346 --SAVLITPDTDVRPGSTGKIVPFHAVKVVDPTTGKIlGPNETGELYFKGDMIMKSYYNNEEATkAIINKDGWLRSGDIA 423
Cdd:PRK07786 330 pvTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDV-PVGEVGEIVYRAPTLMSGYWNNPEAT-AEAFAGGWFHSGDLV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 424 YYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG-KYLNEQIVQNFVS 502
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLT 487
|
330 340 350
....*....|....*....|....*....|....*.
gi 41688574 503 SQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:PRK07786 488 DRLARYKHPK-ALEIVDALPRNPAGKVLKTELRERY 522
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
188-535 |
5.47e-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: 156.08 E-value: 5.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFtCGFRVALMHTF 267
Cdd:cd05919 90 ADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLA-VGASAVLNPGW 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 268 --EEKLFLQSLqdyKVESTLL--VPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTE 343
Cdd:cd05919 169 ptAERVLATLA---RFRPTVLygVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPIL-DGIGATE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 344 TTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINkDGWLRSGDIA 423
Cdd:cd05919 245 VGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-GGWYRTGDKF 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 424 YYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG----KYLNEQIVQn 499
Cdd:cd05919 323 CRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapqESLARDIHR- 401
|
330 340 350
....*....|....*....|....*....|....*.
gi 41688574 500 FVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd05919 402 HLLERLSAHKVPR-RIAFVDELPRTATGKLQRFKLR 436
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
52-534 |
5.57e-42 |
|
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: 157.10 E-value: 5.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGiiAAPVSDKYIER--ELIHslgivkpriiFCsk 129
Cdd:cd05920 43 YRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVPVLALPSHRrsELSA----------FC-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 130 ntfqkvlnvksKLKYVETIIILDLNedlGGYQCLNNFISQNSDINldvkkfkpnsfnrddQVALVMFSSGTTGVSKGVML 209
Cdd:cd05920 109 -----------AHAEAVAYIVPDRH---AGFDHRALARELAESIP---------------EVALFLLSGGTTGTPKLIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 210 THK----NIVARFSHCkdptfgnAINPTTAILTVIPFHHGFGMTT--TLGYFTCGFRVALMHTFEEKLFLQSLQDYKVES 283
Cdd:cd05920 160 THNdyayNVRASAEVC-------GLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 284 TLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTE--TTSAVLITPD-----TDV 356
Cdd:cd05920 233 TALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT-LQQVFGMAEglLNYTRLDDPDeviihTQG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 357 RPGStgkivPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDR 436
Cdd:cd05920 312 RPMS-----PDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 437 LKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgVVVQTGKYLNEQIVQNFVsSQVSTAKW-LRGGV 515
Cdd:cd05920 386 IKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA-FVVLRDPPPSAAQLRRFL-RERGLAAYkLPDRI 463
|
490
....*....|....*....
gi 41688574 516 KFLDEIPKGSTGKIDRKVL 534
Cdd:cd05920 464 EFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
48-537 |
2.78e-41 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 156.37 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 48 ENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFC 127
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 128 SKnTFQK------VLNVKSKLKYVETIIILDLNEDlggyqclNNFISQNSDINLDVKKFKPNSFNRD----DQVALVMFS 197
Cdd:PRK13295 134 PK-TFRGfdhaamARRLRPELPALRHVVVVGGDGA-------DSFEALLITPAWEQEPDAPAILARLrpgpDDVTQLIYT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 198 SGTTGVSKGVMLTHK----NIVARFSHCKdptfgnaINPTTAILTVIPFHH--GFG----MTTTLGYftcgfRVALMHTF 267
Cdd:PRK13295 206 SGTTGEPKGVMHTANtlmaNIVPYAERLG-------LGADDVILMASPMAHqtGFMyglmMPVMLGA-----TAVLQDIW 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 268 EEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSA 347
Cdd:PRK13295 274 DPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIV-SAWGMTENGAV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 348 VLITPDT--DVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEE--ATKAiinkDGWLRSGDIA 423
Cdd:PRK13295 353 TLTKLDDpdERASTTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQlnGTDA----DGWFDTGDLA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 424 YYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSS 503
Cdd:PRK13295 428 RIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKA 507
|
490 500 510
....*....|....*....|....*....|....
gi 41688574 504 QVSTAKWLRGGVKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK13295 508 QKVAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
196-531 |
2.79e-41 |
|
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: 151.02 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 196 FSSGTTGVSKGVMLTHKNIVARFShCKDPTFgnAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQS 275
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFV-CNEDLF--NISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYKVESTLLVPTLMAffpksALVEKYD-LSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLITPDT 354
Cdd:cd17633 84 INQYNATVIYLVPTMLQ-----ALARTLEpESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 355 DVRPGSTGKivPFHAVKVvdpttgKIL--GPNETGELYFKGDMIMKSYYNNEEatkaiINKDGWLRSGDIAYYDNDGHFY 432
Cdd:cd17633 159 SRPPNSVGR--PFPNVEI------EIRnaDGGEIGKIFVKSEMVFSGYVRGGF-----SNPDGWMSVGDIGYVDEEGYLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 433 IVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPaagVVVQTGKYLNEQIVQNFVSSQVSTAKWLR 512
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA---VALYSGDKLTYKQLKRFLKQKLSRYEIPK 302
|
330
....*....|....*....
gi 41688574 513 gGVKFLDEIPKGSTGKIDR 531
Cdd:cd17633 303 -KIIFVDSLPYTSSGKIAR 320
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
52-538 |
1.32e-40 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 153.49 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK07514 31 YGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPAN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKV--LNVKSKLKYVETiiildLNEDLGGyqCLNNFISQNSDinldvkKFKPNSFNRDDqVALVMFSSGTTGVSKGVML 209
Cdd:PRK07514 111 FAWLskIAAAAGAPHVET-----LDADGTG--SLLEAAAAAPD------DFETVPRGADD-LAAILYTSGTTGRSKGAML 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 210 THKNIVArfshckdptfgNAI--------NPTTAILTVIP-FH-HGF--GMTTTLgyfTCGFRVALMHTFEEKLFLQSLQ 277
Cdd:PRK07514 177 SHGNLLS-----------NALtlvdywrfTPDDVLIHALPiFHtHGLfvATNVAL---LAGASMIFLPKFDPDAVLALMP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 278 dykvESTLL--VPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIgemvkkrFKLNFVRQG------YGLTETtsaVL 349
Cdd:PRK07514 243 ----RATVMmgVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAET-------HREFQERTGhailerYGMTET---NM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 350 IT--P-DTDVRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYD 426
Cdd:PRK07514 309 NTsnPyDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKID 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 427 NDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVS 506
Cdd:PRK07514 389 ERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLA 468
|
490 500 510
....*....|....*....|....*....|..
gi 41688574 507 TAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:PRK07514 469 RFKQPK-RVFFVDELPRNTMGKVQKNLLREQY 499
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
48-539 |
1.36e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 153.50 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 48 ENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFC 127
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 128 SKNtfqkvlnvksklkyvetiiiLDLNEDLGGYQCLNNFISQNSDINLDV--KKFKPNSFNRDDQVALVMFSSGTTGVSK 205
Cdd:PRK06145 106 DEE--------------------FDAIVALETPKIVIDAAAQADSRRLAQggLEIPPQAAVAPTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 206 GVMLTHKNIvarfsHCK--DPTFGNAINPTTAILTVIPFHH-GFGMTTTLGYFTCGFRVALMHTFEEKLFLQSLQDYKVE 282
Cdd:PRK06145 166 GVMHSYGNL-----HWKsiDHVIALGLTASERLLVVGPLYHvGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 283 STLLVPTLMAFFPKSALVEKYDLSHLKEIASGGaplsKEIGEMVKKRFKLNFVR----QGYGLTETTSA-VLITPDTDV- 356
Cdd:PRK06145 241 CAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGG----EKTPESRIRDFTRVFTRaryiDAYGLTETCSGdTLMEAGREIe 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 357 RPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDR 436
Cdd:PRK06145 317 KIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 437 LKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVK 516
Cdd:PRK06145 395 KKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPR-QLK 473
|
490 500
....*....|....*....|...
gi 41688574 517 FLDEIPKGSTGKIDRKVLRQMFE 539
Cdd:PRK06145 474 VRDELPRNPSGKVLKRVLRDELN 496
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
51-533 |
1.65e-40 |
|
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: 152.51 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 51 LYEEFLklscRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELihslgivkpRIIFCSKN 130
Cdd:cd17640 11 LYQEIL----DFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEEL---------LYILNHSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TfqkvlnvksklkyveTIIILDlnedlggyqclnnfisqnsdinldvkkfkpnsfNRDDQVALVMFSSGTTGVSKGVMLT 210
Cdd:cd17640 78 S---------------VALVVE---------------------------------NDSDDLATIIYTSGTTGNPKGVMLT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 211 HKNIVARFSHCKD--PTfgnaiNPTTAILTVIPFHHGFGMTTTLGYFTCGfrVALMHTfEEKLFLQSLQDYKvestllvP 288
Cdd:cd17640 110 HANLLHQIRSLSDivPP-----QPGDRFLSILPIWHSYERSAEYFIFACG--CSQAYT-SIRTLKDDLKRVK-------P 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 289 TLMAFFPK--SALVEKYDlshlKEIASGGAPLSKEIGEMV---KKRFKLN-----------F-------VRQGYGLTETT 345
Cdd:cd17640 175 HYIVSVPRlwESLYSGIQ----KQVSKSSPIKQFLFLFFLsggIFKFGISgggalpphvdtFfeaigieVLNGYGLTETS 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 346 SAVLI-TPDTDVRpGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAY 424
Cdd:cd17640 251 PVVSArRLKCNVR-GSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGW 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 425 YDNDGHFYIVDRLKSLIKYK-GYQVAPAEIEGILLQHPYIVDAGVTG----------IP--DEAAGELPAAGVVVQTGK- 490
Cdd:cd17640 330 LTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGqdqkrlgaliVPnfEELEKWAKESGVKLANDRs 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 41688574 491 -YLNEQIV----QNFVSSQVSTAKWLR-----GGVKFLDE--IPKG---STGKIDRKV 533
Cdd:cd17640 410 qLLASKKVlklyKNEIKDEISNRPGFKsfeqiAPFALLEEpfIENGemtQTMKIKRNV 467
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
52-534 |
4.59e-39 |
|
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: 148.06 E-value: 4.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQfflpLIASLyLGIIAA-----PVSDKYIERELIHSLGIVKPRIIF 126
Cdd:cd05930 15 YAELDARANRLARYLRERGVGPGDLVAVLLERSLE----MVVAI-LAVLKAgaayvPLDPSYPAERLAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 127 CSkntfqkvlnvksklkyvetiiildlnedlggyqclnnfisqnsdinldvkkfkpnsfnrDDQVALVMFSSGTTGVSKG 206
Cdd:cd05930 90 TD-----------------------------------------------------------PDDLAYVIYTSGSTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 207 VMLTHKNIVARFSHCKDpTFGnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKL---FLQSLQDYKVES 283
Cdd:cd05930 111 VMVEHRGLVNLLLWMQE-AYP--LTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeaLADLLAEEGITV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 284 TLLVPTLMAFFPKSALVEkyDLSHLKEIASGGAPLSkeiGEMVKKRFKLNFVRQ---GYGLTETTSAVL---ITPDTDVR 357
Cdd:cd05930 188 LHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALP---PDLVRRWRELLPGARlvnLYGPTEATVDATyyrVPPDDEED 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 358 PGST-GKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWL------RSGDIAYYDNDGH 430
Cdd:cd05930 263 GRVPiGRPIPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 431 FYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQ-----V 505
Cdd:cd05930 342 LEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERlpdymV 421
|
490 500
....*....|....*....|....*....
gi 41688574 506 STAkwlrggVKFLDEIPKGSTGKIDRKVL 534
Cdd:cd05930 422 PSA------FVVLDALPLTPNGKVDRKAL 444
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
190-538 |
5.49e-39 |
|
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: 145.17 E-value: 5.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 190 QVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTfgnAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALmhTFEE 269
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL---GFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVL--LERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 270 KLFLQSLQDYKVESTLLVPT-----LMAFFPKSALVEkydlshLKEIASGGAPLSKEIGEMVKKRfKLNfVRQGYGLTET 344
Cdd:cd17630 76 QALAEDLAPPGVTHVSLVPTqlqrlLDSGQGPAALKS------LRAVLLGGAPIPPELLERAADR-GIP-LYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSAVLITPDTDVRPGSTGKIVPFHAVKVVDPttgkilgpnetGELYFKGDMIMKSYYNNEEATKAiiNKDGWLRSGDIAY 424
Cdd:cd17630 148 ASQVATKRPDGFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQLVPEF--NEDGWFTTKDLGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 425 YDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgVVVQTGKYLNEQIVQnFVSSQ 504
Cdd:cd17630 215 LHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVA-VIVGRGPADPAELRA-WLKDK 292
|
330 340 350
....*....|....*....|....*....|....
gi 41688574 505 VSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:cd17630 293 LARFKLPK-RIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
191-531 |
1.02e-38 |
|
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: 144.71 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 191 VALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDptfgNAINPTTAILTVIPFH--HGFGMTTTL-GYFTCGFRVALMHTF 267
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQK----EGLNWVVGDVTYLPLPatHIGGLWWILtCLIHGGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 268 EEKLFLQSLQDYKVESTLLVPTLMAFFP---KSALVEkydLSHLKEIASGGA-PLSKEIgeMVKKRFKLNFVRQGYGLTE 343
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVselKSANAT---VPSLRLIGYGGSrAIAADV--RFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 344 TTSAVLITPDTDVRP-GSTGKIVPFHAVKVVDptTGKILGPN-ETGELYFKGDMIMKSYYNNEEATKAIINkDGWLRSGD 421
Cdd:cd17635 154 TGTALCLPTDDDSIEiNAVGRPYPGVDVYLAA--TDGIAGPSaSFGTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 422 IAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVqtgkylNEQIVQNFV 501
Cdd:cd17635 231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA------SAELDENAI 304
|
330 340 350
....*....|....*....|....*....|....*.
gi 41688574 502 SSQVSTAK------WLRGGVKFLDEIPKGSTGKIDR 531
Cdd:cd17635 305 RALKHTIRrelepyARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
52-535 |
1.42e-38 |
|
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: 148.38 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKY-GLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKN 130
Cdd:cd05928 44 FRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TFQKVLNVKSKLKYVETIIILDlNEDLGGYQCLNNFISQNSDINLDVKkfkpnsfNRDDQVALVMFSSGTTGVSKgvMLT 210
Cdd:cd05928 124 LAPEVDSVASECPSLKTKLLVS-EKSRDGWLNFKELLNEASTEHHCVE-------TGSQEPMAIYFTSGTTGSPK--MAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 211 HknivarfSHCkdpTFGNAINPTTAILTVIPFHHGFGMTTTLGYF--------------TCGFrVALMHTFEEKLFLQSL 276
Cdd:cd05928 194 H-------SHS---SLGLGLKVNGRYWLDLTASDIMWNTSDTGWIksawsslfepwiqgACVF-VHHLPRFDPLVILKTL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 277 QDYKVESTLLVPTLMAFFPKSALvEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETtsaVLI--TPDT 354
Cdd:cd05928 263 SSYPITTFCGAPTVYRMLVQQDL-SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGYGQTET---GLIcaNFKG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 355 -DVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYF-----KGDMIMKSYYNNEEATKAIINKDGWLrSGDIAYYDND 428
Cdd:cd05928 338 mKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDED 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 429 GHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVqTGKYLN---EQI---VQNFVS 502
Cdd:cd05928 416 GYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVL-APQFLShdpEQLtkeLQQHVK 494
|
490 500 510
....*....|....*....|....*....|...
gi 41688574 503 SQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd05928 495 SVTAPYKYPR-KVEFVQELPKTVTGKIQRNELR 526
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
163-470 |
5.34e-38 |
|
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: 146.98 E-value: 5.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 163 LNNFISQNSDINLDVKKFKPNSfnrddqVALVMFSSGTTGVSKGVMLTHKNIVARFSHC-KDPTFGNAINPTTAILTVIP 241
Cdd:cd05927 94 LEEFEKLGKKNKVPPPPPKPED------LATICYTSGTTGNPKGVMLTHGNIVSNVAGVfKILEILNKINPTDVYISYLP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 242 FHHGFGMTTTLGYFTCGFRVALMHTFEEKLflqsLQDYKVestlLVPTLMAFFP----------------KSALVEK--- 302
Cdd:cd05927 168 LAHIFERVVEALFLYHGAKIGFYSGDIRLL----LDDIKA----LKPTVFPGVPrvlnriydkifnkvqaKGPLKRKlfn 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 303 ----YDLSHLKE---------------------------IASGGAPLSKEigemVKKRFKLNF---VRQGYGLTETTSAV 348
Cdd:cd05927 240 falnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPE----VLEFLRVALgcpVLEGYGQTECTAGA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 349 LITPDTDVRPGSTGKIVPFHAVKVVD-PTTG-KILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYD 426
Cdd:cd05927 316 TLTLPGDTSVGHVGGPLPCAEVKLVDvPEMNyDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWL 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 41688574 427 NDGHFYIVDRLKSLIKY-KGYQVAPAEIEGILLQHPYIVDAGVTG 470
Cdd:cd05927 396 PNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYG 440
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
28-541 |
1.25e-37 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 146.10 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 28 ALSRYADISGCIALTNAHTKENVLyEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDK 107
Cdd:PLN02860 12 CLTRLATLRGNAVVTISGNRRRTG-HEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 108 YIERELIHSLGIVKPRIIFCSKNTFQKVLNVKS-KLKYVETIIILDLNEDLGGYQcLNNFISQNSDINLDVKKFKPNSFN 186
Cdd:PLN02860 91 WSFEEAKSAMLLVRPVMLVTDETCSSWYEELQNdRLPSLMWQVFLESPSSSVFIF-LNSFLTTEMLKQRALGTTELDYAW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 187 RDDQVALVMFSSGTTGVSKGVMLTHKNIVARfSHCKDPTFGnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHT 266
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQ-SLAKIAIVG--YGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 FEEKLFLQSLQDYKVESTLLVPTLMA-FFPKSALVEKYDLSH-LKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTET 344
Cdd:PLN02860 247 FDAKAALQAIKQHNVTSMITVPAMMAdLISLTRKSMTWKVFPsVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSAV-------------LITPDTDVRPGST----------GKIVPFHAVKVVDPttgkilGPNETGELYFKGDMIMKSYY 401
Cdd:PLN02860 327 CSSLtfmtlhdptlespKQTLQTVNQTKSSsvhqpqgvcvGKPAPHVELKIGLD------ESSRVGRILTRGPHVMLGYW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 402 NNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPA 481
Cdd:PLN02860 401 GQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41688574 482 AGVVVQTG--------------KYLNEQIVQNFVSSQ-VSTAKWLRGGVKFLDEIPKGSTGKIDRKVLRQMFEKH 541
Cdd:PLN02860 481 ACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKnLSRFKIPKLFVQWRKPFPLTTTGKIRRDEVRREVLSH 555
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
188-536 |
1.50e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 144.36 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNIVArfshCKDpTFGNAINPTTAILTV--IP-FH-HGFgMTTTLGYFTCGFRvaL 263
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAA----DLD-ALAEAWQWTADDVLVhgLPlFHvHGL-VLGVLGPLRIGNR--F 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 264 MHT--FEEKLFLQSLQDykvESTLL--VPTL---MAFFPKSALVekydLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVR 336
Cdd:PRK07787 199 VHTgrPTPEAYAQALSE---GGTLYfgVPTVwsrIAADPEAARA----LRGARLLVSGSAALPVPVFDRLAALTGHRPVE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 337 QgYGLTETtsavLIT----PDTDVRPGSTGKIVPFHAVKVVDPTTGKILGPNET-GELYFKGDMIMKSYYNNEEATKAII 411
Cdd:PRK07787 272 R-YGMTET----LITlstrADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETvGELQVRGPTLFDGYLNRPDATAAAF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 412 NKDGWLRSGDIAYYDNDGHFYIVDRlKS--LIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG 489
Cdd:PRK07787 347 TADGWFRTGDVAVVDPDGMHRIVGR-EStdLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 41688574 490 KYLNEQIvqNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:PRK07787 426 VAADELI--DFVAQQLSVHKRPR-EVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
188-537 |
2.19e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 145.27 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVM------LTHKNIVARfshckdptfGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRV 261
Cdd:PRK06164 180 PDAGALLFTTSGTTSGPKLVLhrqatlLRHARAIAR---------AYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 262 ALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSAlVEKYDLSHLKEIASGG-APLSKEIGEMVKKRfklNFVRQG-Y 339
Cdd:PRK06164 251 VCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTA-GERADFPSARLFGFASfAPALGELAALARAR---GVPLTGlY 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 340 GLTETTSAVLITP-DTDVRPGSTGKIVPFHA---VKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDG 415
Cdd:PRK06164 327 GSSEVQALVALQPaTDPVSVRIEGGGRPASPearVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 416 WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGElPAAGVVVQTGKYLNEQ 495
Cdd:PRK06164 407 YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTV-PVAFVIPTDGASPDEA 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 41688574 496 IVQNFVSSQVSTAKwLRGGVKFLDEIP---KGSTGKIDRKVLRQM 537
Cdd:PRK06164 486 GLMAACREALAGFK-VPARVQVVEAFPvteSANGAKIQKHRLREM 529
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
60-537 |
6.82e-37 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 144.39 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 60 CRLAESFKKYGLKQNDTIAVCSEN-----GLQFFLPLIaslylGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKN---T 131
Cdd:PLN03102 50 CRLAASLISLNITKNDVVSVLAPNtpamyEMHFAVPMA-----GAVLNPINTRLDATSIAAILRHAKPKILFVDRSfepL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKYVETIIILDLNEDlggyQCLNNFISQNSDINLDVKKFKPNSF---------NRDDQVALvMFSSGTTG 202
Cdd:PLN03102 125 AREVLHLLSSEDSNLNLPVIFIHEI----DFPKRPSSEELDYECLIQRGEPTPSlvarmfriqDEHDPISL-NYTSGTTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 203 VSKGVMLTHKnivARFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFT-CGFRVALMHTFEEKLFlQSLQDYKV 281
Cdd:PLN03102 200 DPKGVVISHR---GAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAArGGTSVCMRHVTAPEIY-KNIEMHNV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 282 ESTLLVPTLMAFFPKSalvEKYDLSHLK---EIASGGAPLSkeiGEMVKKRFKLNF-VRQGYGLTETTSAVLIT------ 351
Cdd:PLN03102 276 THMCCVPTVFNILLKG---NSLDLSPRSgpvHVLTGGSPPP---AALVKKVQRLGFqVMHAYGLTEATGPVLFCewqdew 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 352 ----------------------PDTDVRPGSTGKIVPfhavkvvdpTTGKILGpnetgELYFKGDMIMKSYYNNEEATKA 409
Cdd:PLN03102 350 nrlpenqqmelkarqgvsilglADVDVKNKETQESVP---------RDGKTMG-----EIVIKGSSIMKGYLKNPKATSE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 410 IInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG 489
Cdd:PLN03102 416 AF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKG 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 41688574 490 KYLNEQIVQNFVSSQVSTAKWLRGG---------VKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:PLN03102 495 ETTKEDRVDKLVTRERDLIEYCRENlphfmcprkVVFLQELPKNGNGKILKPKLRDI 551
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
52-463 |
7.93e-37 |
|
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: 143.12 E-value: 7.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNt 131
Cdd:cd17639 8 YAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDGK- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqkvlnvksklkyvetiiildlnedlggyqclnnfisqnsdinldvkkfkpnsfnrDDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd17639 87 --------------------------------------------------------PDDLACIMYTSGSTGNPKGVMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVARFsHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTfeEKLFLQSLQDYKVESTLLVPTLM 291
Cdd:cd17639 111 GNLVAGI-AGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSP--RTLTDKSKRGCKGDLTEFKPTLM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 292 AFFP-------------------------------KSALVEKYDLS-----------------HLKEIASGGAPLSKEig 323
Cdd:cd17639 188 VGVPaiwdtirkgvlaklnpmgglkrtlfwtayqsKLKALKEGPGTplldelvfkkvraalggRLRYMLSGGAPLSAD-- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 324 emvKKRFKLNF---VRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTTGKIL--GPNETGELYFKGDMIMK 398
Cdd:cd17639 266 ---TQEFLNIVlcpVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYStdKPPPRGEILIRGPNVFK 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41688574 399 SYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYK-GYQVAPAEIEGILLQHPYI 463
Cdd:cd17639 343 GYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV 408
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
50-538 |
1.21e-36 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 143.10 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 50 VLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFC-- 127
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIda 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 128 ---------SKNTFQKVLNVKSKLKYVETIIILDLNedlggyqclnnfisqnSDINLDVKKFKPNSFNRDDqvALVMFSS 198
Cdd:PRK05852 124 dgphdraepTTRWWPLTVNVGGDSGPSGGTLSVHLD----------------AATEPTPATSTPEGLRPDD--AMIMFTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKNIVARFshcKDPTFGNAINPTTAILTVIPFHHGFG-MTTTLGYFTCGFRVAL--MHTFEEKLFLQS 275
Cdd:PRK05852 186 GTTGLPKMVPWTHANIASSV---RAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLpaRGRFSAHTFWDD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYKVESTLLVPTLMAFFPKSALVEKYDLSH--LKEIASGGAPLSKEIGEMVKKRFkLNFVRQGYGLTETTSAVLIT-- 351
Cdd:PRK05852 263 IKAVGATWYTAVPTIHQILLERAATEPSGRKPaaLRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATHQVTTTqi 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 352 --PDTDVRPGSTGKIVPFHA---VKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINkDGWLRSGDIAYYD 426
Cdd:PRK05852 342 egIGQTENPVVSTGLVGRSTgaqIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLS 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 427 NDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQ-----TGKYLNEQIVQNFV 501
Cdd:PRK05852 420 AAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPResappTAEELVQFCRERLA 499
|
490 500 510
....*....|....*....|....*....|....*..
