|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
14-553 |
0e+00 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 1125.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 14 QKQCSNDVIFRSRLPDIYIPNHLPLHDYIFENISEFAAKPCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMI 93
Cdd:PLN02246 1 EASASEEFIFRSKLPDIYIPNHLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 94 LLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQN-DGVLIVTTDSDaiPENCL 172
Cdd:PLN02246 81 LLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEdDGVTVVTIDDP--PEGCL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 173 RFSELTQSEEprvDSIPE-KISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFNRDDVILCVLPMFH 251
Cdd:PLN02246 159 HFSELTQADE---NELPEvEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 252 IYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELE 331
Cdd:PLN02246 236 IYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 332 DAISAKFPNAKLGQGYGMTEAGPVLAMSLGFAKEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMK 411
Cdd:PLN02246 316 DAFRAKLPNAVLGQGYGMTEAGPVLAMCLAFAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 412 GYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGE 491
Cdd:PLN02246 396 GYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGE 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232507 492 VPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLANG 553
Cdd:PLN02246 476 VPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAAG 537
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
32-546 |
0e+00 |
|
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: 783.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 32 IPNHLPLHDYIFENISEFAAKPCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFI 111
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 112 GAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLqndGVLIVTTDSDaiPENCLRFSELTQsEEPRVDSIPEK 191
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASL---ALPVVLLDSA--EFDSLSFSDLLF-EADEAEPPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 192 ISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILI 271
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 272 MPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTE 351
Cdd:cd05904 233 MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 352 AGPVLAMSLGFAKEPfpVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLH 431
Cdd:cd05904 313 STGVVAMCFAPEKDR--AKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 432 TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIK 511
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIM 470
|
490 500 510
....*....|....*....|....*....|....*
gi 15232507 512 QFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd05904 471 DFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
54-542 |
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: 593.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 54 CLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKA 133
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 134 SAAKLIVTQSRYVDKI----KNLQNDGVLIVTTDSdaiPENCLRFSELTQSEEPRVDS---IPEKISPEDVVALPFSSGT 206
Cdd:cd05911 81 SKPKVIFTDPDGLEKVkeaaKELGPKDKIIVLDDK---PDGVLSIEDLLSPTLGEEDEdlpPPLKDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 207 TGLPKGVMLTHKGLVTSVAQQVDGENPNlyFNRDDVILCVLPMFHIYALNSIMLCSLRvGATILIMPKFEITLLLEQIQR 286
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLYGN--DGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 287 CKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLGFakep 366
Cdd:cd05911 235 YKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDG---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 367 fPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFI 446
Cdd:cd05911 311 -DDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 447 VDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINK 526
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRG 469
|
490
....*....|....*..
gi 15232507 527 -VFFTDSIPKAPSGKIL 542
Cdd:cd05911 470 gVVFVDEIPKSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
38-553 |
3.88e-160 |
|
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: 463.90 E-value: 3.88e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 38 LHDYIFENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTS 117
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 118 ANPFFTPAEISKQAKASAAKLIVTqsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekispedv 197
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 198 VALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEI 277
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 278 TLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLA 357
Cdd:COG0318 179 ERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 358 MSlgfAKEPFPVKSGACGTVVRNAEMKILDPDTGDsLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGF 437
Cdd:COG0318 258 VN---PEDPGERRPGSVGRPLPGVEVRIVDEDGRE-LPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 438 IDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQ 517
Cdd:COG0318 333 LDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRER 412
|
490 500 510
....*....|....*....|....*....|....*.
gi 15232507 518 VVFYKRINKVFFTDSIPKAPSGKILRKDLRARLANG 553
Cdd:COG0318 413 LARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
14-550 |
2.01e-159 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 465.99 E-value: 2.01e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 14 QKQCSNDVIFRSRLPDIYIPNHLPLHDYIFENISEFAAKPCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMI 93
Cdd:PLN02330 6 QKQEDNEHIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 94 LLPNSPE---VVLTFLAAsfiGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLqndGVLIVTTDSDAIpEN 170
Cdd:PLN02330 86 VLPNVAEygiVALGIMAA---GGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGL---GLPVIVLGEEKI-EG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 171 CLRFSELTQSEEPRVD-SIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYfnRDDVILCVLPM 249
Cdd:PLN02330 159 AVNWKELLEAADRAGDtSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMI--GQVVTLGLIPF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 250 FHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRM--VKSGAAPLG 327
Cdd:PLN02330 237 FHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 328 KELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLGFAKEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGN 407
Cdd:PLN02330 317 PELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 408 QIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEE 487
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232507 488 DAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARL 550
Cdd:PLN02330 477 EAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKM 539
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
42-457 |
5.32e-139 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 409.01 E-value: 5.32e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 42 IFENISEFAAKPCLINGPtGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPF 121
Cdd:pfam00501 1 LERQAARTPDKTALEVGE-GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 122 FTPAEISKQAKASAAKLIVTQSRYVDK--IKNLQNDGVLIVTTDSDAIPENCLRFSELTQSEEPRVDSIPEKISPEDVVA 199
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALKLEelLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 200 LPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFE--- 276
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPald 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 277 ITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAkLGQGYGMTEAGPVl 356
Cdd:pfam00501 240 PAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGV- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 357 aMSLGFAKEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVG 436
Cdd:pfam00501 318 -VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLG 396
|
410 420
....*....|....*....|.
gi 15232507 437 FIDDDDELFIVDRLKELIKYK 457
Cdd:pfam00501 397 RRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
44-547 |
2.09e-137 |
|
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: 406.56 E-value: 2.09e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 44 ENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFT 123
Cdd:cd05936 7 EAARRFPDKTALIFM--GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 124 PAEISKQAKASAAKLIVTqsryvdkiknlqndgvlivttdsdAIPenclrFSELTQSEEPRVDsiPEKISPEDVVALPFS 203
Cdd:cd05936 85 PRELEHILNDSGAKALIV------------------------AVS-----FTDLLAAGAPLGE--RVALTPEDVAVLQYT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 204 SGTTGLPKGVMLTHKGLVtSVAQQVDGENPNLYfNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQ 283
Cdd:cd05936 134 SGTTGVPKGAMLTHRNLV-ANALQIKAWLEDLL-EGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 284 IQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAmslgFA 363
Cdd:cd05936 212 IRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVA----VN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 364 KEPFPVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDE 443
Cdd:cd05936 287 PLDGPRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 444 LFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKR 523
Cdd:cd05936 365 FFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKV 444
|
490 500
....*....|....*....|....
gi 15232507 524 INKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd05936 445 PRQVEFRDELPKSAVGKILRRELR 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
22-552 |
3.93e-135 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 404.22 E-value: 3.93e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 22 IFRSRLPDIYIPN--HLPLHDYIFENISEFAAkPCLINGPTGEVYTYADVHVTSRKLAAGLHN-LGVKQHDVVMILLPNS 98
Cdd:PLN02574 24 IYSSKHPPVPLPSdpNLDAVSFIFSHHNHNGD-TALIDSSTGFSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 99 PEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLqndGVLIVTTD-----SDAIPENCLR 173
Cdd:PLN02574 103 VYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPL---GVPVIGVPenydfDSKRIEFPKF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 174 FSELTQSEEPRVDSIpekISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNL-YFNRDDVILCVLPMFHI 252
Cdd:PLN02574 180 YELIKEDFDFVPKPV---IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYeYPGSDNVYLAALPMFHI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 253 YALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYD-LSSVRMVKSGAAPL-GKEL 330
Cdd:PLN02574 257 YGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEvLKSLKQVSCGAAPLsGKFI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 331 EDAISAkFPNAKLGQGYGMTEAGPVlaMSLGFAKEPFPvKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIM 410
Cdd:PLN02574 337 QDFVQT-LPHVDFIQGYGMTESTAV--GTRGFNTEKLS-KYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 411 KGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAG 490
Cdd:PLN02574 413 KGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232507 491 EVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLAN 552
Cdd:PLN02574 493 EIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTN 554
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
41-547 |
3.79e-134 |
|
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: 400.75 E-value: 3.79e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 41 YIFENISEFAAKPCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANP 120
Cdd:cd17642 22 KAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 121 FFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQN-----DGVLIVTTDSDAIPENCLrFSELTQSEEPRVDS---IPEKI 192
Cdd:cd17642 102 IYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKklkiiKTIIILDSKEDYKGYQCL-YTFITQNLPPGFNEydfKPPSF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 193 SPEDVVAL-PFSSGTTGLPKGVMLTHKGLVTSVAQQVD---GENPNlyfnRDDVILCVLPMFHIYALNSiMLCSLRVGAT 268
Cdd:cd17642 181 DRDEQVALiMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQII----PDTAILTVIPFHHGFGMFT-TLGYLICGFR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 269 ILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYG 348
Cdd:cd17642 256 VVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 349 MTEA-GPVLAMSLGFakepfpVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKD 427
Cdd:cd17642 336 LTETtSAILITPEGD------DKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 428 GWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISE 507
Cdd:cd17642 410 GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15232507 508 DEIKQFVSKQVVFYKRI-NKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd17642 490 KEVMDYVASQVSTAKRLrGGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
60-553 |
4.80e-134 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 399.95 E-value: 4.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLI 139
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 140 VTQSRYVDKIKNL--QNDGV--LIVTTDSDAIPENC--LRFSELTQSEEPRVDSIPekISPEDVVALPFSSGTTGLPKGV 213
Cdd:PRK06187 108 LVDSEFVPLLAAIlpQLPTVrtVIVEGDGPAAPLAPevGEYEELLAAASDTFDFPD--IDENDAAAMLYTSGTTGHPKGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 214 MLTHKGLVTSVAQqvdGENPNLyFNRDDVILCVLPMFHIYALNsIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAM 293
Cdd:PRK06187 186 VLSHRNLFLHSLA---VCAWLK-LSRDDVYLVIVPMFHVHAWG-LPYLALMAGAKQVIPRRFDPENLLDLIETERVTFFF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 294 VVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAMSLGFAKEPFPV-KSG 372
Cdd:PRK06187 261 AVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETSPVVSVLPPEDQLPGQWtKRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 373 ACGTVVRNAEMKILDPDtGDSLPRNK--PGEICIRGNQIMKGYLNDPLATASTIDkDGWLHTGDVGFIDDDDELFIVDRL 450
Cdd:PRK06187 340 SAGRPLPGVEARIVDDD-GDELPPDGgeVGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 451 KELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFT 530
Cdd:PRK06187 418 KDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFV 497
|
490 500
....*....|....*....|...
gi 15232507 531 DSIPKAPSGKILRKDLRARLANG 553
Cdd:PRK06187 498 DELPRTSVGKILKRVLREQYAEG 520
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
52-543 |
4.36e-126 |
|
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: 376.57 E-value: 4.36e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQA 131
Cdd:cd17631 11 RTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 132 KASAAKLIVtqsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekispEDVVALPFSSGTTGLPK 211
Cdd:cd17631 89 ADSGAKVLF------------------------------------------------------DDLALLMYTSGTTGRPK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 212 GVMLTHKGLVTSVAQQVDgenpNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTV 291
Cdd:cd17631 115 GAMLTHRNLLWNAVNALA----ALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 292 AMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKfpNAKLGQGYGMTEAGP-VLAMSLGFAKEpfpvK 370
Cdd:cd17631 191 FFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPgVTFLSPEDHRR----K 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 371 SGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRL 450
Cdd:cd17631 265 LGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 451 KELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFT 530
Cdd:cd17631 343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFV 422
|
490
....*....|...
gi 15232507 531 DSIPKAPSGKILR 543
Cdd:cd17631 423 DALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
47-549 |
2.35e-123 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 372.31 E-value: 2.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 47 SEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAE 126
Cdd:PRK07656 16 RRFGDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 127 ISKQAKASAAKLIVTQSRYV-------DKIKNLQNDgVLIVTTDSDAIPENCLRFSELTQSEEPRVDSIPekISPEDVVA 199
Cdd:PRK07656 94 AAYILARGDAKALFVLGLFLgvdysatTRLPALEHV-VICETEEDDPHTEKMKTFTDFLAAGDPAERAPE--VDPDDVAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 200 LPFSSGTTGLPKGVMLTHKGLvTSVAQQVdGENPNLyfNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITL 279
Cdd:PRK07656 171 ILFTSGTTGRPKGAMLTHRQL-LSNAADW-AEYLGL--TEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 280 LLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMS 359
Cdd:PRK07656 247 VFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVTTFN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 360 -LGfakEPFPVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFI 438
Cdd:PRK07656 327 rLD---DDRKTVAGTIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 439 DDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQV 518
Cdd:PRK07656 403 DEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHL 482
|
490 500 510
....*....|....*....|....*....|.
gi 15232507 519 VFYKRINKVFFTDSIPKAPSGKILRKDLRAR 549
Cdd:PRK07656 483 AKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
196-542 |
7.51e-120 |
|
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: 356.98 E-value: 7.51e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 196 DVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFNRDDVILCVLPMFHIYALNSIMLCsLRVGATILIMPKF 275
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA----SGGLTEGDVFLSTLPLFHIGGLFGLLGA-LLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 276 EITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPV 355
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAP-GIKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 356 LAMSLGFAKEpfpVKSGACGTVVRNAEMKILDPDTGDsLPRNKPGEICIRGNQIMKGYLNDPLATASTiDKDGWLHTGDV 435
Cdd:cd04433 155 VATGPPDDDA---RKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 436 GFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVS 515
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 15232507 516 KQVVFYKRINKVFFTDSIPKAPSGKIL 542
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
50-547 |
6.34e-109 |
|
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: 334.28 E-value: 6.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 50 AAKPCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISK 129
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 130 QAKASAAKLIVTQS-RYVDKIKNLQNDGVLIVTTDSD-AIPENCLRFSELTQSEEPRVDSIPEKIS-PEDVVALPFSSGT 206
Cdd:cd05926 81 YLADLGSKLVLTPKgELGPASRAASKLGLAILELALDvGVLIRAPSAESLSNLLADKKNAKSEGVPlPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 207 TGLPKGVMLTHKGLVTSVAQQVDGENpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQR 286
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYK----LTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 287 CKVTVAMVVPPIVLAIAKSPETEKYD-LSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPvlAMSLgfakE 365
Cdd:cd05926 237 YNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAH--QMTS----N 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 PFPVKSGACGTVVR--NAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDE 443
Cdd:cd05926 310 PLPPGPRKPGSVGKpvGVEVRILDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 444 LFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKR 523
Cdd:cd05926 389 LFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKV 468
|
490 500
....*....|....*....|....
gi 15232507 524 INKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd05926 469 PKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
38-554 |
4.09e-105 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 327.34 E-value: 4.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 38 LHDYIFENISEFAAKPCLINgpTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTS 117
Cdd:PRK05605 34 LVDLYDNAVARFGDRPALDF--FGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 118 ANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQNDGVL--IVTTD-SDAIP-------------------------E 169
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLetIVSVNmIAAMPllqrlalrlpipalrkaraaltgpaP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 170 NCLRFSELTQSEEPRVDSI--PEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQ---VDGENPnlyfnRDDVIL 244
Cdd:PRK05605 192 GTVPWETLVDAAIGGDGSDvsHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGkawVPGLGD-----GPERVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 245 CVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAA 324
Cdd:PRK05605 267 AALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 325 PLGKEL----EDAIsakfpNAKLGQGYGMTEAGPVLA---MS----LGFAKEPFPvksgacgtvvrNAEMKILDPDTGD- 392
Cdd:PRK05605 347 ALPVSTvelwEKLT-----GGLLVEGYGLTETSPIIVgnpMSddrrPGYVGVPFP-----------DTEVRIVDPEDPDe 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 393 SLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIG 472
Cdd:PRK05605 411 TMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 473 HPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLAN 552
Cdd:PRK05605 490 HPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLE 569
|
..
gi 15232507 553 GL 554
Cdd:PRK05605 570 KL 571
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
39-552 |
1.08e-101 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 318.21 E-value: 1.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 39 HDYIFENISEFAAKPCLI-NGPTGEV--YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAIT 115
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIwEGEDGEErtLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 116 TSANPFFTPAEISKQAKASAAKLIVTQSRY------------VDKI----KNLQNdgVLIV-TTDSDAIPENCLRFSELT 178
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkekVDEAleelPSLEH--VIVVgRTGADVPMEGDLDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 179 QSEEPRVDsiPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTsvaqQVDGENPNLY-FNRDDVILCVLPMFHIYALNS 257
Cdd:COG0365 170 AAASAEFE--PEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLV----HAATTAKYVLdLKPGDVFWCTADIGWATGHSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 258 IMLCSLRVGATILIM---PKF-EITLLLEQIQRCKVTVAMVVPPIVLAIAKSPET--EKYDLSSVRMVKSGAAPLGKELE 331
Cdd:COG0365 244 IVYGPLLNGATVVLYegrPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEplKKYDLSSLRLLGSAGEPLNPEVW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 332 DAISAKFpNAKLGQGYGMTEAGPVLAMSLGFakepFPVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQ--I 409
Cdd:COG0365 324 EWWYEAV-GVPIVDGWGQTETGGIFISNLPG----LPVKPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVIKGPWpgM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 410 MKGYLNDPLATASTI--DKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEE 487
Cdd:COG0365 398 FRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232507 488 DAGEVPVAFVVRSKDSNISED---EIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLAN 552
Cdd:COG0365 478 IRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
65-546 |
5.30e-100 |
|
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: 309.41 E-value: 5.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSr 144
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 yvdkiknlqndgvlivttdsdaipenclrfsELtqseeprvdsipekispEDVVALPFSSGTTGLPKGVMLTHKGLVTSV 224
Cdd:cd05935 82 -------------------------------EL-----------------DDLALIPYTSGTTGLPKGCMHTHFSAAANA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 225 AQQVDGENpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAK 304
Cdd:cd05935 114 LQSAVWTG----LTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 305 SPETEKYDLSSVRMVKSGAAPL----GKELEDAISAKFpnaklGQGYGMTEAgpvlaMSLGFAKEPFPVKSGACGTVVRN 380
Cdd:cd05935 190 TPEFKTRDLSSLKVLTGGGAPMppavAEKLLKLTGLRF-----VEGYGLTET-----MSQTHTNPPLRPKLQCLGIP*FG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 381 AEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATAS---TIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYK 457
Cdd:cd05935 260 VDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfiEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 458 GFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVV-----RSKdsnISEDEIKQFVSKQVVFYKRINKVFFTDS 532
Cdd:cd05935 340 GFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVlrpeyRGK---VTEEDIIEWAREQMAAYKYPREVEFVDE 416
|
490
....*....|....
gi 15232507 533 IPKAPSGKILRKDL 546
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
37-546 |
1.06e-96 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 305.03 E-value: 1.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 37 PLHDYIFENISEFAAKPCLinGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITT 116
Cdd:PRK06710 25 PLHKYVEQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 117 SANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQNDGVL---IVTTDSDAIP--ENCL-------------RFSE-- 176
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIehvIVTRIADFLPfpKNLLypfvqkkqsnlvvKVSEse 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 177 ---LTQSEEPRVDSIPEKI-SPE-DVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpnLY--FNRDDVILCVLPM 249
Cdd:PRK06710 183 tihLWNSVEKEVNTGVEVPcDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW----LYncKEGEEVVLGVLPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 250 FHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKE 329
Cdd:PRK06710 259 FHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 330 LEDAISaKFPNAKLGQGYGMTEAGPVLAMSLGFAKEpfpvKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQI 409
Cdd:PRK06710 339 VQEKFE-TVTGGKLVEGYGLTESSPVTHSNFLWEKR----VPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 410 MKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDA 489
Cdd:PRK06710 414 MKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYR 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232507 490 GEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKrINKVF-FTDSIPKAPSGKILRKDL 546
Cdd:PRK06710 493 GETVKAFVVLKEGTECSEEELNQFARKYLAAYK-VPKVYeFRDELPKTTVGKILRRVL 549
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
49-551 |
5.29e-94 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 296.84 E-value: 5.29e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 49 FAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEIS 128
Cdd:PRK08316 24 YPDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 129 KQAKASAAKLIVTQSRYVDKIKNLQND------GVLIVTTDSDAiPENCLRFSELTQSEEPRVDSIPekISPEDVVALPF 202
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALlpvdtlILSLVLGGREA-PGGWLDFADWAEAGSVAEPDVE--LADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 203 SSGTTGLPKGVMLTHKGLVTS-VAQQVDGEnpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLL 281
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEyVSCIVAGD-----MSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELIL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 282 EQIQRCKVTvAMVVPPIV-LAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPvLAMSL 360
Cdd:PRK08316 254 RTIEAERIT-SFFAPPTVwISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAP-LATVL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 361 GfaKEPFPVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDD 440
Cdd:PRK08316 332 G--PEEHLRRPGSAGRPVLNVETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 441 DDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVF 520
Cdd:PRK08316 408 EGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAG 487
|
490 500 510
....*....|....*....|....*....|.
gi 15232507 521 YKRINKVFFTDSIPKAPSGKILRKDLRARLA 551
Cdd:PRK08316 488 FKVPKRVIFVDELPRNPSGKILKRELRERYA 518
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
61-542 |
1.12e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 296.49 E-value: 1.12e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHN-LGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLI 139
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 140 VTQSRYVDKIKNLQNDGVL---IVTTDSDAI--------PENCLRFSELTQSEEPRV----DSI-------PEKISPEDV 197
Cdd:PRK08314 113 IVGSELAPKVAPAVGNLRLrhvIVAQYSDYLpaepeiavPAWLRAEPPLQALAPGGVvawkEALaaglappPHTAGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 198 VALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEI 277
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSN----STPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 278 TLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPL----GKELEDAISAKFPnaklgQGYGMTEAg 353
Cdd:PRK08314 269 EAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMpeavAERLKELTGLDYV-----EGYGLTET- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 354 pvlaMSLGFAKEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATA-STIDKDG--WL 430
Cdd:PRK08314 343 ----MAQTHSNPPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAeAFIEIDGkrFF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 431 HTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDS--NISED 508
Cdd:PRK08314 419 RTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEE 498
|
490 500 510
....*....|....*....|....*....|....
gi 15232507 509 EIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKIL 542
Cdd:PRK08314 499 EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
65-550 |
5.54e-89 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 282.62 E-value: 5.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YVDKIKNLQNdgvlivttdsdaipencLRFSELTQSEEPRVDsIPEKISPEDVVALPFSSGTTGLPKGVMLTHKG-LVTS 223
Cdd:PRK03640 109 FEAKLIPGIS-----------------VKFAELMNGPKEEAE-IQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNhWWSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 VAQQVdgenpNLYFNRDDVILCVLPMFHIYALnSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIA 303
Cdd:PRK03640 171 VGSAL-----NLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 304 KSPETEKYDlSSVRMVKSGAAPLGKE-LEDAISAKFPnakLGQGYGMTE-AGPVLAMSLGFAKEpfpvKSGACGTVVRNA 381
Cdd:PRK03640 245 ERLGEGTYP-SSFRCMLLGGGPAPKPlLEQCKEKGIP---VYQSYGMTEtASQIVTLSPEDALT----KLGSAGKPLFPC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 382 EMKILDpdTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQV 461
Cdd:PRK03640 317 ELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 462 APAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVrsKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKI 541
Cdd:PRK03640 394 YPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV--KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKL 471
|
....*....
gi 15232507 542 LRKDLRARL 550
Cdd:PRK03640 472 LRHELKQLV 480
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
61-547 |
5.21e-87 |
|
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: 275.32 E-value: 5.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TqsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekispeDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd05934 81 V------------------------------------------------------DPASILYTSGTTGPPKGVVITHANL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVAQQVDGENpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVL 300
Cdd:cd05934 107 TFAGYYSARRFG----LGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 301 AIAKSPETEKYDLSSVRMVKSGAAPlgKELEDAISAKFpNAKLGQGYGMTEAGPVLAmslgfAKEPFPVKSGACGTVVRN 380
Cdd:cd05934 183 YLLAQPPSPDDRAHRLRAAYGAPNP--PELHEEFEERF-GVRLLEGYGMTETIVGVI-----GPRDEPRRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 381 AEMKILDPDtGDSLPRNKPGEICIRGNQ---IMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYK 457
Cdd:cd05934 255 YEVRIVDDD-GQELPAGEPGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 458 GFQVAPAELESLLIGHPEINDVAVVAMKEEDAG-EVPVAFVVRsKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKA 536
Cdd:cd05934 333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEdEVKAVVVLR-PGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKT 411
|
490
....*....|.
gi 15232507 537 PSGKILRKDLR 547
Cdd:cd05934 412 PTEKVAKAQLR 422
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
62-547 |
8.55e-87 |
|
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: 277.97 E-value: 8.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT 141
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSRYVDKIKNLQND----GVLIVTTDSDAIPE----NCLRFSELTQSEEPRVD--SIPEKispeDVVALPFSSGTTGLPK 211
Cdd:cd12119 104 DRDFLPLLEAIAPRlptvEHVVVMTDDAAMPEpagvGVLAYEELLAAESPEYDwpDFDEN----TAAAICYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 212 GVMLTHKGLV--TSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALNSIMLCSLrVGATiLIMP--KFEITLLLEQIQRC 287
Cdd:cd12119 180 GVVYSHRSLVlhAMAALLTDG----LGLSESDVVLPVVPMFHVNAWGLPYAAAM-VGAK-LVLPgpYLDPASLAELIERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 288 KVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSG--AAP--LGKELEDAISakfpnaKLGQGYGMTEAGPVLAMSL--- 360
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGgsAVPrsLIEAFEERGV------RVIHAWGMTETSPLGTVARpps 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 361 ----GFAKEPFPVKSGAcGTVVRNAEMKILDPDTGdSLPR--NKPGEICIRGNQIMKGYLNDPlATASTIDKDGWLHTGD 434
Cdd:cd12119 328 ehsnLSEDEQLALRAKQ-GRPVPGVELRIVDDDGR-ELPWdgKAVGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 435 VGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFV 514
Cdd:cd12119 405 VATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFL 484
|
490 500 510
....*....|....*....|....*....|...
gi 15232507 515 SKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd12119 485 ADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
64-548 |
3.28e-86 |
|
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: 273.07 E-value: 3.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLivtqs 143
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 ryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekispEDVVALPFSSGTTGLPKGVMLTHKGLVTS 223
Cdd:cd05912 77 ---------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 VAqqvdGENPNLYFNRDDVILCVLPMFHIYALnSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLA-I 302
Cdd:cd05912 106 AI----GSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRlL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 303 AKSPETEKYDLssvRMVKSGAAPLGKE-LEDAISAKFPnakLGQGYGMTEAGpvlAMSLGFAKEPFPVKSGACGTVVRNA 381
Cdd:cd05912 181 EILGEGYPNNL---RCILLGGGPAPKPlLEQCKEKGIP---VYQSYGMTETC---SQIVTLSPEDALNKIGSAGKPLFPV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 382 EMKILDPDTgdslPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQV 461
Cdd:cd05912 252 ELKIEDDGQ----PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 462 APAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDsnISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKI 541
Cdd:cd05912 327 YPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP--ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKL 404
|
....*..