gi 41688574 502 SSQVSTAkwlrggVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:PRK05852 500 AFEIPAS------FQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
24-534 |
2.16e-36 |
|
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: 141.49 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 24 QMFYALSRYAD--ISGCIALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIA 101
Cdd:cd05923 1 QTVFEMLRRAAsrAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 102 APVS--------DKYIERELIHSLgivkpriifcskntfqkvlnvksklkyVETIIILDLNEDLGGYQCLNnFISQNSD- 172
Cdd:cd05923 81 ALINprlkaaelAELIERGEMTAA---------------------------VIAVDAQVMDAIFQSGVRVL-ALSDLVGl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 173 -INLDVKKFKPNSFNRDDQVALVMFSSGTTGVSKGVMLTHKNIVAR---FSHCKDPTFGNAINpttaILTVIPFHHGFGM 248
Cdd:cd05923 133 gEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRvlfMSTQAGLRHGRHNV----VLGLMPLYHVIGF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 249 TTTL-GYFTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVK 327
Cdd:cd05923 209 FAVLvAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 328 kRFKLNFVRQGYGLTETTSAVLitpDTDVRPGSTGKIVPFHAVKVVD--PTTGKILGPNETGELYFK--GDMIMKSYYNN 403
Cdd:cd05923 289 -QHLPGEKVNIYGTTEAMNSLY---MRDARTGTEMRPGFFSEVRIVRigGSPDEALANGEEGELIVAaaADAAFTGYLNQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 404 EEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAG 483
Cdd:cd05923 365 PEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTAC 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 41688574 484 VVVQTGKYLNEQIVQNFVSSQVSTAKWLRGGVkFLDEIPKGSTGKIDRKVL 534
Cdd:cd05923 444 VVPREGTLSADELDQFCRASELADFKRPRRYF-FLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
10-539 |
9.24e-36 |
|
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: 140.50 E-value: 9.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 10 PEPFHPLADGTAGEQMFYALSRYADIsGCIALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFL 89
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTK-GITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 90 PLIASLYLGIIAAPVS----DKYIERELIHSLGIVK----PRIIfCSKNTFQKVLNVKsKLKYVETIIILDLNEDLGGYQ 161
Cdd:cd05906 80 AFWACVLAGFVPAPLTvpptYDEPNARLRKLRHIWQllgsPVVL-TDAELVAEFAGLE-TLSGLPGIRVLSIEELLDTAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 162 CLNNFISQNSDInldvkkfkpnsfnrddqvALVMFSSGTTGVSKGVMLTHKNIVARFShckdptfGNAI----NPTTAIL 237
Cdd:cd05906 158 DHDLPQSRPDDL------------------ALLMLTSGSTGFPKAVPLTHRNILARSA-------GKIQhnglTPQDVFL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 238 TVIPFHH--GFGMTTTLG-YFTCG-FRVALMHTFEEKL-FLQSLQDYKVESTllvptlmaFFPKSAL------VEK---- 302
Cdd:cd05906 213 NWVPLDHvgGLVELHLRAvYLGCQqVHVPTEEILADPLrWLDLIDRYRVTIT--------WAPNFAFallndlLEEiedg 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 303 -YDLSHLKEIASGGAPLSKEIGEMVK---KRFKL--NFVRQGYGLTETTSAV-----LITPDTDVRP--GSTGKIVPFHA 369
Cdd:cd05906 285 tWDLSSLRYLVNAGEAVVAKTIRRLLrllEPYGLppDAIRPAFGMTETCSGViysrsFPTYDHSQALefVSLGRPIPGVS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 370 VKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNdGHFYIVDRLKSLIKYKGYQVA 449
Cdd:cd05906 365 MRIVDDE-GQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 450 PAEIEGILlqhpyivdagvtgipDEAAGELP--AAGVVVQTGKYLNEQIVQNFVSSQ------VSTAKWLRGGVKFL--- 518
Cdd:cd05906 443 SHEIEAAV---------------EEVPGVEPsfTAAFAVRDPGAETEELAIFFVPEYdlqdalSETLRAIRSVVSREvgv 507
|
570 580 590
....*....|....*....|....*....|.
gi 41688574 519 ----------DEIPKGSTGKIDRKVLRQMFE 539
Cdd:cd05906 508 spayliplpkEEIPKTSLGKIQRSKLKAAFE 538
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
272-545 |
1.49e-35 |
|
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: 140.91 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 272 FLQSLQDYKVESTLLVPT----LMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTSA 347
Cdd:cd05967 317 FWRVIEKYQVNALFTAPTairaIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVP-VIDHWWQTETGWP 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 348 VLITP----DTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDM---IMKSYYNNEEATKA--IINKDGWLR 418
Cdd:cd05967 396 ITANPvglePLPIKAGSPGKPVPGYQVQVLDED-GEPVGPNELGNIVIKLPLppgCLLTLWKNDERFKKlyLSKFPGYYD 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 419 SGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG-----KYLN 493
Cdd:cd05967 475 TGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGvkitaEELE 554
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41688574 494 EQIVQnFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMFEKHKSKL 545
Cdd:cd05967 555 KELVA-LVREQIGPVAAFR-LVIFVKRLPKTRSGKILRRTLRKIADGEDYTI 604
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
188-536 |
3.85e-35 |
|
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: 136.88 E-value: 3.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCK-------DPTFGNAINPTTAiltvipfhhgFGM-TTTLGYFTCGF 259
Cdd:cd05973 87 DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRdavdlrpEDSFWNAADPGWA----------YGLyYAITGPLALGH 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 260 RVALMH-TFEEKLFLQSLQDYKVESTLLVPT----LMAFFPKSALVEKydlSHLKEIASGGAPLSKEIGEMVKKRFKLNf 334
Cdd:cd05973 157 PTILLEgGFSVESTWRVIERLGVTNLAGSPTayrlLMAAGAEVPARPK---GRLRRVSSAGEPLTPEVIRWFDAALGVP- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 335 VRQGYGLTETTSAVL--ITPDTDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGD----MIMKSYYNNEEATK 408
Cdd:cd05973 233 IHDHYGQTELGMVLAnhHALEHPVHAGSAGRAMPGWRVAVLD-DDGDELGPGEPGRLAIDIAnsplMWFRGYQLPDTPAI 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 409 AiinkDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQT 488
Cdd:cd05973 312 D----GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 41688574 489 GKYLNEQI---VQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05973 388 GHEGTPALadeLQLHVKKRLSAHAYPR-TIHFVDELPKTPSGKIQRFLLRR 437
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
52-537 |
1.52e-34 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 137.04 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIiaAPVSDKYIER--ELIHSLGIVKPRIIFCSK 129
Cdd:PRK10946 51 YRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFSHQrsELNAYASQIEPALLIADR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 130 -----------NTFQKVLNvksklkyvETIIILDLNEDlgGYQCLNNFISQNSDinldvkKFKPNSfNRDDQVALVMFSS 198
Cdd:PRK10946 129 qhalfsdddflNTLVAEHS--------SLRVVLLLNDD--GEHSLDDAINHPAE------DFTATP-SPADEVAFFQLSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKN----IVARFSHCkdptfgnAINPTTAILTVIPFHHGFGMTT--TLGYFTCGFRVALMHTFEEKLF 272
Cdd:PRK10946 192 GSTGTPKLIPRTHNDyyysVRRSVEIC-------GFTPQTRYLCALPAAHNYPMSSpgALGVFLAGGTVVLAPDPSATLC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 273 LQSLQDYKVESTLLVPTLMAFFPKSALVEKY--DLSHLKEIASGGAPLSKEIGEMVKKRF--KLnfvRQGYGLTE----- 343
Cdd:PRK10946 265 FPLIEKHQVNVTALVPPAVSLWLQAIAEGGSraQLASLKLLQVGGARLSETLARRIPAELgcQL---QQVFGMAEglvny 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 344 ----TTSAVLITpdTDVRPgstgkIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRS 419
Cdd:PRK10946 342 trldDSDERIFT--TQGRP-----MSPDDEVWVAD-ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 420 GDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG-------KYL 492
Cdd:PRK10946 414 GDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPlkavqlrRFL 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 41688574 493 NEQIVQNFvssqvstaKwLRGGVKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK10946 494 REQGIAEF--------K-LPDRVECVDSLPLTAVGKVDKKQLRQW 529
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
61-536 |
4.03e-34 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 135.25 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 61 RLAESFKKYGLKQNDTIAVCSENglqffLPLIASLYLGI-----IAAPVSDKYIERELIHSLGIVKPRIIFCSkntfQKV 135
Cdd:cd05915 36 RLMGGLRALGVGVGDRVATLGFN-----HFRHLEAYFAVpgmgaVLHTANPRLSPKEIAYILNHAEDKVLLFD----PNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 136 LNVKSKLKYVETIIILDLNEDlGGYQCLNNFISQNsdiNLDVKKFKPnsFNRDDQVALvMFSSGTTGVSKGVMLTHkniv 215
Cdd:cd05915 107 LPLVEAIRGELKTVQHFVVMD-EKAPEGYLAYEEA---LGEEADPVR--VPERAACGM-AYTTGTTGLPKGVVYSH---- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 216 aRFSHCKDPTFG----NAINPTTAILTVIPFHH--GFGMTTTLGYFTcGFRVALMHTFEEKLFLQSLQDYKVESTLLVPT 289
Cdd:cd05915 176 -RALVLHSLAASlvdgTALSEKDVVLPVVPMFHvnAWCLPYAATLVG-AKQVLPGPRLDPASLVELFDGEGVTFTAGVPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 290 LMAFFPKSALVEKYDLSHLKEIASGGAPlSKEIGEMVKK--RFKlnfVRQGYGLTET---TSAVLITPDTDVRP------ 358
Cdd:cd05915 254 VWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIARFErmGVE---VRQGYGLTETspvVVQNFVKSHLESLSeeeklt 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 359 --GSTGKIVPFHAVKVVDPTTGKILGPNETGE-LYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVD 435
Cdd:cd05915 330 lkAKTGLPIPLVRLRVADEEGRPVPKDGKALGeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 436 RLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQnFVSSQVSTAKWLRGGV 515
Cdd:cd05915 410 RLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNE-HLLKAGFAKWQLPDAY 488
|
490 500
....*....|....*....|.
gi 41688574 516 KFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05915 489 VFAEEIPRTSAGKFLKRALRE 509
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
52-468 |
4.49e-34 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 133.54 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKY-GLKQNDTIAVCSENGLQfflpLIASLyLGIIAA-----PVSDKYIERELIHSLGIVKPRII 125
Cdd:TIGR01733 2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAE----LVVAI-LAVLKAgaayvPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 126 FCSKNTFQKVLNVksklkyVETIIILDLNEDLGGYQCLNNFisqnsdinldvkkfKPNSFNRDDQVALVMFSSGTTGVSK 205
Cdd:TIGR01733 77 LTDSALASRLAGL------VLPVILLDPLELAALDDAPAPP--------------PPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 206 GVMLTHKNIVARFSHCKDPtfgNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVAL----MHTFEEKLFLQSLQDYKV 281
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLARR---YGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVppedEERDDAALLAALIAEHPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 282 ESTLLVPTLMAFFpksALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETT--SAVLITPDTDVRPG 359
Cdd:TIGR01733 214 TVLNLTPSLLALL---AAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTvwSTATLVDPDDAPRE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 360 ST---GKIVPFHAVKVVDPtTGKILGPNETGELYFKGDMIMKSYYNNEEAT-KAIINKDGWL-------RSGDIAYYDND 428
Cdd:TIGR01733 291 SPvpiGRPLANTRLYVLDD-DLRPVPVGVVGELYIGGPGVARGYLNRPELTaERFVPDPFAGgdgarlyRTGDLVRYLPD 369
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 41688574 429 GHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGV 468
Cdd:TIGR01733 370 GNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
52-536 |
4.55e-34 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 135.66 E-value: 4.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGivkpriifcskNT 131
Cdd:PRK06155 49 YAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILR-----------NS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSK-LKYVETIiiLDLNEDLGGYQCLNNFISQNSDINLDVKKFKPNSFN------RDDQVALVMFSSGTTGVS 204
Cdd:PRK06155 118 GARLLVVEAAlLAALEAA--DPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPapaaavQPGDTAAILYTSGTTGPS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 205 KGVMLTHKNI------VARFSHckdptfgnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQSLQD 278
Cdd:PRK06155 196 KGVCCPHAQFywwgrnSAEDLE---------IGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 279 YKVESTLL----VPTLMAFfPKSAlvekYDLSHLKEIASGGApLSKEIGEMVKKRFKLNfVRQGYGLTETTSAVLITPDT 354
Cdd:PRK06155 267 HGATVTYLlgamVSILLSQ-PARE----SDRAHRVRVALGPG-VPAALHAAFRERFGVD-LLDGYGSTETNFVIAVTHGS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 355 DvRPGSTGKIVP-FHAvKVVDpTTGKILGPNETGELYFKGD---MIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGH 430
Cdd:PRK06155 340 Q-RPGSMGRLAPgFEA-RVVD-EHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 431 FYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKW 510
Cdd:PRK06155 416 FRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAV 495
|
490 500
....*....|....*....|....*.
gi 41688574 511 LRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:PRK06155 496 PR-YVEFVAALPKTENGKVQKFVLRE 520
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
72-539 |
1.21e-33 |
|
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: 134.29 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 72 KQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVK---PRIIFCSKNTFQKVLNVKSKLKYVET- 147
Cdd:cd05931 46 KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLAAILAdagPRVVLTTAAALAAVRAFAASRPAAGTp 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 148 -IIILDLNEDLGGYQCLnnfisqnsdinldvkkfkPNSFNRDDqVALVMFSSGTTGVSKGVMLTHKNIVArfsHCKDPTF 226
Cdd:cd05931 126 rLLVVDLLPDTSAADWP------------------PPSPDPDD-IAYLQYTSGSTGTPKGVVVTHRNLLA---NVRQIRR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 227 GNAINPTTAILTVIPFHHGFGMTTTLgyFT---CGFRVALM--HTFEEK--LFLQSLQDYKVESTLlVPTlMAFfpksAL 299
Cdd:cd05931 184 AYGLDPGDVVVSWLPLYHDMGLIGGL--LTplySGGPSVLMspAAFLRRplRWLRLISRYRATISA-APN-FAY----DL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 300 V---------EKYDLSHLKEIASGGAPLSKEIGEMVKKRFK-LNF----VRQGYGLTETTSAV----------------- 348
Cdd:cd05931 256 CvrrvrdedlEGLDLSSWRVALNGAEPVRPATLRRFAEAFApFGFrpeaFRPSYGLAEATLFVsggppgtgpvvlrvdrd 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 349 -LITPDTDVRPG--------STGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINK------ 413
Cdd:cd05931 336 aLAGRAVAVAADdpaarelvSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGAlaatde 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 414 DGWLRSGDIAYYdNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVT---GIPDEAAGELPAAGVVVQTGK 490
Cdd:cd05931 416 GGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCVaafSVPDDGEERLVVVAEVERGAD 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 41688574 491 YLNEQIVQNFVSSQVSTAKWLR-GGVKFL--DEIPKGSTGKIDRKVLRQMFE 539
Cdd:cd05931 495 PADLAAIAAAIRAAVAREHGVApADVVLVrpGSIPRTSSGKIQRRACRAAYL 546
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
40-535 |
2.17e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 130.13 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 40 ALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSdkyiereliHSLGI 119
Cdd:PRK13390 15 AVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAIN---------HHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 120 VKPRIIFCSKNTfqKVLNVKSKLKYV--ETIIILDLNEDLGGYqcLNNFISQNSDINLDVKKFKPNSFNrddqvALVMFS 197
Cdd:PRK13390 86 PEADYIVGDSGA--RVLVASAALDGLaaKVGADLPLRLSFGGE--IDGFGSFEAALAGAGPRLTEQPCG-----AVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 198 SGTTGVSKGVM--LTHKNIVARfshcKDPTFGNA-----INPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEK 270
Cdd:PRK13390 157 SGTTGFPKGIQpdLPGRDVDAP----GDPIVAIArafydISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 271 LFLQSLQDYKVESTLLVPTLMAFFPK--SALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKlNFVRQGYGLTETTSAV 348
Cdd:PRK13390 233 ATLGHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG-PIVYEYYSSTEAHGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 349 LI-TPDTDVRPGSTGKIVpFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDG--WLRSGDIAYY 425
Cdd:PRK13390 312 FIdSPDWLAHPGSVGRSV-LGDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 426 DNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQ---NFVS 502
Cdd:PRK13390 390 DEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELAReliDYTR 469
|
490 500 510
....*....|....*....|....*....|...
gi 41688574 503 SQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PRK13390 470 SRIAHYKAPR-SVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
189-535 |
4.75e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 129.42 E-value: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIV-------ARFSHCKDptfgnainpTTAILTVIPFHHGFGMTTTLGYFTCGFRV 261
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVAsagvmlaQRFGLGPD---------DVCYVSMPLFHSNAVMAGWAVALAAGASI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 262 ALMHTFEEKLFLQSLQDYKVestllvpTLMAFFPKS-----ALVEKYDLSH--LKeIASG--GAPLSKEigemvkkRFKL 332
Cdd:PRK07867 223 ALRRKFSASGFLPDVRRYGA-------TYANYVGKPlsyvlATPERPDDADnpLR-IVYGneGAPGDIA-------RFAR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 333 NF---VRQGYGLTETTSAVLITPDTdvRPGSTGKIVPfhAVKVVDPTTGKILGPNE------------TGELY-FKGDMI 396
Cdd:PRK07867 288 RFgcvVVDGFGSTEGGVAITRTPDT--PPGALGPLPP--GVAIVDPDTGTECPPAEdadgrllnadeaIGELVnTAGPGG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 397 MKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAA 476
Cdd:PRK07867 364 FEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVV 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 477 GELPAAGVVVQTGKYLNEQIVQNFVSSQVSTA-KWLRGGVKFLDEIPKGSTGKIDRKVLR 535
Cdd:PRK07867 443 GDQVMAALVLAPGAKFDPDAFAEFLAAQPDLGpKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
196-537 |
1.32e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 128.53 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 196 FSSGTTGVSKGVMLTHKnivarfshckdptfGNAINPTTAILTvipfhhgFGMTT------TLGYFTC------------ 257
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHR--------------GAYLNALSNILA-------WGMPKhpvylwTLPMFHCngwcfpwtvaar 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 258 -GFRVALmHTFEEKLFLQSLQDYKVESTLLVPTLMaffpkSALV-----EKYDLSH-LKEIASGGAPLSKEIGEMVKKRF 330
Cdd:PRK08162 248 aGTNVCL-RKVDPKLIFDLIREHGVTHYCGAPIVL-----SALInapaeWRAGIDHpVHAMVAGAAPPAAVIAKMEEIGF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 331 KLNFVrqgYGLTET--TSAV---------LITPDTDVRPGSTGkiVPFH---AVKVVDPTTGKILgPN--ET-GELYFKG 393
Cdd:PRK08162 322 DLTHV---YGLTETygPATVcawqpewdaLPLDERAQLKARQG--VRYPlqeGVTVLDPDTMQPV-PAdgETiGEIMFRG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 394 DMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPD 473
Cdd:PRK08162 396 NIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPD 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688574 474 EAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFlDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK08162 475 PKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPK-AVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
193-537 |
1.41e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 128.22 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 193 LVMFSSGTTGVSKGVMLTH-------KNIVARFSHCKD-------PTF-GNAInptTAILTVIpfhhgfgmtttlgyFTC 257
Cdd:PRK13388 154 MLIFTSGTTGAPKAVRCSHgrlafagRALTERFGLTRDdvcyvsmPLFhSNAV---MAGWAPA--------------VAS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 258 GFRVALMHTFEEKLFLQSLQDYKVestllvpTLMAFFPKS-----ALVEKYDlshlkeiaSGGAPLSKEIGEMVKKRFKL 332
Cdd:PRK13388 217 GAAVALPAKFSASGFLDDVRRYGA-------TYFNYVGKPlayilATPERPD--------DADNPLRVAFGNEASPRDIA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 333 NFVRQ-------GYGLTETtsAVLITPDTDVRPGSTGKivPFHAVKVVDPTT------------GKILGPNET-GEL--- 389
Cdd:PRK13388 282 EFSRRfgcqvedGYGSSEG--AVIVVREPGTPPGSIGR--GAPGVAIYNPETltecavarfdahGALLNADEAiGELvnt 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 390 ----YFKGdmimksYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVD 465
Cdd:PRK13388 358 agagFFEG------YYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINR 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688574 466 AGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQ--VSTaKWLRGGVKFLDEIPKGSTGKIDRKVLRQM 537
Cdd:PRK13388 431 VAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdLGT-KAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
267-536 |
1.77e-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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 126.53 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 FEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVeKYDLShLKEIASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTS 346
Cdd:cd05974 163 FDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA-SFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETTA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 347 AVLITPDTDVRPGSTGKIVPFHAVKVVDPTTGkilgPNETGELYFK-GDM----IMKSYYNNEEATKAIInKDGWLRSGD 421
Cdd:cd05974 240 LVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA----PATEGEVALDlGDTrpvgLMKGYAGDPDKTAHAM-RGGYYRTGD 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 422 IAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG-KYLNEQIVQNF 500
Cdd:cd05974 315 IAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyEPSPETALEIF 394
|
250 260 270
....*....|....*....|....*....|....*...