gi 15232507 542 LRKDLRA 548
Cdd:cd05912 405 LRHELKQ 411
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-547 |
1.40e-85 |
|
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: 269.15 E-value: 1.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 194 PEDVVALPFSSGTTGLPKGVMLTHKGLVTSvAQQVdGENpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGAT-ILIM 272
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFI-GER--LGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATmVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 273 PKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEA 352
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 353 GPVLAMSlgFAKEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHT 432
Cdd:cd05917 157 SPVSTQT--RTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 433 GDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQ 512
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKA 314
|
330 340 350
....*....|....*....|....*....|....*
gi 15232507 513 FVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd05917 315 YCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
61-549 |
4.94e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 271.27 E-value: 4.94e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIKNLQND--GVLIVTTDSDAIPENCLRFSELTQSEEPrvDSIPEKIsPEDVVAL-PFSSGTTGLPKGVMLTH 217
Cdd:PRK07786 120 TEAALAPVATAVRDIvpLLSTVVVAGGSSDDSVLGYEDLLAEAGP--AHAPVDI-PNDSPALiMYTSGTTGRPKGAVLTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 218 KGLVtsvAQQVDGENPNLYFNRDDVILCVLPMFHIYALNSiMLCSLRVGATILIMP--KFEITLLLEQIQRCKVTVAMVV 295
Cdd:PRK07786 197 ANLT---GQAMTCLRTNGADINSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFDPGQLLDVLEAEKVTGIFLV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 296 PPIVLAIAKSPETEKYDLSsVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLGfakEPFPVKSGACG 375
Cdd:PRK07786 273 PAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLG---EDAIRKLGSVG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 376 TVVRNAEMKILDPDTGDsLPRNKPGEICIRGNQIMKGYLNDPLATASTIDkDGWLHTGDVGFIDDDDELFIVDRLKELIK 455
Cdd:PRK07786 349 KVIPTVAARVVDENMND-VPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMII 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 456 YKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFV-VRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIP 534
Cdd:PRK07786 427 SGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALP 506
|
490
....*....|....*
gi 15232507 535 KAPSGKILRKDLRAR 549
Cdd:PRK07786 507 RNPAGKVLKTELRER 521
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
64-541 |
2.33e-83 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 270.14 E-value: 2.33e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT-- 141
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAad 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 ---QSRYVDKIKNL------QNDGVL----------IVTTDSDAIPeNCLRFSEL----TQSEEPRVDSIPEKISPEDVV 198
Cdd:PRK08315 124 gfkDSDYVAMLYELapelatCEPGQLqsarlpelrrVIFLGDEKHP-GMLNFDELlalgRAVDDAELAARQATLDPDDPI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 199 ALPFSSGTTGLPKGVMLTHKGLVTSvAQQVdGENPNLYfNRDDVILCVlPMFHIYALnsIM--LCSLRVGATILIM-PKF 275
Cdd:PRK08315 203 NIQYTSGTTGFPKGATLTHRNILNN-GYFI-GEAMKLT-EEDRLCIPV-PLYHCFGM--VLgnLACVTHGATMVYPgEGF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 276 EITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVR---MvksGAAPLGKELEDAISAKFPNAKLGQGYGMTEA 352
Cdd:PRK08315 277 DPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRtgiM---AGSPCPIEVMKRVIDKMHMSEVTIAYGMTET 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 353 GPVLAMSLgfAKEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHT 432
Cdd:PRK08315 354 SPVSTQTR--TDDPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHT 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 433 GDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQ 512
Cdd:PRK08315 432 GDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRD 511
|
490 500 510
....*....|....*....|....*....|
gi 15232507 513 FVSKQVVFYKrINK-VFFTDSIPKAPSGKI 541
Cdd:PRK08315 512 FCRGKIAHYK-IPRyIRFVDEFPMTVTGKI 540
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
33-482 |
4.12e-83 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 270.82 E-value: 4.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 33 PNHLPlhDYIFENISEFAAKPCLINGPTGE--VYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASF 110
Cdd:COG1022 10 ADTLP--DLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 111 IGAITTSANPFFTPAEISKQAKASAAKLIVTQSRY-VDKIKNLQNDG---VLIVTTDSDAIPE--NCLRFSELTQ----- 179
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEqLDKLLEVRDELpslRHIVVLDPRGLRDdpRLLSLDELLAlgrev 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 180 SEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpnLYFNRDDVILCVLPMFHIYAlNSIM 259
Cdd:COG1022 168 ADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSFLPLAHVFE-RTVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 260 LCSLRVGATILIMPkfEITLLLEQIQRCKVTVAMVVPP--------IVLAIAKSPET------------EKYD------- 312
Cdd:COG1022 243 YYALAAGATVAFAE--SPDTLAEDLREVKPTFMLAVPRvwekvyagIQAKAEEAGGLkrklfrwalavgRRYArarlagk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 313 -----------------LSSVR---------MVkSGAAPLGKELedaisAKFPNAkLG----QGYGMTEAGPVLAMSlgf 362
Cdd:COG1022 321 spslllrlkhaladklvFSKLRealggrlrfAV-SGGAALGPEL-----ARFFRA-LGipvlEGYGLTETSPVITVN--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 363 akEPFPVKSGACGTVVRNAEMKIlDPDtgdslprnkpGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDD 442
Cdd:COG1022 391 --RPGDNRIGTVGPPLPGVEVKI-AED----------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDG 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15232507 443 ELFIVDRLKELI-----KYkgfqVAPAELESLLIGHPEINDVAVV 482
Cdd:COG1022 458 FLRITGRKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVV 498
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
35-551 |
2.93e-82 |
|
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: 266.63 E-value: 2.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 35 HLPLHDYIFENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAI 114
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 115 ttsanPFFT-PA----EISKQAKASAAKLIVTQSR-----YVDKIKNLQNDG----VLIVTTDsdaiPENCLRFSELtqS 180
Cdd:COG1021 102 -----PVFAlPAhrraEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVpslrHVLVVGD----AGEFTSLDAL--L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 181 EEPRVDSIPEkISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVD--GenpnlyFNRDDVILCVLPMFHIYALNSI 258
Cdd:COG1021 171 AAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEicG------LDADTVYLAALPAAHNFPLSSP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 259 -MLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAK 337
Cdd:COG1021 244 gVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 338 FPnAKLGQGYGMTEaGPVlamslgfakepfpvksgaCGT-------VVRNA---------EMKILDPDtGDSLPRNKPGE 401
Cdd:COG1021 324 LG-CTLQQVFGMAE-GLV------------------NYTrlddpeeVILTTqgrpispddEVRIVDED-GNPVPPGEVGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 402 ICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAV 481
Cdd:COG1021 383 LLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAV 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232507 482 VAMKEEDAGEVPVAFVVrSKDSNISEDEIKQFV-SKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLA 551
Cdd:COG1021 463 VAMPDEYLGERSCAFVV-PRGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
62-552 |
1.15e-81 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 264.03 E-value: 1.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGL-HNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIKNLQNDGVLivttdsdaipENCLRFSELTQSEEPRVDSIPEKiSPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:PRK06839 106 VEKTFQNMALSMQKVSYV----------QRVISITSLKEIEDRKIDNFVEK-NESASFIICYTSGTTGKPKGAVLTQENM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVAQQVdgenPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVL 300
Cdd:PRK06839 175 FWNALNNT----FAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 301 AIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAK-FPnakLGQGYGMTEAGPVLAMslgFAKEPFPVKSGACGTVVR 379
Cdd:PRK06839 251 ALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRgFL---FGQGFGMTETSPTVFM---LSEEDARRKVGSIGKPVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 380 NAEMKILDPDTGDsLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGF 459
Cdd:PRK06839 325 FCDYELIDENKNK-VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 460 QVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSG 539
Cdd:PRK06839 403 NIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATG 482
|
490
....*....|...
gi 15232507 540 KIlrkdLRARLAN 552
Cdd:PRK06839 483 KI----QKAQLVN 491
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
29-547 |
4.57e-81 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 264.19 E-value: 4.57e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 29 DIYIPNHLPLHDYIFENISEFAAKPCLINgpTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPN---SPEVVLTF 105
Cdd:PRK07059 16 EIDASQYPSLADLLEESFRQYADRPAFIC--MGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNvlqYPVAIAAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 106 LAASFIgaiTTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKN-LQNDGV--LIVTTDSD----------------- 165
Cdd:PRK07059 94 LRAGYV---VVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQvLAKTAVkhVVVASMGDllgfkghivnfvvrrvk 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 166 ------AIPeNCLRFSELTqSEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFNR 239
Cdd:PRK07059 171 kmvpawSLP-GHVRFNDAL-AEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 240 DD---VILCVLPMFHIYALNSIMLCSLRVGAT-ILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSS 315
Cdd:PRK07059 249 RPdqlNFVCALPLYHIFALTVCGLLGMRTGGRnILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 316 VRMVKSGaaplGKELEDAISAKF---PNAKLGQGYGMTEAGPVLAMSLGFAKEpFpvkSGACGTVVRNAEMKILDpDTGD 392
Cdd:PRK07059 329 LIVANGG----GMAVQRPVAERWlemTGCPITEGYGLSETSPVATCNPVDATE-F---SGTIGLPLPSTEVSIRD-DDGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 393 SLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIG 472
Cdd:PRK07059 400 DLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVAS 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232507 473 HPEINDVAVVAMKEEDAGEVPVAFVVRsKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK07059 480 HPGVLEVAAVGVPDEHSGEAVKLFVVK-KDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
42-547 |
9.15e-81 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 263.45 E-value: 9.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 42 IFEN-ISEFAAKPCLINgpTGEVYTYADVHVTSRKLAAGLHN-LGVKQHDVVMILLPNspevVLTFLAASF----IGAIT 115
Cdd:PRK08974 28 MFEQaVARYADQPAFIN--MGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPN----LLQYPIALFgilrAGMIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 116 TSANPFFTPAEISKQAKASAAKLIVTQSRY---VDKI-KNLQNDGVlIVTTDSDAIPE---------------------- 169
Cdd:PRK08974 102 VNVNPLYTPRELEHQLNDSGAKAIVIVSNFahtLEKVvFKTPVKHV-ILTRMGDQLSTakgtlvnfvvkyikrlvpkyhl 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 170 -NCLRFSElTQSEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVaQQVDGENPNLYFNRDDVILCVLP 248
Cdd:PRK08974 181 pDAISFRS-ALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL-EQAKAAYGPLLHPGKELVVTALP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 249 MFHIYALNSIMLCSLRVGAT-ILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLG 327
Cdd:PRK08974 259 LYHIFALTVNCLLFIELGGQnLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 328 KeledAISAKFPNA---KLGQGYGMTEAGPVLAMSlgfakePFPVK--SGACGTVVRNAEMKILDpDTGDSLPRNKPGEI 402
Cdd:PRK08974 339 Q----AVAERWVKLtgqYLLEGYGLTECSPLVSVN------PYDLDyySGSIGLPVPSTEIKLVD-DDGNEVPPGEPGEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 403 CIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVV 482
Cdd:PRK08974 408 WVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAV 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232507 483 AMKEEDAGEVPVAFVVRsKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK08974 487 GVPSEVSGEAVKIFVVK-KDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
52-548 |
1.23e-79 |
|
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: 256.83 E-value: 1.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLINGptGEVYTYADVHVTSRKLAAGLHNLG-VKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQ 130
Cdd:cd05941 2 RIAIVDD--GDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 131 AKASAAKLIVtqsryvdkiknlqnDGVLIVTTdsdaipenclrfseltqseeprvdsipekispedvvalpfsSGTTGLP 210
Cdd:cd05941 80 ITDSEPSLVL--------------DPALILYT-----------------------------------------SGTTGRP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 211 KGVMLTHKGLVTSVAQQVDGENpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVT 290
Cdd:cd05941 105 KGVVLTHANLAANVRALVDAWR----WTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 291 VAMVVPPIVLAIAKSPET--------EKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLgQGYGMTEAGpvLAMSLGF 362
Cdd:cd05941 181 VFMGVPTIYTRLLQYYEAhftdpqfaRAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLL-ERYGMTEIG--MALSNPL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 363 AKEPFPvksGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDD 442
Cdd:cd05941 258 DGERRP---GTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 443 ELFIVDRLK-ELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDS-NISEDEIKQFVSKQVVF 520
Cdd:cd05941 335 YYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLAP 414
|
490 500
....*....|....*....|....*...
gi 15232507 521 YKRINKVFFTDSIPKAPSGKILRKDLRA 548
Cdd:cd05941 415 YKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
37-551 |
2.97e-78 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 256.89 E-value: 2.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 37 PLHDYIFENISEFAAKPCLINgpTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITT 116
Cdd:PRK06178 34 PLTEYLRAWARERPQRPAIIF--YGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 117 SANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQNDGVL---IVTTDSDAIPE-------NCLR------------F 174
Cdd:PRK06178 112 PVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLrhvIVTSLADVLPAeptlplpDSLRaprlaaagaidlL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 175 SELTQSEEPRVDSIPEkisPEDVVALPFSSGTTGLPKGVMLTHKGLV------TSVAQQVDgenpnlyfnRDDVILCVLP 248
Cdd:PRK06178 192 PALRACTAPVPLPPPA---LDALAALNYTGGTTGMPKGCEHTQRDMVytaaaaYAVAVVGG---------EDSVFLSFLP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 249 MFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVksGAAPLGK 328
Cdd:PRK06178 260 EFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQV--RVVSFVK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 329 ELEDAISAKFPNAK---LGQG-YGMTEAGPVLAMSLGFAKEPFPVKSGA--CGTVVRNAEMKILDPDTGDSLPRNKPGEI 402
Cdd:PRK06178 338 KLNPDYRQRWRALTgsvLAEAaWGMTETHTCDTFTAGFQDDDFDLLSQPvfVGLPVPGTEFKICDFETGELLPLGAEGEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 403 CIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVV 482
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVV 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232507 483 AMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKrINKVFFTDSIPKAPSGKILRKDLRARLA 551
Cdd:PRK06178 497 GRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYK-VPEIRIVDALPMTATGKVRKQDLQALAE 564
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
64-548 |
3.96e-78 |
|
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: 252.64 E-value: 3.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQS 143
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 ryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekispEDVVALPFSSGTTGLPKGVMLTHKGLVTS 223
Cdd:cd05972 81 ---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 VAQQVDGENpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILI--MPKFEITLLLEQIQRCKVTVaMVVPPIVLA 301
Cdd:cd05972 110 IPTAAYWLG----LRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTS-FCGPPTAYR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 302 IAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAMSLGFakepfPVKSGACGTVVRNA 381
Cdd:cd05972 185 MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTVGNFPDM-----PVKPGSMGRPTPGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 382 EMKILDpDTGDSLPRNKPGEICIRGN--QIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGF 459
Cdd:cd05972 259 DVAIID-DDGRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 460 QVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISE---DEIKQFVSKQVVFYKRINKVFFTDSIPKA 536
Cdd:cd05972 337 RIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPREIEFVEELPKT 416
|
490
....*....|..
gi 15232507 537 PSGKILRKDLRA 548
Cdd:cd05972 417 ISGKIRRVELRD 428
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
49-554 |
2.38e-77 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 254.31 E-value: 2.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 49 FAAKPCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEIS 128
Cdd:PRK12583 31 FPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 129 KQAKASAAKLIVTQSRY--VDKIKNLQndGVLIVTTDSDAIPENCLRFSELTQ-----SEEP------------------ 183
Cdd:PRK12583 111 YALGQSGVRWVICADAFktSDYHAMLQ--ELLPGLAEGQPGALACERLPELRGvvslaPAPPpgflawhelqargetvsr 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 184 -RVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTS---VAQQvdgenpnLYFNRDDViLCV-LPMFHIYALNSI 258
Cdd:PRK12583 189 eALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNgyfVAES-------LGLTEHDR-LCVpVPLYHCFGMVLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 259 MLCSLRVGATiLIMPK--FEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISA 336
Cdd:PRK12583 261 NLGCMTVGAC-LVYPNeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 337 KFPNAKLGQGYGMTEAGPVLAMSLgfAKEPFPVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLND 416
Cdd:PRK12583 340 EMHMAEVQIAYGMTETSPVSLQTT--AADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNN 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 417 PLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAF 496
Cdd:PRK12583 417 PEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAW 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232507 497 VVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLANGL 554
Cdd:PRK12583 497 VRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEEL 554
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
49-548 |
1.77e-74 |
|
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: 244.52 E-value: 1.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 49 FAAKPCLINGPTgeVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEIS 128
Cdd:cd12118 17 YPDRTSIVYGDR--RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 129 KQAKASAAKlivtqsryvdkiknlqndgVLIVTTDSDaipenclrFSELTQSEEPRVDSIPEKiSPEDVVALPFSSGTTG 208
Cdd:cd12118 95 FILRHSEAK-------------------VLFVDREFE--------YEDLLAEGDPDFEWIPPA-DEWDPIALNYTSGTTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 209 LPKGVMLTHKG-LVTSVAQQVDGENPNlyfnrDDVILCVLPMFH------IYALNSimlcslrVGATILIMPKFEITLLL 281
Cdd:cd12118 147 RPKGVVYHHRGaYLNALANILEWEMKQ-----HPVYLWTLPMFHcngwcfPWTVAA-------VGGTNVCLRKVDAKAIY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 282 EQIQRCKVTvAMVVPPIVL-AIAKSPETEKYDLS-SVRMVKSGAAPLGKELEDAISAKFpnaKLGQGYGMTEA-GPVLAM 358
Cdd:cd12118 215 DLIEKHKVT-HFCGAPTVLnMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAKMEELGF---DVTHVYGLTETyGPATVC 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 359 SLGFAKEPFPVKSGA-------CGTVVRNaEMKILDPDTGDSLPRNKP--GEICIRGNQIMKGYLNDPLATASTIdKDGW 429
Cdd:cd12118 291 AWKPEWDELPTEERArlkarqgVRYVGLE-EVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGW 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 430 LHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDE 509
Cdd:cd12118 369 FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEE 448
|
490 500 510
....*....|....*....|....*....|....*....
gi 15232507 510 IKQFVSKQVVFYKRINKVFFTDsIPKAPSGKILRKDLRA 548
Cdd:cd12118 449 IIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
32-547 |
5.93e-74 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 245.50 E-value: 5.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 32 IPNHLPLHDY-----IFE-NISEFAAKPCLINgpTGEVYTYADVHVTSRKLAAGL-HNLGVKQHDVVMILLPNSPEVVLT 104
Cdd:PRK12492 14 VPSTIDLAAYksvveVFErSCKKFADRPAFSN--LGVTLSYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 105 FLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQNDGVL------------------IVTTDSDA 166
Cdd:PRK12492 92 VFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIeylieakmgdllpaakgwLVNTVVDK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 167 IPENCLRFSeLTQS-------EEPRVDSI-PEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQ------QVDGEN 232
Cdd:PRK12492 172 VKKMVPAYH-LPQAvpfkqalRQGRGLSLkPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQvraclsQLGPDG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 233 PNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGA-TILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKY 311
Cdd:PRK12492 251 QPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNhNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 312 DLSSVRMVKSGAAPLGKELEDAIsAKFPNAKLGQGYGMTEAGPVLAMSlgfakePFPVKS--GACGTVVRNAEMKILDpD 389
Cdd:PRK12492 331 DFSALKLTNSGGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTN------PYGELArlGTVGIPVPGTALKVID-D 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 390 TGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESL 469
Cdd:PRK12492 403 DGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDV 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232507 470 LIGHPEINDVAVVAMKEEDAGEVPVAFVVrSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK12492 483 VMAHPKVANCAAIGVPDERSGEAVKLFVV-ARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
63-548 |
1.39e-72 |
|
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: 238.43 E-value: 1.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 63 VYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQ 142
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 143 SRYvdkiknlqndgvlivttdsdaipencLRFSELTQseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGLVT 222
Cdd:cd05903 81 ERF--------------------------RQFDPAAM--------------PDAVALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 223 SVAQQVDgenpNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAI 302
Cdd:cd05903 121 SIRQYAE----RLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 303 AKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAMSlgfakEPFPVKSGAC--GTVVRN 380
Cdd:cd05903 197 LNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSI-----TPAPEDRRLYtdGRPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 381 AEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATAsTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQ 460
Cdd:cd05903 271 VEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTA-DAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGEN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 461 VAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQ-VVFYKRINKVFFTDSIPKAPSG 539
Cdd:cd05903 349 IPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSG 428
|
....*....
gi 15232507 540 KILRKDLRA 548
Cdd:cd05903 429 KVQKFRLRE 437
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
45-550 |
2.87e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 239.40 E-value: 2.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 45 NISEFAA--------KPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITT 116
Cdd:PRK06145 3 NLSASIAfharrtpdRAALVYR--DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 117 SANPFFTPAEISKQAKASAAKLIVTQSRYvDKIKNLqndGVLIVTTDSDAIPENclrfSELTQSEEPRVDSIPekISPED 196
Cdd:PRK06145 81 PINYRLAADEVAYILGDAGAKLLLVDEEF-DAIVAL---ETPKIVIDAAAQADS----RRLAQGGLEIPPQAA--VAPTD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 197 VVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFE 276
Cdd:PRK06145 151 LVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIA----LGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 277 ITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTE--AGP 354
Cdd:PRK06145 227 PEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTEtcSGD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 355 VLaMSLGFAKEpfpvKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGD 434
Cdd:PRK06145 307 TL-MEAGREIE----KIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 435 VGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFV 514
Cdd:PRK06145 380 VGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHC 459
|
490 500 510
....*....|....*....|....*....|....*.
gi 15232507 515 SKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARL 550
Cdd:PRK06145 460 RQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-547 |
1.11e-71 |
|
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: 238.04 E-value: 1.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 50 AAKPCLInGPTGEvYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISK 129
Cdd:cd05959 18 GDKTAFI-DDAGS-LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 130 QAKASAAKLIVTQSRYVDKIK----NLQNDGVLIVTTDSDAIPENCLRFSELTQSEEPrvDSIPEKISPEDVVALPFSSG 205
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAaaltKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAE--QLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 206 TTGLPKGVMLTHKGL-VTSV--AQQVdgenpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKF-EITLLL 281
Cdd:cd05959 174 STGRPKGVVHLHADIyWTAElyARNV------LGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 282 EQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLgQGYGMTEAGPVLAMSLg 361
Cdd:cd05959 248 KRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDIL-DGIGSTEMLHIFLSNR- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 362 fakePFPVKSGACGTVVRNAEMKILDPDTGDsLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDD 441
Cdd:cd05959 326 ----PGRVRYGTTGKPVPGYEVELRDEDGGD-VADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 442 DELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVV---RSKDSNISEDEIKQFVSKQV 518
Cdd:cd05959 400 GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpGYEDSEALEEELKEFVKDRL 479
|
490 500
....*....|....*....|....*....
gi 15232507 519 VFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd05959 480 APYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
28-547 |
8.26e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 236.97 E-value: 8.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 28 PDIYiPNhlpLHDYIFENISEFAAKPCLINgpTGEVYTYADVHVTSRKLAAGL-HNLGVKQHDVVMILLPNSPEVVLTFL 106
Cdd:PRK05677 20 PDEY-PN---IQAVLKQSCQRFADKPAFSN--LGKTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 107 AASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKI-KNLQNDGV--LIVTTDSDAIP--------------- 168
Cdd:PRK05677 94 GAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAeKVLPKTGVkhVIVTEVADMLPplkrllinavvkhvk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 169 --------ENCLRFSE-LTQSEEPRVDsiPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQ--QVDGENPNlyf 237
Cdd:PRK05677 174 kmvpayhlPQAVKFNDaLAKGAGQPVT--EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcrALMGSNLN--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 238 NRDDVILCVLPMFHIYALNSIMLCSLRVGA-TILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSV 316
Cdd:PRK05677 249 EGCEILIAPLPLYHIYAFTFHCMAMMLIGNhNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 317 RMVKSGaaplGKELEDAISAKFP---NAKLGQGYGMTEAGPVLAMSlgfakePFP-VKSGACGTVVRNAEMKILDPDtGD 392
Cdd:PRK05677 329 KLTLSG----GMALQLATAERWKevtGCAICEGYGMTETSPVVSVN------PSQaIQVGTIGIPVPSTLCKVIDDD-GN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 393 SLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIG 472
Cdd:PRK05677 398 ELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAA 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232507 473 HPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK05677 478 LPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
75-553 |
9.46e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 236.04 E-value: 9.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 75 KLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTP---AEISKQAKASAakLIVTQSRYVDKIKN 151
Cdd:PRK06188 49 RYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLddhAYVLEDAGIST--LIVDPAPFVERALA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 152 L--QNDGVLIVTTDSDAipENCLRFSELTQSEEPRvDSIPEKISPeDVVALPFSSGTTGLPKGVMLTHKGLVT-SVAQQV 228
Cdd:PRK06188 127 LlaRVPSLKHVLTLGPV--PDGVDLLAAAAKFGPA-PLVAAALPP-DIAGLAYTGGTTGKPKGVMGTHRSIATmAQIQLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 229 DGENPnlyfnRDDVILCVLPMFHiyALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPET 308
Cdd:PRK06188 203 EWEWP-----ADPRFLMCTPLSH--AGGAFFLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 309 EKYDLSSVRMVKSGAAPLGK-ELEDAISAKFPnaKLGQGYGMTEAG-PVLAMSLGFAKEPFPVKSGACGTVVRNAEMKIL 386
Cdd:PRK06188 276 RTRDLSSLETVYYGASPMSPvRLAEAIERFGP--IFAQYYGQTEAPmVITYLRKRDHDPDDPKRLTSCGRPTPGLRVALL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 387 DPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAEL 466
Cdd:PRK06188 354 DED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREV 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 467 ESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVS---------KQVVfykrinkvfFTDSIPKAP 537
Cdd:PRK06188 432 EDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKerkgsvhapKQVD---------FVDSLPLTA 502
|
490
....*....|....*.
gi 15232507 538 SGKILRKDLRARLANG 553
Cdd:PRK06188 503 LGKPDKKALRARYWEG 518
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
64-503 |
1.97e-70 |
|
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: 232.87 E-value: 1.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQS 143
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 ryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKglvtS 223
Cdd:cd05907 86 --------------------------------------------------PDDLATIIYTSGTTGRPKGVMLSHR----N 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 VAQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPkfEITLLLEQIQRCKVTVAMVVP----PIV 299
Cdd:cd05907 112 ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRPTVFLAVPrvweKVY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 300 LAI--AKSPETEK--YDL---SSVRMVKSGAAPLGKELedaiSAKFpnAKLG----QGYGMTEAGPVLAMSLgfakePFP 368
Cdd:cd05907 190 AAIkvKAVPGLKRklFDLavgGRLRFAASGGAPLPAEL----LHFF--RALGipvyEGYGLTETSAVVTLNP-----PGD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 369 VKSGACGTVVRNAEMKIlDPDtgdslprnkpGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVD 448
Cdd:cd05907 259 NRIGTVGKPLPGVEVRI-ADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITG 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232507 449 RLKELIKY-KGFQVAPAELESLLIGHPEINDVAVVAmkeeDAGEVPVAFVVRSKDS 503
Cdd:cd05907 328 RKKDLIITsGGKNISPEPIENALKASPLISQAVVIG----DGRPFLVALIVPDPEA 379
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
196-543 |
2.75e-70 |
|
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: 228.92 E-value: 2.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 196 DVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKF 275
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD----CADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 276 EITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPV 355
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 356 lamSLGFAKEPFPVKSGACGTVVRNAEMKILDPdtgdslprnkpGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDV 435
Cdd:cd17638 157 ---TMCRPGDDAETVATTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 436 GFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVS 515
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCR 302
|
330 340
....*....|....*....|....*...
gi 15232507 516 KQVVFYKRINKVFFTDSIPKAPSGKILR 543
Cdd:cd17638 303 ERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
60-550 |
9.48e-70 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 233.87 E-value: 9.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISK-----QAKAS 134
Cdd:PRK06087 46 HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWvlnkcQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 135 AAKLIVTQSRYVDKIKNLQND-----GVLIVttDSDAIPENCLRFSELTQSEEPRVDSIPekISPEDVVALPFSSGTTGL 209
Cdd:PRK06087 126 FAPTLFKQTRPVDLILPLQNQlpqlqQIVGV--DKLAPATSSLSLSQIIADYEPLTTAIT--THGDELAAVLFTSGTEGL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 210 PKGVMLTHKGLVTSVAQQVDGenpnLYFNRDDVILCVLPMFH----IYALNSIMLcslrVGATILIMPKFEITLLLEQIQ 285
Cdd:PRK06087 202 PKGVMLTHNNILASERAYCAR----LNLTWQDVFMMPAPLGHatgfLHGVTAPFL----IGARSVLLDIFTPDACLALLE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 286 RCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELedAISAKFPNAKLGQGYGMTEAGPVLAMSLGfakE 365
Cdd:PRK06087 274 QQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKV--ARECQQRGIKLLSVYGSTESSPHAVVNLD---D 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 PFPVKSGACGTVVRNAEMKILDPDTGDsLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELF 445
Cdd:PRK06087 349 PLSRFMHTDGYAAAGVEIKVVDEARKT-LPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIK 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 446 IVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNIS--EDEIKQFVSKQVVFYKR 523
Cdd:PRK06087 428 ITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLtlEEVVAFFSRKRVAKYKY 507
|
490 500 510
....*....|....*....|....*....|.
gi 15232507 524 INKVFFTDSIPKAPSGKI----LRKDLRARL 550
Cdd:PRK06087 508 PEHIVVIDKLPRTASGKIqkflLRKDIMRRL 538
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
65-546 |
1.64e-69 |
|
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: 230.03 E-value: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YVDKIknlqndgvlivtTDSDAIPEnclrfselTQSEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSV 224
Cdd:TIGR01923 81 LEEKD------------FQADSLDR--------IEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 225 AqqvdGENPNLYFNRDDVILCVLPMFHIYALnSIMLCSLRVGATILIMPKFeiTLLLEQIQRCKVTVAMVVPPIVLAIAK 304
Cdd:TIGR01923 141 V----GSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKF--NQLLEMIANERVTHISLVPTQLNRLLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 305 SPETEkydlSSVRMVKSGAAPLGKEL-EDAISAKFPnakLGQGYGMTEAGpvlAMSLGFAKEPFPVKSGAcGTVVRNAEM 383
Cdd:TIGR01923 214 EGGHN----ENLRKILLGGSAIPAPLiEEAQQYGLP---IYLSYGMTETC---SQVTTATPEMLHARPDV-GRPLAGREI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 384 KILDPDtgdslpRNKPGEICIRGNQIMKGYL-NDPLATAStiDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVA 462
Cdd:TIGR01923 283 KIKVDN------KEGHGEIMVKGANLMKGYLyQGELTPAF--EQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 463 PAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDsnISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKIL 542
Cdd:TIGR01923 355 PEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD--ISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKIL 432
|
....
gi 15232507 543 RKDL 546
Cdd:TIGR01923 433 RNQL 436
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
53-549 |
2.72e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 226.32 E-value: 2.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 53 PCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAK 132
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 133 ASAAKLIVTQSRYVDKIKNLQND---GVLIVTTDSDAIPeNCLRFSELT--QSEEPrvdsipekisPEDVVA---LPFSS 204
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAElpaGVPLLLVVAGPVP-GFRSYEEALaaQPDTP----------IADETAgadMLYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 205 GTTGLPKGVM--LTHKGLVTSVAQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLcSLRVGATILIMPKFEITLLLE 282
Cdd:PRK08276 150 GTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMS-ALALGGTVVVMEKFDAEEALA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 283 QIQRCKVTVAMVVPPIVLAIAKSPET--EKYDLSSVRMVKSGAAPLGKELEDA-------IsakfpnakLGQGYGMTEAG 353
Cdd:PRK08276 229 LIERYRVTHSQLVPTMFVRMLKLPEEvrARYDVSSLRVAIHAAAPCPVEVKRAmidwwgpI--------IHEYYASSEGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 354 PV-LAMSLGFAKEPfpvksgacGTVVR--NAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWL 430
Cdd:PRK08276 301 GVtVITSEDWLAHP--------GSVGKavLGEVRILDED-GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 431 HTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAfVVRSKDSNIS---- 506
Cdd:PRK08276 372 TVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQPADGADAgdal 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15232507 507 EDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRAR 549
Cdd:PRK08276 451 AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
65-548 |
1.10e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 225.96 E-value: 1.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YVDKIKNLQND--GVLIVTTDSDAIPEnclrfselTQSEEPRVDSIPEKISPEDVVALP-------FSSGTTGLPKGVML 215
Cdd:PRK07788 156 FTDLLSALPPDlgRLRAWGGNPDDDEP--------SGSTDETLDDLIAGSSTAPLPKPPkpggiviLTSGTTGTPKGAPR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 216 THKGLVTSVAQQVDgENPnlyFNRDDVILCVLPMFHIYALNSIMLcSLRVGATILIMPKFEITLLLEQIQRCKVTvAMVV 295
Cdd:PRK07788 228 PEPSPLAPLAGLLS-RVP---FRAGETTLLPAPMFHATGWAHLTL-AMALGSTVVLRRRFDPEATLEDIAKHKAT-ALVV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 296 PPIVLA--IAKSPET-EKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTE-AGPVLAMSLGFAKEPfpvks 371
Cdd:PRK07788 302 VPVMLSriLDLGPEVlAKYDTSSLKIIFVSGSALSPELATRALEAF-GPVLYNLYGSTEvAFATIATPEDLAEAP----- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 372 GACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPlaTASTIDkdGWLHTGDVGFIDDDDELFIVDRLK 451
Cdd:PRK07788 376 GTVGRPPKGVTVKILDEN-GNEVPRGVVGRIFVGNGFPFEGYTDGR--DKQIID--GLLSSGDVGYFDEDGLLFVDGRDD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 452 ELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTD 531
Cdd:PRK07788 451 DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLD 530
|
490
....*....|....*..