gi 41688574 501 VSSQVSTAKWLRggVKFLD--EIPKGSTGKIDRKVLRQ 536
Cdd:cd05974 395 RFSRERLAPYKR--IRRLEfaELPKTISGKIRRVELRR 430
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
52-534 |
2.92e-31 |
|
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: 126.67 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNt 131
Cdd:cd17655 25 YRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSH- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqkvlnVKSKLKYVETIIILDLNEdlggyqclnnfISQNSDINLDVKkfkpnsfNRDDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd17655 104 ------LQPPIAFIGLIDLLDEDT-----------IYHEESENLEPV-------SKSDDLAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVarfsHCKDpTFGNAINPTTA--ILTVIPFHhgFGMTTT-------LGYFTCGFRVALMHTFEEklFLQSLQDYKVE 282
Cdd:cd17655 160 RGVV----NLVE-WANKVIYQGEHlrVALFASIS--FDASVTeifasllSGNTLYIVRKETVLDGQA--LTQYIRQNRIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 283 STLLVPTLMAFFPKSALVEKYDlshLKEIASGGAPLSKEIGEMVKKRFKLNF-VRQGYGLTETT---SAVLITPDTDVRP 358
Cdd:cd17655 231 IIDLTPAHLKLLDAADDSEGLS---LKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTETTvdaSIYQYEPETDQQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 359 G-STGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWL------RSGDIAYYDNDGHF 431
Cdd:cd17655 308 SvPIGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 432 YIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEaagelpaagvvvQTGKYLNEQIVQN--FVSSQVST-- 507
Cdd:cd17655 387 EFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDE------------QGQNYLCAYIVSEkeLPVAQLREfl 454
|
490 500 510
....*....|....*....|....*....|...
gi 41688574 508 AKWLRGG------VKfLDEIPKGSTGKIDRKVL 534
Cdd:cd17655 455 ARELPDYmipsyfIK-LDEIPLTPNGKVDRKAL 486
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
185-534 |
1.14e-30 |
|
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: 124.28 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 185 FNRDDQVALVMFSSGTTGVSKGVMLTHKN-------IVARFSHCKDPTFGNainptTAiltviPFHHGFGMTTTLGYFTC 257
Cdd:cd05945 93 IADGDDNAYIIFTSGSTGRPKGVQISHDNlvsftnwMLSDFPLGPGDVFLN-----QA-----PFSFDLSVMDLYPALAS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 258 G---FRVALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNF 334
Cdd:cd05945 163 GatlVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDAR 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 335 VRQGYGLTETTSAVL---ITPD--TDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKA 409
Cdd:cd05945 243 IYNTYGPTEATVAVTyieVTPEvlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 410 IINKD---GWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIP-DEAAGELPAAGVV 485
Cdd:cd05945 322 AFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYkGEKVTELIAFVVP 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 41688574 486 VQTGKYLNEQIVQNFVSSQVST----AKWLRggvkfLDEIPKGSTGKIDRKVL 534
Cdd:cd05945 402 KPGAEAGLTKAIKAELAERLPPymipRRFVY-----LDELPLNANGKIDRKAL 449
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
48-454 |
6.77e-30 |
|
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: 124.01 E-value: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 48 ENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFC 127
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 128 SKNT-FQKVLNVKSKLKYVETIIIL--DLNEDLGGYQCLNNFISQNSDINLD-----VKKFKPNsfnrddQVALVMFSSG 199
Cdd:cd05933 87 ENQKqLQKILQIQDKLPHLKAIIQYkePLKEKEPNLYSWDEFMELGRSIPDEqldaiISSQKPN------QCCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 200 TTGVSKGVMLTHKNIV------ARFSHCKDPTFGNAInpttaILTVIPFHH----GFGMTTTLGYFTCGF-------RVA 262
Cdd:cd05933 161 TTGMPKGVMLSHDNITwtakaaSQHMDLRPATVGQES-----VVSYLPLSHiaaqILDIWLPIKVGGQVYfaqpdalKGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 263 LMHTF------------------EEKL---FLQS---------------LQDYKVESTLLVPTLMAFFPKSALV-----E 301
Cdd:cd05933 236 LVKTLrevrptafmgvprvwekiQEKMkavGAKSgtlkrkiaswakgvgLETNLKLMGGESPSPLFYRLAKKLVfkkvrK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 302 KYDLSHLKEIASGGAPLSKEIgemvkKRFKLNF---VRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTTG 378
Cdd:cd05933 316 ALGLDRCQKFFTGAAPISRET-----LEFFLSLnipIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDAD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688574 379 KIlgpnetGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQ-VAPAEIE 454
Cdd:cd05933 391 GI------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-530 |
7.19e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 123.07 E-value: 7.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK07798 31 YAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKYVETIIILD---LNEDLGGYQCLNNFISQNSDINLdvkkFKPNSfnRDDQvaLVMFSSGTTGVSKGVM 208
Cdd:PRK07798 111 APRVAEVLPRLPKLRTLVVVEdgsGNDLLPGAVDYEDALAAGSPERD----FGERS--PDDL--YLLYTGGTTGMPKGVM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 209 LTHKNIvaRFSHCKDPTFGN--------------AINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVAL--MHTFEEKLF 272
Cdd:PRK07798 183 WRQEDI--FRVLLGGRDFATgepiedeeelakraAAGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLlpDVRFDADEV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 273 LQSLQDYKVESTLLV------PTLMAFFPKsalvEKYDLSHLKEIASGGAPLSKEigemVKKRFKLNF----VRQGYGLT 342
Cdd:PRK07798 261 WRTIEREKVNVITIVgdamarPLLDALEAR----GPYDLSSLFAIASGGALFSPS----VKEALLELLpnvvLTDSIGSS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 343 ETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTTGKIL-GPNETGELYfKGDMIMKSYYNNEEATKAI---INKDGWLR 418
Cdd:PRK07798 333 ETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEpGSGEIGWIA-RRGHIPLGYYKDPEKTAETfptIDGVRYAI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 419 SGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQ 498
Cdd:PRK07798 412 PGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELR 491
|
490 500 510
....*....|....*....|....*....|..
gi 41688574 499 NFVSSQVSTAKWLRgGVKFLDEIPKGSTGKID 530
Cdd:PRK07798 492 AHCRSSLAGYKVPR-AIWFVDEVQRSPAGKAD 522
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
52-470 |
7.51e-30 |
|
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: 123.69 E-value: 7.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCS-KN 130
Cdd:cd17641 14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEdEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TFQKVLNVKSKLKYVETIIILDlNEDLGGYQ--CLNNFiSQNSDINLDVKKFKPNSFNRD------DQVALVMFSSGTTG 202
Cdd:cd17641 94 QVDKLLEIADRIPSVRYVIYCD-PRGMRKYDdpRLISF-EDVVALGRALDRRDPGLYEREvaagkgEDVAVLCTTSGTTG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 203 VSKGVMLTHKNIVarfSHCKDPTFGNAINPTTAILTVIPFHH-GFGMTTTLGYFTCGFRV-------ALMH--------- 265
Cdd:cd17641 172 KPKLAMLSHGNFL---GHCAAYLAADPLGPGDEYVSVLPLPWiGEQMYSVGQALVCGFIVnfpeepeTMMEdlreigptf 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 ------TFEEKL------------FLQSLQDYKVESTLLV--------PTLMAFFPKSALVEK---------YDLSHLKE 310
Cdd:cd17641 249 vllpprVWEGIAadvrarmmdatpFKRFMFELGMKLGLRAldrgkrgrPVSLWLRLASWLADAllfrplrdrLGFSRLRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 311 IASGGAPLSKEIgemvkKRFKLNF---VRQGYGLTETTSAVLITPDTDVRPGSTGkiVPFHAVKVvdpttgKIlgpNETG 387
Cdd:cd17641 329 AATGGAALGPDT-----FRFFHAIgvpLKQLYGQTELAGAYTVHRDGDVDPDTVG--VPFPGTEV------RI---DEVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 388 ELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIK-YKGYQVAPAEIEGILLQHPYIVDA 466
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPYIAEA 472
|
....
gi 41688574 467 GVTG 470
Cdd:cd17641 473 VVLG 476
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
189-540 |
1.44e-29 |
|
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: 121.50 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHckdptFGNA--INPTTAILTvipF-HHGFGMT-----TTLGYFTCGF- 259
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALA-----HGRAlgLTSESRVLQ---FaSYTFDVSileifTTLAAGGCLCi 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 260 --RVALMHTFEEklflqSLQDYKVESTLLVPTLMAffpksaLVEKYDLSHLKEIASGGAPLSKEI----GEMVKkrfkln 333
Cdd:cd05918 178 psEEDRLNDLAG-----FINRLRVTWAFLTPSVAR------LLDPEDVPSLRTLVLGGEALTQSDvdtwADRVR------ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 334 fVRQGYGLTETT-SAVLITPDTDVRPGSTGKIVPFHAVkVVDPTTGKILGP-NETGELYFKGDMIMKSYYNNEEATKAI- 410
Cdd:cd05918 241 -LINAYGPAECTiAATVSPVVPSTDPRNIGRPLGATCW-VVDPDNHDRLVPiGAVGELLIEGPILARGYLNDPEKTAAAf 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 411 INKDGWL------------RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHP---YIVDAGVTGIPDEA 475
Cdd:cd05918 319 IEDPAWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLpgaKEVVVEVVKPKDGS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 476 AGELPAAGVVVQTGKYLNEQIVQNFVS------SQVSTAK---------------WLrggvkFLDEIPKGSTGKIDRKVL 534
Cdd:cd05918 399 SSPQLVAFVVLDGSSSGSGDGDSLFLEpsdefrALVAELRsklrqrlpsymvpsvFL-----PLSHLPLTASGKIDRRAL 473
|
....*.
gi 41688574 535 RQMFEK 540
Cdd:cd05918 474 RELAES 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
52-542 |
1.70e-29 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 122.17 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKnT 131
Cdd:PRK06018 42 YAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL-T 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLN-VKSKLKYVETIIILDLNE-----DLGGYQCLNNFISQNSdinldvKKFKPNSFNRDDQVALVmFSSGTTGVSK 205
Cdd:PRK06018 121 FVPILEkIADKLPSVERYVVLTDAAhmpqtTLKNAVAYEEWIAEAD------GDFAWKTFDENTAAGMC-YTSGTTGDPK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 206 GVMLTHKNIVArfsHCKDPTFGNAINPTTA--ILTVIPFHHG--FGMTttlgyFTCGFRVALMHTFEEKLFLQS----LQ 277
Cdd:PRK06018 194 GVLYSHRSNVL---HALMANNGDALGTSAAdtMLPVVPLFHAnsWGIA-----FSAPSMGTKLVMPGAKLDGASvyelLD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 278 DYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEigeMVKKRFKLNF-VRQGYGLTET----TSAVLITP 352
Cdd:PRK06018 266 TEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRS---MIKAFEDMGVeVRHAWGMTEMsplgTLAALKPP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 353 DTDVRPGSTGKIV------PFHA-VKVVDPTtGKILgP---NETGELYFKGDMIMKSYYnneEATKAIINKDGWLRSGDI 422
Cdd:PRK06018 343 FSKLPGDARLDVLqkqgypPFGVeMKITDDA-GKEL-PwdgKTFGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 423 AYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVS 502
Cdd:PRK06018 418 ATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMD 497
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 41688574 503 SQVstAK-WLRGGVKFLDEIPKGSTGKIDRKVLRQMFEKHK 542
Cdd:PRK06018 498 GKI--AKwWMPDDVAFVDAIPHTATGKILKTALREQFKDYK 536
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-530 |
1.91e-29 |
|
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: 119.41 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQvaLVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTFGNAI-----------NPTTAILTVIPFHHGFGMTTTLGYFT 256
Cdd:cd05924 4 DDL--YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTpsedahkaaaaAAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 257 CGFRVALMHT-FEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEK--YDLSHLKEIASGGAPLSKEigemVKKRFkLN 333
Cdd:cd05924 82 GGQTVVLPDDrFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAgpYDLSSLFAISSGGALLSPE----VKQGL-LE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 334 FVRQ-----GYGLTETTSavLITPDTDVRPGSTGKIVPF-HAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEAT 407
Cdd:cd05924 157 LVPNitlvdAFGSSETGF--TGSGHSAGSGPETGPFTRAnPDTVVLDDDGRVVPPGSGGVGWIARRGHIPLGYYGDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 408 KAI---INKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGV 484
Cdd:cd05924 235 AETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 41688574 485 VVQTGKYLNEQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKID 530
Cdd:cd05924 315 QLREGAGVDLEELREHCRTRIARYKLPK-QVVFVDEIERSPAGKAD 359
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
52-545 |
2.21e-29 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 122.92 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQ 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKYVETIIILD---LNEDLGGYQCLNNFISQNSDI-NLDVKKFKPNSFNRDDQVALVMFSSGTTGVSKGV 207
Cdd:PLN02387 189 LKKLIDISSQLETVKRVIYMDdegVDSDSSLSGSSNWTVSSFSEVeKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 208 MLTHKNIVARFShckdptfgnainpttAILTVIPfhhGFGMTTT-LGYftcgfrVALMHTFE---EKLFLQS-------- 275
Cdd:PLN02387 269 MMTHGNIVATVA---------------GVMTVVP---KLGKNDVyLAY------LPLAHILElaaESVMAAVgaaigygs 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 ---LQDY--------KVESTLLVPTLMAFFP----------------KSALVEK-YDLSHLKEIA--------------- 312
Cdd:PLN02387 325 pltLTDTsnkikkgtKGDASALKPTLMTAVPaildrvrdgvrkkvdaKGGLAKKlFDIAYKRRLAaiegswfgawglekl 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 313 ----------------------SGGAPLSKEigemvKKRFkLNF-----VRQGYGLTETTSAVLITPDTDVRPGSTGKIV 365
Cdd:PLN02387 405 lwdalvfkkiravlggrirfmlSGGAPLSGD-----TQRF-INIclgapIGQGYGLTETCAGATFSEWDDTSVGRVGPPL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 366 PFHAVKVVDPTTGKIL---GPNETGELYFKGDMIMKSYYNNEEATKAIINKDG----WLRSGDIAYYDNDGHFYIVDRLK 438
Cdd:PLN02387 479 PCCYVKLVSWEEGGYLisdKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKK 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 439 SLIKYK-GYQVAPAEIEGILLQHPYIVDAGVTG-----------IPDEAAGELPAAGVVVQTGKYLN----EQIVQNFVS 502
Cdd:PLN02387 559 DIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHAdpfhsycvalvVPSQQALEKWAKKAGIDYSNFAElcekEEAVKEVQQ 638
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 41688574 503 SQVSTAKWLR-------GGVKFLDEIPKGSTG------KIDRKVLRQMFEKHKSKL 545
Cdd:PLN02387 639 SLSKAAKAARlekfeipAKIKLLPEPWTPESGlvtaalKLKREQIRKKFKDDLKKL 694
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
52-534 |
3.44e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 120.87 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK13383 63 YRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKsklkyvETIIILDlNEDLGGYQCLNNfisqnsdinldvKKFKPNSfnrddqvALVMFSSGTTGVSKGVMlth 211
Cdd:PRK13383 143 AERIAGAD------DAVAVID-PATAGAEESGGR------------PAVAAPG-------RIVLLTSGTTGKPKGVP--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 knivarfshcKDPTFGNAINPTTAIL------------TVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEKLFLQSLQDY 279
Cdd:PRK13383 194 ----------RAPQLRSAVGVWVTILdrtrlrtgsrisVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 280 KVESTLLVPTLMAF---FPKSALVeKYDLSHLKEIASGGAPLSKEIGEMVKKRFKlNFVRQGYGLTETTSAVLITPdTDV 356
Cdd:PRK13383 264 RADAFTAVPVVLARileLPPRVRA-RNPLPQLRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGSTEVGIGALATP-ADL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 357 R--PGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNeeATKAIInkDGWLRSGDIAYYDNDGHFYIV 434
Cdd:PRK13383 341 RdaPETVGKPVAGCPVRILD-RNNRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVV--DGMTSTGDMGYLDNAGRLFIV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 435 DRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKWLRgG 514
Cdd:PRK13383 416 GREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPR-D 494
|
490 500
....*....|....*....|
gi 41688574 515 VKFLDEIPKGSTGKIDRKVL 534
Cdd:PRK13383 495 INIVSSIPRNPTGKVLRKEL 514
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
196-545 |
4.94e-28 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 118.02 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 196 FSSGTTGVSKGVMLTHKN--IVArfshckdptFGNAI----NPTTAILTVIPFHH--GFGMTTTLGYFtCGFRVALMHTf 267
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGayLMA---------LSNALiwgmNEGAVYLWTLPMFHcnGWCFTWTLAAL-CGTNICLRQV- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 268 EEKLFLQSLQDYKVESTLLVPTLMAFF---PKSALVekYDLSHLKEI-ASGGAPLSKEIGEMVKKRFKlnfVRQGYGLTE 343
Cdd:PLN02479 271 TAKAIYSAIANYGVTHFCAAPVVLNTIvnaPKSETI--LPLPRVVHVmTAGAAPPPSVLFAMSEKGFR---VTHTYGLSE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 344 TTSAVLI---TPDTDVRPGSTG---------KIVPFHAVKVVDPTTGKILGPNET--GELYFKGDMIMKSYYNNEEATKA 409
Cdd:PLN02479 346 TYGPSTVcawKPEWDSLPPEEQarlnarqgvRYIGLEGLDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 410 IInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG 489
Cdd:PLN02479 426 AF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPG 504
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41688574 490 ------KYLNEQIVQnFVSSQVStAKWLRGGVKFlDEIPKGSTGKIDRKVLR----QMFEKHKSKL 545
Cdd:PLN02479 505 vdksdeAALAEDIMK-FCRERLP-AYWVPKSVVF-GPLPKTATGKIQKHVLRakakEMGPVKKSRL 567
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
187-536 |
7.19e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 117.17 E-value: 7.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 187 RDDQVALVMFSSGTTGVSKGvmlthknivARFSHCKDPtfgnaiNPTTAILTVIPFHHG------FGMTTTLGYFTCGFR 260
Cdd:PRK13382 194 TGRKGRVILLTSGTTGTPKG---------ARRSGPGGI------GTLKAILDRTPWRAEeptvivAPMFHAWGFSQLVLA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 261 VALMHT------FEEKLFLQSLQDYKVESTLLVPT----LMAFFPKsaLVEKYDLSHLKEIASGGAPLSKEIGEMVKKRF 330
Cdd:PRK13382 259 ASLACTivtrrrFDPEATLDLIDRHRATGLAVVPVmfdrIMDLPAE--VRNRYSGRSLRFAAASGSRMRPDVVIAFMDQF 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 331 KlNFVRQGYGLTETTSAVLITPDtDVR--PGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNeeATK 408
Cdd:PRK13382 337 G-DVIYNNYNATEAGMIATATPA-DLRaaPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGYTSG--STK 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 409 AIInkDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQT 488
Cdd:PRK13382 412 DFH--DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 41688574 489 GKYLNEQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:PRK13382 490 GASATPETLKQHVRDNLANYKVPR-DIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
189-539 |
8.60e-28 |
|
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: 116.82 E-value: 8.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTfgnAINPTTAILTVIPFHHGFGMTTtlGYFTC---GFRVALMH 265
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST---EWKTKDRILSWMPLTHDMGLIA--FHLAPliaGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 TFE----EKLFLQSLQDYKVeSTLLVPT-----LMAFFpKSALVEKYDLSHLKEIASGGAPLSKEIGE-----MVKKRFK 331
Cdd:cd05908 181 TRLfirrPILWLKKASEHKA-TIVSSPNfgykyFLKTL-KPEKANDWDLSSIRMILNGAEPIDYELCHefldhMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 332 LNFVRQGYGLTETTSAVLItPDTD-----------------------------VRPGSTGKIVPFHAVKVVDpTTGKILG 382
Cdd:cd05908 259 RNAILPVYGLAEASVGASL-PKAQspfktitlgrrhvthgepepevdkkdsecLTFVEVGKPIDETDIRICD-EDNKILP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 383 PNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNdGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQhpy 462
Cdd:cd05908 337 DGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPHDIERIAEE--- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 463 ivdagvtgIPDEAAGELPAAGVVVQTGKylNEQIV---------QNFV--SSQVSTAKWLRGG-----VKFLDEIPKGST 526
Cdd:cd05908 413 --------LEGVELGRVVACGVNNSNTR--NEEIFcfiehrkseDDFYplGKKIKKHLNKRGGwqineVLPIRRIPKTTS 482
|
410
....*....|...