gi 15232507 532 SIPKAPSGKILRKDLRA 548
Cdd:PRK07788 531 ELPRNPTGKVLKRELRE 547
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
62-549 |
8.18e-66 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 225.60 E-value: 8.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGaITTSANPFFTPAEISKQAKASAAKLIVT 141
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 ------------QSRYVDKIKNLQN----DG--------VLIVTTDSDAIPENCLRF-SELTQSEEPRVDSiPEKISPED 196
Cdd:PRK07529 136 lgpfpgtdiwqkVAEVLAALPELRTvvevDLarylpgpkRLAVPLIRRKAHARILDFdAELARQPGDRLFS-GRPIGPDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 197 VVALPFSSGTTGLPKGVMLTHKGLVTS--VAQQVDGENPnlyfnrDDVILCVLPMFHIYALNSIMLCSLRVGATILI--- 271
Cdd:PRK07529 215 VAAYFHTGGTTGMPKLAQHTHGNEVANawLGALLLGLGP------GDTVFCGLPLFHVNALLVTGLAPLARGAHVVLatp 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 272 --------MPKF-EItllleqIQRCKVTVAMVVPPIVLAIAKSPeTEKYDLSSVRMVKSGAAPLGKELEDAISAKfPNAK 342
Cdd:PRK07529 289 qgyrgpgvIANFwKI------VERYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAA-TGVR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 343 LGQGYGMTEAGPVLAMS--LGfakepfPVKSGACGTVVRNAEMKI--LDPDTGDS--LPRNKPGEICIRGNQIMKGYLND 416
Cdd:PRK07529 361 IVEGYGLTEATCVSSVNppDG------ERRIGSVGLRLPYQRVRVviLDDAGRYLrdCAVDEVGVLCIAGPNVFSGYLEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 417 PLATASTIDkDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAF 496
Cdd:PRK07529 435 AHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAY 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15232507 497 VVRSKDSNISEDEIKQFVSKQVVFYKRINK-VFFTDSIPKAPSGKILRKDLRAR 549
Cdd:PRK07529 514 VQLKPGASATEAELLAFARDHIAERAAVPKhVRILDALPKTAVGKIFKPALRRD 567
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
54-551 |
4.64e-65 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 220.13 E-value: 4.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 54 CLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKA 133
Cdd:PRK07514 19 PFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 134 SAAKLIVTQSRYVDKIKNL-QNDGVLIVTT-DSDAIPEnclrFSELTQSEEPRVDSIPEkiSPEDVVALPFSSGTTGLPK 211
Cdd:PRK07514 99 AEPALVVCDPANFAWLSKIaAAAGAPHVETlDADGTGS----LLEAAAAAPDDFETVPR--GADDLAAILYTSGTTGRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 212 GVMLTHKGLVTSVAQQVDgenpnlY--FNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCkv 289
Cdd:PRK07514 173 GAMLSHGNLLSNALTLVD------YwrFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMPRA-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 290 TVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLgQGYGMTE---------AGPVLAMSL 360
Cdd:PRK07514 245 TVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAIL-ERYGMTEtnmntsnpyDGERRAGTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 361 GFakePFPvksgacGTVVRnaemkILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDD 440
Cdd:PRK07514 324 GF---PLP------GVSLR-----VTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 441 DDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVF 520
Cdd:PRK07514 390 RGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLAR 469
|
490 500 510
....*....|....*....|....*....|.
gi 15232507 521 YKRINKVFFTDSIPKAPSGKILRKDLRARLA 551
Cdd:PRK07514 470 FKQPKRVFFVDELPRNTMGKVQKNLLREQYA 500
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
60-547 |
1.24e-64 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 219.55 E-value: 1.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEV--YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAK 137
Cdd:PRK08008 32 GGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 138 LIVTQSRYVDKIKNLQNDG------VLIVTTDSDAIpENCLRFSELTQSEEPRVDSIPeKISPEDVVALPFSSGTTGLPK 211
Cdd:PRK08008 112 LLVTSAQFYPMYRQIQQEDatplrhICLTRVALPAD-DGVSSFTQLKAQQPATLCYAP-PLSTDDTAEILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 212 GVMLTHKGLVTS---VAQQVDgenpnlyFNRDDVILCVLPMFHI-YALNSIMlCSLRVGATILIMPKFEITLLLEQIQRC 287
Cdd:PRK08008 190 GVVITHYNLRFAgyySAWQCA-------LRDDDVYLTVMPAFHIdCQCTAAM-AAFSAGATFVLLEKYSARAFWGQVCKY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 288 KVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSgAAPLGKELEDAISAKFpNAKLGQGYGMTEA-GPVLAMSLGFAKE- 365
Cdd:PRK08008 262 RATITECIPMMIRTLMVQPPSANDRQHCLREVMF-YLNLSDQEKDAFEERF-GVRLLTSYGMTETiVGIIGDRPGDKRRw 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 PFPVKSGACgtvvrnAEMKILDpDTGDSLPRNKPGEICIRG---NQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDD 442
Cdd:PRK08008 340 PSIGRPGFC------YEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 443 ELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYK 522
Cdd:PRK08008 413 FFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFK 492
|
490 500
....*....|....*....|....*
gi 15232507 523 RINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK08008 493 VPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
46-547 |
1.99e-64 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 220.13 E-value: 1.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 46 ISEFAAKPCLINgpTGEVYTYADVHVTSRKLAAGLHN-LGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTP 124
Cdd:PRK08751 35 VAKFADRPAYHS--FGKTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 125 AEISKQAKASAAKLIVTQSRYVDKIKNLQNDGVL--IVTTD--------------------SDAIPE----NCLRFSE-L 177
Cdd:PRK08751 113 RELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVkqVITTGlgdmlgfpkaalvnfvvkyvKKLVPEyrinGAIRFREaL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 178 TQSEEPRVDSIpeKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVaQQVDG--ENPNLYFNRDDVILCVLPMFHIYAL 255
Cdd:PRK08751 193 ALGRKHSMPTL--QIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANM-QQAHQwlAGTGKLEEGCEVVITALPLYHIFAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 256 NSIMLCSLRVGA-TILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGaaplGKELEDAI 334
Cdd:PRK08751 270 TANGLVFMKIGGcNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGG----GMAVQRSV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 335 SAKFPNAK---LGQGYGMTEAGPVLAMSlgfakePFPVK--SGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQI 409
Cdd:PRK08751 346 AERWKQVTgltLVEAYGLTETSPAACIN------PLTLKeyNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 410 MKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDA 489
Cdd:PRK08751 419 MKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKS 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232507 490 GEVpVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK08751 499 GEI-VKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
34-549 |
9.35e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 217.89 E-value: 9.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 34 NHLPLH--DYIFENISEFAAKPCLINGPTgeVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFI 111
Cdd:PRK08162 14 NYVPLTplSFLERAAEVYPDRPAVIHGDR--RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 112 GAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKN----LQNDGVLIVTTDSDAIPEN----CLRFSELTQSEEP 183
Cdd:PRK08162 92 GAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREalalLPGPKPLVIDVDDPEYPGGrfigALDYEAFLASGDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 184 RVDSIPekisPED---VVALPFSSGTTGLPKGVMLTHKG-LVTSVAQQVDGENPnlyfnRDDVILCVLPMFH-------- 251
Cdd:PRK08162 172 DFAWTL----PADewdAIALNYTSGTTGNPKGVVYHHRGaYLNALSNILAWGMP-----KHPVYLWTLPMFHcngwcfpw 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 252 -IYALNSIMLCsLRvgatilimpKFEITLLLEQIQRCKVTvAMVVPPIVL-AIAKSPETEKYDLS-SVRMVKSGAAPLGK 328
Cdd:PRK08162 243 tVAARAGTNVC-LR---------KVDPKLIFDLIREHGVT-HYCGAPIVLsALINAPAEWRAGIDhPVHAMVAGAAPPAA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 329 ELEDAISAKFpnaKLGQGYGMTEA-GP--VLAMSLGFAKEPFP---VKSGACGtvVR---NAEMKILDPDTGDSLPRNKP 399
Cdd:PRK08162 312 VIAKMEEIGF---DLTHVYGLTETyGPatVCAWQPEWDALPLDeraQLKARQG--VRyplQEGVTVLDPDTMQPVPADGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 400 --GEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEIN 477
Cdd:PRK08162 387 tiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232507 478 DVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTdSIPKAPSGKILRKDLRAR 549
Cdd:PRK08162 466 VAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQ 536
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
61-543 |
1.20e-62 |
|
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: 212.69 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKqakasaaklIV 140
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHH---------IL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSryvdkiknlqnDGVLIVTTDsdaipenclrfseltqseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd05914 76 NHS-----------EAKAIFVSD------------------------------EDDVALINYTSGTTGNSKGVMLTYRNI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVaqqvDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLL-EQIQRCKVTVAMVVPPIV 299
Cdd:cd05914 115 VSNV----DGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIaLAFAQVTPTLGVPVPLVI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 300 LAIAKSPETEKYDLS-----------------------------SVRMVKSGAAPLGKELE-DAISAKFPNAklgQGYGM 349
Cdd:cd05914 191 EKIFKMDIIPKLTLKkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEeFLRTIGFPYT---IGYGM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 350 TEAGPVLAMSlgfakEPFPVKSGACGTVVRNAEMKILDPDtgdslPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGW 429
Cdd:cd05914 268 TETAPIISYS-----PPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 430 LHTGDVGFIDDDDELFIVDRLKELI-KYKGFQVAPAELESLLIGHP----------EINDVAVVAMKEEDAGEvpVAFVV 498
Cdd:cd05914 338 FHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPfvleslvvvqEKKLVALAYIDPDFLDV--KALKQ 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15232507 499 RSKDSNISEDEIKQfVSKQVVFYKRINKV-FFTDSIPKAPSGKILR 543
Cdd:cd05914 416 RNIIDAIKWEVRDK-VNQKVPNYKKISKVkIVKEEFEKTPKGKIKR 460
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
37-546 |
1.83e-62 |
|
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: 212.96 E-value: 1.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 37 PLHDYIFENISEFAAKPCLINGPTGevYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITT 116
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRR--LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 117 SANPFFTPAEISKQAKASAAKLIVtqsryvdkiknlqndgvlivttdsdaIPENCLRFSELTQSEEPRvDSIPekispeD 196
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYI--------------------------VPDRHAGFDHRALARELA-ESIP------E 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 197 VVALPFSSGTTGLPKGVMLTHKGLVTSV--AQQVDGenpnlyFNRDDVILCVLPMFHIYALNSI-MLCSLRVGATILIMP 273
Cdd:cd05920 141 VALFLLSGGTTGTPKLIPRTHNDYAYNVraSAEVCG------LDQDTVYLAVLPAAHNFPLACPgVLGTLLAGGRVVLAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 274 KFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEaG 353
Cdd:cd05920 215 DPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAE-G 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 354 PVLAMSLGfakEPFPVKSGACG-TVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHT 432
Cdd:cd05920 293 LLNYTRLD---DPDEVIIHTQGrPMSPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 433 GDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVrSKDSNISEDEIKQ 512
Cdd:cd05920 369 GDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVV-LRDPPPSAAQLRR 447
|
490 500 510
....*....|....*....|....*....|....*
gi 15232507 513 FVSKQ-VVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd05920 448 FLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
52-553 |
3.53e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 213.01 E-value: 3.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQA 131
Cdd:PRK13391 13 KPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 132 KASAAKLIVTQSRYVDkiknlqndgvlIVTTDSDAIPENCLRFSELTQSEEPRVDSIPEKIS--PEDVVA-------LPF 202
Cdd:PRK13391 93 DDSGARALITSAAKLD-----------VARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAglPATPIAdeslgtdMLY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 203 SSGTTGLPKGVM--LTHKGLVTSVAqqVDGENPNLY-FNRDDVILCVLPMFHIYALNSIMLcSLRVGATILIMPKFEITL 279
Cdd:PRK13391 162 SSGTTGRPKGIKrpLPEQPPDTPLP--LTAFLQRLWgFRSDMVYLSPAPLYHSAPQRAVML-VIRLGGTVIVMEHFDAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 280 LLEQIQRCKVTVAMVVPPIVLAIAKSPET--EKYDLSSVRMVKSGAAPLGKELEDAIsAKFPNAKLGQGYGMTEAGPVLA 357
Cdd:PRK13391 239 YLALIEEYGVTHTQLVPTMFSRMLKLPEEvrDKYDLSSLEVAIHAAAPCPPQVKEQM-IDWWGPIIHEYYAATEGLGFTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 358 MSlgfaKEPFPVKSGACGTVVRnAEMKILDPDtGDSLPRNKPGEICIRGNQIMKgYLNDPLATASTIDKDG-WLHTGDVG 436
Cdd:PRK13391 318 CD----SEEWLAHPGTVGRAMF-GDLHILDDD-GAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 437 FIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED---EIKQF 513
Cdd:PRK13391 391 YVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPAlaaELIAF 470
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15232507 514 VSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLANG 553
Cdd:PRK13391 471 CRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
61-554 |
6.97e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 211.59 E-value: 6.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIv 140
Cdd:PRK09088 20 GRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 tqsryvdkiknLQNDGVlivtTDSDAIPENCLRFSELTQSEEPrvdSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:PRK09088 99 -----------LGDDAV----AAGRTDVEDLAAFIASADALEP---ADTPSIPPERVSLILFTSGTSGQPKGVMLSERNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VT-----SVAQQVDGENpnlyfnrddVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQI--QRCKVTVAM 293
Cdd:PRK09088 161 QQtahnfGVLGRVDAHS---------SFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLgdPALGITHYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 294 VVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKE-----LEDAIsakfpnaKLGQGYGMTEAGPVLAMSLGFAKepFP 368
Cdd:PRK09088 232 CVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEdilgwLDDGI-------PMVDGFGMSEAGTVFGMSVDCDV--IR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 369 VKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVD 448
Cdd:PRK09088 303 AKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 449 RLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVF 528
Cdd:PRK09088 382 RKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLR 461
|
490 500
....*....|....*....|....*.
gi 15232507 529 FTDSIPKAPSGKILRKDLRARLANGL 554
Cdd:PRK09088 462 LVDALPRTASGKLQKARLRDALAAGR 487
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
52-547 |
1.32e-60 |
|
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: 206.56 E-value: 1.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLINGptGEVYTYADVHVTSRKLAAGL-HNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKq 130
Cdd:cd05958 1 RTCLRSP--EREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 131 akasaaklivtqsrYVDKiknlqndgvlivttdsdAIPENCLRFSELTQSEeprvdsipekispeDVVALPFSSGTTGLP 210
Cdd:cd05958 78 --------------ILDK-----------------ARITVALCAHALTASD--------------DICILAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 211 KGVMLTHKGLVTSV---AQQVDGENPnlyfnrDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRC 287
Cdd:cd05958 113 KATMHFHRDPLASAdryAVNVLRLRE------DDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARY 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 288 KVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLamslgFAKEPF 367
Cdd:cd05958 187 KPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTEMFHIF-----ISARPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 368 PVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKgYLNDPlaTASTIDKDGWLHTGDVGFIDDDDELFIV 447
Cdd:cd05958 261 DARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGPTGCR-YLADK--RQRTYVQGGWNITGDTYSRDPDGYFRHQ 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 448 DRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED---EIKQFVSKQVVFYKRI 524
Cdd:cd05958 337 GRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYP 416
|
490 500
....*....|....*....|...
gi 15232507 525 NKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd05958 417 RAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
49-549 |
1.47e-60 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 209.23 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 49 FAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEIS 128
Cdd:PRK06155 34 YPDRPLLVFG--GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 129 KQAKASAAKLIVTQSRYVDKIKNLQND-----GVLIVTTDSDAIPENCLRFSELTQSEEPrVDsiPEKISPEDVVALPFS 203
Cdd:PRK06155 112 HILRNSGARLLVVEAALLAALEAADPGdlplpAVWLLDAPASVSVPAGWSTAPLPPLDAP-AP--AAAVQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 204 SGTTGLPKGVMLTHkglvtsvAQQ-VDGEN--PNLYFNRDDVILCVLPMFHIYALNSIMLCSLrVGATILIMPKFEITLL 280
Cdd:PRK06155 189 SGTTGPSKGVCCPH-------AQFyWWGRNsaEDLEIGADDVLYTTLPLFHTNALNAFFQALL-AGATYVLEPRFSASGF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 281 LEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPlgKELEDAISAKFpNAKLGQGYGMTEAGPVLAMSL 360
Cdd:PRK06155 261 WPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERF-GVDLLDGYGSTETNFVIAVTH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 361 GFAKepfpvkSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQ---IMKGYLNDPLATASTIdKDGWLHTGDVGF 437
Cdd:PRK06155 338 GSQR------PGSMGRLAPGFEARVVDEH-DQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAW-RNLWFHTGDRVV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 438 IDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAG-EVPVAFVVRSKDSnISEDEIKQFVSK 516
Cdd:PRK06155 410 RDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEdEVMAAVVLRDGTA-LEPVALVRHCEP 488
|
490 500 510
....*....|....*....|....*....|...
gi 15232507 517 QVVFYKRINKVFFTDSIPKAPSGKILRKDLRAR 549
Cdd:PRK06155 489 RLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
49-556 |
1.64e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 208.74 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 49 FAAKPCLINGPtgEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEIS 128
Cdd:PRK07470 20 FPDRIALVWGD--RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 129 KQAKASAAKLIVTQSRYVDKIKNLQNDGVLIVTTDSDAIPENCLRFSELTqSEEPRVDSIPEKISPEDVVALPFSSGTTG 208
Cdd:PRK07470 98 YLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLDYEALV-ARHLGARVANAAVDHDDPCWFFFTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 209 LPKGVMLTHKGLVTSVAQQVDGENPNLyfNRDDVILCVLPMFH---IYALnsimlCSLRVGATILIMP--KFEITLLLEQ 283
Cdd:PRK07470 177 RPKAAVLTHGQMAFVITNHLADLMPGT--TEQDASLVVAPLSHgagIHQL-----CQVARGAATVLLPseRFDPAEVWAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 284 IQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKEledaiSAKFPNAKLG----QGYGMTEAG---PVL 356
Cdd:PRK07470 250 VERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRA-----DQKRALAKLGkvlvQYFGLGEVTgniTVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 357 AMSLGFAKEPFPVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVG 436
Cdd:PRK07470 325 PPALHDAEDGPDARIGTCGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 437 FIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSK 516
Cdd:PRK07470 403 HLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDG 482
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15232507 517 QVVFYKRINKVFFTDSIPKAPSGKILRKDLRARL-ANGLMN 556
Cdd:PRK07470 483 KVARYKLPKRFFFWDALPKSGYGKITKKMVREELeERGLLD 523
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
60-549 |
1.81e-60 |
|
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: 207.57 E-value: 1.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEVYTYADVHVTSRKLAAGLHNlGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLI 139
Cdd:cd05909 4 LGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 140 VTQSRYVDKIKNLQndgvlIVTTDSDA-------------IPENCLRFSELT-QSEEPRVDSIPEKISPEDVVALPFSSG 205
Cdd:cd05909 83 LTSKQFIEKLKLHH-----LFDVEYDArivyledlrakisKADKCKAFLAGKfPPKWLLRIFGVAPVQPDDPAVILFTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 206 TTGLPKGVMLTHKGLVTSVAQ---QVDgenpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPK-FEITLLL 281
Cdd:cd05909 158 SEGLPKGVVLSHKNLLANVEQitaIFD-------PNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 282 EQIQRCKVTVAMVVPPIVLAIAKSpeTEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAMSlg 361
Cdd:cd05909 231 ELIYDKKATILLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSPVISVN-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 362 faKEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATaSTIDKDGWLHTGDVGFIDDD 441
Cdd:cd05909 306 --TPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELT-SFAFGDGWYDTGDIGKIDGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 442 DELFIVDRLKELIKYKGFQVAPAELESLLIGH-PEINDVAVVAMKEEDAGEVPVAFVVrskDSNISEDEIKQFVSK-QVV 519
Cdd:cd05909 383 GFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT---TTDTDPSSLNDILKNaGIS 459
|
490 500 510
....*....|....*....|....*....|
gi 15232507 520 FYKRINKVFFTDSIPKAPSGKILRKDLRAR 549
Cdd:cd05909 460 NLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
55-551 |
6.18e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 207.67 E-value: 6.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 55 LINGPTgeVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKAS 134
Cdd:PRK06164 29 LIDEDR--PLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 135 AAKLIVTQSRY-----------VDKIKNLQNDGVLIVTTDSDAIPEN--CLRFSELTQSEEPRVDSIPEKISPEDVVALP 201
Cdd:PRK06164 107 RARWLVVWPGFkgidfaailaaVPPDALPPLRAIAVVDDAADATPAPapGARVQLFALPDPAPPAAAGERAADPDAGALL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 202 FS-SGTTGLPKGVMLTHKGLVTSVAQ--QVDGENPnlyfnrDDVILCVLPMFHIYALNSImLCSLRVGATILIMPKFEIT 278
Cdd:PRK06164 187 FTtSGTTSGPKLVLHRQATLLRHARAiaRAYGYDP------GAVLLAALPFCGVFGFSTL-LGALAGGAPLVCEPVFDAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 279 LLLEQIQRCKVTVAMVVPPIVLAIAKSpETEKYDLSSVRMVKSGA-APLGKEL-EDAISAKFPNAKLgqgYGMTEagpVL 356
Cdd:PRK06164 260 RTARALRRHRVTHTFGNDEMLRRILDT-AGERADFPSARLFGFASfAPALGELaALARARGVPLTGL---YGSSE---VQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 357 A-MSLGFAKEPFPVKSGACGTVVR-NAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGD 434
Cdd:PRK06164 333 AlVALQPATDPVSVRIEGGGRPASpEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 435 VGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMkEEDAGEVPVAFVVRSKDSNISEDEIKQFV 514
Cdd:PRK06164 413 LGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAAC 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15232507 515 SKQVVFYKRINKVFFTDSIPKAPSG---KILRKDLR----ARLA 551
Cdd:PRK06164 492 REALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRemaqARLA 535
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
66-547 |
1.92e-59 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 205.32 E-value: 1.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 66 YADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTqsrY 145
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA---H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 146 VDKIKNLQND-----GVLIVTT------------DSDAIPENCLRFSELTQSEEPRvdSIPEKISPEDVValpFSSGTTG 208
Cdd:PRK12406 91 ADLLHGLASAlpagvTVLSVPTppeiaaayrispALLTPPAGAIDWEGWLAQQEPY--DGPPVPQPQSMI---YTSGTTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 209 LPKGVMLThKGLVTSVAQQVDGENPNLYFNRDDVILCVLPMFHiYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCK 288
Cdd:PRK12406 166 HPKGVRRA-APTPEQAAAAEQMRALIYGLKPGIRALLTGPLYH-SAPNAYGLRAGRLGGVLVLQPRFDPEELLQLIERHR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 289 VTVAMVVPPIVLAIAKSPET--EKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPV-LAMSLGFAKE 365
Cdd:PRK12406 244 ITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMIEWW-GPVIYEYYGSTESGAVtFATSEDALSH 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 PfpvksGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIR--GNQIMKgYLNDPLATAStIDKDGWLHTGDVGFIDDDDE 443
Cdd:PRK12406 323 P-----GTVGKAAPGAELRFVDED-GRPLPQGEIGEIYSRiaGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 444 LFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKR 523
Cdd:PRK12406 395 LFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKV 474
|
490 500
....*....|....*....|....
gi 15232507 524 INKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK12406 475 PKHIEIMAELPREDSGKIFKRRLR 498
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
59-547 |
4.10e-59 |
|
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: 202.69 E-value: 4.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 59 PTGEVyTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKL 138
Cdd:cd05919 7 ADRSV-TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 139 IVtqsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekISPEDVVALPFSSGTTGLPKGVMLTHK 218
Cdd:cd05919 86 VV---------------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 219 GLVTSV---AQQVDGENPNlyfnrdDVILCVLPMFHIYAL-NSIMLcSLRVGATILIMPKFEI-TLLLEQIQRCKVTVAM 293
Cdd:cd05919 115 DPLLFAdamAREALGLTPG------DRVFSSAKMFFGYGLgNSLWF-PLAVGASAVLNPGWPTaERVLATLARFRPTVLY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 294 VVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLamslgFAKEPFPVKSGA 373
Cdd:cd05919 188 GVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEVGHIF-----LSNRPGAWRLGS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 374 CGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKEL 453
Cdd:cd05919 262 TGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDM 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 454 IKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISE---DEIKQFVSKQVVFYKRINKVFFT 530
Cdd:cd05919 340 LKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFV 419
|
490
....*....|....*..
gi 15232507 531 DSIPKAPSGKILRKDLR 547
Cdd:cd05919 420 DELPRTATGKLQRFKLR 436
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
38-548 |
2.64e-58 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 203.36 E-value: 2.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 38 LHDYIFENISEFAAKPCLI--NGPTGEV--YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGA 113
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTavRLGTGAPrrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 114 ITTSANPFFTPAEISKQAKASAAKLIVTQSRY------------VDKIKNLQNdgVLIVTTDSDAIPENCLrfSELTQSE 181
Cdd:PRK13295 106 VLNPLMPIFRERELSFMLKHAESKVLVVPKTFrgfdhaamarrlRPELPALRH--VVVVGGDGADSFEALL--ITPAWEQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 182 EPRVDSI--PEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFNRDDVILCVLPMFHIYALNSIM 259
Cdd:PRK13295 182 EPDAPAIlaRLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAE----RLGLGADDVILMASPMAHQTGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 260 LCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPL-GKELEDAISAKf 338
Cdd:PRK13295 258 MMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIpGALVERARAAL- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 339 pNAKLGQGYGMTEAGPVLAMSLGFAKEpfpVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPL 418
Cdd:PRK13295 337 -GAKIVSAWGMTENGAVTLTKLDDPDE---RASTTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 419 ATAStiDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVV 498
Cdd:PRK13295 412 LNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVV 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15232507 499 RSKDSNISEDEIKQFVSKQVVFYKRI-NKVFFTDSIPKAPSGKI----LRKDLRA 548
Cdd:PRK13295 490 PRPGQSLDFEEMVEFLKAQKVAKQYIpERLVVRDALPRTPSGKIqkfrLREMLRG 544
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
208-543 |
3.97e-58 |
|
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: 197.11 E-value: 3.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 208 GLPKGVMLTHKGLVTSVAQQvdgeNPNLYFNRDDVILCVLPMFHIYALNsIMLCSLRVGATILIMPKFEITLLLEQIQRC 287
Cdd:cd17637 13 GRPRGAVLSHGNLIAANLQL----IHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKFDPAEALELIEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 288 KVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVksgaapLGKELEDAISA--KFPNAKLGQGYGMTEAGPVLAMSlgfake 365
Cdd:cd17637 88 KVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV------LGLDAPETIQRfeETTGATFWSLYGQTETSGLVTLS------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 PFPVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELF 445
Cdd:cd17637 156 PYRERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 446 IVDRL--KELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKR 523
Cdd:cd17637 234 YAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKK 313
|
330 340
....*....|....*....|
gi 15232507 524 INKVFFTDSIPKAPSGKILR 543
Cdd:cd17637 314 PRYVVFVEALPKTADGSIDR 333
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
76-547 |
9.33e-58 |
|
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: 199.59 E-value: 9.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 76 LAAGLHNLGVKQHD-VVMILLPNSPEVVLTF---LAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKN 151
Cdd:cd05922 6 AASALLEAGGVRGErVVLILPNRFTYIELSFavaYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 152 lqndgVLIVTTDSDAIpencLRFSELTQSEEPRVDSIPEkisPEDVVALPFSSGTTGLPKGVMLTHKGLVT---SVAQQV 228
Cdd:cd05922 86 -----ALPASPDPGTV----LDADGIRAARASAPAHEVS---HEDLALLLYTSGSTGSPKLVRLSHQNLLAnarSIAEYL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 229 DgenpnlyFNRDDVILCVLPMFHIYALnSIMLCSLRVGATILIMPKFE-----ITLLLEQiqrcKVTVAMVVPPI--VLA 301
Cdd:cd05922 154 G-------ITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVlddafWEDLREH----GATGLAGVPSTyaMLT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 302 IAKSPETEkydLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMslgFAKEPFPVKSGACGTVVRNA 381
Cdd:cd05922 222 RLGFDPAK---LPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTY---LPPERILEKPGSIGLAIPGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 382 EMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQV 461
Cdd:cd05922 296 EFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 462 APAELESLLIGHPEINDVAVVAMkEEDAGEVPVAFVVRskDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKI 541
Cdd:cd05922 375 SPTEIEAAARSIGLIIEAAAVGL-PDPLGEKLALFVTA--PDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKV 451
|
....*.