gi 41688574 527 GKIDRKVLRQMFE 539
Cdd:cd05908 483 GKVKRYELAQRYQ 495
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
39-534 |
2.03e-27 |
|
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: 115.38 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 39 IALTnaHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLG 118
Cdd:cd12117 14 VAVV--YGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 119 IVKPRIIFCSKNTFQKVLnvksklkyvETIIILDLNEDLGGYQCLNnfisqnsdinldvkkfkPNSFNRDDQVALVMFSS 198
Cdd:cd12117 92 DAGAKVLLTDRSLAGRAG---------GLEVAVVIDEALDAGPAGN-----------------PAVPVSPDDLAYVMYTS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKNIVaRFshCKDPTFGnAINPTTAILTVIPfhHGFGmTTTLGYFTC---GFRVALMHTfEEKLFLQS 275
Cdd:cd12117 146 GSTGRPKGVAVTHRGVV-RL--VKNTNYV-TLGPDDRVLQTSP--LAFD-ASTFEIWGAllnGARLVLAPK-GTLLDPDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYKVE---STLLVPTlmAFFpkSALVEKYD--LSHLKEIASGGAPLS-KEIGEMVKKRFKLNFVrQGYGLTETT--SA 347
Cdd:cd12117 218 LGALIAEegvTVLWLTA--ALF--NQLADEDPecFAGLRELLTGGEVVSpPHVRRVLAACPGLRLV-NGYGPTENTtfTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 348 VLITPDTDVRPGST--GKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWL------RS 419
Cdd:cd12117 293 SHVVTELDEVAGSIpiGRPIANTRVYVLDED-GRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 420 GDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDeAAGELPAAGVVVQTGKyLNEQIVQN 499
Cdd:cd12117 372 GDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVRED-AGGDKRLVAYVVAEGA-LDAAELRA 449
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 41688574 500 FVssqvstAKWLRGG-----VKFLDEIPKGSTGKIDRKVL 534
Cdd:cd12117 450 FL------RERLPAYmvpaaFVVLDELPLTANGKVDRRAL 483
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
193-530 |
2.50e-27 |
|
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: 112.40 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 193 LVMFSSGTTGVSKGVMLTHKNIVARFSHCKDptfGNAINPTTAILTVIP-FHHGFGMTTtLGYFTCGFRVALMHTFEEKL 271
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAV---LQAIDEGTVFLNSGPlFHIGTLMFT-LATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 272 FLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEI--ASGGAPLSKEIGEMVKKRFKlnfvrqGYGLTETTSAVL 349
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSpaAPEWNDMATVDTSPWGRKPG------GYGQTEVMGLAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 350 ITPDTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEatkaiIN----KDGWLRSGDIAYY 425
Cdd:cd17636 154 FAALGGGAIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPE-----VNarrtRGGWHHTNDLGRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 426 DNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQV 505
Cdd:cd17636 228 EPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARI 307
|
330 340
....*....|....*....|....*
gi 41688574 506 STAKWLRgGVKFLDEIPKGSTGKID 530
Cdd:cd17636 308 ASYKKPK-SVEFADALPRTAGGADD 331
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
188-470 |
4.09e-27 |
|
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: 114.87 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNivarFSHCKDP---TFGnaINPTTAILTVIPFHHGFG-MTTTLGYFTCGFRVAl 263
Cdd:cd05932 136 PEQLATLIYTSGTTGQPKGVMLTFGS----FAWAAQAgieHIG--TEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVA- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 264 mhtFEEKL--FLQSLQDYKVESTLLVPTLMAFFPK--------------------SALVEK-----YDLSHLKEIASGGA 316
Cdd:cd05932 209 ---FAESLdtFVEDVQRARPTLFFSVPRLWTKFQQgvqdkipqqklnlllkipvvNSLVKRkvlkgLGLDQCRLAGCGSA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 317 PLSKEIGEMVKkRFKLNfVRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVvdpttgkilgpNETGELYFKGDMI 396
Cdd:cd05932 286 PVPPALLEWYR-SLGLN-ILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI-----------SEDGEILVRSPAL 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41688574 397 MKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKY-KGYQVAPAEIEGILLQHPYIVDAGVTG 470
Cdd:cd05932 353 MMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
189-534 |
4.45e-27 |
|
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: 113.95 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDpTFGN-------AINPTTAILTVipfhhgFGMTTTLgyfTCGFRV 261
Cdd:cd12115 105 DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAA-AFSAeelagvlASTSICFDLSV------FELFGPL---ATGGKV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 262 ALMHTfeeklfLQSLQDYKV--ESTLL--VPTLMAffpksALVEKYDL-SHLKEIASGGAPLSKEIGEMVKKRFKLNFVR 336
Cdd:cd12115 175 VLADN------VLALPDLPAaaEVTLIntVPSAAA-----ELLRHDALpASVRVVNLAGEPLPRDLVQRLYARLQVERVV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 337 QGYGLTETT--SAVLITPDTDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKD 414
Cdd:cd12115 244 NLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 415 GWL------RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQT 488
Cdd:cd12115 323 PFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEP 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 41688574 489 GKYLNEQIVQNFVSSQVStAKWLRGGVKFLDEIPKGSTGKIDRKVL 534
Cdd:cd12115 403 GAAGLVEDLRRHLGTRLP-AYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
39-534 |
5.56e-27 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 114.72 E-value: 5.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 39 IALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLG 118
Cdd:PRK05857 31 IALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 119 IVKPRIIFCSKNTFQKVLNVKSKLKYVETIIIlDLNEDLGGYQClnnfisqNSDInlDVKKFKPNSfNRDDQVALVmFSS 198
Cdd:PRK05857 111 ITDPAAALVAPGSKMASSAVPEALHSIPVIAV-DIAAVTRESEH-------SLDA--ASLAGNADQ-GSEDPLAMI-FTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKNIVA-----RFSHCKDPTFgnAINPTTaiLTVIPFHHGFGMTTTLgyfTCGFRVALMHTFEEKL-- 271
Cdd:PRK05857 179 GTTGEPKAVLLANRTFFAvpdilQKEGLNWVTW--VVGETT--YSPLPATHIGGLWWIL---TCLMHGGLCVTGGENTts 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 272 FLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGaplSKEIGEMVkkRF-KLNFVR--QGYGLTETTSAV 348
Cdd:PRK05857 252 LLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADV--RFiEATGVRtaQVYGLSETGCTA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 349 LITPDTD-----VRPGSTGKivPFHAVKVV-------DPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGW 416
Cdd:PRK05857 327 LCLPTDDgsivkIEAGAVGR--PYPGVDVYlaatdgiGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVL-IDGW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 417 LRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGEL------PAAGVVVQTGK 490
Cdd:PRK05857 404 VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALvglavvASAELDESAAR 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 41688574 491 YLNEQIVQNFVSSQVSTAKwlRGGVKFLDEIPKGSTGKIDRKVL 534
Cdd:PRK05857 484 ALKHTIAARFRRESEPMAR--PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
48-534 |
2.66e-25 |
|
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: 109.10 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 48 ENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERelihslgivkpRIIFC 127
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEE-----------RRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 128 SKNTFQKVL----NVKSKLKYVETIIILDlnedlggyqclNNFISQNSDINLdvkkfkpNSFNRDDQVALVMFSSGTTGV 203
Cdd:cd17656 81 MLDSGVRVVltqrHLKSKLSFNKSTILLE-----------DPSISQEDTSNI-------DYINNSDDLLYIIYTSGTTGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 204 SKGVMLTHKNIVARFSHCKDPTfgnainpttailtVIPFHHGfgmttTLGYFTCGFRVALMHTFEEKLFLQSLQDYKVES 283
Cdd:cd17656 143 PKGVQLEHKNMVNLLHFEREKT-------------NINFSDK-----VLQFATCSFDVCYQEIFSTLLSGGTLYIIREET 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 284 TLLVPTL----------MAFFPKSAL---VEKYDLSH-----LKEIASGGAPL--SKEIGEMVKKR-FKL-NFvrqgYGL 341
Cdd:cd17656 205 KRDVEQLfdlvkrhnieVVFLPVAFLkfiFSEREFINrfptcVKHIITAGEQLviTNEFKEMLHEHnVHLhNH----YGP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 342 TET--TSAVLITPDTDV-------RPGSTGKIVPFHAVKVVDPTtGKIlgpnetGELYFKGDMIMKSYYNNEEATKAIIN 412
Cdd:cd17656 281 SEThvVTTYTINPEAEIpelppigKPISNTWIYILDQEQQLQPQ-GIV------GELYISGASVARGYLNRQELTAEKFF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 413 KDGW------LRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAG-ELPAAGVV 485
Cdd:cd17656 354 PDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEkYLCAYFVM 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 41688574 486 VQTgkyLNEQIVQNFVSSQVS----TAKWLRggvkfLDEIPKGSTGKIDRKVL 534
Cdd:cd17656 434 EQE---LNISQLREYLAKQLPeymiPSFFVP-----LDQLPLTPNGKVDRKAL 478
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
73-534 |
2.75e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 110.22 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 73 QNDTIAVCSENGLQfflPLIASLYLGIIAAP---VSDKYIERELIHSLGIVKPRIIFCSKNTF--QKVLNVKSKLKYVET 147
Cdd:PTZ00237 116 KNDNVLIYMANTLE---PLIAMLSCARIGAThcvLFDGYSVKSLIDRIETITPKLIITTNYGIlnDEIITFTPNLKEAIE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 148 IIILDLNEDLGGYQclNNFISQNSDINLDVKKFKPNSFNRDDQVA----------------------LVMFSSGTTGVSK 205
Cdd:PTZ00237 193 LSTFKPSNVITLFR--NDITSESDLKKIETIPTIPNTLSWYDEIKkikennqspfyeyvpvesshplYILYTSGTTGNSK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 206 GVM----------------LTHKNIVAR-FSHCKdptfgnainpttaiLTVIPFHHGFGMTTTLGYFTCGFRVALMHTFE 268
Cdd:PTZ00237 271 AVVrsngphlvglkyywrsIIEKDIPTVvFSHSS--------------IGWVSFHGFLYGSLSLGNTFVMFEGGIIKNKH 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 269 -EKLFLQSLQDYKVESTLLVPTLMAFFPK-----SALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRqGYGLT 342
Cdd:PTZ00237 337 iEDDLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR-GYGQT 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 343 ETTSAVLITPDTDVRPGSTgKIVPFHAVK-VVDPTTGKILGPNETGELYFKGDM---IMKSYYNNEEATKAIINK-DGWL 417
Cdd:PTZ00237 416 EIGITYLYCYGHINIPYNA-TGVPSIFIKpSILSEDGKELNVNEIGEVAFKLPMppsFATTFYKNDEKFKQLFSKfPGYY 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 418 RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGK------- 490
Cdd:PTZ00237 495 NSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQsnqsidl 574
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 41688574 491 -----YLNEQIVQNFVSSQVSTAkwlrggVKFLDEIPKGSTGKIDRKVL 534
Cdd:PTZ00237 575 nklknEINNIITQDIESLAVLRK------IIIVNQLPKTKTGKIPRQII 617
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
125-470 |
3.54e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 109.80 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 125 IFCSKNTFQKVLNVKSKLKYVETIIILDLNEDL-----GGYQC----LNNFISQNsdiNLDVKKFKPNsfnRDDQVALVM 195
Cdd:PLN02736 154 IFCVPQTLNTLLSCLSEIPSVRLIVVVGGADEPlpslpSGTGVeivtYSKLLAQG---RSSPQPFRPP---KPEDVATIC 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 196 FSSGTTGVSKGVMLTHKNIVArfsHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVAlmhtFEEKLFLQS 275
Cdd:PLN02736 228 YTSGTTGTPKGVVLTHGNLIA---NVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVG----FYQGDNLKL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYkvesTLLVPTLMAFFPK-----------------------------------------SALVEKYDLSHLKE---- 310
Cdd:PLN02736 301 MDDL----AALRPTIFCSVPRlynriydgitnavkesgglkerlfnaaynakkqalengknpSPMWDRLVFNKIKAklgg 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 311 ----IASGGAPLSKEIGEMVKKRFKlNFVRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVD-P----TTGKil 381
Cdd:PLN02736 377 rvrfMSSGASPLSPDVMEFLRICFG-GRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvPemnyTSED-- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 382 GPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKY-KGYQVAPAEIEGILLQH 460
Cdd:PLN02736 454 QPYPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYAKC 533
|
410
....*....|
gi 41688574 461 PYIVDAGVTG 470
Cdd:PLN02736 534 KFVAQCFVYG 543
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
52-538 |
7.03e-25 |
|
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: 108.73 E-value: 7.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:cd05968 94 YGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQ--KVLNVKSKLKY-------VETIIIL-DLNEDLGGYqcLNNFISQNsdinlDVKKFKPNSFNR---DDQVaLVMFSS 198
Cdd:cd05968 174 TRrgREVNLKEEADKacaqcptVEKVVVVrHLGNDFTPA--KGRDLSYD-----EEKETAGDGAERtesEDPL-MIIYTS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKN--IVARFshckDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALM-----HTFEEKL 271
Cdd:cd05968 246 GTTGKPKGTVHVHAGfpLKAAQ----DMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYdgapdHPKADRL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 272 FlQSLQDYKVESTLLVPTLM-AFFPK-SALVEKYDLSHLKEIASGGAPLSKE----IGEMVKKRFK--LNFVrqgyGLTE 343
Cdd:cd05968 322 W-RMVEDHEITHLGLSPTLIrALKPRgDAPVNAHDLSSLRVLGSTGEPWNPEpwnwLFETVGKGRNpiINYS----GGTE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 344 TTSA----VLITPdtdVRPGSTGKIVPFHAVKVVDPTTGKIlgPNETGELYFKGDMI--MKSYYNNEEA-TKAIINK-DG 415
Cdd:cd05968 397 ISGGilgnVLIKP---IKPSSFNGPVPGMKADVLDESGKPA--RPEVGELVLLAPWPgmTRGFWRDEDRyLETYWSRfDN 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 416 WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQ 495
Cdd:cd05968 472 VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEA 551
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 41688574 496 I---VQNFVSSQVstAKWLR-GGVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:cd05968 552 LaeeLMERVADEL--GKPLSpERILFVKDLPKTRNAKVMRRVIRAAY 596
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
186-534 |
9.45e-25 |
|
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: 107.01 E-value: 9.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 186 NRDDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCkDPTFGnaINPTTAILTvipFHH---GFGMTTTLGYFTCGFRVA 262
Cdd:cd17643 90 TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT-QRWFG--FNEDDVWTL---FHSyafDFSVWEIWGALLHGGRLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 263 LMH---TFEEKLFLQSLQDYKVesTLLVPTLMAF--FPKSALVEKYDLSHLKEIASGGAPLskEIGeMVK---KRFKLNF 334
Cdd:cd17643 164 VVPyevARSPEDFARLLRDEGV--TVLNQTPSAFyqLVEAADRDGRDPLALRYVIFGGEAL--EAA-MLRpwaGRFGLDR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 335 VR--QGYGLTETTSAVLITP-DTDVRPGST----GKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEE-- 405
Cdd:cd17643 239 PQlvNMYGITETTVHVTFRPlDAADLPAAAaspiGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPElt 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 406 ATKAIINKDG-----WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELP 480
Cdd:cd17643 318 AERFVANPFGgpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRL 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688574 481 AAGVVVQtgkylneqivqnfvSSQVSTAKWLRGGVK-------------FLDEIPKGSTGKIDRKVL 534
Cdd:cd17643 398 VAYVVAD--------------DGAAADIAELRALLKellpdymvparyvPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
186-536 |
2.07e-24 |
|
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: 105.85 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 186 NRDDQVALVMFSSGTTGVSKGVMLTHKNIVarfSHCKDPTFGNAINPTTAILTV--IPFHHGFGMT-TTLGYftcGFRVA 262
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVL---NYVSQPPARLDVGPGSRVAQVlsIAFDACIGEIfSTLCN---GGTLV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 263 L---MHTFEEKLflqslqdYKVESTLLVPTLMAFFPKSalvekyDLSHLKEIASGGAPLSKEIGEMVKKRFKL-NfvrqG 338
Cdd:cd17653 176 LadpSDPFAHVA-------RTVDALMSTPSILSTLSPQ------DFPNLKTIFLGGEAVPPSLLDRWSPGRRLyN----A 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 YGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPTTGKILGPnETGELYFKGDMIMKSYYNNEEAT--KAIINKD-- 414
Cdd:cd17653 239 YGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEG-VVGEICISGVQVARGYLGNPALTasKFVPDPFwp 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 415 GWL--RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEA--AGELPAAGVVVQTGK 490
Cdd:cd17653 318 GSRmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGRlvAFVTPETVDVDGLRS 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 41688574 491 YLNEQIVQNFVSSqvstaKWLRggvkfLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd17653 398 ELAKHLPSYAVPD-----RIIA-----LDSFPLTANGKVDRKALRE 433
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
62-468 |
7.22e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 105.83 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 62 LAEsfkkYGLKQNDTIAVCSENGLQFFlpliASLYlGI-----IAAPVSDKYIERELIHSLGIVKPRIIFCSKNTFQKVL 136
Cdd:PTZ00216 138 LAE----LGLTKGSNVAIYEETRWEWL----ASIY-GIwsqsmVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 137 NVKSKLKYVETIII----LDLNEDLGGYQclnnfISQNSDI----NLDVKKFKPNSFNRDDQVALVMFSSGTTGVSKGVM 208
Cdd:PTZ00216 209 RLMKSGGMPNTTIIyldsLPASVDTEGCR-----LVAWTDVvakgHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVM 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 209 LTHKNIVARFSHCkDPTFGNAINPTT---AILTVIPFHH-----------------GFGMTTTLG--------------- 253
Cdd:PTZ00216 284 HTHGSLTAGILAL-EDRLNDLIGPPEedeTYCSYLPLAHimefgvtniflargaliGFGSPRTLTdtfarphgdltefrp 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 254 YFTCGF-RV--ALMHTFEEKL-----FLQSLQDYKVESTLlvptlmaffpkSALVEKYDLSHLKE--------------- 310
Cdd:PTZ00216 363 VFLIGVpRIfdTIKKAVEAKLppvgsLKRRVFDHAYQSRL-----------RALKEGKDTPYWNEkvfsapravlggrvr 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 311 -IASGGAPLSKEIGEMVKKRFKLnfVRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPT----TGKilgPNE 385
Cdd:PTZ00216 432 aMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEeykhTDT---PEP 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 386 TGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIK-YKGYQVAPAEIEGILLQHPYIV 464
Cdd:PTZ00216 507 RGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNELVV 586
|
....
gi 41688574 465 DAGV 468
Cdd:PTZ00216 587 PNGV 590
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
52-472 |
1.46e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 104.57 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK08279 65 YAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKVLNVKSKLKYVETIIILDLNE--DLGGYQCLNNFISQNSDINLDVKKfkpNSFNRDDqvALVMFSSGTTGVSKGVML 209
Cdd:PRK08279 145 VEAFEEARADLARPPRLWVAGGDTldDPEGYEDLAAAAAGAPTTNPASRS---GVTAKDT--AFYIYTSGTTGLPKAAVM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 210 THKNIVARFShckdpTFGN--AINPTTAILTVIPFHHGFGMTTTLG-YFTCGFRVALMHTFEEKLFLQSLQDYKVesTL- 285
Cdd:PRK08279 220 SHMRWLKAMG-----GFGGllRLTPDDVLYCCLPLYHNTGGTVAWSsVLAAGATLALRRKFSASRFWDDVRRYRA--TAf 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 286 -----LVPTLMAFFPKSAlvekyDLSH-LKEIAsgGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLitpDTDVRPG 359
Cdd:PRK08279 293 qyigeLCRYLLNQPPKPT-----DRDHrLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFI---NVFNFDG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 360 STGkIVPF---HAVKVV--DPTTGKIL----------GPNETGELY--------FKGdmimksyYNNEEATKAIINKDG- 415
Cdd:PRK08279 363 TVG-RVPLwlaHPYAIVkyDVDTGEPVrdadgrcikvKPGEVGLLIgritdrgpFDG-------YTDPEASEKKILRDVf 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41688574 416 -----WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIP 472
Cdd:PRK08279 435 kkgdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVE 496
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
52-529 |
3.59e-23 |
|
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: 103.43 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVcsenglqfFLPLI--------ASLYLGIIAAPVSDKYIERELIHSLGIVKPR 123
Cdd:cd17634 87 YRELHREVCRFAGTLLDLGVKKGDRVAI--------YMPMIpeaavamlACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 124 IIFCSKNTFQ--KVLNVKS--------KLKYVETIIILDLNEDLGGYQCLNNFiSQNSDINLDVKKFKPNSFNRDDQVaL 193
Cdd:cd17634 159 LLITADGGVRagRSVPLKKnvddalnpNVTSVEHVIVLKRTGSDIDWQEGRDL-WWRDLIAKASPEHQPEAMNAEDPL-F 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 194 VMFSSGTTGVSKGVMLTHKnivarfshckdptfGNAINPTTAILTVIPFHHG--FGMTTTLGYFT-----------CGFR 260
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTG--------------GYLVYAATTMKYVFDYGPGdiYWCTADVGWVTghsyllygplaCGAT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 261 VALmhtFEEK-------LFLQSLQDYKVESTLLVPT----LMAFFPKSalVEKYDLSHLKEIASGGAPLSKEIGEMVKKR 329
Cdd:cd17634 303 TLL---YEGVpnwptpaRMWQVVDKHGVNILYTAPTairaLMAAGDDA--IEGTDRSSLRILGSVGEPINPEAYEWYWKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 330 FKLNF--VRQGYGLTETTSAVlITP---DTDVRPGSTGKIVPFHAVKVVDpTTGKILGPNETGELYFKGD---MIMKSYY 401
Cdd:cd17634 378 IGKEKcpVVDTWWQTETGGFM-ITPlpgAIELKAGSATRPVFGVQPAVVD-NEGHPQPGGTEGNLVITDPwpgQTRTLFG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 402 NNEEATKAIINK-DGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELP 480
Cdd:cd17634 456 DHERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAP 535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 41688574 481 AAGVVVQTGKYLNEQI---VQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKI 529
Cdd:cd17634 536 YAYVVLNHGVEPSPELyaeLRNWVRKEIGPLATPD-VVHWVDSLPKTRSGKI 586
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
52-489 |
3.60e-23 |
|
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: 104.17 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQfflpLIASLyLGIIAA-----PVSDKY-IEReLIHSLGIVKPRII 125
Cdd:COG1020 504 YAELNARANRLAHHLRALGVGPGDLVGVCLERSLE----MVVAL-LAVLKAgaayvPLDPAYpAER-LAYMLEDAGARLV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 126 FCSKNTFQKVLNvksklkYVETIIILDLNEdlggyqclnnfISQNSDINldvkkfkPNSFNRDDQVALVMFSSGTTGVSK 205
Cdd:COG1020 578 LTQSALAARLPE------LGVPVLALDALA-----------LAAEPATN-------PPVPVTPDDLAYVIYTSGSTGRPK 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 206 GVMLTHKNIVARFSHCKDpTFGnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALM---HTFEEKLFLQSLQDYKVE 282
Cdd:COG1020 634 GVMVEHRALVNLLAWMQR-RYG--LGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAppeARRDPAALAELLARHRVT 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 283 STLLVPTLMAffpksALVE--KYDLSHLKEIASGGAPLSKEIGEMVKKRFK----LNfvrqGYGLTETT---SAVLITPD 353
Cdd:COG1020 711 VLNLTPSLLR-----ALLDaaPEALPSLRLVLVGGEALPPELVRRWRARLPgarlVN----LYGPTETTvdsTYYEVTPP 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 354 TDVRPGST-GKIVPFHAVKVVDPtTGKILGPNETGELYFKGDMIMKSYYNNEEATKA--IIN---KDG--WLRSGDIAYY 425
Cdd:COG1020 782 DADGGSVPiGRPIANTRVYVLDA-HLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfVADpfgFPGarLYRTGDLARW 860
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688574 426 DNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG 489
Cdd:COG1020 861 LPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
52-536 |
5.34e-23 |
|
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: 102.13 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKK-YGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIvkpriifcSKN 130
Cdd:cd05937 8 YSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKL--------SGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 131 TFqkvlnvksklkyvetiIILDlnedlggyqclnnfisqnsdinldvkkfkpnsfnrDDQVALVMFSSGTTGVSKGVMLT 210
Cdd:cd05937 80 RF----------------VIVD-----------------------------------PDDPAILIYTSGTTGLPKAAAIS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 211 -HKNIVAR--FSHckdpTFGNAINPTTaiLTVIPFHHGFGmtTTLGYFTC---GFRVALMHTFEEKLFLQslQDYKVEST 284
Cdd:cd05937 109 wRRTLVTSnlLSH----DLNLKNGDRT--YTCMPLYHGTA--AFLGACNClmsGGTLALSRKFSASQFWK--DVRDSGAT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 285 LLVPT------LMAFfPKSalveKYDLSHlKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLitpDTDVRP 358
Cdd:cd05937 179 IIQYVgelcryLLST-PPS----PYDRDH-KVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALT---NHNVGD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 359 GSTGKI--------VPFHAVKV---VDPTTGKILGPNETG-----ELYFKGDMIMK----------SYYNNEEATKA--- 409
Cdd:cd05937 250 FGAGAIghhglirrWKFENQVVlvkMDPETDDPIRDPKTGfcvraPVGEPGEMLGRvpfknreafqGYLHNEDATESklv 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 410 --IINK-DGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIP----DEAAGelpAA 482
Cdd:cd05937 330 rdVFRKgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghDGRAG---CA 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41688574 483 GVVVQTgkylNEQIVQNFVSSqvSTAKWLRGG---------VKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05937 407 AITLEE----SSAVPTEFTKS--LLASLARKNlpsyavplfLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
186-540 |
5.36e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 103.51 E-value: 5.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 186 NRDDQVALVMFSSGTTGVSKGVMLTHKNIVArfsHCKDPTFGNAINPTTAILTVIPFHHGFGMTTtlgyftcGFRVALMH 265
Cdd:PRK06814 790 RDPDDPAVILFTSGSEGTPKGVVLSHRNLLA---NRAQVAARIDFSPEDKVFNALPVFHSFGLTG-------GLVLPLLS 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 TFeeKLFL-QSLQDYKV--------ESTLLVPT---LMAFfPKSAlvEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLN 333
Cdd:PRK06814 860 GV--KVFLyPSPLHYRIipeliydtNATILFGTdtfLNGY-ARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIR 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 334 fVRQGYGLTETtSAVLI--TPDTDvRPGSTGKIVPfhavkVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAII 411
Cdd:PRK06814 935 -ILEGYGVTET-APVIAlnTPMHN-KAGTVGRLLP-----GIEYRLEPVPGIDEGGRLFVRGPNVMLGYLRAENPGVLEP 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 412 NKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGilLQHPYIVDAG--VTGIPDEAAGElpaAGVVVQTG 489
Cdd:PRK06814 1007 PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE--LAAELWPDALhaAVSIPDARKGE---RIILLTTA 1081
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 41688574 490 KYLNEQIVQNFVSSQVSTAKWLRGGVKFLDEIPKGSTGKIDRKVLRQMFEK 540
Cdd:PRK06814 1082 SDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEE 1132
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
189-535 |
1.08e-22 |
|
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: 100.91 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVArfsHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVAL--MHT 266
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAA---HCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLrpDEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 FEEKLFLQSLQDYKVESTLLVPTlmAFFPKSALVEKYDLSH----LKEIASGGAPLSkeiGEMVKKRFKLNfVR--QGYG 340
Cdd:cd17649 171 WASADELAEMVRELGVTVLDLPP--AYLQQLAEEADRTGDGrppsLRLYIFGGEALS---PELLRRWLKAP-VRlfNAYG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 341 LTETTsavlITPDT-DVRPGST--------GKIVPFHAVKVVDPTTGkILGPNETGELYFKGDMIMKSYYNNEEATKA-- 409
Cdd:cd17649 245 PTEAT----VTPLVwKCEAGAAragasmpiGRPLGGRSAYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTAErf 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 410 IINKDG-----WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELpAAGV 484
Cdd:cd17649 320 VPDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VAYV 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 485 VVQTGKYLNEQIVQnfvssqvsTAKWLRGG---------VKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd17649 399 VLRAAAAQPELRAQ--------LRTALRASlpdymvpahLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
188-538 |
1.36e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 101.40 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKnivARFSHCKD--PTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGfrvALMH 265
Cdd:PRK05620 180 ETTAAAICYSTGTTGAPKGVVYSHR---SLYLQSLSlrTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSG---TPLV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 TFEEKLFLQSLQdyKVESTLL------VPTLMAffpksALVEKYDLSH-----LKEIASGGAPLSKEIGEMVKKRFKLNF 334
Cdd:PRK05620 254 FPGPDLSAPTLA--KIIATAMprvahgVPTLWI-----QLMVHYLKNPpermsLQEIYVGGSAVPPILIKAWEERYGVDV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 335 VrQGYGLTETTsavliTPDTDVRPG-------------STGKivpFHA---VKVVDptTGKILGPNE--TGELYFKGDMI 396
Cdd:PRK05620 327 V-HVWGMTETS-----PVGTVARPPsgvsgearwayrvSQGR---FPAsleYRIVN--DGQVMESTDrnEGEIQVRGNWV 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 397 MKSYYNNE----------------EATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQH 460
Cdd:PRK05620 396 TASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAA 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 461 PYIVDAGVTGIPDEAAGELPAAGVVVQTGkylneqivqnfVSSQVSTAKWLRGGVK-------------FLDEIPKGSTG 527
Cdd:PRK05620 476 PEVVECAVIGYPDDKWGERPLAVTVLAPG-----------IEPTRETAERLRDQLRdrlpnwmlpeywtFVDEIDKTSVG 544
|
410
....*....|.