gi 15232507 542 LRKDLR 547
Cdd:cd05922 452 DYAALR 457
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
74-550 |
2.30e-57 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 201.18 E-value: 2.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 74 RKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQ 153
Cdd:PLN02860 43 LSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 154 NDG-------VLIVTTDSDAIPE--NCLRFSELTQseepRVDSIPE---KISPEDVVALPFSSGTTGLPKGVMLTHKGLV 221
Cdd:PLN02860 123 NDRlpslmwqVFLESPSSSVFIFlnSFLTTEMLKQ----RALGTTEldyAWAPDDAVLICFTSGTTGRPKGVTISHSALI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 222 T-SVAQ-QVDGenpnlyFNRDDVILCVLPMFHIYALNSIMlCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPI- 298
Cdd:PLN02860 199 VqSLAKiAIVG------YGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMm 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 299 --VLAIAKSPETEKyDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEA----------GPVLAMSLGFAKE- 365
Cdd:PLN02860 272 adLISLTRKSMTWK-VFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhDPTLESPKQTLQTv 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 ------PFPVKSGAC-GTVVRNAEMKILDPDTgdslprNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFI 438
Cdd:PLN02860 351 nqtkssSVHQPQGVCvGKPAPHVELKIGLDES------SRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 439 DDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFV--------------VRSKDSN 504
Cdd:PLN02860 425 DKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwsdnekeNAKKNLT 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15232507 505 ISEDEIKQFVSKQVVFYKRINKVFFT--DSIPKAPSGKILRKDLRARL 550
Cdd:PLN02860 505 LSSETLRHHCREKNLSRFKIPKLFVQwrKPFPLTTTGKIRRDEVRREV 552
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
50-546 |
2.93e-57 |
|
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: 199.27 E-value: 2.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 50 AAKPCLINGPTGEV-YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEIS 128
Cdd:cd05923 14 APDACAIADPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 129 KQ-AKASAAKLIVTQSRYVDKIKNLQNDGVLIVTTD-SDAIPENclrFSELTQSEEPRvdsipekisPEDVVALPFSSGT 206
Cdd:cd05923 94 ELiERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLvGLGEPES---AGPLIEDPPRE---------PEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 207 TGLPKGVMLTHKGL---VTSVAQQVdgenpNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQ 283
Cdd:cd05923 162 TGLPKGAVIPQRAAesrVLFMSTQA-----GLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 284 IQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQgYGMTEAgpvlaMSLGFA 363
Cdd:cd05923 237 IEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTEA-----MNSLYM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 364 KEPFPvksgacGTVVR---NAEMKILDPDTGDS--LPRNKPGEICIR--GNQIMKGYLNDPLATASTIdKDGWLHTGDVG 436
Cdd:cd05923 311 RDART------GTEMRpgfFSEVRIVRIGGSPDeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 437 FIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKdSNISEDEIKQF-VS 515
Cdd:cd05923 384 YVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-GTLSADELDQFcRA 462
|
490 500 510
....*....|....*....|....*....|.
gi 15232507 516 KQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd05923 463 SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
60-548 |
3.91e-57 |
|
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: 197.65 E-value: 3.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLI 139
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 140 VTqsryvdkikNLQNDGVLIVttdsdaipenclrfseltqseeprvdsipekispedvvalpFSSGTTGLPKGVMLTHKG 219
Cdd:cd05971 83 VT---------DGSDDPALII-----------------------------------------YTSGTTGPPKGALHAHRV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 220 LVtsvaqqvdGENPNLYF------NRDDVILCVLPMFHIYALNSIMLCSLRVGATILI--MPKFEITLLLEQIQRCKVTV 291
Cdd:cd05971 113 LL--------GHLPGVQFpfnlfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYGVTT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 292 AMVvPPIVLAIAKS--PETEKYDLSsVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAMSLGFakepFPV 369
Cdd:cd05971 185 AFL-PPTALKMMRQqgEQLKHAQVK-LRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSAL----FPI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 370 KSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQ--IMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIV 447
Cdd:cd05971 258 KPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 448 DRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSK---DSNISEDEIKQFVSKQVVFYKRI 524
Cdd:cd05971 336 GRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPgetPSDALAREIQELVKTRLAAHEYP 415
|
490 500
....*....|....*....|....
gi 15232507 525 NKVFFTDSIPKAPSGKILRKDLRA 548
Cdd:cd05971 416 REIEFVNELPRTATGKIRRRELRA 439
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
61-546 |
2.90e-56 |
|
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: 195.05 E-value: 2.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd05930 10 DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd05930 90 TD---------------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTsvaqQVDGENPNLYFNRDDVILCVLPMFHIYALNSImLCSLRVGATILIMPK---FEITLLLEQIQRCKVTVAMVVPP 297
Cdd:cd05930 119 VN----LLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 298 IVLAIAKSPETEkyDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGpVLAMSLGFAKEPFPVKSGACGTV 377
Cdd:cd05930 194 LLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEAT-VDATYYRVPPDDEEDGRVPIGRP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 378 VRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKD-----GWLH-TGDVGFIDDDDELFIVDRLK 451
Cdd:cd05930 271 IPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfgpgERMYrTGDLVRWLPDGNLEFLGRID 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 452 ELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTD 531
Cdd:cd05930 350 DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLD 429
|
490
....*....|....*
gi 15232507 532 SIPKAPSGKILRKDL 546
Cdd:cd05930 430 ALPLTPNGKVDRKAL 444
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
64-549 |
4.07e-55 |
|
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: 192.33 E-value: 4.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAK-LIVTQ 142
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKvLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 143 SRYvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVT 222
Cdd:cd05969 81 ELY--------------------------------------------ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 223 S--VAQQVDGENPnlyfnrDDVILCVLPMFHIYALNSIMLCSLRVGATILIMP-KFEITLLLEQIQRCKVTVAMVVPPIV 299
Cdd:cd05969 117 YyfTGKYVLDLHP------DDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 300 LAIAKSPE--TEKYDLSSVRMVKSGAAPLGKELEdAISAKFPNAKLGQGYGMTEAGPVLamslgFAKEP-FPVKSGACGT 376
Cdd:cd05969 191 RMLMKEGDelARKYDLSSLRFIHSVGEPLNPEAI-RWGMEVFGVPIHDTWWQTETGSIM-----IANYPcMPIKPGSMGK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 377 VVRNAEMKILDPDtGDSLPRNKPGEICIRGN--QIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELI 454
Cdd:cd05969 265 PLPGVKAAVVDEN-GNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDII 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 455 KYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISE---DEIKQFVSKQVVFYKRINKVFFTD 531
Cdd:cd05969 343 KTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLGAHVAPREIEFVD 422
|
490
....*....|....*...
gi 15232507 532 SIPKAPSGKILRKDLRAR 549
Cdd:cd05969 423 NLPKTRSGKIMRRVLKAK 440
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
64-481 |
9.44e-55 |
|
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: 193.59 E-value: 9.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHD--VVMILLPNSPEVVLTFLAASFIGAITTsanPFFtpaeisKQAKASAAKLIVT 141
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPAPasFVGIYSINRPEWIISELACYAYSLVTV---PLY------DTLGPEAIEYILN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSR----YVDKiknlqndGVLIVTtdsdaipenclrFSEL-TQSEEPRVDSIPEKisPEDVVALPFSSGTTGLPKGVMLT 216
Cdd:cd05927 77 HAEisivFCDA-------GVKVYS------------LEEFeKLGKKNKVPPPPPK--PEDLATICYTSGTTGNPKGVMLT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 217 HKGLVTSVAQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCsLRVGATILIMPKfEITLLLEQIQRCKVTVAMVVP 296
Cdd:cd05927 136 HGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALF-LYHGAKIGFYSG-DIRLLLDDIKALKPTVFPGVP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 297 --------PIVLAIAKSP-----------ETEKYDLSS------------------------VRMVKSGAAPLGKELEda 333
Cdd:cd05927 214 rvlnriydKIFNKVQAKGplkrklfnfalNYKLAELRSgvvraspfwdklvfnkikqalggnVRLMLTGSAPLSPEVL-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 334 isaKFPNAKLG----QGYGMTE--AGpvlamslGFAKEPFPVKSGACGTVVRNAEMKILD-PDTG-DSLPRNKPGEICIR 405
Cdd:cd05927 292 ---EFLRVALGcpvlEGYGQTEctAG-------ATLTLPGDTSVGHVGGPLPCAEVKLVDvPEMNyDAKDPNPRGEVCIR 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232507 406 GNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKY-KGFQVAPAELESLLIGHPEINDVAV 481
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
62-554 |
3.56e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 190.76 E-value: 3.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQHDVVmILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT 141
Cdd:PRK07638 25 RVLTYKDWFESVCKVANWLNEKESKNKTIA-ILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSRYVDKIKNLQNDGVLIvttdsdaipENClrfSELTQSEEPRVDSIpekispEDVVALPF----SSGTTGLPKGVMLTH 217
Cdd:PRK07638 104 ERYKLNDLPDEEGRVIEI---------DEW---KRMIEKYLPTYAPI------ENVQNAPFymgfTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 218 KGLVTSVAQQVDgenpNLYFNRDDVILCVLPMFH---IYALNSimlcSLRVGATILIMPKFEITLLLEQIQRCKVTVAMV 294
Cdd:PRK07638 166 QSWLHSFDCNVH----DFHMKREDSVLIAGTLVHslfLYGAIS----TLYVGQTVHLMRKFIPNQVLDKLETENISVMYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 295 VPPIVLAIAKSPETEKydlSSVRMVKSGAApLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMSlgfaKEPFPVKSGAC 374
Cdd:PRK07638 238 VPTMLESLYKENRVIE---NKMKIISSGAK-WEAEAKEKIKNIFPYAKLYEFYGASELSFVTALV----DEESERRPNSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 375 GTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPlATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELI 454
Cdd:PRK07638 310 GRPFHNVQVRICNEA-GEEVQKGEIGTVYVKSPQFFMGYIIGG-VLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 455 KYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNisedEIKQFVSKQVVFYKRINKVFFTDSIP 534
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQ----QLKSFCLQRLSSFKIPKEWHFVDEIP 463
|
490 500
....*....|....*....|
gi 15232507 535 KAPSGKILRKDLRARLANGL 554
Cdd:PRK07638 464 YTNSGKIARMEAKSWIENQE 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
70-548 |
8.40e-54 |
|
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: 189.51 E-value: 8.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 70 HVTSRKLAAGLHN---LGVKQHDVVMILLPNSPEVVLTFLAASFIGAittsanpfftpaeiSKQAKASAAKLIVTQsryv 146
Cdd:cd05929 21 DVYSIALNRNARAaaaEGVWIADGVYIYLINSILTVFAAAAAWKCGA--------------CPAYKSSRAPRAEAC---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 147 DKIKNLQNDGVLIVTTDSDAIPenclRFSELtqseEPRVDSIPEKISPEDVV--ALPFSSGTTGLPKGVMLTHKGLVTSV 224
Cdd:cd05929 83 AIIEIKAAALVCGLFTGGGALD----GLEDY----EAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGLPGGPPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 225 AQQVDGENpNLYFNRDDVILCVLPMFHIYALNSIMLcSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAK 304
Cdd:cd05929 155 DTLMAAAL-GFGPGADSVYLSPAPLYHAAPFRWSMT-ALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 305 SPETE--KYDLSSVRMVKSGAAPLGKELEDAISAKFPnAKLGQGYGMTEA-GPVLAMSLGFAKEPfpvksGACGTVVRnA 381
Cdd:cd05929 233 LPEAVrnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGG-PIIWEYYGGTEGqGLTIINGEEWLTHP-----GSVGRAVL-G 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 382 EMKILDPDtGDSLPRNKPGEICIRGNQiMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQV 461
Cdd:cd05929 306 KVHILDED-GNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 462 APAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSN---ISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPS 538
Cdd:cd05929 384 YPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADagtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDT 463
|
490
....*....|
gi 15232507 539 GKILRKDLRA 548
Cdd:cd05929 464 GKLYRRLLRD 473
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
58-552 |
1.09e-53 |
|
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: 190.91 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 58 GPTGEVYTYADVHVTSRKLAAGLHNLGvKQHDVVMILLPNSPEVVLTFLAASFIGAIttsANPFFTPAEISKQAKASA-- 135
Cdd:cd05931 19 GGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI---AVPLPPPTPGRHAERLAAil 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 136 ----AKLIVTQSRYVDKIK-----NLQNDGVLIVTTDSDAipenclrfseltqsEEPRVDSIPEKISPEDVVALPFSSGT 206
Cdd:cd05931 95 adagPRVVLTTAAALAAVRafaasRPAAGTPRLLVVDLLP--------------DTSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 207 TGLPKGVMLTHKGLVTSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEIT----LLLE 282
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRA----YGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLrrplRWLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 283 QIQRCKVTVaMVVP----PIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKF------PNAkLGQGYGMTEA 352
Cdd:cd05931 237 LISRYRATI-SAAPnfayDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFapfgfrPEA-FRPSYGLAEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 353 gpVLAMSLGFAKEPFPVKSGA-----------------------CGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQI 409
Cdd:cd05931 315 --TLFVSGGPPGTGPVVLRVDrdalagravavaaddpaarelvsCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 410 MKGYLNDPLATAST------IDKDGWLHTGDVGFIdDDDELFIVDRLKELIKYKGFQVAPAELE-SLLIGHPEINDVAVV 482
Cdd:cd05931 393 ASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPGCVA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 483 AMKEEDAGEVPVAFVVRSKDSNISED------EIKQFVSKQ-------VVFYKRinkvfftDSIPKAPSGKILRKDLRAR 549
Cdd:cd05931 472 AFSVPDDGEERLVVVAEVERGADPADlaaiaaAIRAAVAREhgvapadVVLVRP-------GSIPRTSSGKIQRRACRAA 544
|
...
gi 15232507 550 LAN 552
Cdd:cd05931 545 YLD 547
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
60-553 |
4.46e-53 |
|
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: 189.03 E-value: 4.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLA---ASFIGAITTsanpfftPAEISKQAKASAA 136
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAcvlAGFVPAPLT-------VPPTYDEPNARLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 137 KL-----------IVTQSRYVDKIKNL-QNDGVLIVTTDSDAIPENCLRFSELTQSEeprvdsipekisPEDVVALPFSS 204
Cdd:cd05906 109 KLrhiwqllgspvVLTDAELVAEFAGLeTLSGLPGIRVLSIEELLDTAADHDLPQSR------------PDDLALLMLTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 205 GTTGLPKGVMLTHKGLVTSVAqqvdGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGA--------TILIMPkfe 276
Cdd:cd05906 177 GSTGFPKAVPLTHRNILARSA----GKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqvhvpteEILADP--- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 277 iTLLLEQIQRCKVTVAMVvPPIVLAI----AKSPETEKYDLSSVRMVKSG--------AAPLGKELE------DAISAkf 338
Cdd:cd05906 250 -LRWLDLIDRYRVTITWA-PNFAFALlndlLEEIEDGTWDLSSLRYLVNAgeavvaktIRRLLRLLEpyglppDAIRP-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 339 pnaklgqGYGMTEAGPVLAMSLGFAKEPFPVKS--GACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLND 416
Cdd:cd05906 326 -------AFGMTETCSGVIYSRSFPTYDHSQALefVSLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 417 PLATASTIDKDGWLHTGDVGFIdDDDELFIVDRLKELIKYKGFQVAPAELESLLighPEINDV-----AVVAMKEEDAG- 490
Cdd:cd05906 398 PEANAEAFTEDGWFRTGDLGFL-DNGNLTITGRTKDTIIVNGVNYYSHEIEAAV---EEVPGVepsftAAFAVRDPGAEt 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232507 491 -EVPVAFVVRSK-DSNISE--DEIKQFVSKQVVFykRINKV--FFTDSIPKAPSGKILRKDLRARLANG 553
Cdd:cd05906 474 eELAIFFVPEYDlQDALSEtlRAIRSVVSREVGV--SPAYLipLPKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
64-547 |
5.99e-53 |
|
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: 186.18 E-value: 5.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTsanPFFT---PAEISKQAKASAAKLIV 140
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGARLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIKnlqndgvlivttdsdaipenclrfseltqseeprvdsipekispEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd05973 78 TDAANRHKLD--------------------------------------------SDPFVMMFTSGTTGLPKGVPVPLRAL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVG-ATILIMPKFEITLLLEQIQRCKVTVAMVVPPIV 299
Cdd:cd05973 114 AAFGAYLRDA----VDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWRVIERLGVTNLAGSPTAY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 300 -LAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDaisakFPNAKLG----QGYGMTEAGPVLAMSLGFAKepfPVKSGAC 374
Cdd:cd05973 190 rLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIR-----WFDAALGvpihDHYGQTELGMVLANHHALEH---PVHAGSA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 375 GTVVRNAEMKILDpDTGDSLPRNKPGEICI--RGNQIM--KGYLNDPLATAStidkDGWLHTGDVGFIDDDDELFIVDRL 450
Cdd:cd05973 262 GRAMPGWRVAVLD-DDGDELGPGEPGRLAIdiANSPLMwfRGYQLPDTPAID----GGYYLTGDTVEFDPDGSFSFIGRA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 451 KELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNIS---EDEIKQFVSKQVVFYKRINKV 527
Cdd:cd05973 337 DDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPRTI 416
|
490 500
....*....|....*....|
gi 15232507 528 FFTDSIPKAPSGKILRKDLR 547
Cdd:cd05973 417 HFVDELPKTPSGKIQRFLLR 436
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
202-550 |
3.06e-51 |
|
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: 178.29 E-value: 3.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 202 FSSGTTGLPKGVMLTHKGLVTSVaqqvDGENPNLYFNRDDVILCVLPMFHIYALnSIMLCSLRVGATILIMPKFEitLLL 281
Cdd:cd17630 7 LTSGSTGTPKAVVHTAANLLASA----AGLHSRLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQ--ALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 282 EQIQRCKVTVAMVVPPIVLAIAKSPETEKyDLSSVRMVKSGAAPLGKELEDAISAKfpNAKLGQGYGMTEAGpvlamSLG 361
Cdd:cd17630 80 EDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTETA-----SQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 362 FAKEPFPVKSGACGTVVRNAEMKILDPdtgdslprnkpGEICIRGNQIMKGYLNDPLATAStiDKDGWLHTGDVGFIDDD 441
Cdd:cd17630 152 ATKRPDGFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQLVPEF--NEDGWFTTKDLGELHAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 442 DELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVrsKDSNISEDEIKQFVSKQVVFY 521
Cdd:cd17630 219 GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKDKLARF 296
|
330 340
....*....|....*....|....*....
gi 15232507 522 KRINKVFFTDSIPKAPSGKILRKDLRARL 550
Cdd:cd17630 297 KLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
60-546 |
9.74e-51 |
|
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: 180.52 E-value: 9.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLI 139
Cdd:cd05945 13 GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 140 VTqsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekiSPEDVVALPFSSGTTGLPKGVMLTHKG 219
Cdd:cd05945 93 IA---------------------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 220 LVTSVAQQVDGENpnlyFNRDDVILCVLP------MFHIYalnsimlCSLRVGATILIMPKFEI---TLLLEQIQRCKVT 290
Cdd:cd05945 122 LVSFTNWMLSDFP----LGPGDVFLNQAPfsfdlsVMDLY-------PALASGATLVPVPRDATadpKQLFRFLAEHGIT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 291 VAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAG----------PVLAmsl 360
Cdd:cd05945 191 VWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATvavtyievtpEVLD--- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 361 gfAKEPFPVksgacGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATAS---TIDKDGWLHTGDVGF 437
Cdd:cd05945 268 --GYDRLPI-----GYAKPGAKLVILDED-GRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 438 IDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNIS-EDEIKQFVSK 516
Cdd:cd05945 340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGlTKAIKAELAE 419
|
490 500 510
....*....|....*....|....*....|
gi 15232507 517 QVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd05945 420 RLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
65-552 |
1.01e-50 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 182.64 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YV-------DKIKNLQNdgvLIVTTDSDAIPENCLR----FSELTqsEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGV 213
Cdd:PRK06018 121 FVpilekiaDKLPSVER---YVVLTDAAHMPQTTLKnavaYEEWI--AEADGDFAWKTFDENTAAGMCYTSGTTGDPKGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 214 MLTHKGLV--TSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALnSIMLCSLRVGATiLIMP--KFEITLLLEQIQRCKV 289
Cdd:PRK06018 196 LYSHRSNVlhALMANNGDA----LGTSAADTMLPVVPLFHANSW-GIAFSAPSMGTK-LVMPgaKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 290 TVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGaaplGKELEDAISAKFPN--AKLGQGYGMTEAGPVlaMSLGFAKEPF 367
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCG----GSAMPRSMIKAFEDmgVEVRHAWGMTEMSPL--GTLAALKPPF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 368 PVKSGACGTVVR--------NAEMKILDPDtGDSLPR--NKPGEICIRGNQIMKGYLNdplATASTIDKDGWLHTGDVGF 437
Cdd:PRK06018 344 SKLPGDARLDVLqkqgyppfGVEMKITDDA-GKELPWdgKTFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVAT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 438 IDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQ 517
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGK 499
|
490 500 510
....*....|....*....|....*....|....*
gi 15232507 518 VVFYKRINKVFFTDSIPKAPSGKILRKDLRARLAN 552
Cdd:PRK06018 500 IAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
65-551 |
1.54e-50 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 182.01 E-value: 1.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YV-DKIKNLQNDGVLIVTTDSDAIPENCLRFSELTQSEEPRVD-SIPEKISPEDVVALpFSSGTTGLPKGVMLTHKGLVT 222
Cdd:PRK05852 125 GPhDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPAtSTPEGLRPDDAMIM-FTGGTTGLPKMVPWTHANIAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 223 SVAQQVDGENpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILiMP---KFEITLLLEQIQRCKVTVAMVVPPIV 299
Cdd:PRK05852 204 SVRAIITGYR----LSPRDATVAVMPLYHGHGLIAALLATLASGGAVL-LPargRFSAHTFWDDIKAVGATWYTAVPTIH 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 300 LAIAKSPETEKYDL--SSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAMS--LGFAKEPFPVKSgaCG 375
Cdd:PRK05852 279 QILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATHQVTTTqiEGIGQTENPVVS--TG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 376 TVVRN--AEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKEL 453
Cdd:PRK05852 356 LVGRStgAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKEL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 454 IKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSI 533
Cdd:PRK05852 434 INRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGL 513
|
490
....*....|....*...
gi 15232507 534 PKAPSGKILRKDLRARLA 551
Cdd:PRK05852 514 PHTAKGSLDRRAVAEQFG 531
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
31-556 |
4.46e-50 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 185.90 E-value: 4.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 31 YIPNHLPLHDYIFENISEFAAKPCLINGPTGEVyTYADVHVTSRKLAAGLHNLGVKQhDVVMILLPNSPEVVLTFLAASF 110
Cdd:PRK08633 610 RKEALPPLAEAWIDTAKRNWSRLAVADSTGGEL-SYGKALTGALALARLLKRELKDE-ENVGILLPPSVAGALANLALLL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 111 IGaiTTSANPFFTPAEIS-KQAKASAA-KLIVTQSRYVDKIKN-------LQNDGVLIVTTDSDAIPENCLRFSELTQSE 181
Cdd:PRK08633 688 AG--KVPVNLNYTASEAAlKSAIEQAQiKTVITSRKFLEKLKNkgfdlelPENVKVIYLEDLKAKISKVDKLTALLAARL 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 182 EPR---VDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQ--QVdgenpnLYFNRDDVILCVLPMFHIYALN 256
Cdd:PRK08633 766 LPArllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQisDV------FNLRNDDVILSSLPFFHSFGLT 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 257 SIMLCSLRVGATILIMPK----FEITLLleqIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELED 332
Cdd:PRK08633 840 VTLWLPLLEGIKVVYHPDptdaLGIAKL---VAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVAD 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 333 AISAKFpNAKLGQGYGMTEAGPVLAMSL------GFAKEPFPvKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRG 406
Cdd:PRK08633 917 AFEEKF-GIRILEGYGATETSPVASVNLpdvlaaDFKRQTGS-KEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGG 994
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 407 NQIMKGYLNDPLATAS---TIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLL---IGHPEInDVA 480
Cdd:PRK08633 995 PQVMKGYLGDPEKTAEvikDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELakaLGGEEV-VFA 1073
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 481 VVAMKEEDAGEvpvAFVVRSKDSNISEDEIKQFVSKQvvfykRINKVFF------TDSIPKAPSGKIlrkDLRA--RLAN 552
Cdd:PRK08633 1074 VTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKES-----GLPNLWKpsryfkVEALPLLGSGKL---DLKGlkELAL 1142
|
....
gi 15232507 553 GLMN 556
Cdd:PRK08633 1143 ALLG 1146
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
184-548 |
5.16e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 179.03 E-value: 5.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 184 RVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKglvtSVAQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSL 263
Cdd:PRK07787 117 RSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRR----AIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 264 RVGATILIMPKFEITLLLEQIQRcKVTVAMVVPPIVLAIAKSPETEKYdLSSVRMVKSGAAPLGKELEDAISAKfpnakL 343
Cdd:PRK07787 193 RIGNRFVHTGRPTPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAAL-----T 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 344 GQG----YGMTEAgpVLAMSLGFAKEPFPvksGACGTVVRNAEMKILDpDTGDSLPRNKP--GEICIRGNQIMKGYLNDP 417
Cdd:PRK07787 266 GHRpverYGMTET--LITLSTRADGERRP---GWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 418 LATASTIDKDGWLHTGDVGFIDDDDELFIVDRLK-ELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAF 496
Cdd:PRK07787 340 DATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAY 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15232507 497 VVRSKDsnISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRA 548
Cdd:PRK07787 420 VVGADD--VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
202-543 |
8.35e-50 |
|
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: 174.52 E-value: 8.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 202 FSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALNSIMLcSLRVGATILIMPKFEITLLL 281
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDL----FNISGEDAILAPGPLSHSLFLYGAIS-ALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 282 EQIQRCKVTVAMVVPPIVLAIAKSPETEkydlSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLG 361
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 362 FAKEPFPVksgacGTVVRNAEMKILDPDTGdslprnKPGEICIRGNQIMKGYLndplaTASTIDKDGWLHTGDVGFIDDD 441
Cdd:cd17633 158 ESRPPNSV-----GRPFPNVEIEIRNADGG------EIGKIFVKSEMVFSGYV-----RGGFSNPDGWMSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 442 DELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVvrsKDSNISEDEIKQFVSKQVVFY 521
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQLKRFLKQKLSRY 298
|
330 340
....*....|....*....|..
gi 15232507 522 KRINKVFFTDSIPKAPSGKILR 543
Cdd:cd17633 299 EIPKKIIFVDSLPYTSSGKIAR 320
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
65-481 |
4.88e-49 |
|
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: 174.76 E-value: 4.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNL-GVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQS 143
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 RYVDKIKNLQNDGVLIVTTDSDAIPEnclrfseltqseEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTS 223
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDD------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 VAqqvdGENPNLYFNRDDVILCVLPmFHIYALNSIMLCSLRVGATILIMP----KFEITLLLEQIQRCKVTVAMVVPPIV 299
Cdd:TIGR01733 149 LA----WLARRYGLDPDDRVLQFAS-LSFDASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 300 LAIAKSPETekyDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAgPVLAMSLGFAKEPFPVKSGAC-GTVV 378
Cdd:TIGR01733 224 ALLAAALPP---ALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTET-TVWSTATLVDPDDAPRESPVPiGRPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 379 RNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATA--------STIDKDGWLHTGDVGFIDDDDELFIVDRL 450
Cdd:TIGR01733 300 ANTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYLPDGNLEFLGRI 378
|
410 420 430
....*....|....*....|....*....|.
gi 15232507 451 KELIKYKGFQVAPAELESLLIGHPEINDVAV 481
Cdd:TIGR01733 379 DDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
64-528 |
6.71e-49 |
|
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: 176.01 E-value: 6.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAIttsanpfftpaEISKQAKASAAKL--IVT 141
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV-----------DVVRGSDSSVEELlyILN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSRYVdkiknlqndgVLIVttdsdaipENclrfseltqseeprvdsipekiSPEDVVALPFSSGTTGLPKGVMLTHKGLV 221
Cdd:cd17640 75 HSESV----------ALVV--------EN----------------------DSDDLATIIYTSGTTGNPKGVMLTHANLL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 222 TSVAQQVDGENPNLyfnrDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFeitlLLEQIQRCKVTVAMVVPPIVLA 301
Cdd:cd17640 115 HQIRSLSDIVPPQP----GDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRT----LKDDLKRVKPHYIVSVPRLWES 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 302 IAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISA---------KFPNA---KLGQGYGMTEAGPVLAmslgfAKEPFPV 369
Cdd:cd17640 187 LYSGIQKQVSKSSPIKQFLFLFFLSGGIFKFGISGggalpphvdTFFEAigiEVLNGYGLTETSPVVS-----ARRLKCN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 370 KSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDR 449
Cdd:cd17640 262 VRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 450 LKELIKYK-GFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFV------VRSKDSNISEDEIKQFVSKQVV-FY 521
Cdd:cd17640 342 AKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPNFeelekwAKESGVKLANDRSQLLASKKVLkLY 421
|
....*..
gi 15232507 522 KRINKVF 528
Cdd:cd17640 422 KNEIKDE 428
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
34-555 |
1.81e-48 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 177.13 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 34 NHLPLHDYIF-ENISE-FAAKPCLINGPTGevYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFI 111
Cdd:PLN03102 10 NNVPLTPITFlKRASEcYPNRTSIIYGKTR--FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 112 GAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQNdgvLIVTTDSDAIPE----NCLRFSELTQSEEPRVDS 187
Cdd:PLN03102 88 GAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLH---LLSSEDSNLNLPvifiHEIDFPKRPSSEELDYEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 188 IPEKISP--------------EDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYfnrdDVILCVLPMFHIY 253
Cdd:PLN03102 165 LIQRGEPtpslvarmfriqdeHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTC----PVYLWTLPMFHCN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 254 ALNSIMLCSLRvGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAP----LGKE 329
Cdd:PLN03102 241 GWTFTWGTAAR-GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPppaaLVKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 330 LEdaisakfpnaKLG----QGYGMTEA-GPVLAMSLGFAKEPFP------VKSGACGTVVRNAEMKILDPDTGDSLPRNK 398
Cdd:PLN03102 320 VQ----------RLGfqvmHAYGLTEAtGPVLFCEWQDEWNRLPenqqmeLKARQGVSILGLADVDVKNKETQESVPRDG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 399 P--GEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEI 476
Cdd:PLN03102 390 KtmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 477 NDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQ--VVFYKRIN--------KVFFTDSIPKAPSGKILRKDL 546
Cdd:PLN03102 469 LETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRErdLIEYCRENlphfmcprKVVFLQELPKNGNGKILKPKL 548
|
....*....
gi 15232507 547 RaRLANGLM 555
Cdd:PLN03102 549 R-DIAKGLV 556
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
59-553 |
3.31e-48 |
|
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: 177.12 E-value: 3.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 59 PTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKL 138
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 139 IVTQS---------RY---VDKIKNL---QNDGVLI-----VTTDSDAiPENCLRFSELTQSEEPrVDSIPekISPEDVV 198
Cdd:cd05967 158 IVTAScgiepgkvvPYkplLDKALELsghKPHHVLVlnrpqVPADLTK-PGRDLDWSELLAKAEP-VDCVP--VAATDPL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 199 ALPFSSGTTGLPKGVMLTHKG----LVTSVAQQVDGENPNLYFNRDDVILCVLPMFHIYAlnsimlcSLRVGATilimpk 274
Cdd:cd05967 234 YILYTSGTTGKPKGVVRDNGGhavaLNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYG-------PLLHGAT------ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 275 feiTLLLEQ--------------IQRCKVTVAMVVPPIVLAIAKSPET----EKYDLSSVRMVKSGAAPLGKELEDAISA 336
Cdd:cd05967 301 ---TVLYEGkpvgtpdpgafwrvIEKYQVNALFTAPTAIRAIRKEDPDgkyiKKYDLSSLRTLFLAGERLDPPTLEWAEN 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 337 KFPNAKLGQgYGMTEAG-PVLAMSLGFakEPFPVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRG----NQIMK 411
Cdd:cd05967 378 TLGVPVIDH-WWQTETGwPITANPVGL--EPLPIKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLplppGCLLT 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 412 GYLNDPLATASTIDKD-GWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAG 490
Cdd:cd05967 454 LWKNDERFKKLYLSKFpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKG 533
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232507 491 EVPVAFVVRSKDSNISED----EIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRArLANG 553
Cdd:cd05967 534 QVPLGLVVLKEGVKITAEelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK-IADG 599
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
64-549 |
4.95e-48 |
|
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: 174.99 E-value: 4.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT-- 141
Cdd:cd05970 48 FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAia 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 ----QSRYVDKIKNLQNDGVLIVTTDSDaiPENCLRFSELTQSEEPRVDSIPEKISP--EDVVALPFSSGTTGLPKgvML 215
Cdd:cd05970 128 edniPEEIEKAAPECPSKPKLVWVGDPV--PEGWIDFRKLIKNASPDFERPTANSYPcgEDILLVYFSSGTTGMPK--MV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 216 THKG------LVTSVAQQvdgenpNLyfNRDDVILCVLPMFHIYALNSIMLCSLRVGATILI--MPKFEITLLLEQIQRC 287
Cdd:cd05970 204 EHDFtyplghIVTAKYWQ------NV--REGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVydYDKFDPKALLEKLSKY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 288 KVTvAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISaKFPNAKLGQGYGMTEAgpVLAMSLGFAKEPf 367
Cdd:cd05970 276 GVT-TFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK-EKTGIKLMEGFGQTET--TLTIATFPWMEP- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 368 pvKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQ-----IMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDD 442
Cdd:cd05970 351 --KPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 443 ELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED---EIKQFVSKQVV 519
Cdd:cd05970 427 YLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQDHVKKVTA 506
|
490 500 510
....*....|....*....|....*....|
gi 15232507 520 FYKRINKVFFTDSIPKAPSGKILRKDLRAR 549
Cdd:cd05970 507 PYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-548 |
2.86e-47 |
|
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: 168.81 E-value: 2.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 194 PEDVVALPFSSGTTGLPKGVMLTHKGLVtsvaqqVDGE--NPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILI 271
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV------YNAWmlALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 272 MP------KFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEkyDLSSVRMVKSGAAPLGKELEDAISAKfPNAKLGQ 345
Cdd:cd05944 75 AGpagyrnPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAAPLPVELRARFEDA-TGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 346 GYGMTEAGPVLAMSLgfakEPFPVKSGACGTVVRNAEMKI--LDPDTGDSLP--RNKPGEICIRGNQIMKGYLNDPLATA 421
Cdd:cd05944 152 GYGLTEATCLVAVNP----PDGPKRPGSVGLRLPYARVRIkvLDGVGRLLRDcaPDEVGEICVAGPGVFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 422 STIDkDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSK 501
Cdd:cd05944 228 AFVA-DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15232507 502 DSNISEDEIKQFVSKQVVFYKRINK-VFFTDSIPKAPSGKILRKDLRA 548
Cdd:cd05944 307 GAVVEEEELLAWARDHVPERAAVPKhIEVLEELPVTAVGKVFKPALRA 354
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
60-546 |
4.17e-46 |
|
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: 168.61 E-value: 4.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLI 139
Cdd:cd17646 20 EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 140 VTQSRYVDKIKNLQNDGVLIVTTDSDAipenclrfseltQSEEPRVDSipekiSPEDVVALPFSSGTTGLPKGVMLTHKG 219
Cdd:cd17646 100 LTTADLAARLPAGGDVALLGDEALAAP------------PATPPLVPP-----RPDNLAYVIYTSGSTGRPKGVMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 220 LVTSVAQQVDgENPnlyFNRDDVILCVLPM-FHIyALNSIMLcSLRVGATILIMP---KFEITLLLEQIQRCKVTVAMVV 295
Cdd:cd17646 163 IVNRLLWMQD-EYP---LGPGDRVLQKTPLsFDV-SVWELFW-PLVAGARLVVARpggHRDPAYLAALIREHGVTTCHFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 296 PPIVLAIAKSPETEkyDLSSVRMVKSGAAPLGKELEDAIsAKFPNAKLGQGYGMTEAgpVLAMSLGFAKEPFPVKSGACG 375
Cdd:cd17646 237 PSMLRVFLAEPAAG--SCASLRRVFCSGEALPPELAARF-LALPGAELHNLYGPTEA--AIDVTHWPVRGPAETPSVPIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 376 TVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLH------TGDVGFIDDDDELFIVDR 449
Cdd:cd17646 312 RPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 450 LKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKD-SNISEDEIKQFVSKQVVFYKrINKVF 528
Cdd:cd17646 391 SDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGaAGPDTAALRAHLAERLPEYM-VPAAF 469
|
490
....*....|....*....
gi 15232507 529 FT-DSIPKAPSGKILRKDL 546
Cdd:cd17646 470 VVlDALPLTANGKLDRAAL 488
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
53-540 |
1.48e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 168.14 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 53 PCLINGPtgEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAK 132
Cdd:PRK07798 20 VALVCGD--RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 133 ASAAKLIVTQSRYVDKIKNLQNDG----VLIVTTDSDAIPENC--LRFSELTQSEEPRVDSIPEkiSPEDVVALpFSSGT 206
Cdd:PRK07798 98 DSDAVALVYEREFAPRVAEVLPRLpklrTLVVVEDGSGNDLLPgaVDYEDALAAGSPERDFGER--SPDDLYLL-YTGGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 207 TGLPKGVMLTHKGL---------------VTSVAQQVDG--ENPNLyfnrddVILCVLPMFHIYALNSIMLcSLRVGATI 269
Cdd:PRK07798 175 TGMPKGVMWRQEDIfrvllggrdfatgepIEDEEELAKRaaAGPGM------RRFPAPPLMHGAGQWAAFA-ALFSGQTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 270 LIMP--KFEITLLLEQIQRCKVTVAMVV-----PPIVLAIAkspETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAK 342
Cdd:PRK07798 248 VLLPdvRFDADEVWRTIEREKVNVITIVgdamaRPLLDALE---ARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 343 LGQGYGMTEAGpvlAMSLGFAKePFPVKSGAcGTVVRNAEMKILDPDTGDSLP-RNKPGEICIRGNqIMKGYLNDPLATA 421
Cdd:PRK07798 325 LTDSIGSSETG---FGGSGTVA-KGAVHTGG-PRFTIGPRTVVLDEDGNPVEPgSGEIGWIARRGH-IPLGYYKDPEKTA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 422 ST---IDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVV 498
Cdd:PRK07798 399 ETfptIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15232507 499 RSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGK 540
Cdd:PRK07798 479 LREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
62-549 |
6.44e-45 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 166.99 E-value: 6.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT 141
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 -----QSRYVDKIKNLQNdgVLIVTTDSDAIPeNCLRFSELTQSEEPRVDsiPEKISPEDVVALPFSSGTTGLPKGVMLT 216
Cdd:PRK04319 152 tpallERKPADDLPSLKH--VLLVGEDVEEGP-GTLDFNALMEQASDEFD--IEWTDREDGAILHYTSGSTGKPKGVLHV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 217 HKGLVT--SVAQQVdgenpnLYFNRDDVILC--------------VLPMFHiyalnsimlcslrvGATILIM-PKFEITL 279
Cdd:PRK04319 227 HNAMLQhyQTGKYV------LDLHEDDVYWCtadpgwvtgtsygiFAPWLN--------------GATNVIDgGRFSPER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 280 LLEQIQRCKVTVAMVVPPivlAI-----AKSPETEKYDLSSVRMVKSGAAPLGKEledAIsaKFPNAKLGQ----GYGMT 350
Cdd:PRK04319 287 WYRILEDYKVTVWYTAPT---AIrmlmgAGDDLVKKYDLSSLRHILSVGEPLNPE---VV--RWGMKVFGLpihdNWWMT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 351 EAGPVLamslgFAKEP-FPVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGN--QIMKGYLNDPLATASTIdKD 427
Cdd:PRK04319 359 ETGGIM-----IANYPaMDIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYF-AG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 428 GWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISE 507
Cdd:PRK04319 432 DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15232507 508 D---EIKQFVSKQV---VFYKRINkvfFTDSIPKAPSGKILRKDLRAR 549
Cdd:PRK04319 512 ElkeEIRGFVKKGLgahAAPREIE---FKDKLPKTRSGKIMRRVLKAW 556
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
65-549 |
2.97e-44 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 164.55 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YVDKIKNLQNDgvLIVTTDSDAIPENCLRFSELTQSEEPRVDSIPEKISPEDVVALpfSSGTTGLPKGVmlTHKGLVT-S 223
Cdd:PRK13382 150 FSATVDRALAD--CPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILL--TSGTTGTPKGA--RRSGPGGiG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 VAQQVDGENPnlyFNRDDVILCVLPMFHIYALNSIMLCSLrVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIA 303
Cdd:PRK13382 224 TLKAILDRTP---WRAEEPTVIVAPMFHAWGFSQLVLAAS-LACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIM 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 304 KSPET--EKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAkLGQGYGMTEAGPV-LAMSLGFAKEPFPVKSGACGTvvrn 380
Cdd:PRK13382 300 DLPAEvrNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMIaTATPADLRAAPDTAGRPAEGT---- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 381 aEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYlndplATASTID-KDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGF 459
Cdd:PRK13382 375 -EIRILDQD-FREVPTGEVGTIFVRNDTQFDGY-----TSGSTKDfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 460 QVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSG 539
Cdd:PRK13382 448 NVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATG 527
|
490
....*....|
gi 15232507 540 KILRKDLRAR 549
Cdd:PRK13382 528 KILRRELQAR 537
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
52-547 |
6.74e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 162.87 E-value: 6.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLINGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQA 131
Cdd:PRK13390 13 RPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 132 KASAAKLIVTQSRYVDKIKNLQNDGVLIVTTDSDAipENCLRFSELTQSEEPRVDSipekiSPEDVVALpFSSGTTGLPK 211
Cdd:PRK13390 93 GDSGARVLVASAALDGLAAKVGADLPLRLSFGGEI--DGFGSFEAALAGAGPRLTE-----QPCGAVML-YSSGTTGFPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 212 GVM--LTHKGL------VTSVAQQVDGenpnlyFNRDDVILCVLPMFHIYALNsimLCSL--RVGATILIMPKFEITLLL 281
Cdd:PRK13390 165 GIQpdLPGRDVdapgdpIVAIARAFYD------ISESDIYYSSAPIYHAAPLR---WCSMvhALGGTVVLAKRFDAQATL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 282 EQIQRCKVTVAMVVPPIVLAIAK--SPETEKYDLSSVRMVKSGAAPLGKELEDAIsAKFPNAKLGQGYGMTEA-GPVLAM 358
Cdd:PRK13390 236 GHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAM-IDWLGPIVYEYYSSTEAhGMTFID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 359 SLGFAKEPFPVKSGACGTvvrnaeMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDG--WLHTGDVG 436
Cdd:PRK13390 315 SPDWLAHPGSVGRSVLGD------LHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 437 FIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED---EIKQF 513
Cdd:PRK13390 388 SVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDElarELIDY 467
|
490 500 510
....*....|....*....|....*....|....
gi 15232507 514 VSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK13390 468 TRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
65-498 |
9.92e-44 |
|
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: 162.77 E-value: 9.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAAsfigaittsanpfftpaeiskqakASAAKLIVTQsr 144
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGC------------------------WSQNIPIVTV-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YvdkiKNLQNDGVL--IVTTDSDAIpenclrfseLTQSeeprvdsipekiSPEDVVALPFSSGTTGLPKGVMLTHKGLVT 222
Cdd:cd17639 61 Y----ATLGEDALIhsLNETECSAI---------FTDG------------KPDDLACIMYTSGSTGNPKGVMLTHGNLVA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 223 SVAQQvdGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRvGATI-LIMPKfeiTLLLEQIQRC-------KVTVAMV 294
Cdd:cd17639 116 GIAGL--GDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYR-GGTIgYGSPR---TLTDKSKRGCkgdltefKPTLMVG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 295 VPPI-------VLA-----------------------IAKSPETEKYDL-----------SSVRMVKSGAAPLGKELEDA 333
Cdd:cd17639 190 VPAIwdtirkgVLAklnpmgglkrtlfwtayqsklkaLKEGPGTPLLDElvfkkvraalgGRLRYMLSGGAPLSADTQEF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 334 ISAKFpnAKLGQGYGMTE---AGPVLamslgfakEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKP--GEICIRGNQ 408
Cdd:cd17639 270 LNIVL--CPVIQGYGLTEtcaGGTVQ--------DPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPprGEILIRGPN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 409 IMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYK-GFQVAPAELESLLIGHPEINDVAVVAMKEE 487
Cdd:cd17639 340 VFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDK 419
|
490
....*....|.
gi 15232507 488 DAgevPVAFVV 498
Cdd:cd17639 420 SY---PVAIVV 427
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
58-542 |
1.88e-43 |
|
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: 163.13 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 58 GPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAK 137
Cdd:cd17634 79 TSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 138 LIVTQSRY------------VDKIKNLQNDGV--LIVT----TDSDAIPENCLRFSELTQSEEPRVDsiPEKISPEDVVA 199
Cdd:cd17634 159 LLITADGGvragrsvplkknVDDALNPNVTSVehVIVLkrtgSDIDWQEGRDLWWRDLIAKASPEHQ--PEAMNAEDPLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 200 LPFSSGTTGLPKGVMLTHKG----LVTSVAQQVDGENPNLYFNRDDVILCvlpMFHIYALNSIMLCslrvGATILImpkF 275
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGylvyAATTMKYVFDYGPGDIYWCTADVGWV---TGHSYLLYGPLAC----GATTLL---Y 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 276 E-------ITLLLEQIQRCKVTVAMVVPPIVLAIAKSPE--TEKYDLSSVRMVKSGAAPLGKEledaiSAKFPNAKLGQG 346
Cdd:cd17634 307 EgvpnwptPARMWQVVDKHGVNILYTAPTAIRALMAAGDdaIEGTDRSSLRILGSVGEPINPE-----AYEWYWKKIGKE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 347 -------YGMTEAGPVLAMSLGFAKepfPVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRG---NQIMKGYLND 416
Cdd:cd17634 382 kcpvvdtWWQTETGGFMITPLPGAI---ELKAGSATRPVFGVQPAVVD-NEGHPQPGGTEGNLVITDpwpGQTRTLFGDH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 417 PLATASTIDK-DGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVA 495
Cdd:cd17634 458 ERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15232507 496 FVVRS---KDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKIL 542
Cdd:cd17634 538 YVVLNhgvEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
207-539 |
3.03e-43 |
|
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: 157.08 E-value: 3.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 207 TGLPKGVMLTHKGLVTSVAQQVDGENpnlyFNRDDVILCVLPMFHIYALNSiMLCSLRVGATILIMPKFEITLLLEQIQR 286
Cdd:cd17636 12 SGRPNGALLSHQALLAQALVLAVLQA----IDEGTVFLNSGPLFHIGTLMF-TLATFHAGGTNVFVRRVDAEEVLELIEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 287 CKVTVAMVVPPIVLAIAKSPETEKYDLSSVRmvksgAAPLGKELEDAISAKFP--NAKLGqGYGMTEAGPVLAMS----- 359
Cdd:cd17636 87 ERCTHAFLLPPTIDQIVELNADGLYDLSSLR-----SSPAAPEWNDMATVDTSpwGRKPG-GYGQTEVMGLATFAalggg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 360 -LGFAKEPFPVksgacgtvvrnAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFI 438
Cdd:cd17636 161 aIGGAGRPSPL-----------VQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 439 DDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQV 518
Cdd:cd17636 228 EPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARI 307
|
330 340
....*....|....*....|.
gi 15232507 519 VFYKRINKVFFTDSIPKAPSG 539
Cdd:cd17636 308 ASYKKPKSVEFADALPRTAGG 328
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
56-549 |
3.79e-43 |
|
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: 161.48 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 56 INGPTGEV-YTYADVHVTSRKLAAGLHNL-GVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKA 133
Cdd:cd05928 33 VNGKGDEVkWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 134 SAAKLIVTQ---SRYVDKI----KNLQNDgvLIVttdSDAIPENCLRFSELTQSEEPrvDSIPEKISPEDVVALPFSSGT 206
Cdd:cd05928 113 SKAKCIVTSdelAPEVDSVasecPSLKTK--LLV---SEKSRDGWLNFKELLNEAST--EHHCVETGSQEPMAIYFTSGT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 207 TGLPKgvMLTHKGLVTSVAQQVDGENPnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILI--MPKFEITLLLEQI 284
Cdd:cd05928 186 TGSPK--MAEHSHSSLGLGLKVNGRYW-LDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVhhLPRFDPLVILKTL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 285 QRCKVTVaMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKfPNAKLGQGYGMTEAGPVLAMSLGFAk 364
Cdd:cd05928 263 SSYPITT-FCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ-TGLDIYEGYGQTETGLICANFKGMK- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 365 epfpVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQ-----IMKGYLNDPLATASTIDKDGWLhTGDVGFID 439
Cdd:cd05928 340 ----IKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRVKPirpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 440 DDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVV-----RSKDSNISEDEIKQFV 514
Cdd:cd05928 414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqfLSHDPEQLTKELQQHV 493
|
490 500 510
....*....|....*....|....*....|....*
gi 15232507 515 SKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRAR 549
Cdd:cd05928 494 KSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
195-543 |
4.10e-43 |
|
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: 157.04 E-value: 4.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 195 EDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQ-QVDGENpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMP 273
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDIlQKEGLN----WVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 274 KFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAA-PLGKELEDAISakFPNAKLGQGYGMTEA 352
Cdd:cd17635 77 NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSrAIAADVRFIEA--TGLTNTAQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 353 GPVLAMSLGFAKepfpVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHT 432
Cdd:cd17635 155 GTALCLPTDDDS----IEINAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 433 GDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRS--KDSNISEDeI 510
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASaeLDENAIRA-L 307
|
330 340 350
....*....|....*....|....*....|...
gi 15232507 511 KQFVSKQVVFYKRINKVFFTDSIPKAPSGKILR 543
Cdd:cd17635 308 KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
61-547 |
1.02e-42 |
|
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: 159.43 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKiknlqndgvlivtTDSDAIPENCLRFSELTQseEPRVDSIPEKiSPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd17651 98 THPALAGE-------------LAVELVAVTLLDQPGAAA--GADAEPDPAL-DADDLAYVIYTSGSTGRPKGVVMPHRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVAQQvdgenpNLYFN---RDDVILCVLPMFHiYALNSImLCSLRVGATILIMP---KFEITLLLEQIQRCKVTVAMV 294
Cdd:cd17651 162 ANLVAWQ------ARASSlgpGARTLQFAGLGFD-VSVQEI-FSTLCAGATLVLPPeevRTDPPALAAWLDEQRISRVFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 295 VPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLG-KELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLGFAKEPFPvKSGA 373
Cdd:cd17651 234 PTVALRALAEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWP-APPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 374 CGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWL------HTGDVGFIDDDDELFIV 447
Cdd:cd17651 313 IGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 448 DRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAmkEEDAGEVP--VAFVVRSKDSNISEDEIKQFVSKQVVFYKRIN 525
Cdd:cd17651 392 GRADDQVKIRGFRIELGEIEAALARHPGVREAVVLA--REDRPGEKrlVAYVVGDPEAPVDAAELRAALATHLPEYMVPS 469
|
490 500
....*....|....*....|..
gi 15232507 526 KVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd17651 470 AFVLLDALPLTPNGKLDRRALP 491
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
64-556 |
2.74e-42 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 159.00 E-value: 2.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTsaNPFFT--PAEISKQAKASAAKLIVT 141
Cdd:PRK10946 49 FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPV--NALFShqRSELNAYASQIEPALLIA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSR--------YVDKIKNlQNDGVLIVTTDSDAiPENCLrfSELTQSEEPRVDSIPekiSPEDVVA-LPFSSGTTGLPKG 212
Cdd:PRK10946 127 DRQhalfsdddFLNTLVA-EHSSLRVVLLLNDD-GEHSL--DDAINHPAEDFTATP---SPADEVAfFQLSGGSTGTPKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 213 VMLTHKGLVTSVAqqvdGENPNLYFNRDDVILCVLPMFHIYALNSI-MLCSLRVGATILIMPKFEITLLLEQIQRCKVTV 291
Cdd:PRK10946 200 IPRTHNDYYYSVR----RSVEICGFTPQTRYLCALPAAHNYPMSSPgALGVFLAGGTVVLAPDPSATLCFPLIEKHQVNV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 292 AMVVPPIVL----AIAKSpeTEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEaGPVLAMSLG------ 361
Cdd:PRK10946 276 TALVPPAVSlwlqAIAEG--GSRAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQQVFGMAE-GLVNYTRLDdsderi 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 362 FAKEPFPVKSgacgtvvrNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDD 441
Cdd:PRK10946 352 FTTQGRPMSP--------DDEVWVADAD-GNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 442 DELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVrSKDSnISEDEIKQFVSKQ-VVF 520
Cdd:PRK10946 423 GYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLV-VKEP-LKAVQLRRFLREQgIAE 500
|
490 500 510
....*....|....*....|....*....|....*.
gi 15232507 521 YKRINKVFFTDSIPKAPSGKILRKDLRARLANGLMN 556
Cdd:PRK10946 501 FKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA 536
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
33-551 |
4.67e-42 |
|
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: 162.33 E-value: 4.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 33 PNHLPLHDYIFENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIG 112
Cdd:COG1020 473 PADATLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 113 A----ITTSAnpfftPAE-ISKQAKASAAKLIVTQSRYVDKiknLQNDGVLIVTTDSDAIPEnclrfseltQSEEPRvds 187
Cdd:COG1020 551 AayvpLDPAY-----PAErLAYMLEDAGARLVLTQSALAAR---LPELGVPVLALDALALAA---------EPATNP--- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 188 iPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFNRDDVILcvlpMFHiyALN---SI--MLCS 262
Cdd:COG1020 611 -PVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQR----RYGLGPGDRVL----QFA--SLSfdaSVweIFGA 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 263 LRVGATILIMPK---FEITLLLEQIQRCKVTVAMVVPPIVLAIAkspETEKYDLSSVRMVKSGAAPLGKELEDAISAKFP 339
Cdd:COG1020 680 LLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRWRARLP 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 340 NAKLGQGYGMTEAGpvlAMSLGFAKEPFPVKSGAC--GTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDP 417
Cdd:COG1020 757 GARLVNLYGPTETT---VDSTYYEVTPPDADGGSVpiGRPIANTRVYVLDAH-LQPVPVGVPGELYIGGAGLARGYLNRP 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 418 LATAS-----TIDKDG--WLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAG 490
Cdd:COG1020 833 ELTAErfvadPFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGD 912
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232507 491 EVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLA 551
Cdd:COG1020 913 KRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAA 973
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
61-548 |
5.12e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 158.31 E-value: 5.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQ---HdvVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAK 137
Cdd:PRK07867 26 DSFTSWREHIRGSAARAAALRARLDPTrppH--VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 138 LIVTQSRYVDKIKNLQNdGVLIVTTDSDAipenclRFSELTQSEEPRVDsiPEKISPEDVVALPFSSGTTGLPKGVMLTH 217
Cdd:PRK07867 104 LVLTESAHAELLDGLDP-GVRVINVDSPA------WADELAAHRDAEPP--FRVADPDDLFMLIFTSGTSGDPKAVRCTH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 218 KGLVT---SVAQQvdgenpnlyFN--RDDVILCVLPMFHIyalNSIMLC---SLRVGATILIMPKFEITLLLEQIQRCKV 289
Cdd:PRK07867 175 RKVASagvMLAQR---------FGlgPDDVCYVSMPLFHS---NAVMAGwavALAAGASIALRRKFSASGFLPDVRRYGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 290 TVAMVVPPIVLAIAKSPETEKYDLSSVRMVksgaapLGKELEDAISAKFP---NAKLGQGYGMTEAGpvlamsLGFAKEP 366
Cdd:PRK07867 243 TYANYVGKPLSYVLATPERPDDADNPLRIV------YGNEGAPGDIARFArrfGCVVVDGFGSTEGG------VAITRTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 367 FPvKSGACGTVVrnAEMKILDPDTGDSLPrnkPGEIC----------------IRGNQIMKGYLNDPLATASTIdKDGWL 430
Cdd:PRK07867 311 DT-PPGALGPLP--PGVAIVDPDTGTECP---PAEDAdgrllnadeaigelvnTAGPGGFEGYYNDPEADAERM-RGGVY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 431 HTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEI 510
Cdd:PRK07867 384 WSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAF 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15232507 511 KQFVS-------KQVVFYKRINkvfftDSIPKAPSGKILRKDLRA 548
Cdd:PRK07867 464 AEFLAaqpdlgpKQWPSYVRVC-----AELPRTATFKVLKRQLSA 503
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
65-547 |
3.35e-41 |
|
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: 155.67 E-value: 3.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSR-------KLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAK 137
Cdd:cd05915 19 TGEVHRTTYAevyqrarRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 138 LIVTQSRYVDKIKnlQNDGVLIVTTDSDAIPENCLRFSELTQSEEPRVDSIpEKISPEDVVALPFSSGTTGLPKGVMLTH 217
Cdd:cd05915 99 VLLFDPNLLPLVE--AIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADP-VRVPERAACGMAYTTGTTGLPKGVVYSH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 218 KG-LVTSVAQQVDGEnpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVP 296
Cdd:cd05915 176 RAlVLHSLAASLVDG---TALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 297 PIVLAIAKSPETEKYDLS-SVRMVKSGAAPLGKELEdaiSAKFPNAKLGQGYGMTEAGPVLAMSLGFAK-EPFP----VK 370
Cdd:cd05915 253 TVWLALADYLESTGHRLKtLRRLVVGGSAAPRSLIA---RFERMGVEVRQGYGLTETSPVVVQNFVKSHlESLSeeekLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 371 SGACGTVVRNAE-MKILDPDTGdSLPRNKPG--EICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIV 447
Cdd:cd05915 330 LKAKTGLPIPLVrLRVADEEGR-PVPKDGKAlgEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 448 DRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFvVRSKDSNISEDEIKQFVSKQVVFYKRINK- 526
Cdd:cd05915 409 DRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-VVPRGEKPTPEELNEHLLKAGFAKWQLPDa 487
|
490 500
....*....|....*....|.