gi 41688574 528 KIDRKVLRQMF 538
Cdd:PRK05620 545 KFDKKDLRQHL 555
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
189-534 |
1.36e-22 |
|
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: 100.40 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNI-------VARFshckdptfgnAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRV 261
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLanlaaaqIAAF----------DVGPGSRVLQFASPSFDASVWELLMALLAGATL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 262 ALMHTfEEKL----FLQSLQDYKVESTLLVPTLMAFFPKSALVEkydlshLKEIASGGAPLSkeiGEMVKK----RFKLN 333
Cdd:cd17652 163 VLAPA-EELLpgepLADLLREHRITHVTLPPAALAALPPDDLPD------LRTLVVAGEACP---AELVDRwapgRRMIN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 334 fvrqGYGLTETT-SAVLITPDTDVRPGSTGKIVPFHAVKVVDPTTgKILGPNETGELYFKGDMIMKSYYNNEEAT--KAI 410
Cdd:cd17652 233 ----AYGPTETTvCATMAGPLPGGGVPPIGRPVPGTRVYVLDARL-RPVPPGVPGELYIAGAGLARGYLNRPGLTaeRFV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 411 INKDGWL-----RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVV 485
Cdd:cd17652 308 ADPFGAPgsrmyRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 41688574 486 VQTGK---------YLNEQIVQNFVSSQVSTakwlrggvkfLDEIPKGSTGKIDRKVL 534
Cdd:cd17652 388 PAPGAaptaaelraHLAERLPGYMVPAAFVV----------LDALPLTPNGKLDRRAL 435
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
180-470 |
1.55e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 101.82 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 180 FKPNSFNrddqVALVMFSSGTTGVSKGVMLTHKNiVARFSHCKD---PTFGNAINPTTAILTVIPFHHGFGMTTTLGYFT 256
Cdd:PLN02430 215 NPPKPLD----ICTIMYTSGTSGDPKGVVLTHEA-VATFVRGVDlfmEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 257 CGFRVALMHTFeeklfLQSLQDYKVEstlLVPTLMAFFP----------KSALVE-------------KYDLSHLKE--- 310
Cdd:PLN02430 290 KGASVGYYHGD-----LNALRDDLME---LKPTLLAGVPrvferihegiQKALQElnprrrlifnalyKYKLAWMNRgys 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 311 --------------------------IASGGAPLSKEIGEMVKKRfKLNFVRQGYGLTETTSAVLIT-PDTDVRPGSTGK 363
Cdd:PLN02430 362 hkkaspmadflafrkvkaklggrlrlLISGGAPLSTEIEEFLRVT-SCAFVVQGYGLTETLGPTTLGfPDEMCMLGTVGA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 364 IVPFHAVKVVD-PTTG-KILGPNETGELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLI 441
Cdd:PLN02430 441 PAVYNELRLEEvPEMGyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLI 519
|
330 340 350
....*....|....*....|....*....|
gi 41688574 442 KY-KGYQVAPAEIEGILLQHPYIVDAGVTG 470
Cdd:PLN02430 520 KLsQGEYVALEYLENVYGQNPIVEDIWVYG 549
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
189-534 |
1.67e-22 |
|
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: 100.32 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVaRFSHCKDPTFGNAINPTTAILTVIPFHhGFGMTTtLGYFTCGfrvALMHTFE 268
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEWHRPYFGVTPADKSLVYASFSFD-ASAWEI-FPHLTAG---AALHVVP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 269 E--KLFLQSLQDYKVESTLLVptlmAFFPkSALVEKY---DLSHLKEIASGGAPLSKeigeMVKKRFKLnfvRQGYGLTE 343
Cdd:cd17645 178 SerRLDLDALNDYFNQEGITI----SFLP-TGAAEQFmqlDNQSLRVLLTGGDKLKK----IERKGYKL---VNNYGPTE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 344 TTSAVLITP-DTDVRPGSTGKivPFHAVKVVDPTTGKILGP-NETGELYFKGDMIMKSYYNNEEAT--KAIINK----DG 415
Cdd:cd17645 246 NTVVATSFEiDKPYANIPIGK--PIDNTRVYILDEALQLQPiGVAGELCIAGEGLARGYLNRPELTaeKFIVHPfvpgER 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 416 WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNE- 494
Cdd:cd17645 324 MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEEl 403
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 41688574 495 -QIVQNFVSSQVSTAKWLRggvkfLDEIPKGSTGKIDRKVL 534
Cdd:cd17645 404 rEWLKNDLPDYMIPTYFVH-----LKALPLTANGKVDRKAL 439
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
51-538 |
2.39e-22 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 100.85 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 51 LYEEFLKLSCRLAesfkKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVS--------DKYIErELIHSLGIVKP 122
Cdd:PRK09192 55 LRARAEAGARRLL----ALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlpmgfggrESYIA-QLRGMLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 123 RIIFCSK--NTFQKVLNVKSKLKYVETIIILDLNEDlggyqclnnfisqnSDINLDVkkfkpnsfNRDDQVALVMFSSGT 200
Cdd:PRK09192 130 AAIITPDelLPWVNEATHGNPLLHVLSHAWFKALPE--------------ADVALPR--------PTPDDIAYLQYSSGS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 201 TGVSKGVMLTHKNIVARFS-HCKDptfGNAINPTTAILTVIPFHHGFGMtttLGYF----TCGFRVALMHTFEeklF--- 272
Cdd:PRK09192 188 TRFPRGVIITHRALMANLRaISHD---GLKVRPGDRCVSWLPFYHDMGL---VGFLltpvATQLSVDYLPTRD---Farr 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 273 -LQSLQDY-KVESTLLV-PT----LMAFFPKSALVEKYDLSHLKeIASGGAplskeigEMVK----KRFKLNFVRQG--- 338
Cdd:PRK09192 259 pLQWLDLIsRNRGTISYsPPfgyeLCARRVNSKDLAELDLSCWR-VAGIGA-------DMIRpdvlHQFAEAFAPAGfdd 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 ------YGLTETTSAVLITP------------------DTDVRPGS----------TGKIVPFHAVKVVDPTtGKILGPN 384
Cdd:PRK09192 331 kafmpsYGLAEATLAVSFSPlgsgivveevdrdrleyqGKAVAPGAetrrvrtfvnCGKALPGHEIEIRNEA-GMPLPER 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 385 ETGELYFKGDMIMKSYYNNEEATKAIiNKDGWLRSGDIAYYdNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIV 464
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELR 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 465 --DAGVTGIPDEaAGELPAAGVVVQTGKYLNEQIVQNFVSSQVSTAKwlrgGVKFLDE------IPKGSTGKIDRKVLRQ 536
Cdd:PRK09192 488 sgDAAAFSIAQE-NGEKIVLLVQCRISDEERRGQLIHALAALVRSEF----GVEAAVElvpphsLPRTSSGKLSRAKAKK 562
|
..
gi 41688574 537 MF 538
Cdd:PRK09192 563 RY 564
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
52-472 |
2.75e-22 |
|
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: 99.74 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFcsknt 131
Cdd:cd05940 6 YAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqkvlnvksklkyVETiiildlnedlggyqclnnfisqnsdinldvkkfkpnsfnrddqvALVMFSSGTTGVSKGVMLTH 211
Cdd:cd05940 81 -------------VDA--------------------------------------------ALYIYTSGTTGLPKAAIISH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIV---ARFSHckdpTFGNAinPTTAILTVIPFHHGFGMTttLGYFTC---GFRVALMHTFEEKLFLQSLQDYKVESTL 285
Cdd:cd05940 104 RRAWrggAFFAG----SGGAL--PSDVLYTCLPLYHSTALI--VGWSAClasGATLVIRKKFSASNFWDDIRKYQATIFQ 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 286 LVPTLMAFFPKSALVEkYDLSHLKEIASGGApLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLitpDTDVRPGSTGKIV 365
Cdd:cd05940 176 YIGELCRYLLNQPPKP-TERKHKVRMIFGNG-LRPDIWEEFKERFGVPRIAEFYAATEGNSGFI---NFFGKPGAIGRNP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 366 PFHA-------VKVvDPTTGKIL----------GPNETGELY--------FKGdmimksYYNNEEATKAIIN---KDG-- 415
Cdd:cd05940 251 SLLRkvaplalVKY-DLESGEPIrdaegrcikvPRGEPGLLIsrinplepFDG------YTDPAATEKKILRdvfKKGda 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 41688574 416 WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIP 472
Cdd:cd05940 324 WFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
39-535 |
4.63e-22 |
|
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: 99.34 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 39 IALTNAHTKenVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLG 118
Cdd:cd17651 12 PALVAEGRR--LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 119 IVKPRIIFcSKNTFQKVLNVKsklkyVETIIILDLNEDLGGyqclnnfisqnSDINLDVKKfkpnsfNRDDQvALVMFSS 198
Cdd:cd17651 90 DAGPVLVL-THPALAGELAVE-----LVAVTLLDQPGAAAG-----------ADAEPDPAL------DADDL-AYVIYTS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 199 GTTGVSKGVMLTHKNIV------ARFShckdptfgnAINPTTAILTVIPFhhGFGMTT--TLGYFTCGfrvALMHTFEEK 270
Cdd:cd17651 146 GSTGRPKGVVMPHRSLAnlvawqARAS---------SLGPGARTLQFAGL--GFDVSVqeIFSTLCAG---ATLVLPPEE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 271 L------FLQSLQDYKVESTLLvPTLMAffpkSALVEKYD-----LSHLKEIASGGAPLS--KEIGEMVKKRFKLNFVRQ 337
Cdd:cd17651 212 VrtdppaLAAWLDEQRISRVFL-PTVAL----RALAEHGRplgvrLAALRYLLTGGEQLVltEDLREFCAGLPGLRLHNH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 338 gYGLTETTSAVLITPDTDV----RPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINK 413
Cdd:cd17651 287 -YGPTETHVVTALSLPGDPaawpAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 414 DGWL------RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQ 487
Cdd:cd17651 365 DPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGD 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 41688574 488 TGKY-----LNEQIVQNFVSSQVSTAkwlrggVKFLDEIPKGSTGKIDRKVLR 535
Cdd:cd17651 445 PEAPvdaaeLRAALATHLPEYMVPSA------FVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
187-534 |
1.05e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 98.13 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 187 RDDQVALVMFSSGTTGVSKGVMLTHKNIVArFSHCKDPTFGnaINPTTAILTVIPFhhGFGMTT--TLGYFTCGFRVALM 264
Cdd:cd12116 124 SPDDLAYVIYTSGSTGRPKGVVVSHRNLVN-FLHSMRERLG--LGPGDRLLAVTTY--AFDISLleLLLPLLAGARVVIA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 265 ---HTFEEKLFLQSLQDYKVesTLL--VPTLMAFFPKSALVEKYDLSHLkeiaSGGAPLSKEIGEmvkkrfklNFVRQG- 338
Cdd:cd12116 199 preTQRDPEALARLIEAHSI--TVMqaTPATWRMLLDAGWQGRAGLTAL----CGGEALPPDLAA--------RLLSRVg 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 -----YGLTETT--SAVlitpdTDVRPGST----GKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEAT 407
Cdd:cd12116 265 slwnlYGPTETTiwSTA-----ARVTAAAGpipiGRPLANTQVYVLDAA-LRPVPPGVPGELYIGGDGVAQGYLGRPALT 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 408 KAIINKDG-------WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELp 480
Cdd:cd12116 339 AERFVPDPfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL- 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 41688574 481 AAGVVVQTGKYLNEQIVQNFVSSQVStAKWLRGGVKFLDEIPKGSTGKIDRKVL 534
Cdd:cd12116 418 VAYVVLKAGAAPDAAALRAHLRATLP-AYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
39-534 |
1.86e-21 |
|
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: 97.34 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 39 IALtnAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVS-DKYIER-ELIHS 116
Cdd:cd12114 4 TAV--ICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDiDQPAARrEAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 117 LGIVKpRIIFCSKNTFQKVLnvksklkyVETIIILDLNEDLGgyqclnnfisqnSDINLDVKkfkPNSfnrdDQVALVMF 196
Cdd:cd12114 82 DAGAR-LVLTDGPDAQLDVA--------VFDVLILDLDALAA------------PAPPPPVD---VAP----DDLAYVIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 197 SSGTTGVSKGVMLTHKN-------IVARFshckdptfgnAINPTTAILTVIPFHH-----------GFGMTTTLgyftcg 258
Cdd:cd12114 134 TSGSTGTPKGVMISHRAalntildINRRF----------AVGPDDRVLALSSLSFdlsvydifgalSAGATLVL------ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 259 frVALMHTFEEKLFLQSLQDYKVesTLL--VPTLMAFFPKSALVEKYDLSHLKEIASGG--APLSKEigEMVKKRFK-LN 333
Cdd:cd12114 198 --PDEARRRDPAHWAELIERHGV--TLWnsVPALLEMLLDVLEAAQALLPSLRLVLLSGdwIPLDLP--ARLRALAPdAR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 334 FVRQGyGLTETT--SAVL-ITP-DTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKA 409
Cdd:cd12114 272 LISLG-GATEASiwSIYHpIDEvPPDWRSIPYGRPLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 410 --IINKDG--WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELpaAGVV 485
Cdd:cd12114 350 rfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL--AAFV 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 41688574 486 VQTGKY-------LNEQIVQNFVSSQVSTAkwlrggVKFLDEIPKGSTGKIDRKVL 534
Cdd:cd12114 428 VPDNDGtpiapdaLRAFLAQTLPAYMIPSR------VIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
189-534 |
1.98e-21 |
|
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: 97.35 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDpTFGnaINPTTAILTVIPFhhGF--GMTTTLGYFTCGFRVALM-- 264
Cdd:cd17646 138 DNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQD-EYP--LGPGDRVLQKTPL--SFdvSVWELFWPLVAGARLVVArp 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 265 --HTFEEKLfLQSLQDYKVESTLLVPTLMAFFPKSALVEkyDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLT 342
Cdd:cd17646 213 ggHRDPAYL-AALIREHGVTTCHFVPSMLRVFLAEPAAG--SCASLRRVFCSGEALPPELAARFLALPGAELH-NLYGPT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 343 ETT---SAVLITPDTDVRPGSTGKIVPFHAVKVVDPTtGKILGPNETGELYFKGDMIMKSYYNNEEATKA--IINKDG-- 415
Cdd:cd17646 289 EAAidvTHWPVRGPAETPSVPIGRPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPALTAErfVPDPFGpg 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 416 --WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGE------LPAAGVVVQ 487
Cdd:cd17646 368 srMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAArlvgyvVPAAGAAGP 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 41688574 488 TGKYLNEQIVQNFVSSQVSTAkwlrggVKFLDEIPKGSTGKIDRKVL 534
Cdd:cd17646 448 DTAALRAHLAERLPEYMVPAA------FVVLDALPLTANGKLDRAAL 488
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
277-536 |
5.09e-21 |
|
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: 96.86 E-value: 5.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 277 QDYKVESTLLVPT----LMAFFPksALVEKYDLSHLKEIASGGAPLSKE--------IGEmvkkrFKLNFVrQGYGLTET 344
Cdd:cd05966 322 EKHKVTIFYTAPTairaLMKFGD--EWVKKHDLSSLRVLGSVGEPINPEawmwyyevIGK-----ERCPIV-DTWWQTET 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSaVLITP---DTDVRPGSTGKivPFHAVK--VVDPTTGKILGPNEtGELYFK----GdmIMKSYYNNEEATKAIINKD- 414
Cdd:cd05966 394 GG-IMITPlpgATPLKPGSATR--PFFGIEpaILDEEGNEVEGEVE-GYLVIKrpwpG--MARTIYGDHERYEDTYFSKf 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 415 -GWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLN 493
Cdd:cd05966 468 pGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPS 547
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41688574 494 EQIVQNFVssqvstaKWLR---------GGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05966 548 DELRKELR-------KHVRkeigpiatpDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
187-454 |
6.60e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 6.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 187 RDDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDpTFGNAINPTTAILTVIPFHHGFGMTTTL--GYFTcGFRVALM 264
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLlqPIFS-GVPCVLM 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 265 ---HTFEEKL-FLQSLQDYKveSTLLVPTLMAF------FPKSALvEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKL-- 332
Cdd:PRK05691 242 spaYFLERPLrWLEAISEYG--GTISGGPDFAYrlcserVSESAL-ERLDLSRWRVAYSGSEPIRQDSLERFAEKFAAcg 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 333 ----NFVrQGYGLTETTSAV----------LITPDTD------VRPG------STGKIVPFHAVKVVDPTTGKILGPNET 386
Cdd:PRK05691 319 fdpdSFF-ASYGLAEATLFVsggrrgqgipALELDAEalarnrAEPGtgsvlmSCGRSQPGHAVLIVDPQSLEVLGDNRV 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41688574 387 GELYFKGDMIMKSYYNNEEAT-KAIINKDG--WLRSGDIAYYdNDGHFYIVDRLKSLIKYKGYQVAPAEIE 454
Cdd:PRK05691 398 GEIWASGPSIAHGYWRNPEASaKTFVEHDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIE 467
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
52-431 |
6.88e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 96.12 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIaaPV------SDKYIERELIHS-----LGIV 120
Cdd:PRK09274 44 FAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAV--PVlvdpgmGIKNLKQCLAEAqpdafIGIP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 121 KP---RIIFC-SKNTFQKVLNVKSKLKyvetiiildlnedLGGYQcLNNFISQNSDINLDVKKFKPnsfnrdDQVALVMF 196
Cdd:PRK09274 122 KAhlaRRLFGwGKPSVRRLVTVGGRLL-------------WGGTT-LATLLRDGAAAPFPMADLAP------DDMAAILF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 197 SSGTTGVSKGVMLTHKNIVARFSHCKDpTFGnaINPTTAILTVIP----FHHGFGMTTTLGY--FTcgfRVALMHTfeEK 270
Cdd:PRK09274 182 TSGSTGTPKGVVYTHGMFEAQIEALRE-DYG--IEPGEIDLPTFPlfalFGPALGMTSVIPDmdPT---RPATVDP--AK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 271 LFlQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFK-----LNfvrqGYGLTE-- 343
Cdd:PRK09274 254 LF-AAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPpdaeiLT----PYGATEal 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 344 -----TTSAVL--ITPDTDVRPGS-TGKIVPFHAVKVVDPTTGKI--------LGPNETGELYFKGDMIMKSYYNNEEAT 407
Cdd:PRK09274 329 pissiESREILfaTRAATDNGAGIcVGRPVDGVEVRIIAISDAPIpewddalrLATGEIGEIVVAGPMVTRSYYNRPEAT 408
|
410 420
....*....|....*....|....*...