gi 15232507 527 VFFTDSIPKAPSGKILRKDLR 547
Cdd:cd05915 488 YVFAEEIPRTSAGKFLKRALR 508
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
64-549 |
4.78e-41 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 153.49 E-value: 4.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQakasaaklivtqs 143
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 ryvdkiknLQNDGVLIVTTDsdaipenclrfsELTQSEEPrvdsipekispedvVALPFSSGTTGLPKGVMLTHKGLVTs 223
Cdd:cd05974 68 --------VDRGGAVYAAVD------------ENTHADDP--------------MLLYFTSGTTSKPKLVEHTHRSYPV- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 vaqqvdGENPNLYF---NRDDVILCVL-PMFHIYALnSIMLCSLRVGATILIM--PKFEITLLLEQIQRCKVTvAMVVPP 297
Cdd:cd05974 113 ------GHLSTMYWiglKPGDVHWNISsPGWAKHAW-SCFFAPWNAGATVFLFnyARFDAKRVLAALVRYGVT-TLCAPP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 298 IVLAIAKSPETEKYDLSsVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAMSLGFakepfPVKSGACGTV 377
Cdd:cd05974 185 TVWRMLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTALVGNSPGQ-----PVKAGSMGRP 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 378 VRNAEMKILDPDTGDSlprnKPGEICI-----RGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKE 452
Cdd:cd05974 258 LPGYRVALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 453 LIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED---EIKQFVSKQVVFYKRINKVFF 529
Cdd:cd05974 333 VFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEF 412
|
490 500
....*....|....*....|
gi 15232507 530 TDsIPKAPSGKILRKDLRAR 549
Cdd:cd05974 413 AE-LPKTISGKIRRVELRRR 431
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
55-549 |
7.37e-41 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 155.77 E-value: 7.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 55 LINGPTGevYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKAS 134
Cdd:PLN02479 39 VVHGSVR--YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 135 AAKLIVTQSRYV-----------DKIKNLQNDGVLIVTTD--------SDAIPENCLRFSELTQSEEPRVDSIPekisPE 195
Cdd:PLN02479 117 KSEVVMVDQEFFtlaeealkilaEKKKSSFKPPLLIVIGDptcdpkslQYALGKGAIEYEKFLETGDPEFAWKP----PA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 196 D---VVALPFSSGTTGLPKGVMLTHKGlvtsvAQQVDGENPNLY-FNRDDVILCVLPMFHI----YALNSIMLCslrvgA 267
Cdd:PLN02479 193 DewqSIALGYTSGTTASPKGVVLHHRG-----AYLMALSNALIWgMNEGAVYLWTLPMFHCngwcFTWTLAALC-----G 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 268 TILIMPKFEITLLLEQIQRCKVTvAMVVPPIVL-AIAKSPETEKY-DLS-SVRMVKSGAAPLGKELEdAISAKfpNAKLG 344
Cdd:PLN02479 263 TNICLRQVTAKAIYSAIANYGVT-HFCAAPVVLnTIVNAPKSETIlPLPrVVHVMTAGAAPPPSVLF-AMSEK--GFRVT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 345 QGYGMTEA-GPVLAMSLGFAKEPFPVKSGA---CGTVVRNAEMK---ILDPDTGDSLPRNKP--GEICIRGNQIMKGYLN 415
Cdd:PLN02479 339 HTYGLSETyGPSTVCAWKPEWDSLPPEEQArlnARQGVRYIGLEgldVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 416 DPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVA 495
Cdd:PLN02479 419 NPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCA 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232507 496 FV-----VRSKDSNISEDEIKQFVSKQVVFYKRINKVFFtDSIPKAPSGKILRKDLRAR 549
Cdd:PLN02479 498 FVtlkpgVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
62-470 |
1.44e-40 |
|
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: 155.21 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT 141
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QS-RYVDKIKNLQN-----DGVLIVTTDSDAIPENCLRFSELTQ----SEEPRVDSIPEKISPEDVVALPFSSGTTGLPK 211
Cdd:cd05933 87 ENqKQLQKILQIQDklphlKAIIQYKEPLKEKEPNLYSWDEFMElgrsIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 212 GVMLTHKGLV---TSVAQQVDGENPNlyfNRDDVILCVLPMFHIYALNSIMLCSLRVGATI-----------LIMPKFEI 277
Cdd:cd05933 167 GVMLSHDNITwtaKAASQHMDLRPAT---VGQESVVSYLPLSHIAAQILDIWLPIKVGGQVyfaqpdalkgtLVKTLREV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 278 --TLLL------EQIQRCKVTV--------------AMVV--------------PPIVLAIAK----SPETEKYDLSSVR 317
Cdd:cd05933 244 rpTAFMgvprvwEKIQEKMKAVgaksgtlkrkiaswAKGVgletnlklmggespSPLFYRLAKklvfKKVRKALGLDRCQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 318 MVKSGAAPLGKE-LEDAISAkfpNAKLGQGYGMTE-AGPVlAMSLgfakePFPVKSGACGTVVRNAEMKILDPDTgdslp 395
Cdd:cd05933 324 KFFTGAAPISREtLEFFLSL---NIPIMELYGMSEtSGPH-TISN-----PQAYRLLSCGKALPGCKTKIHNPDA----- 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232507 396 rNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQ-VAPAELESLL 470
Cdd:cd05933 390 -DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIEDAV 464
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
61-546 |
2.43e-40 |
|
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: 152.74 E-value: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIKNLQnDGVLIVTTDSDAIPENclrfseltqseePRVDsipekISPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd12117 100 TDRSLAGRAGGLE-VAVVIDEALDAGPAGN------------PAVP-----VSPDDLAYVMYTSGSTGRPKGVAVTHRGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVaqqvdgENPN-LYFNRDDVILCVLP------MFHIYA--LNsimlcslrvGATILIMPK---FEITLLLEQIQRCK 288
Cdd:cd12117 162 VRLV------KNTNyVTLGPDDRVLQTSPlafdasTFEIWGalLN---------GARLVLAPKgtlLDPDALGALIAEEG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 289 VTVAMVVPPIVLAIAKS-PETekydLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEaGPVLAMSLGFAKEPF 367
Cdd:cd12117 227 VTVLWLTAALFNQLADEdPEC----FAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTE-NTTFTTSHVVTELDE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 368 PVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWL------HTGDVGFIDDD 441
Cdd:cd12117 302 VAGSIPIGRPIANTRVYVLDED-GRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 442 DELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVrsKDSNISEDEIKQFVSKQVVFY 521
Cdd:cd12117 381 GRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAAELRAFLRERLPAY 458
|
490 500
....*....|....*....|....*
gi 15232507 522 KRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd12117 459 MVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
52-552 |
2.28e-39 |
|
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: 151.94 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLI----NGPTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEI 127
Cdd:cd05966 69 KVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 128 SKQAKASAAKLIVT--QSRYVDKIKNLQN--DGVLIVTTDsdaiPENCLRF-----------------SELTQSEEPRVD 186
Cdd:cd05966 149 ADRINDAQCKLVITadGGYRGGKVIPLKEivDEALEKCPS----VEKVLVVkrtggevpmtegrdlwwHDLMAKQSPECE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 187 siPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnlyFN--RDDVILCVLPMF----HIYALNS 257
Cdd:cd05966 225 --PEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAAttfKYV--------FDyhPDDIYWCTADIGwitgHSYIVYG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 258 IMLCslrvGATILImpkFEITL-------LLEQIQRCKVTVAMVVPPIVLAIAKSPE--TEKYDLSSVRMVKSGAAPLGK 328
Cdd:cd05966 295 PLAN----GATTVM---FEGTPtypdpgrYWDIVEKHKVTIFYTAPTAIRALMKFGDewVKKHDLSSLRVLGSVGEPINP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 329 EledaiSAKFPNAKLGQG-------YGMTEAGPVLAMSLGFAkepFPVKSGACGTVVRNAEMKILDPDTGdslPRNKPGE 401
Cdd:cd05966 368 E-----AWMWYYEVIGKErcpivdtWWQTETGGIMITPLPGA---TPLKPGSATRPFFGIEPAILDEEGN---EVEGEVE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 402 --ICIR----GnqIMKGYLNDPLATASTIDKD--GWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGH 473
Cdd:cd05966 437 gyLVIKrpwpG--MARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAH 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 474 PEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED---EIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARL 550
Cdd:cd05966 515 PAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIA 594
|
..
gi 15232507 551 AN 552
Cdd:cd05966 595 AG 596
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
61-546 |
1.35e-38 |
|
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: 147.44 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIknlqNDGVLIVTTDSDAIPENclrfseltqseeprVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd12116 90 TDDALPDRL----PAGLPVLLLALAAAAAA--------------PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 V---TSVAQQvdgenpnLYFNRDDVILCVL-PMFHIYALNsiMLCSLRVGATILIMPKfEIT----LLLEQIQRCKVTVA 292
Cdd:cd12116 152 VnflHSMRER-------LGLGPGDRLLAVTtYAFDISLLE--LLLPLLAGARVVIAPR-ETQrdpeALARLIEAHSITVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 293 MVVPP---IVLAiakspeTEKYDLSSVRMVKSGAA---PLGKELEDAISAkfpnakLGQGYGMTEAGP-VLAMSLGFAKE 365
Cdd:cd12116 222 QATPAtwrMLLD------AGWQGRAGLTALCGGEAlppDLAARLLSRVGS------LWNLYGPTETTIwSTAARVTAAAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 PFPVksgacGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLH-------TGDVGFI 438
Cdd:cd12116 290 PIPI-----GRPLANTQVYVLDAA-LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 439 DDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAmKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQV 518
Cdd:cd12116 364 RADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVV-REDGGDRRLVAYVVLKAGAAPDAAALRAHLRATL 442
|
490 500
....*....|....*....|....*...
gi 15232507 519 VFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd12116 443 PAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-540 |
6.88e-38 |
|
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: 143.29 E-value: 6.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 193 SPEDVVALpFSSGTTGLPKGVMLTH----------KGLVTSVAQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCS 262
Cdd:cd05924 2 SADDLYIL-YTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 263 LRVGATILIMPKFEITLLLEQIQRCKVTVAMVV-----PPIVLAIaKSPETekYDLSSVRMVKSGAAPLGKELEDAISAK 337
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVgdamaRPLIDAL-RDAGP--YDLSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 338 FPNAKLGQGYGMTEAGPV-LAMSLGFAKEPFPVKSGACGTVVrnaemkiLDPDTGDSLP-RNKPGEICIRGNqIMKGYLN 415
Cdd:cd05924 158 VPNITLVDAFGSSETGFTgSGHSAGSGPETGPFTRANPDTVV-------LDDDGRVVPPgSGGVGWIARRGH-IPLGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 416 DPLATAST---IDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEV 492
Cdd:cd05924 230 DEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15232507 493 PVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGK 540
Cdd:cd05924 310 VVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
64-509 |
7.78e-38 |
|
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: 146.07 E-value: 7.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIvtqs 143
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 rYVDKIKNLQN------DGVLIVTTDSDAIPENCLRFSELTQSEEPRVDSIPEkiSPEDVVALPFSSGTTGLPKGVMLTH 217
Cdd:cd05932 83 -FVGKLDDWKAmapgvpEGLISISLPPPSAANCQYQWDDLIAQHPPLEERPTR--FPEQLATLIYTSGTTGQPKGVMLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 218 KGLVTSVAQQVDgenpNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPkfEITLLLEQIQRCKVTVAMVVP- 296
Cdd:cd05932 160 GSFAWAAQAGIE----HIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLDTFVEDVQRARPTLFFSVPr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 297 ------------------------PIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISakfpnaKLG----QGYG 348
Cdd:cd05932 234 lwtkfqqgvqdkipqqklnlllkiPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYR------SLGlnilEAYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 349 MTEAGPVLAMSlgfakEPFPVKSGACGTVVRNAEMKIlDPDtgdslprnkpGEICIRGNQIMKGYLNDPLATASTIDKDG 428
Cdd:cd05932 308 MTENFAYSHLN-----YPGRDKIGTVGNAGPGVEVRI-SED----------GEILVRSPALMMGYYKDPEATAEAFTADG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 429 WLHTGDVGFIDDDDELFIVDRLKELIKY-KGFQVAPAELESLLIGHPEINDVAVVAmkeedAG-EVPVAFVVRSKDSNIS 506
Cdd:cd05932 372 FLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIG-----SGlPAPLALVVLSEEARLR 446
|
...
gi 15232507 507 EDE 509
Cdd:cd05932 447 ADA 449
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
52-548 |
1.82e-37 |
|
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: 146.48 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLI-NGPTGEV--YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEIS 128
Cdd:cd05968 77 RPALRwEGEDGTSrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 129 KQAKASAAKLIVTQSRYV--DKIKNL------------QNDGVLIVTTDSDAIPENCLRFSELTQSEEPRVDSIpEKISP 194
Cdd:cd05968 157 TRLQDAEAKALITADGFTrrGREVNLkeeadkacaqcpTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGA-ERTES 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 195 EDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQqvdgenpNLYFNRD----DVILCVLPM------FHIYAlnsimlcSLR 264
Cdd:cd05968 236 EDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQ-------DMYFQFDlkpgDLLTWFTDLgwmmgpWLIFG-------GLI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 265 VGATILI---MPKF-EITLLLEQIQRCKVTVAMVVPPIVLAIAKSPE--TEKYDLSSVRMVKSGAAPLGKE-----LEDA 333
Cdd:cd05968 302 LGATMVLydgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDapVNAHDLSSLRVLGSTGEPWNPEpwnwlFETV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 334 ISAKFPNAKLGQGygmTE-AGPVLAMSLgfakePFPVKSGACGTVVRNAEMKILDpDTGDSLpRNKPGEICIRGNQI--M 410
Cdd:cd05968 382 GKGRNPIINYSGG---TEiSGGILGNVL-----IKPIKPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVLLAPWPgmT 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 411 KGYLNDP---LATASTIDKDGWLHtGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEE 487
Cdd:cd05968 452 RGFWRDEdryLETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHP 530
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232507 488 DAGEVPVAFVVRSKD---SNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRA 548
Cdd:cd05968 531 VKGEAIVCFVVLKPGvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
64-550 |
3.36e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 144.85 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 64 YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQS 143
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 RYV-------DKIKNLQNdgvLIVTTDSDAIPENC---LRFSELTQSEEPRVD--SIPEKISPedvvALPFSSGTTGLPK 211
Cdd:PRK07008 120 TFLplvdalaPQCPNVKG---WVAMTDAAHLPAGStplLCYETLVGAQDGDYDwpRFDENQAS----SLCYTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 212 GVMLTHKglvTSVAQQVDGENPN-LYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVT 290
Cdd:PRK07008 193 GALYSHR---STVLHAYGAALPDaMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDLDGKSLYELIEAERVT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 291 VAMVVPPIVLAIAKSPETEKYDLSSVRMVKSG--AAP--LGKELEDAISAKFPNAklgqgYGMTEAGPVLAMS-LGFAKE 365
Cdd:PRK07008 270 FSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGgsACPpaMIRTFEDEYGVEVIHA-----WGMTEMSPLGTLCkLKWKHS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 PFPVKSG-----ACGTVVRNAEMKILDPDtGDSLPRNKP--GEICIRGNQIMKGYL---NDPLAtastidkDGWLHTGDV 435
Cdd:PRK07008 345 QLPLDEQrklleKQGRVIYGVDMKIVGDD-GRELPWDGKafGDLQVRGPWVIDRYFrgdASPLV-------DGWFPTGDV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 436 GFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVS 515
Cdd:PRK07008 417 ATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYE 496
|
490 500 510
....*....|....*....|....*....|....*
gi 15232507 516 KQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARL 550
Cdd:PRK07008 497 GKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
194-553 |
7.62e-37 |
|
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: 143.01 E-value: 7.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 194 PEDVVALPFSSGTTGLPKGVMLTHKGLVT---SVAQQVDgenpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATIL 270
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHnmfAILNSTE-------WKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 271 IMPKFEI----TLLLEQIQRCKVTVamVVPP-----IVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNA 341
Cdd:cd05908 178 LMPTRLFirrpILWLKKASEHKATI--VSSPnfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 342 KLGQG-----YGMTEAGpvLAMSLGFAKEPF--------------PV-----KSGACGTVVR------NAEMKILDpDTG 391
Cdd:cd05908 256 GLKRNailpvYGLAEAS--VGASLPKAQSPFktitlgrrhvthgePEpevdkKDSECLTFVEvgkpidETDIRICD-EDN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 392 DSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIdDDDELFIVDRLKELIKYKGFQVAPAELESLLI 471
Cdd:cd05908 333 KILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 472 GHPEINDVAVVAM---KEEDAGEVPVAFVVRSKdsniSEDEIKQFVSK-QVVFYKR----INKVFFTDSIPKAPSGKILR 543
Cdd:cd05908 412 ELEGVELGRVVACgvnNSNTRNEEIFCFIEHRK----SEDDFYPLGKKiKKHLNKRggwqINEVLPIRRIPKTTSGKVKR 487
|
410
....*....|
gi 15232507 544 KDLRARLANG 553
Cdd:cd05908 488 YELAQRYQSG 497
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
93-478 |
1.69e-36 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 142.65 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 93 ILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQNDGVlivTTDSDAIPENCL 172
Cdd:PRK06334 72 IMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQTHGEDA---EYPFSLIYMEEV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 173 RfSELTQSEEPRVD---SIP----------EKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNlyfnR 239
Cdd:PRK06334 149 R-KELSFWEKCRIGiymSIPfewlmrwfgvSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK----E 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 240 DDVILCVLPMFHIYALNSIMLCSLRVGATIL-----IMPKfeitLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLS 314
Cdd:PRK06334 224 DDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVfaynpLYPK----KIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 315 SVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMSlgfaKEPFPVKSGACGTVVRNAEMKILDPDTGDSL 394
Cdd:PRK06334 300 SLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVITIN----TVNSPKHESCVGMPIRGMDVLIVSEETKVPV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 395 PRNKPGEICIRGNQIMKGYL-NDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGH 473
Cdd:PRK06334 376 SSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
....*
gi 15232507 474 PEIND 478
Cdd:PRK06334 456 FGQNA 460
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
52-546 |
1.46e-35 |
|
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: 138.94 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQA 131
Cdd:cd12114 3 ATAVICG--DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 132 KASAAKLIVTQSRYVdkiknLQNDGVLIVTTDSDAipenclrfseltqSEEPRVDSIPEKISPEDVVALPFSSGTTGLPK 211
Cdd:cd12114 81 ADAGARLVLTDGPDA-----QLDVAVFDVLILDLD-------------ALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 212 GVMLTHKGLVTSVAQ-----QVDGenpnlyfnrDDVILCV------LPMFHIYALnsimlcsLRVGATiLIMP----KFE 276
Cdd:cd12114 143 GVMISHRAALNTILDinrrfAVGP---------DDRVLALsslsfdLSVYDIFGA-------LSAGAT-LVLPdearRRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 277 ITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAK---LGqgyGMTEAG 353
Cdd:cd12114 206 PAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARlisLG---GATEAS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 354 ------PVlamslgfAKEPFPVKSGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATAST--ID 425
Cdd:cd12114 283 iwsiyhPI-------DEVPPDWRSIPYGRPLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAARfvTH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 426 KDG--WLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDS 503
Cdd:cd12114 355 PDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGT 434
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15232507 504 NISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd12114 435 PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
65-546 |
4.01e-35 |
|
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: 138.23 E-value: 4.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFtPAE-ISKQAKASAAKLIVTQS 143
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY-PEErIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 RYVDKIKNLQndgvLIVTTDSDAIpenclrfseltqsEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVts 223
Cdd:cd17655 103 HLQPPIAFIG----LIDLLDEDTI-------------YHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVV-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 vaQQVDGENPNLYFNRDDVILCVLPmFHIYALNSIMLCSLRVGATILIMPKFEIT---LLLEQIQRCKVTVAMVVPPIVL 300
Cdd:cd17655 164 --NLVEWANKVIYQGEHLRVALFAS-ISFDASVTEIFASLLSGNTLYIVRKETVLdgqALTQYIRQNRITIIDLTPAHLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 301 AIAKSPETEKydlSSVRMVKSGAAPLGKELEDAISAKF-PNAKLGQGYGMTEAgPVLAMSLGFAKEPFPVKSGACGTVVR 379
Cdd:cd17655 241 LLDAADDSEG---LSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTET-TVDASIYQYEPETDQQVSVPIGKPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 380 NAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWL------HTGDVGFIDDDDELFIVDRLKEL 453
Cdd:cd17655 317 NTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 454 IKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISedEIKQFVSKQVVFYkrINKVFFT--D 531
Cdd:cd17655 396 VKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVA--QLREFLARELPDY--MIPSYFIklD 471
|
490
....*....|....*
gi 15232507 532 SIPKAPSGKILRKDL 546
Cdd:cd17655 472 EIPLTPNGKVDRKAL 486
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
76-548 |
5.74e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 138.24 E-value: 5.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 76 LAAGLHNLGVKQHdvVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQND 155
Cdd:PRK13388 42 ALIALADPDRPLH--VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLDLP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 156 GVLIVTTDSDAIPENCLRFSELTQSEEprvdsipekISPEDVVALPFSSGTTGLPKGVMLTHkGLVTSVAQQvdgeNPNL 235
Cdd:PRK13388 120 GVRVLDVDTPAYAELVAAAGALTPHRE---------VDAMDPFMLIFTSGTTGAPKAVRCSH-GRLAFAGRA----LTER 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 236 Y-FNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVT-VAMVVPPI--VLAIAKSPEteky 311
Cdd:PRK13388 186 FgLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATyFNYVGKPLayILATPERPD---- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 312 dlssvrmvkSGAAPL----GKELEDAISAKFP---NAKLGQGYGMTEAGPVLamslgfAKEP-FPvkSGACGtvvRNAE- 382
Cdd:PRK13388 262 ---------DADNPLrvafGNEASPRDIAEFSrrfGCQVEDGYGSSEGAVIV------VREPgTP--PGSIG---RGAPg 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 383 MKILDPDTGDSLPR-------------NKPGEIC-IRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVD 448
Cdd:PRK13388 322 VAIYNPETLTECAVarfdahgallnadEAIGELVnTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 449 RLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVF-------Y 521
Cdd:PRK13388 401 RTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDLgtkawprY 480
|
490 500
....*....|....*....|....*..
gi 15232507 522 KRInkvffTDSIPKAPSGKILRKDLRA 548
Cdd:PRK13388 481 VRI-----AADLPSTATNKVLKRELIA 502
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
48-497 |
6.05e-35 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 138.60 E-value: 6.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 48 EFAAKpclinGPTG-----------EVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAItt 116
Cdd:PRK09192 28 DYAAL-----GEAGmnfydrrgqleEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLV-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 117 sanPFFTPAEISKQAKASaaklivtqsrYVDKIKNL--QNDGVLIVTTD------SDAIPENCLRFS----ELTQSEEPR 184
Cdd:PRK09192 101 ---PVPLPLPMGFGGRES----------YIAQLRGMlaSAQPAAIITPDellpwvNEATHGNPLLHVlshaWFKALPEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 185 VDsIPEkISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQV-DGenpnLYFNRDDVILCVLPMFHIYALNSIMLCSL 263
Cdd:PRK09192 168 VA-LPR-PTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIShDG----LKVRPGDRCVSWLPFYHDMGLVGFLLTPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 264 RVGATILIMPKFEIT----LLLEQIQRCKVTVAmVVPPIVLAI----AKSPETEKYDLSSVRMVKSGAAPLGKELEDAIS 335
Cdd:PRK09192 242 ATQLSVDYLPTRDFArrplQWLDLISRNRGTIS-YSPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 336 AKF------PNAKLGQgYGMTEAgpVLAMSL-----GF--------------AKEPFPVKSGA------CGTVVRNAEMK 384
Cdd:PRK09192 321 EAFapagfdDKAFMPS-YGLAEA--TLAVSFsplgsGIvveevdrdrleyqgKAVAPGAETRRvrtfvnCGKALPGHEIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 385 ILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPlATASTIDKDGWLHTGDVGFIdDDDELFIVDRLKELIKYKGFQVAPA 464
Cdd:PRK09192 398 IRNEA-GMPLPERVVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQ 474
|
490 500 510
....*....|....*....|....*....|....*
gi 15232507 465 ELESLLIGHPEIN--DVAVVAMkEEDAGEVPVAFV 497
Cdd:PRK09192 475 DIEWIAEQEPELRsgDAAAFSI-AQENGEKIVLLV 508
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
38-552 |
2.00e-34 |
|
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: 135.75 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 38 LHDYIFENISEFAAKPClINGPTGEVyTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLA-----ASFIg 112
Cdd:cd05918 1 VHDLIEERARSQPDAPA-VCAWDGSL-TYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAvlkagGAFV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 113 AITTSAnpfftPAE----ISKQAKASaaklivtqsryvdkiknlqndgvLIVTTDsdaipenclrfseltqseeprvdsi 188
Cdd:cd05918 78 PLDPSH-----PLQrlqeILQDTGAK-----------------------VVLTSS------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 189 pekisPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQvdgeNPNLYFNRDDVILCvlpmFHIYALN-SIM--LCSLRV 265
Cdd:cd05918 105 -----PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAH----GRALGLTSESRVLQ----FASYTFDvSILeiFTTLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 266 GATILIMPKFE-ITLLLEQIQRCKVTVAMVVPpiVLAIAKSPEtekyDLSSVRMVKSGAAPLGKELEDAISakfPNAKLG 344
Cdd:cd05918 172 GGCLCIPSEEDrLNDLAGFINRLRVTWAFLTP--SVARLLDPE----DVPSLRTLVLGGEALTQSDVDTWA---DRVRLI 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 345 QGYGMTEAGPVLAMSLGFAKEP-----FPVKSGACgtvvrnaemkILDPDTGDSL-PRNKPGEICIRGNQIMKGYLNDPL 418
Cdd:cd05918 243 NAYGPAECTIAATVSPVVPSTDprnigRPLGATCW----------VVDPDNHDRLvPIGAVGELLIEGPILARGYLNDPE 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 419 ATA-STIDKDGWLH------------TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGH-PEINDVAVVAM 484
Cdd:cd05918 313 KTAaAFIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 485 KEEDAGEVP--VAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKV-----------------FFTDSIPKAPSGKILRKD 545
Cdd:cd05918 393 KPKDGSSSPqlVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELrsklrqrlpsymvpsvfLPLSHLPLTASGKIDRRA 472
|
....*..
gi 15232507 546 LRARLAN 552
Cdd:cd05918 473 LRELAES 479
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
63-553 |
2.40e-34 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 137.39 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 63 VYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQ 142
Cdd:PRK10524 84 TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 143 ---SR--YVDKIKNLQNDG----------VLIVTTDSDAIPENCLR---FSEL-TQSEEPRVDsiPEKISPEDVVALPFS 203
Cdd:PRK10524 164 dagSRggKVVPYKPLLDEAialaqhkprhVLLVDRGLAPMARVAGRdvdYATLrAQHLGARVP--VEWLESNEPSYILYT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 204 SGTTGLPKGVMLTHKG----LVTSVAQQVDGENPNLYFNRDDVILCVLPMFHIYAlnsimlcSLRVG-ATIL-----IMP 273
Cdd:PRK10524 242 SGTTGKPKGVQRDTGGyavaLATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYA-------PLLAGmATIMyeglpTRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 274 KFEItlLLEQIQRCKVTVAMVVPPIVLAIAKSPET--EKYDLSSVRMVKSGAAPLgkeleDAISAKFPNAKLGQ----GY 347
Cdd:PRK10524 315 DAGI--WWRIVEKYKVNRMFSAPTAIRVLKKQDPAllRKHDLSSLRALFLAGEPL-----DEPTASWISEALGVpvidNY 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 348 GMTEAG-PVLAMSLGFakEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGnqimkgylndPLATA--STI 424
Cdd:PRK10524 388 WQTETGwPILAIARGV--EDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEG----------PLPPGcmQTV 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 425 DKDG-------WLH-------TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAG 490
Cdd:PRK10524 456 WGDDdrfvktyWSLfgrqvysTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKG 535
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232507 491 EVPVAFVVrSKDSNISED---------EIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRArLANG 553
Cdd:PRK10524 536 QVAVAFVV-PKDSDSLADrearlalekEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQA-IAEG 605
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
25-467 |
2.70e-34 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 137.54 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 25 SRLPDIyiPNHLPLHDYIFENISEFAAKPCL-----INGPTGEvY---TYADVHVTSRKLAAGLHNLGVKQHDVVMILLP 96
Cdd:PLN02736 35 SRFPDH--PEIGTLHDNFVYAVETFRDYKYLgtrirVDGTVGE-YkwmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 97 NSPEVVLTFLAAS-------------------FIGAITTSANPFFTPAEI----SKQAKASAAKLIVTQSRYVDKIKNL- 152
Cdd:PLN02736 112 NRPEWLIVDHACSaysyvsvplydtlgpdavkFIVNHAEVAAIFCVPQTLntllSCLSEIPSVRLIVVVGGADEPLPSLp 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 153 QNDGVLIVTtdsdaipenclrFSELTQseEPRVDS---IPEKisPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAqqvd 229
Cdd:PLN02736 192 SGTGVEIVT------------YSKLLA--QGRSSPqpfRPPK--PEDVATICYTSGTTGTPKGVVLTHGNLIANVA---- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 230 GENPNLYFNRDDVILCVLPMFHIYALNSIMLCsLRVGATIlimpKF---EITLLLEQIQRCKVTVAMVVP--------PI 298
Cdd:PLN02736 252 GSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAV----GFyqgDNLKLMDDLAALRPTIFCSVPrlynriydGI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 299 VLAI----------------AK----------SPETEKYDLSS--------VRMVKSGAAPLGKELEDAISAKFpNAKLG 344
Cdd:PLN02736 327 TNAVkesgglkerlfnaaynAKkqalengknpSPMWDRLVFNKikaklggrVRFMSSGASPLSPDVMEFLRICF-GGRVL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 345 QGYGMTEAGPVLAmslgfAKEPFPVKSGACGTVVRNAEMKILDPDTGDSLPRNKP---GEICIRGNQIMKGYLNDPLATA 421
Cdd:PLN02736 406 EGYGMTETSCVIS-----GMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPyprGEICVRGPIIFKGYYKDEVQTR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15232507 422 STIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKY-KGFQVAPAELE 467
Cdd:PLN02736 481 EVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIE 527
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
61-546 |
6.38e-34 |
|
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: 133.97 E-value: 6.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd17643 10 DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd17643 90 TD---------------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVAqqvdGENPNLYFNRDDVILcvlpMFHIYALN-SI--MLCSLRVGATILIMPKfEITL----LLEQIQRCKVTVAM 293
Cdd:cd17643 119 LALFA----ATQRWFGFNEDDVWT----LFHSYAFDfSVweIWGALLHGGRLVVVPY-EVARspedFARLLRDEGVTVLN 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 294 VVPPIVLAIAKSPETEKYDLSSVRMVKSGaaplGKELEDAISAKF------PNAKLGQGYGMTE--------------AG 353
Cdd:cd17643 190 QTPSAFYQLVEAADRDGRDPLALRYVIFG----GEALEAAMLRPWagrfglDRPQLVNMYGITEttvhvtfrpldaadLP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 354 PVLAMSLGfakEPFPvksgacGTVVRnaemkILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATAS-------TIDK 426
Cdd:cd17643 266 AAAASPIG---RPLP------GLRVY-----VLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 427 DGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNIS 506
Cdd:cd17643 331 SRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAAD 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15232507 507 EDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd17643 411 IAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
65-546 |
2.08e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 133.58 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YVDKIKNlQNDGVLIVTTdSDAIPENClrfseltqseeprvDSIPEKISPEDVVALpfSSGTTGLPKGVMLTHKgLVTSV 224
Cdd:PRK13383 142 FAERIAG-ADDAVAVIDP-ATAGAEES--------------GGRPAVAAPGRIVLL--TSGTTGKPKGVPRAPQ-LRSAV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 225 AQQVDgenpnlYFNRDDV-----ILCVLPMFHIYALNSIMLcSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIV 299
Cdd:PRK13383 203 GVWVT------ILDRTRLrtgsrISVAMPMFHGLGLGMLML-TIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 300 LAIAKSPET--EKYDLSSVRMVKSGaaplGKELEDAISAKFPNAK---LGQGYGMTEAG-PVLAMSLGFAKEPFPVKSGA 373
Cdd:PRK13383 276 ARILELPPRvrARNPLPQLRVVMSS----GDRLDPTLGQRFMDTYgdiLYNGYGSTEVGiGALATPADLRDAPETVGKPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 374 CGTVVRnaemkILDPDTGDSLPRnKPGEICIRGNQIMKGYlNDPLATASTidkDGWLHTGDVGFIDDDDELFIVDRLKEL 453
Cdd:PRK13383 352 AGCPVR-----ILDRNNRPVGPR-VTGRIFVGGELAGTRY-TDGGGKAVV---DGMTSTGDMGYLDNAGRLFIVGREDDM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 454 IKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSI 533
Cdd:PRK13383 422 IISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSI 501
|
490
....*....|...