gi 41688574 408 KA--IINKDG--WLRSGDIAYYDNDGHF 431
Cdd:PRK09274 409 RLakIPDGQGdvWHRMGDLGYLDAQGRL 436
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
286-541 |
1.21e-20 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 94.68 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 286 LVPTLMAFFPKSALVEkydLSHLKEIASGGAPLSKEIGEMVKkRFKLNfVRQGYGLTETTSAVL-ITPDtDVRPG--STG 362
Cdd:PRK07445 213 LVPTQLQRLLQLRPQW---LAQFRTILLGGAPAWPSLLEQAR-QLQLR-LAPTYGMTETASQIAtLKPD-DFLAGnnSSG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 363 KIVPfHA-VKVVDPTTGKIlgpNETGELYFKGdmimksYYNNeeatkaIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLI 441
Cdd:PRK07445 287 QVLP-HAqITIPANQTGNI---TIQAQSLALG------YYPQ------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKI 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 442 KYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKyLNEQIVQNFVSSQVSTAK----WLRggvkf 517
Cdd:PRK07445 351 ITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKqpkhWIP----- 424
|
250 260
....*....|....*....|....
gi 41688574 518 LDEIPKGSTGKIDRKVLRQMFEKH 541
Cdd:PRK07445 425 VPQLPRNPQGKINRQQLQQIAVQR 448
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
188-538 |
2.10e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 92.80 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNIVARfshcKDPTFGNAINPTTAILTViPFHHGFGMTTTLGYFTCGFR---VALM 264
Cdd:PRK07824 34 DDDVALVVATSGTTGTPKGAMLTAAALTAS----ADATHDRLGGPGQWLLAL-PAHHIAGLQVLVRSVIAGSEpveLDVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 265 HTFEEKLFLQSLQDYKVES--TLLVPT-LMAFFPKSALVEKydLSHLKEIASGGAPLSKEIGEMVKKrFKLNFVRQgYGL 341
Cdd:PRK07824 109 AGFDPTALPRAVAELGGGRryTSLVPMqLAKALDDPAATAA--LAELDAVLVGGGPAPAPVLDAAAA-AGINVVRT-YGM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 342 TETTSAVlitpdtdVRPGstgkiVPFHAVKVvdpttgKIlgpnETGELYFKGDMIMKSYYNNEEatKAIINKDGWLRSGD 421
Cdd:PRK07824 185 SETSGGC-------VYDG-----VPLDGVRV------RV----EDGRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 422 IAYYDnDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFV 501
Cdd:PRK07824 241 LGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHV 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 41688574 502 SSQV-STAkwLRGGVKFLDEIPKGSTGKIDRKVLRQMF 538
Cdd:PRK07824 320 ARTLdRTA--APRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
188-542 |
3.23e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 90.92 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVM-FSSGTTGVSKGVMLTHKNIVArfsHckdpTFGNA------INPTTAILTVIP-FH-HGFGMTttlgyftcg 258
Cdd:PRK07008 174 DENQASSLcYTSGTTGNPKGALYSHRSTVL---H----AYGAAlpdamgLSARDAVLPVVPmFHvNAWGLP--------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 259 FRVALMHTfeeKLFL-------QSLQDY----KVESTLLVPT--LMAffpksalvekydLSHLKEIASGGAPLSKE-IG- 323
Cdd:PRK07008 238 YSAPLTGA---KLVLpgpdldgKSLYELieaeRVTFSAGVPTvwLGL------------LNHMREAGLRFSTLRRTvIGg 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 324 -----EMVKKrFKLNF---VRQGYGLTET----TSAVLITPDTDVRPGSTGKIV--PFHAVKVVDPttgKILGPNET--- 386
Cdd:PRK07008 303 sacppAMIRT-FEDEYgveVIHAWGMTEMsplgTLCKLKWKHSQLPLDEQRKLLekQGRVIYGVDM---KIVGDDGRelp 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 387 ------GELYFKGDMIMKSYYNNEEATKAiinkDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQH 460
Cdd:PRK07008 379 wdgkafGDLQVRGPWVIDRYFRGDASPLV----DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAH 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 461 PYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVstAKW-LRGGVKFLDEIPKGSTGKIDRKVLRQMFE 539
Cdd:PRK07008 455 PAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKV--AKWwIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
...
gi 41688574 540 KHK 542
Cdd:PRK07008 533 DYV 535
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
50-479 |
7.01e-19 |
|
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: 89.80 E-value: 7.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 50 VLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKY--IERE---LIHSLGIVKPRI 124
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslMSQDlakLKHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 125 IFCSK-NTFQKVLnvkSKLKYVETIIILDLNEDLGgyqclNNFISQNSDINLDVKKFKPNSFNR--DDQVALVMFSSGTT 201
Cdd:cd05921 106 VFAQDaAPFARAL---AAIFPLGTPLVVSRNAVAG-----RGAISFAELAATPPTAAVDAAFAAvgPDTVAKFLFTSGST 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 202 GVSKGVMLTHKNIVARFSHCKDpTFGNAINPTTAILTVIPFHHGFGMTTTLG---------YFTCGFRVALMhtFEEKlf 272
Cdd:cd05921 178 GLPKAVINTQRMLCANQAMLEQ-TYPFFGEEPPVLVDWLPWNHTFGGNHNFNlvlynggtlYIDDGKPMPGG--FEET-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 273 LQSLQDYKVESTLLVP----TLMAFFPK-SALVEKYdLSHLKEIASGGAPLS------------KEIGEMVKkrfklnfV 335
Cdd:cd05921 253 LRNLREISPTVYFNVPagweMLVAALEKdEALRRRF-FKRLKLMFYAGAGLSqdvwdrlqalavATVGERIP-------M 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 336 RQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVdPTTGKIlgpnetgELYFKGDMIMKSYYNNEEATKAIINKDG 415
Cdd:cd05921 325 MAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV-PSGGKY-------EVRVKGPNVTPGYWRQPELTAQAFDEEG 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41688574 416 WLRSGDIAYY--DNDGH--FYIVDRLKSLIKYKG---YQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGEL 479
Cdd:cd05921 397 FYCLGDAAKLadPDDPAkgLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLVHDAVVAGEDRAEVGAL 467
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
188-534 |
3.09e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.06 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNIVARFsHCKDPTFGnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVAL---- 263
Cdd:PRK12467 1717 PQNLAYVIYTSGSTGRPKGAGNRHGALVNRL-CATQEAYQ--LSAADVVLQFTSFAFDVSVWELFWPLINGARLVIappg 1793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 264 MHTFEEKlFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLShLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTE 343
Cdd:PRK12467 1794 AHRDPEQ-LIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTE 1871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 344 TTSAVLITPDTDVRP-----GSTGKIVPFHAVKVVDPTTGkILGPNETGELYFKGDMIMKSYYNNEE--ATKAIINKDGW 416
Cdd:PRK12467 1872 TAVDVTHWTCRRKDLegrdsVPIGQPIANLSTYILDASLN-PVPIGVAGELYLGGVGLARGYLNRPAltAERFVADPFGT 1950
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 417 L-----RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVtgIPDEAAGELPAAGVVVQTGKY 491
Cdd:PRK12467 1951 VgsrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDGANGKQLVAYVVPTDPG 2028
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 41688574 492 LNEQIVqnfvsSQVSTAKWLRGGVK-------------FLDEIPKGSTGKIDRKVL 534
Cdd:PRK12467 2029 LVDDDE-----AQVALRAILKNHLKaslpeymvpahlvFLARMPLTPNGKLDRKAL 2079
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
189-539 |
5.90e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 87.46 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCK---DPTfgnainPTTAILTVIPFHHGFGMttTLGYFT---CGFRVa 262
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKtiaDFT------PNDRFMSALPLFHSFGL--TVGLFTpllTGAEV- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 263 lmhtfeeklFL-QSLQDYKVestllVPTLM------AFFPKSALV-------EKYDLSHLKEIASGGAPLSKEIGEMVKK 328
Cdd:PRK08043 436 ---------FLyPSPLHYRI-----VPELVydrnctVLFGTSTFLgnyarfaNPYDFARLRYVVAGAEKLQESTKQLWQD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 329 RFKLNfVRQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVdpttgKILGPNETGELYFKGDMIMKSYYNNE---- 404
Cdd:PRK08043 502 KFGLR-ILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL-----SVPGIEQGGRLQLKGPNIMNGYLRVEkpgv 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 405 -EATKAI----INKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGEl 479
Cdd:PRK08043 576 lEVPTAEnargEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE- 654
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41688574 480 paAGVVVQTGKYLN-EQIVQNFVSSQVSTAKWLRgGVKFLDEIPKGSTGKIDRKVLRQMFE 539
Cdd:PRK08043 655 --ALVLFTTDSELTrEKLQQYAREHGVPELAVPR-DIRYLKQLPLLGSGKPDFVTLKSMVD 712
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-534 |
6.47e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.09 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 40 ALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGi 119
Cdd:PRK12316 527 APALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLE- 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 120 vKPRIIFCSKNTFqkvlnVKSKLKYVETIIILDLNEdlgGYQCLNNFISQNSDINLDvkkfkpnsfnrDDQVALVMFSSG 199
Cdd:PRK12316 606 -DSGVQLLLSQSH-----LGRKLPLAAGVQVLDLDR---PAAWLEGYSEENPGTELN-----------PENLAYVIYTSG 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 200 TTGVSKGVMLTHKNIVARFSHCKDpTFGNAINPTtaILTVIPFHHGFGMTTTLGYFTCGFRVAL----MHTFEEKLfLQS 275
Cdd:PRK12316 666 STGKPKGAGNRHRALSNRLCWMQQ-AYGLGVGDT--VLQKTPFSFDVSVWEFFWPLMSGARLVVaapgDHRDPAKL-VEL 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYKVESTLLVPTLMAFFPKSALVEkyDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTsaVLITPDTD 355
Cdd:PRK12316 742 INREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAA--IDVTHWTC 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 356 VRPG----STGKIVPFHAVKVVDPTtgkiLGP---NETGELYFKGDMIMKSYYNNEEAT------KAIINKDGWLRSGDI 422
Cdd:PRK12316 818 VEEGgdsvPIGRPIANLACYILDAN----LEPvpvGVLGELYLAGRGLARGYHGRPGLTaerfvpSPFVAGERMYRTGDL 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 423 AYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTgipdeAAGELPAAGVVVQT--GKYLNEQIVQNF 500
Cdd:PRK12316 894 ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL-----AVDGKQLVGYVVLEseGGDWREALKAHL 968
|
490 500 510
....*....|....*....|....*....|....*..
gi 41688574 501 VSS---QVSTAKWLrggvkFLDEIPKGSTGKIDRKVL 534
Cdd:PRK12316 969 AASlpeYMVPAQWL-----ALERLPLTPNGKLDRKAL 1000
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
47-534 |
9.91e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.52 E-value: 9.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 47 KENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIF 126
Cdd:PRK12467 535 EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 127 cSKNTFQKVLNVKSKLKYvetiIILDLNEDLggyqclnnfISQNSDINLDVKkFKPnsfnrdDQVALVMFSSGTTGVSKG 206
Cdd:PRK12467 615 -TQSHLLAQLPVPAGLRS----LCLDEPADL---------LCGYSGHNPEVA-LDP------DNLAYVIYTSGSTGQPKG 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 207 VMLTHKNIVARF-SHCKDPTFGnainPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALM---HTFEEKLFLQSLQDYKVE 282
Cdd:PRK12467 674 VAISHGALANYVcVIAERLQLA----ADDSMLMVSTFAFDLGVTELFGALASGATLHLLppdCARDAEAFAALMADQGVT 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 283 STLLVPTLMAFFPKSALVEKyDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQgYGLTETTSAVLITP----DTDVRP 358
Cdd:PRK12467 750 VLKIVPSHLQALLQASRVAL-PRPQRALVCGGEALQVDLLARVRALGPGARLINH-YGPTETTVGVSTYElsdeERDFGN 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 359 GSTGKIVPFHAVKVVDPTTgKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGW-------LRSGDIAYYDNDGHF 431
Cdd:PRK12467 828 VPIGQPLANLGLYILDHYL-NPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVI 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 432 YIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGEL-----PAAGVVVQTGKYLNEQI---VQNFVSS 503
Cdd:PRK12467 907 EYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLvaylvPAAVADGAEHQATRDELkaqLRQVLPD 986
|
490 500 510
....*....|....*....|....*....|.
gi 41688574 504 QVSTAKWLrggvkFLDEIPKGSTGKIDRKVL 534
Cdd:PRK12467 987 YMVPAHLL-----LLDSLPLTPNGKLDRKAL 1012
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
52-456 |
1.01e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 86.61 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKY----IERELIHSlgivKPRIIFC 127
Cdd:PLN02614 82 YQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLgagaVEFIISHS----EVSIVFV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 128 SKNTFQKVLNV-KSKLKYVETIIIL--------DLNEDLG-GYQCLNNFISQNSDINLDVKKFKPNSfnrddqVALVMFS 197
Cdd:PLN02614 158 EEKKISELFKTcPNSTEYMKTVVSFggvsreqkEEAETFGlVIYAWDEFLKLGEGKQYDLPIKKKSD------ICTIMYT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 198 SGTTGVSKGVMLTHKNIVARFSHCKD--PTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTfEEKLFLQS 275
Cdd:PLN02614 232 SGTTGDPKGVMISNESIVTLIAGVIRllKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRG-DVKLLIED 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 276 LQDYKVESTLLVPTLM--------------AFFPK-----------------------SALVEKYDLSHLKE-------- 310
Cdd:PLN02614 311 LGELKPTIFCAVPRVLdrvysglqkklsdgGFLKKfvfdsafsykfgnmkkgqshveaSPLCDKLVFNKVKQglggnvri 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 311 IASGGAPLSKEIGEMVKKRFKLNfVRQGYGLTETTSAVLIT-PDTDVRPGSTGKIVPFHAVKV--VDPTTGKILGPNETG 387
Cdd:PLN02614 391 ILSGAAPLASHVESFLRVVACCH-VLQGYGLTESCAGTFVSlPDELDMLGTVGPPVPNVDIRLesVPEMEYDALASTPRG 469
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 388 ELYFKGDMIMKSYYNNEEATKAIInKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKY-KGYQVAPAEIEGI 456
Cdd:PLN02614 470 EICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
189-534 |
1.10e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.14 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVarfSHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFR--VALMHT 266
Cdd:PRK12467 3237 ENLAYVIYTSGSTGKPKGVGVRHGALA---NHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGClvVRDNDL 3313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 FEEKLFLQSLQDYKVESTLLVPTLMAFFPKSAlvEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTS 346
Cdd:PRK12467 3314 WDPEELWQAIHAHRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVV 3391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 347 AVLI-TPDTDVRPGST----GKIVPFHAVKVVDPTtgkiLGP---NETGELYFKGDMIMKSYYNNEEATKAIINKDGWL- 417
Cdd:PRK12467 3392 TVTLwKCGGDAVCEAPyapiGRPVAGRSIYVLDGQ----LNPvpvGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSg 3467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 418 ------RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKY 491
Cdd:PRK12467 3468 sggrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGD 3547
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 41688574 492 LNEQIVQNFVSS---QVSTAKWLrggvkFLDEIPKGSTGKIDRKVL 534
Cdd:PRK12467 3548 WRETLRDHLAASlpdYMVPAQLL-----VLAAMPLGPNGKVDRKAL 3588
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
188-454 |
1.12e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 86.20 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNIVAR----FSHCK-DPTfgnainpTTAILTVIPFHHGFGMTttlGYFT----CG 258
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGNLYANaeamFVAAEfDVE-------TDVMVSWLPLFHDMGMV---GFLTvpmyFG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 259 FRVALMHTFEeklFLQSlqdykvesTLLVPTLMAFF-------PKSA--LVEK----------YDLSHLKEIASGGAPLS 319
Cdd:PRK07768 221 AELVKVTPMD---FLRD--------PLLWAELISKYrgtmtaaPNFAyaLLARrlrrqakpgaFDLSSLRFALNGAEPID 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 320 KEIGE---MVKKRFKLN--FVRQGYGLTETTSAVLITP----------DTD----------VRPGST------GKIVPFH 368
Cdd:PRK07768 290 PADVEdllDAGARFGLRpeAILPAYGMAEATLAVSFSPcgaglvvdevDADllaalrravpATKGNTrrlatlGPPLPGL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 369 AVKVVDpTTGKILGPNETGELYFKGDMIMKsYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQV 448
Cdd:PRK07768 370 EVRVVD-EDGQVLPPRGVGVIELRGESVTP-GYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNI 447
|
....*.
gi 41688574 449 APAEIE 454
Cdd:PRK07768 448 YPTDIE 453
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-534 |
1.34e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.93 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 40 ALTNAHTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGI 119
Cdd:PRK12316 3073 AVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLED 3152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 120 VKPRIIFCSKNTfqkvlnvksKLKYVETIIILDLNEDLGGYQclnnfiSQNSDINLDvkkfkpnsfnrDDQVALVMFSSG 199
Cdd:PRK12316 3153 SGAQLLLSQSHL---------RLPLAQGVQVLDLDRGDENYA------EANPAIRTM-----------PENLAYVIYTSG 3206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 200 TTGVSKGVMLTHKnivARFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHT---FEEKLFLQSL 276
Cdd:PRK12316 3207 STGKPKGVGIRHS---ALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPedwRDPALLVELI 3283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 277 QDYKVESTLLVPTLMAFFPKSalVEKYDLSHLKEIASGGAPLSkeiGEMVKKRFKLNFVRQGYGLTETTSAVLITPDTDV 356
Cdd:PRK12316 3284 NSEGVDVLHAYPSMLQAFLEE--EDAHRCTSLKRIVCGGEALP---ADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEE 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 357 RPGS--TGKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGW------LRSGDIAYYDND 428
Cdd:PRK12316 3359 GKDAvpIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRAD 3437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 429 GHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTG----------IPDEAAGELPAAgvvvqtgkyLNEQIVQ 498
Cdd:PRK12316 3438 GVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAvdgrqlvayvVPEDEAGDLREA---------LKAHLKA 3508
|
490 500 510
....*....|....*....|....*....|....*.
gi 41688574 499 NFVSSQVStAKWLrggvkFLDEIPKGSTGKIDRKVL 534
Cdd:PRK12316 3509 SLPEYMVP-AHLL-----FLERMPLTPNGKLDRKAL 3538
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
42-539 |
1.85e-17 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 85.48 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 42 TNAHTKENVLYEEFLKLSCRLAESF-KKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIV 120
Cdd:cd05905 7 SKGKEATTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 121 KPRIIFCSKNTFqkVLNVKSKLKYVETiiilDLNEDLGGYQCLNNFISQNSDINLDVKKFKPNSFNRDDQVALVMFSSGT 200
Cdd:cd05905 87 KVRVALTVEACL--KGLPKKLLKSKTA----AEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 201 TGVSKGVMLTHKNIvarFSHCKDPTFGNAINPTTAILTVIPFHHGFG------MTTTLGYFTCGFRVALMHTfEEKLFLQ 274
Cdd:cd05905 161 DGSLSGVAVSHSSL---LAHCRALKEACELYESRPLVTVLDFKSGLGlwhgclLSVYSGHHTILIPPELMKT-NPLLWLQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 275 SLQDYKVESTLL----------------------------VPTLMAFF---PKSALVEKYdLSHLKEIASGGAPLSKEIG 323
Cdd:cd05905 237 TLSQYKVRDAYVklrtlhwclkdlsstlaslknrdvnlssLRMCMVPCenrPRISSCDSF-LKLFQTLGLSPRAVSTEFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 324 EMVKKRFKLnfvrQGYGLTETTSAVL---------ITPDTDVRPGS-----TGKIVPFHAVKVVDPTTGKILGPNETGEL 389
Cdd:cd05905 316 TRVNPFICW----QGTSGPEPSRVYLdmralrhgvVRLDERDKPNSlplqdSGKVLPGAQVAIVNPETKGLCKDGEIGEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 390 ----------YFKGDMIMKSYYNNEEATK--AIINKDGWLRSGDIAYYDNDGHF----------YIVDRLKSLIKYKGYQ 447
Cdd:cd05905 392 wvnspanasgYFLLDGETNDTFKVFPSTRlsTGITNNSYARTGLLGFLRPTKCTdlnveehdllFVVGSIDETLEVRGLR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 448 VAPAEIEG-ILLQHPYIVDAGVTGIpdeaaGELPaagVVVQTGKYLNEQIVQNFVSSQVSTA----KWLRGGVKFLD--E 520
Cdd:cd05905 472 HHPSDIEAtVMRVHPYRGRCAVFSI-----TGLV---VVVAEQPPGSEEEALDLVPLVLNAIleehQVIVDCVALVPpgS 543
|
570
....*....|....*....
gi 41688574 521 IPKGSTGKIDRKVLRQMFE 539
Cdd:cd05905 544 LPKNPLGEKQRMEIRQAFL 562
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
189-535 |
2.40e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 85.47 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMltHKnivarfsHCKDPTFGNA-------INPTTAILTVIPFHHGFGMTTTLGYFTCGFRV 261
Cdd:PRK06060 145 DALAYATYTSGTTGPPKAAI--HR-------HADPLTFVDAmcrkalrLTPEDTGLCSARMYFAYGLGNSVWFPLATGGS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 262 ALMHTFEEKLFLQSLQDYKVESTLL--VPTLMAFFPKSALVEKYdlSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGY 339
Cdd:PRK06060 216 AVINSAPVTPEAAAILSARFGPSVLygVPNFFARVIDSCSPDSF--RSLRCVVSAGEALELGLAERLMEFFGGIPILDGI 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 340 GLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVDPtTGKILGPNETGELYFKGDMIMKSYYNNEEatkAIINKDGWLRS 419
Cdd:PRK06060 294 GSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAP-DGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDT 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 420 GDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQN 499
Cdd:PRK06060 370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRD 449
|
330 340 350
....*....|....*....|....*....|....*...