gi 15232507 534 PKAPSGKILRKDL 546
Cdd:PRK13383 502 PRNPTGKVLRKEL 514
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
42-547 |
2.27e-33 |
|
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: 132.05 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 42 IFENISEfaAKPCLI--NGPTGEVyTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAIttsan 119
Cdd:cd17653 2 AFERIAA--AHPDAVavESLGGSL-TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 120 pfFTPAEISkqAKASAAKLIVTQSRyvdkiknlqndGVLIVTTDSdaipenclrfseltqseeprvdsipekisPEDVVA 199
Cdd:cd17653 74 --YVPLDAK--LPSARIQAILRTSG-----------ATLLLTTDS-----------------------------PDDLAY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 200 LPFSSGTTGLPKGVMLTHKGlVTSVAQQvdgENPNLYFNRDDVILCVL-PMFHIYALnsIMLCSLRVGAT-ILIMPKFEI 277
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHRG-VLNYVSQ---PPARLDVGPGSRVAQVLsIAFDACIG--EIFSTLCNGGTlVLADPSDPF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 278 TLLLEqiqrcKVTVAMVVPPIVLAIakSPEtekyDLSSVRMVKSGAAPLGKELEDAISakfPNAKLGQGYGMTEAGPVLA 357
Cdd:cd17653 184 AHVAR-----TVDALMSTPSILSTL--SPQ----DFPNLKTIFLGGEAVPPSLLDRWS---PGRRLYNAYGPTECTISST 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 358 MSLGFAKEPFPVksgacGTVVRNAEMKILDPDTGDSlPRNKPGEICIRGNQIMKGYLNDPLATAS----TIDKDGWLH-- 431
Cdd:cd17653 250 MTELLPGQPVTI-----GKPIPNSTCYILDADLQPV-PEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyr 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 432 TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIG-HPEINDVAVVAmkeedAGEVPVAFVVrskDSNISEDEI 510
Cdd:cd17653 324 TGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIV-----VNGRLVAFVT---PETVDVDGL 395
|
490 500 510
....*....|....*....|....*....|....*..
gi 15232507 511 KQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd17653 396 RSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
62-553 |
5.92e-33 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 132.98 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHN-LGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIKNLQND-----GVLIVTTDSDAIPENCLRFSELTQSEEPRVDSIPE-----KISPEDVVALPFSSGTTGLP 210
Cdd:PRK05620 117 ADPRLAEQLGEILKEcpcvrAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTvydwpELDETTAAAICYSTGTTGAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 211 KGVMLTHKGLVTSvAQQVDGENpNLYFNRDDVILCVLPMFHIYALnSIMLCSLRVGATiLIMPKFEIT--LLLEQIQRCK 288
Cdd:PRK05620 197 KGVVYSHRSLYLQ-SLSLRTTD-SLAVTHGESFLCCVPIYHVLSW-GVPLAAFMSGTP-LVFPGPDLSapTLAKIIATAM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 289 VTVAMVVPPI-----VLAIAKSPETekydlSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVlamslGFA 363
Cdd:PRK05620 273 PRVAHGVPTLwiqlmVHYLKNPPER-----MSLQEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTETSPV-----GTV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 364 KEPfpvKSGACGTVVRN-----------AEMKILDPDTG-DSLPRNKpGEICIRGNQIMKGYLNDPLAT----ASTID-- 425
Cdd:PRK05620 342 ARP---PSGVSGEARWAyrvsqgrfpasLEYRIVNDGQVmESTDRNE-GEIQVRGNWVTASYYHSPTEEgggaASTFRge 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 426 ----------KDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVA 495
Cdd:PRK05620 418 dvedandrftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLA 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232507 496 FVVRSKDSNISE---DEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLANG 553
Cdd:PRK05620 498 VTVLAPGIEPTRetaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLADG 558
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
60-552 |
1.05e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 131.66 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 60 TGEVY-----TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSAN-PffTP--------A 125
Cdd:PRK07768 21 TGEPDapvrhTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHqP--TPrtdlavwaE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 126 EISKQAKASAAKLIVTQSRYVDKIKNLQNDGVLIVTtdsdaipenclrFSELTQSEEPRvdsiPEKISPEDVVALPFSSG 205
Cdd:PRK07768 99 DTLRVIGMIGAKAVVVGEPFLAAAPVLEEKGIRVLT------------VADLLAADPID----PVETGEDDLALMQLTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 206 TTGLPKGVMLTHKGLVTSVAQQVDGENpnlYFNRDDVILCVLPMFH----IYALNSIMLCslrvGAT-ILIMP-KFEITL 279
Cdd:PRK07768 163 STGSPKAVQITHGNLYANAEAMFVAAE---FDVETDVMVSWLPLFHdmgmVGFLTVPMYF----GAElVKVTPmDFLRDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 280 LL--EQIQRCKVTvaMVVPP----IVLA--IAKSPETEKYDLSSVRMVKSGAAPLGKE-LEDAISA----KFPNAKLGQG 346
Cdd:PRK07768 236 LLwaELISKYRGT--MTAAPnfayALLArrLRRQAKPGAFDLSSLRFALNGAEPIDPAdVEDLLDAgarfGLRPEAILPA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 347 YGMTEA-----------GPVL---------AMSLGFAKEPFPVKSGAC-GTVVRNAEMKILDPDtGDSLPRNKPGEICIR 405
Cdd:PRK07768 314 YGMAEAtlavsfspcgaGLVVdevdadllaALRRAVPATKGNTRRLATlGPPLPGLEVRVVDED-GQVLPPRGVGVIELR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 406 GNQIMKGYLnDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMK 485
Cdd:PRK07768 393 GESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVR 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232507 486 EE--DAGEvPVAFVVRSKDSNiSEDEIKQF-------VSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLAN 552
Cdd:PRK07768 472 LDagHSRE-GFAVAVESNAFE-DPAEVRRIrhqvaheVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAELVTP 545
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
56-541 |
1.59e-32 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 133.17 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 56 INGPTGEVYTYADV----HVTSRKLAAGLH---NLGVkqhdvvmiLLPNSPEVVLTFLAASFIGAITTSANpfFT--PAE 126
Cdd:PRK06814 651 VEDPVNGPLTYRKLltgaFVLGRKLKKNTPpgeNVGV--------MLPNANGAAVTFFALQSAGRVPAMIN--FSagIAN 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 127 ISKQAKASAAKLIVTQSRYVDK------IKNLQNDGVLIVTTDSDAIPENCLRFSELTQSEEPRVdSIPEKiSPEDVVAL 200
Cdd:PRK06814 721 ILSACKAAQVKTVLTSRAFIEKarlgplIEALEFGIRIIYLEDVRAQIGLADKIKGLLAGRFPLV-YFCNR-DPDDPAVI 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 201 PFSSGTTGLPKGVMLTHKGLVTSVAQ---QVDgenpnlyFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPK-FE 276
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLANRAQvaaRID-------FSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSpLH 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 277 ITLLLEQIQRCKVTVAMVVPPIVLAIAKSpeTEKYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVL 356
Cdd:PRK06814 872 YRIIPELIYDTNATILFGTDTFLNGYARY--AHPYDFRSLRYVFAGAEKVKEETRQTWMEKF-GIRILEGYGVTETAPVI 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 357 AMSlgfakEPFPVKSGACGTVVRNAEMKiLDPDTGdslpRNKPGEICIRGNQIMKGYLN-------DPLAtastidkDGW 429
Cdd:PRK06814 949 ALN-----TPMHNKAGTVGRLLPGIEYR-LEPVPG----IDEGGRLFVRGPNVMLGYLRaenpgvlEPPA-------DGW 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 430 LHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLlighpeINDV------AVVAMKEEDAGEVPVAFVVRskdS 503
Cdd:PRK06814 1012 YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEEL------AAELwpdalhAAVSIPDARKGERIILLTTA---S 1082
|
490 500 510
....*....|....*....|....*....|....*....
gi 15232507 504 NISEDEIKQFVSKQVVFYKRINKVFFT-DSIPKAPSGKI 541
Cdd:PRK06814 1083 DATRAAFLAHAKAAGASELMVPAEIITiDEIPLLGTGKI 1121
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
62-482 |
3.48e-31 |
|
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: 127.54 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT 141
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSR-YVDKIKNLQND--GVL-IVTTDSDAIPE----NCLRFSELTQ------SEEP-RVDSIPEKISPEDVVALPFSSGT 206
Cdd:cd17641 90 EDEeQVDKLLEIADRipSVRyVIYCDPRGMRKyddpRLISFEDVVAlgraldRRDPgLYEREVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 207 TGLPKGVMLTHKGLVTSVA--QQVDGENPnlyfnrDDVILCVLP----MFHIYALNSIMLC---------------SLR- 264
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAayLAADPLGP------GDEYVSVLPlpwiGEQMYSVGQALVCgfivnfpeepetmmeDLRe 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 265 VGATILIMPK------------------------FEITL-----LLEQIQRCKVTVAMVVPPIVLA--IAKSPETEKYDL 313
Cdd:cd17641 244 IGPTFVLLPPrvwegiaadvrarmmdatpfkrfmFELGMklglrALDRGKRGRPVSLWLRLASWLAdaLLFRPLRDRLGF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 314 SSVRMVKSGAAPLGKELEDAISAKFPNAKlgQGYGMTE-AGPVLAMSLGfakepfPVKSGACGTVVRNAEMKIldpdtgd 392
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFHAIGVPLK--QLYGQTElAGAYTVHRDG------DVDPDTVGVPFPGTEVRI------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 393 slprNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIK-YKGFQVAPAELESLLI 471
Cdd:cd17641 389 ----DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLK 464
|
490
....*....|.
gi 15232507 472 GHPEINDvAVV 482
Cdd:cd17641 465 FSPYIAE-AVV 474
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
65-546 |
1.55e-30 |
|
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: 124.12 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQsr 144
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 yvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKglvtSV 224
Cdd:cd17650 92 -------------------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHR----NV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 225 AQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMP---KFEITLLLEQIQRCKVTVAMVVPPIVLA 301
Cdd:cd17650 119 AHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPALIRP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 302 IAKSPETEKYDLSSVRMVKsgaapLGKELEDAISAKFPNAKLGQG------YGMTEA---GPVLAMSLGFAKE------- 365
Cdd:cd17650 199 VMAYVYRNGLDLSAMRLLI-----VGSDGCKAQDFKTLAARFGQGmriinsYGVTEAtidSTYYEEGRDPLGDsanvpig 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 -PFPvksgacgtvvrNAEMKILDPdTGDSLPRNKPGEICIRGNQIMKGYLNDPLATAS---------------TIDKDGW 429
Cdd:cd17650 274 rPLP-----------NTAMYVLDE-RLQPQPVGVAGELYIGGAGVARGYLNRPELTAErfvenpfapgermyrTGDLARW 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 430 LHTGDVGFIDdddelfivdRLKELIKYKGFQVAPAELESLLIGHPEInDVAVVAMKEEDAGEVP-VAFVVRSKDSNISed 508
Cdd:cd17650 342 RADGNVELLG---------RVDHQVKIRGFRIELGEIESQLARHPAI-DEAVVAVREDKGGEARlCAYVVAAATLNTA-- 409
|
490 500 510
....*....|....*....|....*....|....*...
gi 15232507 509 EIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd17650 410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
65-546 |
1.56e-30 |
|
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: 123.97 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQsr 144
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 yvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGLVTSV 224
Cdd:cd12115 104 -------------------------------------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 225 aqQVDGENpnlyFNRDDvilcvlpMFHIYALNSI--------MLCSLRVGATILIMPkfEITLLLEQIQRCKVTVAMVVP 296
Cdd:cd12115 135 --QWAAAA----FSAEE-------LAGVLASTSIcfdlsvfeLFGPLATGGKVVLAD--NVLALPDLPAAAEVTLINTVP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 297 PIV---LAIAKSPEtekydlsSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEA---GPVLAMSLGFAKEPfpvk 370
Cdd:cd12115 200 SAAaelLRHDALPA-------SVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDttySTVAPVPPGASGEV---- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 371 sgACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWL------HTGDVGFIDDDDEL 444
Cdd:cd12115 269 --SIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 445 FIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRI 524
Cdd:cd12115 346 EFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVP 425
|
490 500
....*....|....*....|..
gi 15232507 525 NKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd12115 426 SRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
62-549 |
2.21e-30 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 125.91 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT 141
Cdd:PRK06060 29 DVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSRYVDKIKnlqndgvlivttdsdaiPENCLRFSELTqSEEPRVDSIPEKISPEDVVALP-FSSGTTGLPKGVMLTHKGL 220
Cdd:PRK06060 109 SDALRDRFQ-----------------PSRVAEAAELM-SEAARVAPGGYEPMGGDALAYAtYTSGTTGPPKAAIHRHADP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVAQQVDGEnpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMP---KFEITLLLEqiQRCKVTVAMVVPP 297
Cdd:PRK06060 171 LTFVDAMCRKA---LRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSapvTPEAAAILS--ARFGPSVLYGVPN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 298 IVLAI--AKSPETekydLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLGFAKEPfpvksGACG 375
Cdd:PRK06060 246 FFARVidSCSPDS----FRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRL-----GTLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 376 TVVRNAEMKILDPDTGDSLPRNKpGEICIRGNQIMKGYLNDPlatASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIK 455
Cdd:PRK06060 317 RVLPPYEIRVVAPDGTTAGPGVE-GDLWVRGPAIAKGYWNRP---DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 456 YKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED---EIKQFVSKQVVFYKRINKVFFTDS 532
Cdd:PRK06060 393 IGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSvmrDLHRGLLNRLSAFKVPHRFAVVDR 472
|
490
....*....|....*..
gi 15232507 533 IPKAPSGKILRKDLRAR 549
Cdd:PRK06060 473 LPRTPNGKLVRGALRKQ 489
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
61-546 |
2.46e-30 |
|
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: 123.52 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd17652 10 DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd17652 90 TT---------------------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVAQQVDGENPnlyfNRDDVIL-CVLPMFHIYALNSIMlcSLRVGATILIMPKFEITL---LLEQIQRCKVTvAMVVP 296
Cdd:cd17652 119 ANLAAAQIAAFDV----GPGSRVLqFASPSFDASVWELLM--ALLAGATLVLAPAEELLPgepLADLLREHRIT-HVTLP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 297 PIVLAiAKSPEtekyDLSSVRMVKSGAAPLGKELED--AISAKFPNAklgqgYGMTEAGPVLAMSLGFAKEPFPvksgAC 374
Cdd:cd17652 192 PAALA-ALPPD----DLPDLRTLVVAGEACPAELVDrwAPGRRMINA-----YGPTETTVCATMAGPLPGGGVP----PI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 375 GTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKD------GWLH-TGDVGFIDDDDELFIV 447
Cdd:cd17652 258 GRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 448 DRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYkRINKV 527
Cdd:cd17652 337 GRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGY-MVPAA 415
|
490 500
....*....|....*....|
gi 15232507 528 FFT-DSIPKAPSGKILRKDL 546
Cdd:cd17652 416 FVVlDALPLTPNGKLDRRAL 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
61-553 |
3.00e-30 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 126.82 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQhDVVMILLPNSPEVVLTFLAASFIGAITTSAnpffTPAEISKQAKasaakliv 140
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQARASFG-DRAVLLFPSGPDYVAAFFGCLYAGVIAVPA----YPPESARRHH-------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 tQSRYVDKIKNLQNDGVLIVTTDSDAIpencLRFSELTQSEEPR---VDSIPE---------KISPEDVVALPFSSGTTG 208
Cdd:PRK05691 105 -QERLLSIIADAEPRLLLTVADLRDSL----LQMEELAAANAPEllcVDTLDPalaeawqepALQPDDIAFLQYTSGSTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 209 LPKGVMLTHKGLVTSvaQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIM-PKFEITL---LLEQI 284
Cdd:PRK05691 180 LPKGVQVSHGNLVAN--EQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPAYFLERplrWLEAI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 285 QRCKVTVAMVvPPIV--LAIAKSPET--EKYDLSSVRMVKSGAAPLGKELEDAISAKF------PNAKLGQgYGMTEA-- 352
Cdd:PRK05691 258 SEYGGTISGG-PDFAyrLCSERVSESalERLDLSRWRVAYSGSEPIRQDSLERFAEKFaacgfdPDSFFAS-YGLAEAtl 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 353 -----------------GPVLAMSLGFAKEPFPVKSgaCGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLN 415
Cdd:PRK05691 336 fvsggrrgqgipaleldAEALARNRAEPGTGSVLMS--CGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 416 DPLATAST-IDKDG--WLHTGDVGFIdDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEI---NDVAVVAMKEEDA 489
Cdd:PRK05691 414 NPEASAKTfVEHDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVvrkGRVAAFAVNHQGE 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232507 490 GEVPVAF-VVRSKDSNISEDE----IKQFVSKqvVFYKRINKVFFTD--SIPKAPSGKILRKDLRARLANG 553
Cdd:PRK05691 493 EGIGIAAeISRSVQKILPPQAliksIRQAVAE--ACQEAPSVVLLLNpgALPKTSSGKLQRSACRLRLADG 561
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
61-481 |
9.33e-29 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 120.75 E-value: 9.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:PRK08279 60 DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIKNLQND--GVLIVTTDSDAIPENCLRFSELTQSEEPRVDSIP---EKISPEDVVALPFSSGTTGLPKGVML 215
Cdd:PRK08279 140 VGEELVEAFEEARADlaRPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPasrSGVTAKDTAFYIYTSGTTGLPKAAVM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 216 THKGLVTSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVV 295
Cdd:PRK08279 220 SHMRWLKAMGGFGGL----LRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 296 PPIVLAIAKSPETEKYDLSSVR-MVKSGAAPlgkELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLGFakepfpvkSGAC 374
Cdd:PRK08279 296 GELCRYLLNQPPKPTDRDHRLRlMIGNGLRP---DIWDEFQQRFGIPRILEFYAASEGNVGFINVFNF--------DGTV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 375 GTV----VRNAEMKILDPDTGDSLpRN--------KPGEIC-----IRGNQIMKGYlNDPLATASTI------DKDGWLH 431
Cdd:PRK08279 365 GRVplwlAHPYAIVKYDVDTGEPV-RDadgrcikvKPGEVGlligrITDRGPFDGY-TDPEASEKKIlrdvfkKGDAWFN 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15232507 432 TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAV 481
Cdd:PRK08279 443 TGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVV 492
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
65-442 |
2.40e-28 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 119.60 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAittsanPFftpAEISKQ-AKASA--AKL--I 139
Cdd:PRK08180 71 TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGV------PY---APVSPAySLVSQdfGKLrhV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 140 VTQ-----------SRYVDKIKNLQNDGVLIVTTDSDAIPENCLRFSEL-TQSEEPRVDSIPEKISPEDVVALPFSSGTT 207
Cdd:PRK08180 142 LELltpglvfaddgAAFARALAAVVPADVEVVAVRGAVPGRAATPFAALlATPPTAAVDAAHAAVGPDTIAKFLFTSGST 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 208 GLPKGVMLTHkGLVTSVAQQ------VDGENPnlyfnrdDVILCVLPMFHIYALNSIMLCSLRVGATILI-----MP-KF 275
Cdd:PRK08180 222 GLPKAVINTH-RMLCANQQMlaqtfpFLAEEP-------PVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpTPgGF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 276 EITL-LLEQIQRckvTVAMVVPP----IVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAkFPNAKLGQ----- 345
Cdd:PRK08180 294 DETLrNLREISP---TVYFNVPKgwemLVPALERDAALRRRFFSRLKLLFYAGAALSQDVWDRLDR-VAEATCGErirmm 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 346 -GYGMTEAGPVLAmslgFAKEPFpVKSGACGTVVRNAEMKILdpDTGDSLprnkpgEICIRGNQIMKGYLNDPLATASTI 424
Cdd:PRK08180 370 tGLGMTETAPSAT----FTTGPL-SRAGNIGLPAPGCEVKLV--PVGGKL------EVRVKGPNVTPGYWRAPELTAEAF 436
|
410
....*....|....*....
gi 15232507 425 DKDGWLHTGD-VGFIDDDD 442
Cdd:PRK08180 437 DEEGYYRSGDaVRFVDPAD 455
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
65-467 |
4.03e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 118.68 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGvKQHDVVMILLPNSPEVVLTFLAASFIGAIttsANPFFTPAEISkqakasaaklivtqsr 144
Cdd:PRK07769 57 TWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRI---AVPLFDPAEPG---------------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YVDKIknlqnDGVL-------IVTTDSDAipENCLRF-SELTQSEEPR---VDSIPEK---------ISPEDVVALPFSS 204
Cdd:PRK07769 117 HVGRL-----HAVLddctpsaILTTTDSA--EGVRKFfRARPAKERPRviaVDAVPDEvgatwvppeANEDTIAYLQYTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 205 GTTGLPKGVMLTHKGLVTSVAQQVDGenpnLYFNRDDVILCVLPMFHIYALNSIMLCSLrVGATILIM--------PKFE 276
Cdd:PRK07769 190 GSTRIPAGVQITHLNLPTNVLQVIDA----LEGQEGDRGVSWLPFFHDMGLITVLLPAL-LGHYITFMspaafvrrPGRW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 277 ITLLLEQIQRCKVTVAmVVPPIVLAIAKS----PETEK-YDLSSVRMVKSGAAPLG----KELEDAISA-KFPNAKLGQG 346
Cdd:PRK07769 265 IRELARKPGGTGGTFS-AAPNFAFEHAAArglpKDGEPpLDLSNVKGLLNGSEPVSpasmRKFNEAFAPyGLPPTAIKPS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 347 YGMTEAgPVLAMSLGFAKEP---------------FPVKSGA--------CGTVVRNAEMKILDPDTGDSLPRNKPGEIC 403
Cdd:PRK07769 344 YGMAEA-TLFVSTTPMDEEPtviyvdrdelnagrfVEVPADApnavaqvsAGKVGVSEWAVIVDPETASELPDGQIGEIW 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 404 IRGNQIMKGYLNDPLATASTI-----------------DKDGWLHTGDVGfIDDDDELFIVDRLKELIKYKGFQVAPAEL 466
Cdd:PRK07769 423 LHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDYG-VYFDGELYITGRVKDLVIIDGRNHYPQDL 501
|
.
gi 15232507 467 E 467
Cdd:PRK07769 502 E 502
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
61-547 |
5.69e-28 |
|
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: 116.70 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFtPAEiskqakasaakliv 140
Cdd:cd17649 10 DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEY-PAE-------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 tQSRYVdkiknLQNDGVLIVttdsdaipenclrfseLTQSeeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd17649 75 -RLRYM-----LEDSGAGLL----------------LTHH-------------PRQLAYVIYTSGSTGTPKGVAVSHGPL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVaqQVDGENPNLyfNRDDVILCVLPM-FHIYAlnSIMLCSLRVGATILIMPK---FEITLLLEQIQRCKVTVAMVVP 296
Cdd:cd17649 120 AAHC--QATAERYGL--TPGDRELQFASFnFDGAH--EQLLPPLICGACVVLRPDelwASADELAEMVRELGVTVLDLPP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 297 PIVLAIAKSPETEKYDL-SSVRMVKSGAAPLGKELedaISAKFPNAK-LGQGYGMTEAgpvLAMSLGFAKEPFPVKSGA- 373
Cdd:cd17649 194 AYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPEL---LRRWLKAPVrLFNAYGPTEA---TVTPLVWKCEAGAARAGAs 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 374 --CGTVVRNAEMKILDPDTGdSLPRNKPGEICIRGNQIMKGYLNDPLATASTI--DKDG-----WLHTGDVGFIDDDDEL 444
Cdd:cd17649 268 mpIGRPLGGRSAYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 445 FIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAmKEEDAGEVPVAFVVRSKDSNISED--EIKQFVSKQVVFYK 522
Cdd:cd17649 347 EYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVA-LDGAGGKQLVAYVVLRAAAAQPELraQLRTALRASLPDYM 425
|
490 500
....*....|....*....|....*
gi 15232507 523 RINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd17649 426 VPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-554 |
8.44e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.29 E-value: 8.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 25 SRLPDIYiPNHLPLHDYIFENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLT 104
Cdd:PRK12316 1993 DRTPEAY-PRGPGVHQRIAEQAARAPEAIAVVFG--DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVA 2069
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 105 FLAASFIGAITTSANPFFtPAE-ISKQAKASAAKLIVTQSRYVDKIKNLQNDGVLIVTTDSD--AIPEnclrfseltqsE 181
Cdd:PRK12316 2070 LLAVLKAGGAYVPLDPNY-PAErLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAEwaDYPD-----------T 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 182 EPRVDsipekISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSV--AQQVDGENPNlyfnrdDVILCVLPmFHIYALNSIM 259
Cdd:PRK12316 2138 APAVQ-----LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCqaAGERYELSPA------DCELQFMS-FSFDGAHEQW 2205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 260 LCSLRVGATILIMPKfEITL---LLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSsVRMVKSGAAPLGKELEDAISA 336
Cdd:PRK12316 2206 FHPLLNGARVLIRDD-ELWDpeqLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWE 2283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 337 KFPNAKLGQGYGMTEAGPVLAMSLGFAKEPFPVKSGACGTVVRNAEMKILDPDTgDSLPRNKPGEICIRGNQIMKGYLND 416
Cdd:PRK12316 2284 ALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLARGYLNR 2362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 417 PLATASTIDKDGWLH-------TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAmKEEDA 489
Cdd:PRK12316 2363 PGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA-QDGAS 2441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232507 490 GEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLANGL 554
Cdd:PRK12316 2442 GKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQL 2506
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
61-546 |
2.04e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 117.96 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:PRK05691 1154 GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIKnlQNDGVLIVTTDS---DAIPenclrfseltqSEEPRVDsipekISPEDVVALPFSSGTTGLPKGVMLTH 217
Cdd:PRK05691 1234 TQSHLLERLP--QAEGVSAIALDSlhlDSWP-----------SQAPGLH-----LHGDNLAYVIYTSGSTGQPKGVGNTH 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 218 KGLvtsvAQQVDGENPNLYFNRDDVILCVLPM-FHIyalnSIMLC--SLRVGATILIMPKFE---ITLLLEQIQRCKVTV 291
Cdd:PRK05691 1296 AAL----AERLQWMQATYALDDSDVLMQKAPIsFDV----SVWECfwPLITGCRLVLAGPGEhrdPQRIAELVQQYGVTT 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 292 AMVVPPIVLAIAKSPETEkyDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYGMTEAgpvlAMSLGFAK------E 365
Cdd:PRK05691 1368 LHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTET----AINVTHWQcqaedgE 1441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 366 PFPVksgacGTVVRNAEMKILDPDTgDSLPRNKPGEICIRGNQIMKGYLNDPLATAS--TIDKDG-----WLHTGDVGFI 438
Cdd:PRK05691 1442 RSPI-----GRPLGNVLCRVLDAEL-NLLPPGVAGELCIGGAGLARGYLGRPALTAErfVPDPLGedgarLYRTGDRARW 1515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 439 DDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDvAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQV 518
Cdd:PRK05691 1516 NADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ-AAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAEL 1594
|
490 500
....*....|....*....|....*...