gi 41688574 500 FVSSQVSTAKWLRGGVKF--LDEIPKGSTGKIDRKVLR 535
Cdd:PRK06060 450 LHRGLLNRLSAFKVPHRFavVDRLPRTPNGKLVRGALR 487
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
148-534 |
4.18e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 84.18 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 148 IIILDLNEDLGGYQCLNnfISQNSDINLDVKKFKPNSFNRDDQVALVMFSSGTTGVSKGVMLTHKNIVArFSH--CKDpt 225
Cdd:PRK04813 104 IATEELPLEILGIPVIT--LDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVS-FTNwmLED-- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 226 FGNAINPTtaILTVIPFhhGFGM-------TTTLGyftcGFRVALMH--TFEEKLFLQSLQDYKVE---ST-------LL 286
Cdd:PRK04813 179 FALPEGPQ--FLNQAPY--SFDLsvmdlypTLASG----GTLVALPKdmTANFKQLFETLPQLPINvwvSTpsfadmcLL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 287 VPTLMAffpksalvEKYdlSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETT---SAVLITPD--TDVRPGST 361
Cdd:PRK04813 251 DPSFNE--------EHL--PNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATvavTSIEITDEmlDQYKRLPI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 362 GKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEAT-KAIINKDGW--LRSGDIAYYDNDGHFYiVDRLK 438
Cdd:PRK04813 321 GYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTaEAFFTFDGQpaYHTGDAGYLEDGLLFY-QGRID 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 439 SLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGI-PDEAAGELPAAgVVVQTGKY-----LNEQI---VQNFVSSQVSTAK 509
Cdd:PRK04813 399 FQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnKDHKVQYLIAY-VVPKEEDFerefeLTKAIkkeLKERLMEYMIPRK 477
|
410 420
....*....|....*....|....*
gi 41688574 510 WLrggvkFLDEIPKGSTGKIDRKVL 534
Cdd:PRK04813 478 FI-----YRDSLPLTPNGKIDRKAL 497
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
183-474 |
6.17e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 83.71 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 183 NSFNRD-DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDptfgnAINPTT--AILTVIPFHHGFGMTT-TLGYFTCG 258
Cdd:PRK06334 176 GVSDKDpEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLK-----FFSPKEddVMMSFLPPFHAYGFNScTLFPLLSG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 259 FRVALMHT-FEEKLFLQSLQDYKVesTLL--VPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFV 335
Cdd:PRK06334 251 VPVVFAYNpLYPKKIVEMIDEAKV--TFLgsTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 336 RQGYGLTETTSAVLITPDTDVRPGS-TGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAI-INK 413
Cdd:PRK06334 329 RQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVeLGG 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688574 414 DGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQH---PYIVDAG---VTGIPDE 474
Cdd:PRK06334 409 ETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGplvVCGLPGE 475
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
189-534 |
6.37e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.01 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVArfsHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALM---H 265
Cdd:PRK12316 2146 ENLAYVIYTSGSTGLPKGVAVSHGALVA---HCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRddeL 2222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 TFEEKLFLQsLQDYKVESTLLVPTLMAFFPKSALVEKYDLShLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETT 345
Cdd:PRK12316 2223 WDPEQLYDE-MERHGVTILDFPPVYLQQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAV 2300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 346 SAVLITPDTDVRPGST-----GKIVPFHAVKVVDPTTgKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGW---- 416
Cdd:PRK12316 2301 VTPLLWKCRPQDPCGAayvpiGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasg 2379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 417 ---LRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIpDEAAGELPAAGVVVQTGKYLN 493
Cdd:PRK12316 2380 erlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDL 2458
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 41688574 494 EQIVQNFVsSQVSTAKWLRGGVKFLDEIPKGSTGKIDRKVL 534
Cdd:PRK12316 2459 LAELRAWL-AARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
52-536 |
1.11e-16 |
|
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: 82.47 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLgivkpriifcsknt 131
Cdd:cd05939 6 FRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCI-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 fqKVLNVKSklkyvetiIILDLNEDLggyqclnnfisqNSDINLDVKKFKPNSFnrdDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:cd05939 72 --TVSKAKA--------LIFNLLDPL------------LTQSSTEPPSQDDVNF---RDKLFYIYTSGTTGLPKAAVIVH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNI--VARFSHckdptFGNAINPTTAILTVIPFHHGFGMTTTLGY-FTCGFRVALMHTFEEKLFLQSLQDYKVESTLLVP 288
Cdd:cd05939 127 SRYyrIAAGAY-----YAFGMRPEDVVYDCLPLYHSAGGIMGVGQaLLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 289 TLMAFFPKSALVEkYDLSHLKEIASGGApLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLitpDTDVRPGSTG------ 362
Cdd:cd05939 202 EICRYLLAQPPSE-EEQKHNVRLAVGNG-LRPQIWEQFVRRFGIPQIGEFYGATEGNSSLV---NIDNHVGACGfnsril 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 363 -KIVPFHAVKVvDPTTGKIL----------GPNETGELY---FKGDMIMKSY-YNNEEATKAIINKDGWLR------SGD 421
Cdd:cd05939 277 pSVYPIRLIKV-DEDTGELIrdsdglcipcQPGEPGLLVgkiIQNDPLRRFDgYVNEGATNKKIARDVFKKgdsaflSGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 422 IAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTG--IPdEAAGELPAAGVVVQTGKYLNEQIVQN 499
Cdd:cd05939 356 VLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGveVP-GVEGRAGMAAIVDPERKVDLDRFSAV 434
|
490 500 510
....*....|....*....|....*....|....*....
gi 41688574 500 FVSSQVSTAK--WLRggvkFLDEIPKGSTGKIDRKVLRQ 536
Cdd:cd05939 435 LAKSLPPYARpqFIR----LLPEVDKTGTFKLQKTDLQK 469
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
192-534 |
1.60e-16 |
|
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: 82.10 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 192 ALVMFSSGTTGVSKGVMLTHKNIVaRFSHCKDPTFGNAINPTTAILTVIPFHHGFG--MTTTLGYFTCGFRVALMHtFEE 269
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEHQSLV-NLSHGLIKEYGITSSDRVLQFASIAFDVAAEeiYVTLLSGATLVLRPEEMR-SSL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 270 KLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDL-SHLKEIASGGAPLSKEIGEMVKK--RFKLNFVrQGYGLTETTS 346
Cdd:cd17644 187 EDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKnvGNFIQLI-NVYGPTEATI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 347 AV---LITPDTDVRPGST--GKIVPFHAVKVVDPTTgKILGPNETGELYFKGDMIMKSYYNNEEAT--KAIINK------ 413
Cdd:cd17644 266 AAtvcRLTQLTERNITSVpiGRPIANTQVYILDENL-QPVPVGVPGELHIGGVGLARGYLNRPELTaeKFISHPfnsses 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 414 DGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLN 493
Cdd:cd17644 345 ERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPS 424
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 41688574 494 EQIVQNFVSSQVSTAKWLRGGVkFLDEIPKGSTGKIDRKVL 534
Cdd:cd17644 425 TVELRQFLKAKLPDYMIPSAFV-VLEELPLTPNGKIDRRAL 464
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
277-536 |
3.02e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 81.73 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 277 QDYKVesTLL--VPT----LMAFfpKSALVEKYDLSHLKEIASGGAPLSKE--------IGEMvkkrfKLNFVR---Qgy 339
Cdd:PRK00174 336 DKHKV--TIFytAPTairaLMKE--GDEHPKKYDLSSLRLLGSVGEPINPEawewyykvVGGE-----RCPIVDtwwQ-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 340 glTETtSAVLITP---DTDVRPGSTGKivPFHAVK--VVDpTTGKILGPNETGELYFK-----------GDM--IMKSYY 401
Cdd:PRK00174 405 --TET-GGIMITPlpgATPLKPGSATR--PLPGIQpaVVD-EEGNPLEGGEGGNLVIKdpwpgmmrtiyGDHerFVKTYF 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 402 NNEeatkaiinKDGWLrSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPA 481
Cdd:PRK00174 479 STF--------KGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIY 549
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688574 482 AGVVVQTGKYLNEQIVQNFVssqvstaKWLR---------GGVKFLDEIPKGSTGKIDRKVLRQ 536
Cdd:PRK00174 550 AFVTLKGGEEPSDELRKELR-------NWVRkeigpiakpDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
48-423 |
3.72e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 81.63 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 48 ENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYI-----ERELIHSLGIVKP 122
Cdd:PRK12582 79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSlmshdHAKLKHLFDLVKP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 123 RIIFC-SKNTFQKVLNVkSKLKYVETIIILDLNEDLGG--YQCLnnfisQNSDINLDVKKfkpnSFNR--DDQVALVMFS 197
Cdd:PRK12582 159 RVVFAqSGAPFARALAA-LDLLDVTVVHVTGPGEGIASiaFADL-----AATPPTAAVAA----AIAAitPDTVAKYLFT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 198 SGTTGVSKGVMLTHKNIVARFSHCKDPTFGNAINPTTAILTVIPFHHGFGMTTTLG---------YFTCGFRVALMhtFE 268
Cdd:PRK12582 229 SGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNgllwgggtlYIDDGKPLPGM--FE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 269 EKLflQSLQDykvestlLVPTLMAFFPK--SALVEKYD---------LSHLKEIASGGAPLSKEIGEmvkkRFKLNFVRQ 337
Cdd:PRK12582 307 ETI--RNLRE-------ISPTVYGNVPAgyAMLAEAMEkddalrrsfFKNLRLMAYGGATLSDDLYE----RMQALAVRT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 338 ---------GYGLTETTSAVLITP-DTDvRPGSTGKIVPFHAVKVVdPTTGKIlgpnetgELYFKGDMIMKSYYNNEEAT 407
Cdd:PRK12582 374 tghripfytGYGATETAPTTTGTHwDTE-RVGLIGLPLPGVELKLA-PVGDKY-------EVRVKGPNVTPGYHKDPELT 444
|
410
....*....|....*.
gi 41688574 408 KAIINKDGWLRSGDIA 423
Cdd:PRK12582 445 AAAFDEEGFYRLGDAA 460
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
189-534 |
5.91e-16 |
|
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: 80.20 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIvARFSHCKDPTFGNAINPTtAILTVIPFhhgfgmttTLGYFTCGFRVALMH--- 265
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNV-AHAAHAWRREYELDSFPV-RLLQMASF--------SFDVFAGDFARSLLNggt 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 --------TFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGaplskeigEMVKKRFKLNFVRQ 337
Cdd:cd17650 163 lvicpdevKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGS--------DGCKAQDFKTLAAR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 338 ---------GYGLTETTSAVLITPDTDVRPGST-----GKIVPFHAVKVVDPTtgkiLGPNETG---ELYFKGDMIMKSY 400
Cdd:cd17650 235 fgqgmriinSYGVTEATIDSTYYEEGRDPLGDSanvpiGRPLPNTAMYVLDER----LQPQPVGvagELYIGGAGVARGY 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 401 YNNEEATKAIINKDGW------LRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTgIPDE 474
Cdd:cd17650 311 LNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VRED 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688574 475 AAGELPAAGVVVQTGK--------YLNEQIVQNFVSSQVSTakwlrggvkfLDEIPKGSTGKIDRKVL 534
Cdd:cd17650 390 KGGEARLCAYVVAAATlntaelraFLAKELPSYMIPSYYVQ----------LDALPLTPNGKVDRRAL 447
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
162-442 |
1.58e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 79.76 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 162 CLNNFISQNSDINLDVKKFKPNsfNRD-DQVALVMFSSGTTGVSKGVMLTHKNIV-ARFSHCKDPTFGNaINPTTAiLTV 239
Cdd:PTZ00342 278 LGISIILFDDMTKNKTTNYKIQ--NEDpDFITSIVYTSGTSGKPKGVMLSNKNLYnTVVPLCKHSIFKK-YNPKTH-LSY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 240 IPFHHGFGMTTTLGYFTCGFRVALMHTfEEKLFLQSLQDYKVESTLLVP--------TLMA-----FFPKSALVEKY--- 303
Cdd:PTZ00342 354 LPISHIYERVIAYLSFMLGGTINIWSK-DINYFSKDIYNSKGNILAGVPkvfnriytNIMTeinnlPPLKRFLVKKIlsl 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 304 --------------DLSH------------LKEIASGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETTSAVLITPDTDVR 357
Cdd:PTZ00342 433 rksnnnggfskfleGITHisskikdkvnpnLEVILNGGGKLSPKIAEELSVLLNVNYY-QGYGLTETTGPIFVQHADDNN 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 358 PGSTG-KIVPFHAVKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDR 436
Cdd:PTZ00342 512 TESIGgPISPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDR 591
|
....*.
gi 41688574 437 LKSLIK 442
Cdd:PTZ00342 592 SKGLVK 597
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
189-536 |
2.51e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.62 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFsHCKDPTFGnaINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHT-- 266
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAVSHGSLVNHL-HATGERYE--LTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDsl 4770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 FEEKLFLQSLQDYKVESTLLVPTLMAFFPKSAlVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETTS 346
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHA-ERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTV 4849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 347 AVLI--TPDTDVRPGST---GKIVPFHAVKVVDpTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGW----- 416
Cdd:PRK12316 4850 TVLLwkARDGDACGAAYmpiGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgg 4928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 417 --LRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDeAAGELPAAGVVVQTGKYLNE 494
Cdd:PRK12316 4929 rlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEG-AVGKQLVGYVVPQDPALADA 5007
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 41688574 495 QIVQNFVSSQVSTAkwLRGGVK---------FLDEIPKGSTGKIDRKVLRQ 536
Cdd:PRK12316 5008 DEAQAELRDELKAA--LRERLPeymvpahlvFLARMPLTPNGKLDRKALPQ 5056
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
277-539 |
4.25e-15 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 78.07 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 277 QDYKVESTLLVPTLMAFFPKS--ALVEKYDLSHLKEIASGGAPL----SKEIGEMVKKRfklnfVRQGYGLTETTSAVL- 349
Cdd:PRK10524 324 EKYKVNRMFSAPTAIRVLKKQdpALLRKHDLSSLRALFLAGEPLdeptASWISEALGVP-----VIDNYWQTETGWPILa 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 350 ITP---DTDVRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKG--------------DMIMKSYYNNeeatkaiIN 412
Cdd:PRK10524 399 IARgveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGplppgcmqtvwgddDRFVKTYWSL-------FG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 413 KDGWlRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYL 492
Cdd:PRK10524 472 RQVY-STFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSL 550
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 41688574 493 N--------EQIVQNFVSSQV-STAKWLRggVKFLDEIPKGSTGKIDRKVLRQMFE 539
Cdd:PRK10524 551 AdrearlalEKEIMALVDSQLgAVARPAR--VWFVSALPKTRSGKLLRRAIQAIAE 604
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
189-471 |
4.42e-15 |
|
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: 77.50 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDpTFGnaINPTTAILTVIP----FHHGFGMTTTLGY--FTCGFRVA 262
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQ-LYG--IRPGEVDLATFPlfalFGPALGLTSVIPDmdPTRPARAD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 263 lmhtfEEKLFlQSLQDYKVESTLLVPTLMAFFPKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKrfklnFVRQG---- 338
Cdd:cd05910 162 -----PQKLV-GAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRK-----MLSDEaeil 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 --YGLTETTSAVLITpDTDVRPGST-----------GKIVPFHAVKVVDPTTGKI--------LGPNETGELYFKGDMIM 397
Cdd:cd05910 231 tpYGATEALPVSSIG-SRELLATTTaatsggagtcvGRPIPGVRVRIIEIDDEPIaewddtleLPRGEIGEITVTGPTVT 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688574 398 KSYYNNEEATKAIINKDG----WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGI 471
Cdd:cd05910 310 PTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
190-534 |
5.42e-15 |
|
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: 77.44 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 190 QVALVMFSSGTTGVSKGVMLTHKNIV-ARFSHCKdpTFGNAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMH--- 265
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGSVVnLRTSLSE--RYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPdem 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 266 TFEEKLFLQSLQDYKVesTLLVPTlmaffpkSALVEKYDLS---HLKEIASGGAPLSKEIGEMVKKRFK---LNfvrqGY 339
Cdd:cd17648 173 RFDPDRFYAYINREKV--TYLSGT-------PSVLQQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRFAgliIN----AY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 340 GLTETTSAVLITPDTDVRP--GSTGKIVPFHAVKVVDPTTgKILGPNETGELYFKGDMIMKSYYNNEEAT--KAIIN--- 412
Cdd:cd17648 240 GPTETTVTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTaeRFLPNpfq 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 413 --KDGWL-------RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVtgIPDEAAGELPAAG 483
Cdd:cd17648 319 teQERARgrnarlyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAV--VAKEDASQAQSRI 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 484 VVVQTGKYLNEqivQNFVSSQvSTAKWLRGG---------VKFLDEIPKGSTGKIDRKVL 534
Cdd:cd17648 397 QKYLVGYYLPE---PGHVPES-DLLSFLRAKlprymvparLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
196-455 |
2.52e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 75.75 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 196 FSSGTTGVSKGVMLTHKNIVARFSHCKDPTF---GNAINPTTAILTVIPFHHGFGMTttLGYFT---CGFRVALMHTFEe 269
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANFEQLMSDYFgdtGGVPPPDTTVVSWLPFYHDMGLV--LGVCApilGGCPAVLTSPVA- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 270 klFLQS----LQdykvestllvptLMAFFPK--SA--------LVEK--------YDLSHLKEIASGgaplSKEIGEMVK 327
Cdd:PRK05850 244 --FLQRparwMQ------------LLASNPHafSAapnfafelAVRKtsdddmagLDLGGVLGIISG----SERVHPATL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 328 KRF-----KLNF----VRQGYGLTETTSAVLITPdtdvrPGSTGKIVPF--------HA--------------------- 369
Cdd:PRK05850 306 KRFadrfaPFNLretaIRPSYGLAEATVYVATRE-----PGQPPESVRFdyeklsagHAkrcetgggtplvsygsprspt 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 370 VKVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATK-----AIINK-----DG-WLRSGDIAYYDnDGHFYIVDRLK 438
Cdd:PRK05850 381 VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETErtfgaTLVDPspgtpEGpWLRTGDLGFIS-EGELFIVGRIK 459
|
330
....*....|....*..
gi 41688574 439 SLIKYKGYQVAPAEIEG 455
Cdd:PRK05850 460 DLLIVDGRNHYPDDIEA 476
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
188-463 |
1.15e-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: 73.64 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHkNIVARFSHCKDPTFGNAInPTTAILTVIPFHHGFG---MTTTL-----GYFTCGf 259
Cdd:cd17632 222 DDPLALLIYTSGSTGTPKGAMYTE-RLVATFWLKVSSIQDIRP-PASITLNFMPMSHIAGrisLYGTLarggtAYFAAA- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 260 rvALMHTFEEKLflqslqdykvesTLLVPTLMAFFPK--------------SALVEKYDLSHLKEIA------------- 312
Cdd:cd17632 299 --SDMSTLFDDL------------ALVRPTELFLVPRvcdmlfqryqaeldRRSVAGADAETLAERVkaelrervlggrl 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 313 ----SGGAPLSKEIGEMVKKRFKLNFVrQGYGLTETtSAVLITpDTDVRPgstgkivPFHAVKVVD-PTTGKIL--GPNE 385
Cdd:cd17632 365 laavCGSAPLSAEMKAFMESLLDLDLH-DGYGSTEA-GAVILD-GVIVRP-------PVLDYKLVDvPELGYFRtdRPHP 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41688574 386 TGELYFKGDMIMKSYYNNEEATKAIINKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKY-KGYQVAPAEIEGILLQHPYI 463
Cdd:cd17632 435 RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLV 513
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
52-421 |
9.72e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 70.68 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKY--IERE---LIHSLGIVKPRIIF 126
Cdd:PRK08180 72 YAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYslVSQDfgkLRHVLELLTPGLVF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 127 CSKNT-FQKVLNVkskLKYVETIIILDLNEDLGGYQC-LNNFISQNSDINLDvkkfkpNSFNR--DDQVALVMFSSGTTG 202
Cdd:PRK08180 152 ADDGAaFARALAA---VVPADVEVVAVRGAVPGRAATpFAALLATPPTAAVD------AAHAAvgPDTIAKFLFTSGSTG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 203 VSKGVMLTHKNIVArfshckdptfgNAinptTAILTVIPF--------------HHGFGMTTTLGYftcgfrvALMH--T 266
Cdd:PRK08180 223 LPKAVINTHRMLCA-----------NQ----QMLAQTFPFlaeeppvlvdwlpwNHTFGGNHNLGI-------VLYNggT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 F---EEK----LFLQSLQDYK-VESTLL--VPT----LMAFFPK-SALVEKYdLSHLKEIASGGAPLS------------ 319
Cdd:PRK08180 281 LyidDGKptpgGFDETLRNLReISPTVYfnVPKgwemLVPALERdAALRRRF-FSRLKLLFYAGAALSqdvwdrldrvae 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 320 KEIGEmvkkrfKLNFVrQGYGLTETTSAVLITPDTDVRPGSTGKIVPFHAVKVVdPTTGKIlgpnetgELYFKGDMIMKS 399
Cdd:PRK08180 360 ATCGE------RIRMM-TGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLV-PVGGKL-------EVRVKGPNVTPG 424
|
410 420
....*....|....*....|..
gi 41688574 400 YYNNEEATKAIINKDGWLRSGD 421
Cdd:PRK08180 425 YWRAPELTAEAFDEEGYYRSGD 446
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
193-534 |
1.10e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 70.07 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 193 LVMFSSGTTGVSKGVMLTHKNI-------VARFShckdptfgnaINPTTAILTVIPFHHGFGmtttlgyFTCGFRVAL-- 263
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSWTEIdreieayNEALN----------CEQDETPIVACPVTHSYG-------LICGVLAALtr 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 264 ------MHTFEEKLFLQSLQDYKVE----STLLVPTLMAFFPKSALVEKydlshlkeIASGGAPLSKEIgeMVKKRFKLN 333
Cdd:PRK08308 168 gskpviITNKNPKFALNILRNTPQHilyaVPLMLHILGRLLPGTFQFHA--------VMTSGTPLPEAW--FYKLRERTT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 334 FVRQGYGLTEtTSAVLITPdtDVR-PGSTGKIVPFHAVkvvdpttgkilgpnETGElyfkgdmimksyynNEEATKAII- 411
Cdd:PRK08308 238 YMMQQYGCSE-AGCVSICP--DMKsHLDLGNPLPHVSV--------------SAGS--------------DENAPEEIVv 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 412 -NKDGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTG- 489
Cdd:PRK08308 287 kMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEi 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 41688574 490 --KYLNEQIVQNFVSSQVSTAkwlrggVKFLDEIPKGSTGKIDRKVL 534
Cdd:PRK08308 367 dpVQLREWCIQHLAPYQVPHE------IESVTEIPKNANGKVSRKLL 407
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-534 |
1.82e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.58 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 52 YEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKNT 131
Cdd:PRK05691 1159 YAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHL 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 132 FQKvlnvkskLKYVETIIILDLNEdlggyQCLNNFISQNSDINLDvkkfkpnsfnrDDQVALVMFSSGTTGVSKGVMLTH 211
Cdd:PRK05691 1239 LER-------LPQAEGVSAIALDS-----LHLDSWPSQAPGLHLH-----------GDNLAYVIYTSGSTGQPKGVGNTH 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 212 KNIVARFSHCKDpTFgnAINPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHTFEEK---LFLQSLQDYKVESTLLVP 288
Cdd:PRK05691 1296 AALAERLQWMQA-TY--ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRdpqRIAELVQQYGVTTLHFVP 1372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 289 TLMAFFPKSALVEkyDLSHLKEIASGGAPLSKEIGEMVKKRFKLNFVRQGYGLTETtsAVLIT------PDTDVRPgsTG 362
Cdd:PRK05691 1373 PLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTET--AINVThwqcqaEDGERSP--IG 1446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 363 KIVPFHAVKVVDPTTgKILGPNETGELYFKGDMIMKSYYNNE--EATKAIINKDG-----WLRSGDIAYYDNDGHFYIVD 435
Cdd:PRK05691 1447 RPLGNVLCRVLDAEL-NLLPPGVAGELCIGGAGLARGYLGRPalTAERFVPDPLGedgarLYRTGDRARWNADGALEYLG 1525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 436 RLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTgIPDEAAG-------------ELPAAGVVVQTGKYLNEQIVqnfvs 502
Cdd:PRK05691 1526 RLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGaqlvgyytgeagqEAEAERLKAALAAELPEYMV----- 1599
|
490 500 510
....*....|....*....|....*....|..
gi 41688574 503 sqvsTAKWLRggvkfLDEIPKGSTGKIDRKVL 534
Cdd:PRK05691 1600 ----PAQLIR-----LDQMPLGPSGKLDRRAL 1622
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
72-536 |
2.76e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 69.37 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 72 KQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDK----YIERelIHS-LGIVKPRIIFCSKNTFQKVLNVKSKLKYVE 146
Cdd:PRK07769 77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPaepgHVGR--LHAvLDDCTPSAILTTTDSAEGVRKFFRARPAKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 147 T--IIILDLNEDLGGyqclnnfisqnsdinldvKKFKPNSFNRDDqVALVMFSSGTTGVSKGVMLTHKNIvarfshckdP 224
Cdd:PRK07769 155 RprVIAVDAVPDEVG------------------ATWVPPEANEDT-IAYLQYTSGSTRIPAGVQITHLNL---------P 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 225 TfgNAINPTTAI--------LTVIPFHHGFGMTTTLGYFTCGFRVALMH--TFEEKLF-----LQSLQDYKVESTLLVPT 289
Cdd:PRK07769 207 T--NVLQVIDALegqegdrgVSWLPFFHDMGLITVLLPALLGHYITFMSpaAFVRRPGrwireLARKPGGTGGTFSAAPN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 290 LmAF-------FPKSALVEkYDLSHLKEIASGGAPLSkeIGEMvkKRFKLNF---------VRQGYGLTETTSAVLITP- 352
Cdd:PRK07769 285 F-AFehaaargLPKDGEPP-LDLSNVKGLLNGSEPVS--PASM--RKFNEAFapyglpptaIKPSYGMAEATLFVSTTPm 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 353 ---------DTD---------VRPGSTGKIVPFHAVKV--------VDPTTGKILGPNETGELYFKGDMIMKSYYNNEEA 406
Cdd:PRK07769 359 deeptviyvDRDelnagrfveVPADAPNAVAQVSAGKVgvsewaviVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 407 TKAIIN-----------------KDGWLRSGDIAYYdNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVT 469
Cdd:PRK07769 439 TAATFQnilksrlseshaegapdDALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYV 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 470 GIPDEAAGELPAAgVVVQTGKYLN-------EQIV-------------QNFVSSQVSTAKWLRGGVKFLD-------EIP 522
Cdd:PRK07769 518 AAFSVPANQLPQV-VFDDSHAGLKfdpedtsEQLVivaerapgahkldPQPIADDIRAAIAVRHGVTVRDvllvpagSIP 596
|
570
....*....|....
gi 41688574 523 KGSTGKIDRKVLRQ 536
Cdd:PRK07769 597 RTSSGKIARRACRA 610
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
452-528 |
3.16e-12 |
|
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: 62.18 E-value: 3.16e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688574 452 EIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQIVQNFVSSQVstAKWLR-GGVKFLDEIPKGSTGK 528
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREEL--GPYAVpKEVVFVDELPKTRSGK 76
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
187-528 |
9.65e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 67.56 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 187 RDDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTF--GNAINPTTAILTVIPFHHGFGMT---------TTLGYF 255
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKvtDRVATEEDSYFSYLPLAHVYDQVietyciskgASIGFW 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 256 TCGFRVaLMHTFEE--------------KLFLQSLQdyKVEST-LLVPTLMAF------------FPK---SALVEKYDL 305
Cdd:PLN02861 298 QGDIRY-LMEDVQAlkptifcgvprvydRIYTGIMQ--KISSGgMLRKKLFDFaynyklgnlrkgLKQeeaSPRLDRLVF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 306 SHLKE--------IASGGAPLSKEIGEMVKKRfKLNFVRQGYGLTETTSAVLiTPDTDVRP--GSTGKIVPFHAVKVVD- 374
Cdd:PLN02861 375 DKIKEglggrvrlLLSGAAPLPRHVEEFLRVT-SCSVLSQGYGLTESCGGCF-TSIANVFSmvGTVGVPMTTIEARLESv 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 375 PTTG-KILGPNETGELYFKGDMIMKSYYNNEEATKAIINkDGWLRSGDIAYYDNDGHFYIVDRLKSLIKY-KGYQVAPAE 452
Cdd:PLN02861 453 PEMGyDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVEN 531
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41688574 453 IEGILLQHPYIVDAGVTGIPDEAAgelpAAGVVVQTGKYLNEQIVQNFVSSQVST-AKWLRGGVKFLDEIpkGSTGK 528
Cdd:PLN02861 532 LENTYSRCPLIASIWVYGNSFESF----LVAVVVPDRQALEDWAANNNKTGDFKSlCKNLKARKYILDEL--NSTGK 602
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
48-472 |
1.01e-11 |
|
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: 67.32 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 48 ENVLYEEFLKLSCRLAESFKKY-GLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRIIF 126
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 127 CSKNTFQKVLNVKSKLKyVETIIILDLNEDL--GGYQCLNNFISQNSDINLDVKKFKPNSFNrddQVALVMFSSGTTGVS 204
Cdd:cd05938 84 VAPELQEAVEEVLPALR-ADGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASLRAHVTIK---SPALYIYTSGTTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 205 KGVMLTHKNIVArfshCKDPTFGNAINPTTAILTVIPFHHGFGMTttLGYFTC---GFRVALMHTFEEKLFLQSLQDYKV 281
Cdd:cd05938 160 KAARISHLRVLQ----CSGFLSLCGVTADDVIYITLPLYHSSGFL--LGIGGCielGATCVLKPKFSASQFWDDCRKHNV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 282 ESTLLVPTLMAFF---PKSalveKYDLSHLKEIASGGApLSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLITPDtdvRP 358
Cdd:cd05938 234 TVIQYIGELLRYLcnqPQS----PNDRDHKVRLAIGNG-LRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTG---KI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 359 GSTG-------KIVPFHAVKVvDPTTGKIL----------GPNETGELY--------FKGdmimksYYNNEEATKAIINK 413
Cdd:cd05938 306 GAVGrvsylykLLFPFELIKF-DVEKEEPVrdaqgfcipvAKGEPGLLVakitqqspFLG------YAGDKEQTEKKLLR 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41688574 414 D----G--WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIP 472
Cdd:cd05938 379 DvfkkGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVT 443
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
345-545 |
1.64e-10 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 63.76 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 345 TSAVLITPDTDV---RPGSTgkIVPFHAVK--VVDPTTGKILGPNeTGELYFKGDM--IMKSYYNNEEATKAIINK--DG 415
Cdd:PLN02654 437 TGGFMITPLPGAwpqKPGSA--TFPFFGVQpvIVDEKGKEIEGEC-SGYLCVKKSWpgAFRTLYGDHERYETTYFKpfAG 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 416 WLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAGVVVQTGKYLNEQ 495
Cdd:PLN02654 514 YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41688574 496 IvqnfVSSQVSTAKWLRGGVKFLDEI------PKGSTGKIDRKVLRQMFEKHKSKL 545
Cdd:PLN02654 594 L----RKSLILTVRNQIGAFAAPDKIhwapglPKTRSGKIMRRILRKIASRQLDEL 645
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
347-538 |
5.04e-09 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 58.98 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 347 AVLITPDTD--VRPGSTGKIVP-FHAVkVVDPTTGKILGPNETGELYFKGDMIMKSYYNNEEATKAII-NK--------- 413
Cdd:PRK12476 388 AVRVAADAPnaVAHVSCGQVARsQWAV-IVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgAKlqsrlaegs 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 414 -------DG-WLRSGDIAYYdNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAG-VTG--IPDEAAGEL--- 479
Cdd:PRK12476 467 hadgaadDGtWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGyVTAftVPAEDNERLviv 545
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41688574 480 --PAAGvvvqTGKYLNEQIVQNF---VSSQ----VSTAKWLRGGVkfldeIPKGSTGKIDRKVLRQMF 538
Cdd:PRK12476 546 aeRAAG----TSRADPAPAIDAIraaVSRRhglaVADVRLVPAGA-----IPRTTSGKLARRACRAQY 604
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
189-463 |
1.10e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.47 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHK------NIVARFSHC----KDPTFGNAIN--PTTAIL-----------TVIPfhHG 245
Cdd:COG1541 83 EEIVRIHASSGTTGKPTVVGYTRKdldrwaELFARSLRAagvrPGDRVQNAFGygLFTGGLglhygaerlgaTVIP--AG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 246 FGMTttlgyftcgfrvalmhtfeEKLfLQSLQDYKVesTLLVPTlmAFFPKsALVEK-----YDL--SHLKEIASGGAPL 318
Cdd:COG1541 161 GGNT-------------------ERQ-LRLMQDFGP--TVLVGT--PSYLL-YLAEVaeeegIDPrdLSLKKGIFGGEPW 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 319 SKEIGEMVKKRFKLNfVRQGYGLTETTSAVLI-TPDTD---VRPGStgkivpFHaVKVVDPTTGKILGPNETGELYFkgd 394
Cdd:COG1541 216 SEEMRKEIEERWGIK-AYDIYGLTEVGPGVAYeCEAQDglhIWEDH------FL-VEIIDPETGEPVPEGEEGELVV--- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 395 mimksyynneeaTkaIINKDGW----LRSGDIAYYDND------GHF---YIVDRLKSLIKYKGYQVAPAEIEGILLQHP 461
Cdd:COG1541 285 ------------T--TLTKEAMplirYRTGDLTRLLPEpcpcgrTHPrigRILGRADDMLIIRGVNVFPSQIEEVLLRIP 350
|
..
gi 41688574 462 YI 463
Cdd:COG1541 351 EV 352
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
188-539 |
1.57e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.08 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 DDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDPTFGNAinPTTAILTVIPFHHGFGMTTTLGYFTCGFRVALMHT- 266
Cdd:PRK05851 151 SGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDA--ATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTt 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 267 -FEEKLF--LQSLQDYKveSTLLVPTLMAFfpksALVEKY-------DLSHLKEIASGGAPLSKE-----IGEMVKKRFK 331
Cdd:PRK05851 229 aFSASPFrwLSWLSDSR--ATLTAAPNFAY----NLIGKYarrvsdvDLGALRVALNGGEPVDCDgferfATAMAPFGFD 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 332 LNFVRQGYGLTETTSAV-------------LITPDTDV--RPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYFKGDMI 396
Cdd:PRK05851 303 AGAAAPSYGLAESTCAVtvpvpgiglrvdeVTTDDGSGarRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASM 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 397 MKSYYNNEEatkaiINKDGWLRSGDIAYYdNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGI----- 471
Cdd:PRK05851 383 MSGYLGQAP-----IDPDDWFPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVgtgeg 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 472 --------------PDEAAgelpAAGVVVQTgkylneqivqnfVSSQVSTAKwlrGGVKFLD--EIPKGSTGKIDRKVLR 535
Cdd:PRK05851 457 sarpglviaaefrgPDEAG----ARSEVVQR------------VASECGVVP---SDVVFVApgSLPRTSSGKLRRLAVK 517
|
....
gi 41688574 536 QMFE 539
Cdd:PRK05851 518 RSLE 521
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
61-536 |
3.31e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 56.03 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 61 RLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIErELIHSLgivkpriifCSKNTFQkvlnvks 140
Cdd:PRK09029 40 QLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQ-PLLEEL---------LPSLTLD------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 141 klkyvetiIILDLNEDlGGYQCLNNFISQNSDINLDVKKfkpnsfnRDDQVALVMFSSGTTGVSKGVMLTHKNIVArfsh 220
Cdd:PRK09029 103 --------FALVLEGE-NTFSALTSLHLQLVEGAHAVAW-------QPQRLATMTLTSGSTGLPKAAVHTAQAHLA---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 221 ckdptfgNAInpttAILTVIPFH------------HGFGMTTTLGYFTCGfrvALMHTFEEKLFLQSLQDYKVEStlLVP 288
Cdd:PRK09029 163 -------SAE----GVLSLMPFTaqdswllslplfHVSGQGIVWRWLYAG---ATLVVRDKQPLEQALAGCTHAS--LVP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 289 TLMaffpKSALVEKYDLSHLKEIASGGAPLSKEIGEMVKKRFklnfVRQ--GYGLTETTSAVLITPdTDVRPGsTGKIVP 366
Cdd:PRK09029 227 TQL----WRLLDNRSEPLSLKAVLLGGAAIPVELTEQAEQQG----IRCwcGYGLTEMASTVCAKR-ADGLAG-VGSPLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 367 FHAVKVVDpttgkilgpnetGELYFKGDMIMKSYYNNEEATkAIINKDGWLRSGDIAYYdNDGHFYIVDRLKSLIKYKGY 446
Cdd:PRK09029 297 GREVKLVD------------GEIWLRGASLALGYWRQGQLV-PLVNDEGWFATRDRGEW-QNGELTILGRLDNLFFSGGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 447 QVAPAEIEGILLQHPYIVDAGVTGIPDEAAGELPAAgvVVQTgkylneqivqNFVSSQVSTAKWLRGGV-KF-------- 517
Cdd:PRK09029 363 GIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA--VVES----------DSEAAVVNLAEWLQDKLaRFqqpvayyl 430
|
490
....*....|....*....
gi 41688574 518 LDEIPKGSTGKIDRKVLRQ 536
Cdd:PRK09029 431 LPPELKNGGIKISRQALKE 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
182-545 |
1.17e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 182 PNSFNRDDQVALVMFSSGTTGVSKGVMLTHKNIVArfsHCKdptfgnainpttailTVIpfhHGFGMTTT---LGYFTCG 258
Cdd:PRK05691 2326 LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAM---HCQ---------------AVI---ERFGMRADdceLHFYSIN 2384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 259 FRVAlmhtfEEKLFLQSLQDYKV-----------ESTLLVP----TLMAFFPKSA------LVEKYDLSHLKEIASGGAP 317
Cdd:PRK05691 2385 FDAA-----SERLLVPLLCGARVvlraqgqwgaeEICQLIReqqvSILGFTPSYGsqlaqwLAGQGEQLPVRMCITGGEA 2459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 318 LSKEIGEMVKKRFKLNFVRQGYGLTETTSAVLITPDTDVRPGSTGKiVPFHavKVVDPTTGKILGPN-------ETGELY 390
Cdd:PRK05691 2460 LTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAAS-VPIG--RVVGARVAYILDADlalvpqgATGELY 2536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 391 FKGDMIMKSYYNNEEATKAIINKD------GWL-RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYI 463
Cdd:PRK05691 2537 VGGAGLAQGYHDRPGLTAERFVADpfaadgGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAV 2616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 464 VDAGVTGIpDEAAGELPAAGVVVQTGKYLNEQIVQnfvssqvstakwLRGGVK-----------------FLDEIPKGST 526
Cdd:PRK05691 2617 REAVVLAL-DTPSGKQLAGYLVSAVAGQDDEAQAA------------LREALKahlkqqlpdymvpahliLLDSLPLTAN 2683
|
410 420
....*....|....*....|....*..
gi 41688574 527 GKIDRKVL--------RQMFEKHKSKL 545
Cdd:PRK05691 2684 GKLDRRALpapdpelnRQAYQAPRSEL 2710
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
14-534 |
1.45e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 54.67 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 14 HPLADGTAGEQMFYALSRYADISgciALTNAHTKenVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIA 93
Cdd:PRK10252 453 VEIPETTLSALVAQQAAKTPDAP---ALADARYQ--FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 94 SLYLGIIAAPVSDKYIERELIHSLGIVKPRIIFCSKntfqkvlnvksklkyvetiiildlnEDLGGYQCLNNFISQNSDI 173
Cdd:PRK10252 528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA-------------------------DQLPRFADVPDLTSLCYNA 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 174 NLDVKKFKPNSFNRDDQVALVMFSSGTTGVSKGVMLTHKNIVARFSHCKDpTFGnaINPTTAILTVIPfhhgfgmtttlg 253
Cdd:PRK10252 583 PLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQN-HYP--LTADDVVLQKTP------------ 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 254 yftCGFRVALMHTF-----------------EEKLFLQSL-QDYKVESTLLVPTLMAFFPKSALVE--KYDLSHLKEIAS 313
Cdd:PRK10252 648 ---CSFDVSVWEFFwpfiagaklvmaepeahRDPLAMQQFfAEYGVTTTHFVPSMLAAFVASLTPEgaRQSCASLRQVFC 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 314 GGAPLSKEIGEMVKKRFKL---NFvrqgYGLTEttSAVLIT------PDTDVRPGSTgkiVPF------HAVKVVDpTTG 378
Cdd:PRK10252 725 SGEALPADLCREWQQLTGAplhNL----YGPTE--AAVDVSwypafgEELAAVRGSS---VPIgypvwnTGLRILD-ARM 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 379 KILGPNETGELYFKGDMIMKSYYNNEEATKAIINKDGWL------RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAE 452
Cdd:PRK10252 795 RPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGE 874
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 453 IEGILLQHPYI----VDAGVTGIPDEAAGELP--AAGVVVQTGKYLNEQIVQNFVSSQVStAKWLRGGVKFLDEIPKGST 526
Cdd:PRK10252 875 IDRAMQALPDVeqavTHACVINQAAATGGDARqlVGYLVSQSGLPLDTSALQAQLRERLP-PHMVPVVLLQLDQLPLSAN 953
|
....*...
gi 41688574 527 GKIDRKVL 534
Cdd:PRK10252 954 GKLDRKAL 961
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
45-529 |
2.37e-07 |
|
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: 53.43 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 45 HTKENVLYEEFLKLSCRLAESFKKYGLKQNDTIAVCSENGLQFFLPLIASLYLGIIAAPVSDKYIERELIHSLGIVKPRI 124
Cdd:cd05943 94 GERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 125 IF-CSKNTFQ-KVLNVKSKLKYV--------ETIII----LDLNEDLGGYQC---LNNFISQNSDINLDvkkFKPNSFnr 187
Cdd:cd05943 174 LFaVDAYTYNgKRHDVREKVAELvkglpsllAVVVVpytvAAGQPDLSKIAKaltLEDFLATGAAGELE---FEPLPF-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 188 dDQVALVMFSSGTTGVSK-------GVMLTHKNIVARfsHCkDPTFGNAInpttailtvipfhhgFGMTTTlGYFTCGFR 260
Cdd:cd05943 249 -DHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHIL--HC-DLRPGDRL---------------FYYTTC-GWMMWNWL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 261 VALMHT------FEEKLF---LQSLQDY--KVESTLLV--PTLMAFFPKSALV--EKYDLSHLKEIASGGAPLSKE---- 321
Cdd:cd05943 309 VSGLAVgativlYDGSPFypdTNALWDLadEEGITVFGtsAKYLDALEKAGLKpaETHDLSSLRTILSTGSPLKPEsfdy 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 322 IGEMVKKRFKLNFVRQGyglTETTSA-VLITPDTDVRPGSTGKIVPFHAVKVVDPTTGKILGpnETGELYFKGDM-IMKS 399
Cdd:cd05943 389 VYDHIKPDVLLASISGG---TDIISCfVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWG--EKGELVCTKPFpSMPV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 400 YY-NNEEATK---AIINK-DGWLRSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDE 474
Cdd:cd05943 464 GFwNDPDGSRyraAYFAKyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWK 543
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41688574 475 AAGELPAAGVVVQTGKYLNEQIVQNFVSSqvstakwLRGGV-------KFL--DEIPKGSTGKI 529
Cdd:cd05943 544 DGDERVILFVKLREGVELDDELRKRIRST-------IRSALsprhvpaKIIavPDIPRTLSGKK 600
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
192-534 |
1.43e-06 |
|
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: 50.93 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 192 ALVMFSSGTTGVSKGVMLTHKNIVARFSH----CKdpTFGNAINPTTAILTVIPFHHGFGMT----TTLGYFTCGFRVaL 263
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHfrslFN--ITSEDILFLTSPLTFDPSVVEIFLSlssgATLLIVPTSVKV-L 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 264 MHTFEEKLFlqslQDYKVESTLLVPTLMAFFPkSALVEKYDLSHLKEI---ASGGAPLSKEIgEMVKKRFKLNFVR--QG 338
Cdd:cd17654 198 PSKLADILF----KRHRITVLQATPTLFRRFG-SQSIKSTVLSATSSLrvlALGGEPFPSLV-ILSSWRGKGNRTRifNI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 YGLTETTSAVL--ITPDTDVrPGSTGKIVPFHAVKVVDpttgkILGPNETGELYFKGdmIMKSYYNNEEATKAiinKDGW 416
Cdd:cd17654 272 YGITEVSCWALayKVPEEDS-PVQLGSPLLGTVIEVRD-----QNGSEGTGQVFLGG--LNRVCILDDEVTVP---KGTM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 417 LRSGDIAYYDnDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVTGIPDEAAgelpaagVVVQTGKYLNEQI 496
Cdd:cd17654 341 RATGDFVTVK-DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL-------IAFIVGESSSSRI 412
|
330 340 350
....*....|....*....|....*....|....*...
gi 41688574 497 VQNFVSSQVSTAKwLRGGVKFLDEIPKGSTGKIDRKVL 534
Cdd:cd17654 413 HKELQLTLLSSHA-IPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
418-534 |
1.64e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 418 RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGILLQHPYIVDAGVtGIPDEAAGE------LPAAGVVVQTGky 491
Cdd:PRK05691 4105 RTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKhlvgylVPHQTVLAQGA-- 4181
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 41688574 492 LNEQIVQNFVSS---QVSTAKWLrggvkFLDEIPKGSTGKIDRKVL 534
Cdd:PRK05691 4182 LLERIKQRLRAElpdYMVPLHWL-----WLDRLPLNANGKLDRKAL 4222
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
189-461 |
3.59e-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: 49.54 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 189 DQVALVMFSSGTTGVSKGVMLTHK------NIVARFSHC----KDPTFGNAinpttailtvipfhHGFGMTTT-LGYFT- 256
Cdd:cd05913 78 EKVVRIHASSGTTGKPTVVGYTKNdldvwaELVARCLDAagvtPGDRVQNA--------------YGYGLFTGgLGFHYg 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 257 ---CGFRVALMHTFEEKLFLQSLQDYKVESTLLVPTLMAFFPKSALVEKYDL--SHLKEIASGGAPLSKEIGEMVKKRFK 331
Cdd:cd05913 144 aerLGALVIPAGGGNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPreLSLKVGIFGAEPWTEEMRKRIERRLG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 332 LNfVRQGYGLTETTSAVliTPDTDVRPGSTGKIVPFHAVKVVDPTTGKILGPNETGELYF----KGDMIMKSYynneeat 407
Cdd:cd05913 224 IK-AYDIYGLTEIIGPG--VAFECEEKDGLHIWEDHFIPEIIDPETGEPVPPGEVGELVFttltKEAMPLIRY------- 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41688574 408 kaiinkdgwlRSGDIA---YYDND-GHFY-----IVDRLKSLIKYKGYQVAPAEIEGILLQHP 461
Cdd:cd05913 294 ----------RTRDITrllPGPCPcGRTHrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIP 346
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
339-521 |
1.04e-03 |
|
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: 41.73 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 339 YGLTETTSAV-------------LITPDTDVRPGSTG-KIVPFHAVKVVDPTtgKILGPNETGELYFKGDMIMKSYYNNE 404
Cdd:cd17647 256 YGTTETQRAVsyfevpsrssdptFLKNLKDVMPAGRGmLNVQLLVVNRNDRT--QICGIGEVGEIYVRAGGLAEGYRGLP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 405 EATKA------IINKDGWL----------------------RSGDIAYYDNDGHFYIVDRLKSLIKYKGYQVAPAEIEGI 456
Cdd:cd17647 334 ELNKEkfvnnwFVEPDHWNyldkdnnepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTH 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41688574 457 LLQHPyIVDAGVTGIPDEAAGElPA--AGVVVQTGKYLNEQIVQNFVSSQVST---AKWLRGGVKFLDEI 521
Cdd:cd17647 414 ISQHP-LVRENITLVRRDKDEE-PTlvSYIVPRFDKPDDESFAQEDVPKEVSTdpiVKGLIGYRKLIKDI 481
|
|
| |