gi 15232507 519 VFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:PRK05691 1595 PEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-546 |
2.34e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 117.75 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 33 PNHLPLHDYIFENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIG 112
Cdd:PRK12316 4548 PATRCVHQLVAERARMTPDAVAVVFD--EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 113 AITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKnlQNDGVLIVTTDSDaipENCLRFSEltqsEEPRVdsipeKI 192
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLP--IPDGLASLALDRD---EDWEGFPA----HDPAV-----RL 4691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 193 SPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAqqVDGENPNLyfNRDDVILCVLPM-FHIYALNsiMLCSLRVGATILI 271
Cdd:PRK12316 4692 HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH--ATGERYEL--TPDDRVLQFMSFsFDGSHEG--LYHPLINGASVVI 4765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 272 mPKFEITL---LLEQIQRCKVTVAMVVPPIVLAIAKSPEtEKYDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLGQGYG 348
Cdd:PRK12316 4766 -RDDSLWDperLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYG 4843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 349 MTEAGPVLAMSLGFAKEPFPVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATA-----ST 423
Cdd:PRK12316 4844 PTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTAerfvpDP 4922
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 424 IDKDG--WLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAmKEEDAGEVPVAFVV--- 498
Cdd:PRK12316 4923 FGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA-QEGAVGKQLVGYVVpqd 5001
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15232507 499 -RSKDSNISE----DEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:PRK12316 5002 pALADADEAQaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
181-488 |
3.69e-27 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 116.07 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 181 EEPRVDSIPEkisPEDVVALPFSSGTTGLPKGVMLTHKGlVTSVAQQVDgenpnLYFNR-------DDVILCVLPMFHIY 253
Cdd:PLN02430 209 ENPSETNPPK---PLDICTIMYTSGTSGDPKGVVLTHEA-VATFVRGVD-----LFMEQfedkmthDDVYLSFLPLAHIL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 254 AlNSIMLCSLRVGATILIMPKfEITLLLEQIQRCKVTVAMVVPPIV-----------------------------LAIAK 304
Cdd:PLN02430 280 D-RMIEEYFFRKGASVGYYHG-DLNALRDDLMELKPTLLAGVPRVFerihegiqkalqelnprrrlifnalykykLAWMN 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 305 SPETEKY-----DLSSVRMVK-----------SGAAPLGKELEDAISAKfPNAKLGQGYGMTEA-GPVlamSLGFAKEPF 367
Cdd:PLN02430 358 RGYSHKKaspmaDFLAFRKVKaklggrlrlliSGGAPLSTEIEEFLRVT-SCAFVVQGYGLTETlGPT---TLGFPDEMC 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 368 PVksGACGTVVRNAEMKILD-PDTG-DSLPRNKPGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELF 445
Cdd:PLN02430 434 ML--GTVGAPAVYNELRLEEvPEMGyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLK 510
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232507 446 IVDRLKELIKY-KGFQVAPAELESLLIGHPEIND------------VAVVAMKEED 488
Cdd:PLN02430 511 IIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDiwvygdsfksmlVAVVVPNEEN 566
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
26-442 |
4.41e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 115.53 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 26 RLPD--IYIPNHLPLHDY---IFENISEFAA----KPCLI--NGPTG--EVYTYADVHVTSRKLAAGLHNLGVKQHDVVM 92
Cdd:PRK12582 30 RRADgsIVIKSRHPLGPYprsIPHLLAKWAAeapdRPWLAqrEPGHGqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 93 ILLPNSPEVVLTFLAASFIGAITTSANPFFTP-----AEISKQAKASAAKLIVTQS--RYVDKIKNLQNDGVLIVTTDSD 165
Cdd:PRK12582 110 ILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSgaPFARALAALDLLDVTVVHVTGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 166 AIPENCLRFSEL-TQSEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHkGLVTSVAQQVDGENPNLYFNRDDVIL 244
Cdd:PRK12582 190 GEGIASIAFADLaATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQ-RMMCANIAMQEQLRPREPDPPPPVSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 245 CVLPMFHIYALNSIMLCSLRVGATILI-----MP-KFEITllLEQIQRCKVTVAMVVPP----IVLAIAKSPETEKYDLS 314
Cdd:PRK12582 269 DWMPWNHTMGGNANFNGLLWGGGTLYIddgkpLPgMFEET--IRNLREISPTVYGNVPAgyamLAEAMEKDDALRRSFFK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 315 SVRMVKSGAAPLGKELED-----AISAKFPNAKLGQGYGMTEAGPVL------AMSLGFAKEPFPvksgacGTvvrnaEM 383
Cdd:PRK12582 347 NLRLMAYGGATLSDDLYErmqalAVRTTGHRIPFYTGYGATETAPTTtgthwdTERVGLIGLPLP------GV-----EL 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 384 KILdPdTGDSLprnkpgEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVG-FIDDDD 442
Cdd:PRK12582 416 KLA-P-VGDKY------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAArFVDPDD 467
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
20-546 |
5.32e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.80 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 20 DVIFRSRLPDIYIPNHlPLHDYIFENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSP 99
Cdd:PRK12467 497 RELVRWNAPATEYAPD-CVHQLIEAQARQHPERPALVFG--EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSI 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 100 EVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKnlQNDGVLIVTTDSDAiPENCLRFSELTq 179
Cdd:PRK12467 574 EMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLP--VPAGLRSLCLDEPA-DLLCGYSGHNP- 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 180 seEPRVDsipekisPEDVVALPFSSGTTGLPKGVMLTHKGL---VTSVAQQVDgenpnlyFNRDDVILcvlpMFHIYALN 256
Cdd:PRK12467 650 --EVALD-------PDNLAYVIYTSGSTGQPKGVAISHGALanyVCVIAERLQ-------LAADDSML----MVSTFAFD 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 257 ---SIMLCSLRVGATILIMPK---FEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKyDLSSVRMVKSGAApLGKEL 330
Cdd:PRK12467 710 lgvTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL-PRPQRALVCGGEA-LQVDL 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 331 EDAISAKFPNAKLGQGYGMTEAgPVLAMSLGFAKEPFPVKSGACGTVVRNAEMKILDPDTgDSLPRNKPGEICIRGNQIM 410
Cdd:PRK12467 788 LARVRALGPGARLINHYGPTET-TVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYL-NPVPVGVVGELYIGGAGLA 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 411 KGYLNDPLATASTIDKD------GWLH-TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVA 483
Cdd:PRK12467 866 RGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA 945
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232507 484 MkEEDAGEVPVAFVVRSKDSNISE-----DEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:PRK12467 946 Q-PGDAGLQLVAYLVPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
65-548 |
5.82e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.41 E-value: 5.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YVDKIknlqndgvlivttdsdAIPENcLRFSELTQSE---EPRVDSIPE-KISPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:PRK12467 1681 LQARL----------------PLPDG-LRSLVLDQEDdwlEGYSDSNPAvNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL 1743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSV--AQQVDGenpnlyFNRDDVILcvlpMFHIYALN-SI--MLCSLRVGATILIMPkFEITL----LLEQIQRCKVTV 291
Cdd:PRK12467 1744 VNRLcaTQEAYQ------LSAADVVL----QFTSFAFDvSVweLFWPLINGARLVIAP-PGAHRdpeqLIQLIERQQVTT 1812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 292 AMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAApLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLGFAKEPFPVKS 371
Cdd:PRK12467 1813 LHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEA-LEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDS 1891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 372 GACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTI------DKDGWLH-TGDVGFIDDDDEL 444
Cdd:PRK12467 1892 VPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVI 1970
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 445 FIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAmKEEDAGEVPVAFVVRSKDSNISEDE--------IKQFVSK 516
Cdd:PRK12467 1971 EYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVPTDPGLVDDDEaqvalraiLKNHLKA 2049
|
490 500 510
....*....|....*....|....*....|..
gi 15232507 517 QVVFYKRINKVFFTDSIPKAPSGKILRKDLRA 548
Cdd:PRK12467 2050 SLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
61-481 |
6.61e-27 |
|
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: 113.60 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAIttsanpfftPAEISKQAKASAAKLIV 140
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV---------AALINYNLRGESLAHCL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 tqsryvdkikNLQNDGVLIVTTdsdaipenCLrfseltqseeprvdsipekispedvvaLPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd05940 72 ----------NVSSAKHLVVDA--------AL---------------------------YIYTSGTTGLPKAAIISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 V--TSVAQQVDGENPNlyfnrdDVILCVLPMFHIYALnsiMLC---SLRVGATILIMPKFEITLLLEQIQRCKVTVAMVV 295
Cdd:cd05940 107 WrgGAFFAGSGGALPS------DVLYTCLPLYHSTAL---IVGwsaCLASGATLVIRKKFSASNFWDDIRKYQATIFQYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 296 PPIVLAIAKSPETEKYDLSSVRMVksgaapLGKELEDAISAKFPN----AKLGQGYGMTEAgpvlamSLGFAKepFPVKS 371
Cdd:cd05940 178 GELCRYLLNQPPKPTERKHKVRMI------FGNGLRPDIWEEFKErfgvPRIAEFYAATEG------NSGFIN--FFGKP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 372 GACG------TVVRNAEMKILDPDTGDSL----------PRNKPGE-IC-IRGNQIMKGYLnDPLATASTI------DKD 427
Cdd:cd05940 244 GAIGrnpsllRKVAPLALVKYDLESGEPIrdaegrcikvPRGEPGLlISrINPLEPFDGYT-DPAATEKKIlrdvfkKGD 322
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15232507 428 GWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAV 481
Cdd:cd05940 323 AWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANV 376
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
47-523 |
9.27e-27 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 113.04 E-value: 9.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 47 SEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAE 126
Cdd:PRK09029 14 QVRPQAIALRLN--DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 127 ISKQAKASAAKLIVTqsryvdkiknlqndgvlivttdsdaiPENCLRFSELT-QSEEPRVDSIPEKISPEDVVALPFSSG 205
Cdd:PRK09029 92 LEELLPSLTLDFALV--------------------------LEGENTFSALTsLHLQLVEGAHAVAWQPQRLATMTLTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 206 TTGLPKGVMLTHKGLVTSvAQQVDGENPnlyFNRDDVILCVLPMFHIYALnSIMLCSLRVGATiLIMPkfEITLLLEQIQ 285
Cdd:PRK09029 146 STGLPKAAVHTAQAHLAS-AEGVLSLMP---FTAQDSWLLSLPLFHVSGQ-GIVWRWLYAGAT-LVVR--DKQPLEQALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 286 RCkvTVAMVVPPIVLAIAKSPETEkydlSSVRMVKSGAAPLGKELEDAIsakfpnAKLG----QGYGMTEAGpvlamSLG 361
Cdd:PRK09029 218 GC--THASLVPTQLWRLLDNRSEP----LSLKAVLLGGAAIPVELTEQA------EQQGircwCGYGLTEMA-----STV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 362 FAKEPfPVKSGAcGTVVRNAEMKILDpdtgdslprnkpGEICIRGNQIMKGYLND----PLAtastiDKDGWLHTGDVGF 437
Cdd:PRK09029 281 CAKRA-DGLAGV-GSPLPGREVKLVD------------GEIWLRGASLALGYWRQgqlvPLV-----NDEGWFATRDRGE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 438 IDDDdELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAfVVRSkDSNISEDEIKQFVSKQ 517
Cdd:PRK09029 342 WQNG-ELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA-VVES-DSEAAVVNLAEWLQDK 418
|
....*.
gi 15232507 518 VVFYKR 523
Cdd:PRK09029 419 LARFQQ 424
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
61-481 |
3.72e-26 |
|
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: 112.38 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHN-LGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPfftpaEISKQA-----KAS 134
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNT-----NIRSKSllhcfRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 135 AAKLIVTQSRYVDKIKN----LQNDGVLIVTTDSDAIPENCLRFSEL--TQSEEPRVDSIPEKISPEDVVALPFSSGTTG 208
Cdd:cd05938 78 GAKVLVVAPELQEAVEEvlpaLRADGVSVWYLSHTSNTEGVISLLDKvdAASDEPVPASLRAHVTIKSPALYIYTSGTTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 209 LPKGVMLTH-KGLVTSVAQQVDGenpnlyFNRDDVILCVLPMFHIYA-LNSIMLCsLRVGATILIMPKFEITLLLEQIQR 286
Cdd:cd05938 158 LPKAARISHlRVLQCSGFLSLCG------VTADDVIYITLPLYHSSGfLLGIGGC-IELGATCVLKPKFSASQFWDDCRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 287 CKVTVAMVVPPIVLAIAKSPETEKYDLSSVRM-VKSGAAP-LGKELEDaisaKFPNAKLGQGYGMTEAgpvlamSLGFAK 364
Cdd:cd05938 231 HNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLaIGNGLRAdVWREFLR----RFGPIRIREFYGSTEG------NIGFFN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 365 epFPVKSGACGTVvrNAEMKIL--------DPDTGDSLpRN--------KPGE----IC-IRGNQIMKGYLNDPlatAST 423
Cdd:cd05938 301 --YTGKIGAVGRV--SYLYKLLfpfelikfDVEKEEPV-RDaqgfcipvAKGEpgllVAkITQQSPFLGYAGDK---EQT 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232507 424 IDK---------DGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAV 481
Cdd:cd05938 373 EKKllrdvfkkgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNV 439
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
187-474 |
4.33e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 112.76 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 187 SIPEkiSPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAqqvdGENPNLY-----FNRDDVILCVLPMFHI--YALNSIM 259
Cdd:PTZ00216 258 NIPE--NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGIL----ALEDRLNdligpPEEDETYCSYLPLAHImeFGVTNIF 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 260 L--------CSLRvgaTILIM------------PKFEITL--LLEQIQRckvTVAMVVPPI---------------VLAI 302
Cdd:PTZ00216 332 LargaligfGSPR---TLTDTfarphgdltefrPVFLIGVprIFDTIKK---AVEAKLPPVgslkrrvfdhayqsrLRAL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 303 AKSPET----EK-YDL------SSVRMVKSGAAPLGKELEDAISAKFpnAKLGQGYGMTEAgpVLAMSLGFAKEpfpVKS 371
Cdd:PTZ00216 406 KEGKDTpywnEKvFSApravlgGRVRAMLSGGGPLSAATQEFVNVVF--GMVIQGWGLTET--VCCGGIQRTGD---LEP 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 372 GACGTVVRNAEMKILDPD----TGDSLPRnkpGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIV 447
Cdd:PTZ00216 479 NAVGQLLKGVEMKLLDTEeykhTDTPEPR---GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRII 555
|
330 340
....*....|....*....|....*...
gi 15232507 448 DRLKELIK-YKGFQVAPAELESLLIGHP 474
Cdd:PTZ00216 556 GRVKALAKnCLGEYIALEALEALYGQNE 583
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
61-547 |
1.40e-25 |
|
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: 109.83 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLH-NLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANpfftpaeiskqakasaakli 139
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 140 vtqsryvdkiKNLQNDGVLivttdsdaipeNCLRFSELTQSeeprvdsipeKISPEDVVALPFSSGTTGLPKGVMLT-HK 218
Cdd:cd05937 63 ----------YNLSGDPLI-----------HCLKLSGSRFV----------IVDPDDPAILIYTSGTTGLPKAAAISwRR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 219 GLVTSvaqQVDGENPNLYFNrDDVILCvLPMFHIYALNSIMLCSLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPI 298
Cdd:cd05937 112 TLVTS---NLLSHDLNLKNG-DRTYTC-MPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGEL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 299 ---VLAIAKSPETEKYdlsSVRMV-KSGAAPlgkELEDAISAKFPNAKLGQGYGMTEAgpvLAMSLGFAKEPFpvKSGAC 374
Cdd:cd05937 187 cryLLSTPPSPYDRDH---KVRVAwGNGLRP---DIWERFRERFNVPEIGEFYAATEG---VFALTNHNVGDF--GAGAI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 375 G--------------TVVR---NAEMKILDPDTG--DSLPRNKPGEICIRGNQIMK----GYLNDPLATASTIDK----- 426
Cdd:cd05937 256 GhhglirrwkfenqvVLVKmdpETDDPIRDPKTGfcVRAPVGEPGEMLGRVPFKNReafqGYLHNEDATESKLVRdvfrk 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 427 -DGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMK----EEDAGEVPVAFVVRSK 501
Cdd:cd05937 336 gDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghDGRAGCAAITLEESSA 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15232507 502 D-SNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd05937 416 VpTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
30-555 |
1.85e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 110.60 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 30 IYIPNHLPLHDYIFENISEFAAKPclingptgeVYTYAD---------VHVTSRKLAAGLHNLG--VKQH----DVVMIL 94
Cdd:PRK12476 28 IALPPGTTLISLIERNIANVGDTV---------AYRYLDhshsaagcaVELTWTQLGVRLRAVGarLQQVagpgDRVAIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 95 LPNSPEVVLTFLAASFIGAIttsANPFFTPaEISKQAKASAAKLivtqsryvdkiKNLQNDGVLIVTTDSDAIpENCLRf 174
Cdd:PRK12476 99 APQGIDYVAGFFAAIKAGTI---AVPLFAP-ELPGHAERLDTAL-----------RDAEPTVVLTTTAAAEAV-EGFLR- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 175 sELTQSEEPRV---DSIPEK---------ISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQ---QVDGENPNLYFnr 239
Cdd:PRK12476 162 -NLPRLRRPRViaiDAIPDSagesfvpveLDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQmilSIDLLDRNTHG-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 240 ddviLCVLPMFHIYALNSIMLCSLRVGATILIMPkfeiTLLLEQIQR---------CKVTVAMVVPPIVLAIAKS----P 306
Cdd:PRK12476 239 ----VSWLPLYHDMGLSMIGFPAVYGGHSTLMSP----TAFVRRPQRwikalsegsRTGRVVTAAPNFAYEWAAQrglpA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 307 ETEKYDLSSVRMVkSGAAPLGKELEDAISAKF-----PNAKLGQGYGMTEAGPVLAmSLGFAKEP--------------- 366
Cdd:PRK12476 311 EGDDIDLSNVVLI-IGSEPVSIDAVTTFNKAFapyglPRTAFKPSYGIAEATLFVA-TIAPDAEPsvvyldreqlgagra 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 367 FPVKSGA--------CGTVVRNAEMKILDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPLAT------------------ 420
Cdd:PRK12476 389 VRVAADApnavahvsCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegsha 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 421 ASTIDKDGWLHTGDVGFIdDDDELFIVDRLKELIKYKGFQVAPAELE------SLLI--GHpeindVAVVAMKEEDAGEV 492
Cdd:PRK12476 469 DGAADDGTWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEatvaeaSPMVrrGY-----VTAFTVPAEDNERL 542
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232507 493 PV----AFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLANGLM 555
Cdd:PRK12476 543 VIvaerAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRL 609
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
65-490 |
2.17e-25 |
|
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: 110.21 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFtpAEISKQ-AK-ASAAKLIVTQ 142
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY--SLMSQDlAKlKHLFELLKPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 143 SRYV-------DKIKNLQNDGVLIVTTDSDAIPENCLRFSELTQSEE-PRVDSIPEKISPEDVVALPFSSGTTGLPKGVM 214
Cdd:cd05921 105 LVFAqdaapfaRALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPtAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 215 LTHkGLVTSVAQQVDGENPnlYFNRDD-VILCVLPMFHIYALNSIMLCSLRVGATILI-----MP-KFEITllLEQIQRC 287
Cdd:cd05921 185 NTQ-RMLCANQAMLEQTYP--FFGEEPpVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddgkpMPgGFEET--LRNLREI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 288 KVTVAMVVPP----IVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISA-----KFPNAKLGQGYGMTEAGPVLAM 358
Cdd:cd05921 260 SPTVYFNVPAgwemLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavatVGERIPMMAGLGATETAPTATF 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 359 SLGFAKepfpvKSGACGTVVRNAEMKIldpdtgdsLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVG-F 437
Cdd:cd05921 340 THWPTE-----RSGLIGLPAPGTELKL--------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAkL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15232507 438 IDDDDE---LFIVDRLKELIKYKG---FQVAPAELESLLIGHPEINDVAVVAMKEEDAG 490
Cdd:cd05921 407 ADPDDPakgLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLVHDAVVAGEDRAEVG 465
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
55-469 |
3.32e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 110.11 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 55 LINGPTGEVY--TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIG--------AITTSANPFF-T 123
Cdd:PLN02614 69 IVDGKPGKYVwqTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGlycvplydTLGAGAVEFIiS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 124 PAEIS----KQAKASaaKLIVTQSRYVDKIKNLQNDGVLIVTTDSDAIPENCLRFS--ELTQSEEPRVDSIPEKiSPEDV 197
Cdd:PLN02614 149 HSEVSivfvEEKKIS--ELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAwdEFLKLGEGKQYDLPIK-KKSDI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 198 VALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDG-ENPNLYFNRDDVILCVLPMFHIYAlNSIMLCSLRVGATILIMpKFE 276
Cdd:PLN02614 226 CTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLlKSANAALTVKDVYLSYLPLAHIFD-RVIEECFIQHGAAIGFW-RGD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 277 ITLLLEQIQRCKVTVAMVVPPIV-------------------------------------LAIAKSPETEKYDLS----- 314
Cdd:PLN02614 304 VKLLIEDLGELKPTIFCAVPRVLdrvysglqkklsdggflkkfvfdsafsykfgnmkkgqSHVEASPLCDKLVFNkvkqg 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 315 ---SVRMVKSGAAPLGKELEDAISAkFPNAKLGQGYGMTE--AGPVLAmslgfakepFPVKSGACGTV---VRNAEMKI- 385
Cdd:PLN02614 384 lggNVRIILSGAAPLASHVESFLRV-VACCHVLQGYGLTEscAGTFVS---------LPDELDMLGTVgppVPNVDIRLe 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 386 ----LDPDTGDSLPRnkpGEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKY-KGFQ 460
Cdd:PLN02614 454 svpeMEYDALASTPR---GEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEY 529
|
....*....
gi 15232507 461 VAPAELESL 469
Cdd:PLN02614 530 VAVENIENI 538
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
61-546 |
5.64e-25 |
|
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: 107.64 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd17645 21 GQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQsryvdkiknlqndgvlivttdsdaipenclrfseltqseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd17645 101 TN---------------------------------------------------PDDLAYVIYTSGSTGLPKGVMIEHHNL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VT---------SVAQQvdgENPNLY--FNRDDVILCVLPmfhiyalnsimlcSLRVGATILIMPKfEITLLLEQIQRCKV 289
Cdd:cd17645 130 VNlcewhrpyfGVTPA---DKSLVYasFSFDASAWEIFP-------------HLTAGAALHVVPS-ERRLDLDALNDYFN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 290 TVAmvvppIVLAIAKSPETEKY---DLSSVRMVKSGAAPLGKELEDAIsakfpnaKLGQGYGMTEAGPVLAMslgFAKEP 366
Cdd:cd17645 193 QEG-----ITISFLPTGAAEQFmqlDNQSLRVLLTGGDKLKKIERKGY-------KLVNNYGPTENTVVATS---FEIDK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 367 fPVKSGACGTVVRNAEMKILDPDTgDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWL------HTGDVGFIDD 440
Cdd:cd17645 258 -PYANIPIGKPIDNTRVYILDEAL-QLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 441 DDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNIseDEIKQFVSKQVVF 520
Cdd:cd17645 336 DGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPH--EELREWLKNDLPD 413
|
490 500
....*....|....*....|....*..
gi 15232507 521 YKrINKVFFT-DSIPKAPSGKILRKDL 546
Cdd:cd17645 414 YM-IPTYFVHlKALPLTANGKVDRKAL 439
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
62-546 |
5.98e-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: 107.95 E-value: 5.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVT 141
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSRYVDKiknLQNDGVLIVTTDSDaipenclrfseLTQSEEPRVDSIPEKispEDVVALPFSSGTTGLPKGVMLTHKGLV 221
Cdd:cd17656 92 QRHLKSK---LSFNKSTILLEDPS-----------ISQEDTSNIDYINNS---DDLLYIIYTSGTTGKPKGVQLEHKNMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 222 TSVAQQVDGENPNLYfnrDDVILCVLPMFHI-YALNSIMLCSlrvGATILIMP---KFEITLLLEQIQRCKVTVAMVVPP 297
Cdd:cd17656 155 NLLHFEREKTNINFS---DKVLQFATCSFDVcYQEIFSTLLS---GGTLYIIReetKRDVEQLFDLVKRHNIEVVFLPVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 298 IVLAIAKSPETEKYDLSSVRMVKSGAAPL--GKELEDAISAKfpNAKLGQGYGMTEAGPVLAMSlgFAKEPFPVKSGACG 375
Cdd:cd17656 229 FLKFIFSEREFINRFPTCVKHIITAGEQLviTNEFKEMLHEH--NVHLHNHYGPSETHVVTTYT--INPEAEIPELPPIG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 376 TVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGW------LHTGDVGFIDDDDELFIVDR 449
Cdd:cd17656 305 KPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 450 LKELIKYKGFQVAPAELESLLIGHPEINDvAVVAMKEEDAGEVPV-AFVVRSKDSNISedEIKQFVSKQVVFYKRINKVF 528
Cdd:cd17656 384 ADHQVKIRGYRIELGEIEAQLLNHPGVSE-AVVLDKADDKGEKYLcAYFVMEQELNIS--QLREYLAKQLPEYMIPSFFV 460
|
490
....*....|....*...
gi 15232507 529 FTDSIPKAPSGKILRKDL 546
Cdd:cd17656 461 PLDQLPLTPNGKVDRKAL 478
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
65-483 |
1.62e-24 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 107.90 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPE-------------VVLTFLAASFIGAITTSANPFFTPAEI--SK 129
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEwlialqgcfrqniTVVTIYASLGEEALCHSLNETEVTTVIcdSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 130 QAKasaaKLIVTQSRyVDKIKN---LQNDGVLIVTTDSDAIPENCLRFSELTQ--SEEPRVDSIPekiSPEDVVALPFSS 204
Cdd:PLN02387 188 QLK----KLIDISSQ-LETVKRviyMDDEGVDSDSSLSGSSNWTVSSFSEVEKlgKENPVDPDLP---SPNDIAVIMYTS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 205 GTTGLPKGVMLTHKGLVTSVAQqVDGENPNLyfNRDDVILCVLPMFHIYAL--NSIMLCslrVGATILIMPKFEITLLLE 282
Cdd:PLN02387 260 GSTGLPKGVMMTHGNIVATVAG-VMTVVPKL--GKNDVYLAYLPLAHILELaaESVMAA---VGAAIGYGSPLTLTDTSN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 283 QIQR-CKVTVAMVVPPIVLAI----------------AKSPETEK-YDLS------------------------------ 314
Cdd:PLN02387 334 KIKKgTKGDASALKPTLMTAVpaildrvrdgvrkkvdAKGGLAKKlFDIAykrrlaaiegswfgawglekllwdalvfkk 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 315 -------SVRMVKSGAAPLGKEledaiSAKFPN----AKLGQGYGMTE--AGPVLA----MSLGFAKEPFPvksgaCGTV 377
Cdd:PLN02387 414 iravlggRIRFMLSGGAPLSGD-----TQRFINiclgAPIGQGYGLTEtcAGATFSewddTSVGRVGPPLP-----CCYV 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 378 vrnaemKILDPDTGDSLPRNKP---GEICIRGNQIMKGYLNDPLAT--ASTIDKDG--WLHTGDVGFIDDDDELFIVDRL 450
Cdd:PLN02387 484 ------KLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTdeVYKVDERGmrWFYTGDIGQFHPDGCLEIIDRK 557
|
490 500 510
....*....|....*....|....*....|....
gi 15232507 451 KELIKYK-GFQVAPAELESLLIGHPEINDVAVVA 483
Cdd:PLN02387 558 KDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHA 591
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-546 |
6.67e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 107.17 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 33 PNHLPLHDYIFENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIG 112
Cdd:PRK12467 3092 PSERLVHQLIEAQVARTPEAPALVFG--DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAG 3169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 113 AITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLQNDGVLIVTTDS-DAIPENCLrfseltqseEPRVDsipek 191
Cdd:PRK12467 3170 GAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLDlNGYSENNP---------STRVM----- 3235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 192 isPEDVVALPFSSGTTGLPKGVMLTHKGLV--TSVAQQVDGENPNlyfnrDDVILcvlpmFHIYALNSI---MLCSLRVG 266
Cdd:PRK12467 3236 --GENLAYVIYTSGSTGKPKGVGVRHGALAnhLCWIAEAYELDAN-----DRVLL-----FMSFSFDGAqerFLWTLICG 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 267 ATILIMPKFEIT--LLLEQIQRCKVTVAMVVPPIVLAIAKspETEKYDLSSV-RMVKSGAAPLGKELEdAISAKFPNAKL 343
Cdd:PRK12467 3304 GCLVVRDNDLWDpeELWQAIHAHRISIACFPPAYLQQFAE--DAGGADCASLdIYVFGGEAVPPAAFE-QVKRKLKPRGL 3380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 344 GQGYGMTEAG-PVLAMSLGFAKEPFPVKSgACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATAS 422
Cdd:PRK12467 3381 TNGYGPTEAVvTVTLWKCGGDAVCEAPYA-PIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAE 3458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 423 TIDKD------GWLH-TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEdAGEVPVA 495
Cdd:PRK12467 3459 RFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVA 3537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15232507 496 FVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:PRK12467 3538 YVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-546 |
1.25e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.19 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 33 PNHLPLHDYIFENISEFAAKPCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIG 112
Cdd:PRK12316 3054 PLERGVHRLFEEQVERTPDAVALAFG--EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAG 3131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 113 AITTSANPFFTPAEISKQAKASAAKLIVTQSRyvdkIKNLQNDGVLIVTTDSDAipenclrfsELTQSEEPrvdsiPEKI 192
Cdd:PRK12316 3132 GAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH----LRLPLAQGVQVLDLDRGD---------ENYAEANP-----AIRT 3193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 193 SPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFNRDDVILCVLPM-FHIYALNsiMLCSLRVGATILI 271
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ----AYGLGVGDRVLQFTTFsFDVFVEE--LFWPLMSGARVVL 3267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 272 MPK---FEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYdlSSVRMVKSGAAPLGKELEDAISAKFPnakLGQGYG 348
Cdd:PRK12316 3268 AGPedwRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRC--TSLKRIVCGGEALPADLQQQVFAGLP---LYNLYG 3342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 349 MTEAgpVLAMSLGFAKEPFPvKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDG 428
Cdd:PRK12316 3343 PTEA--TITVTHWQCVEEGK-DAVPIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDP 3418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 429 W------LHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAmkeeDAGEVPVAFVVRSKD 502
Cdd:PRK12316 3419 FvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE 3494
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15232507 503 SNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:PRK12316 3495 AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
61-546 |
1.55e-23 |
|
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: 103.67 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAAsfigaittsanpfftpaeiskqAKASAAKLIV 140
Cdd:cd17644 23 DQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAI----------------------LKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TQSRYVDKIKNLQNDGVLIVTtdsdaipenclrfseLTQseeprvdsipekisPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVL---------------LTQ--------------PENLAYVIYTSGSTGKPKGVMIEHQSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 V--TSVAQQVDGENpnlyfNRDDVILCVLPMFHIYALNSIMLcsLRVGATILIMPK---FEITLLLEQIQRCKVTVAMVV 295
Cdd:cd17644 132 VnlSHGLIKEYGIT-----SSDRVLQFASIAFDVAAEEIYVT--LLSGATLVLRPEemrSSLEDFVQYIQQWQLTVLSLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 296 PPI--VLAIAKSPETEKYDlSSVRMVKSGA-APLGKELEDAISAKFPNAKLGQGYGMTEAGPVLAMSLGFAKEPFPVKSG 372
Cdd:cd17644 205 PAYwhLLVLELLLSTIDLP-SSLRLVIVGGeAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 373 ACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWLH--------TGDVGFIDDDDEL 444
Cdd:cd17644 284 PIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 445 FIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRI 524
Cdd:cd17644 363 EYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIP 442
|
490 500
....*....|....*....|..
gi 15232507 525 NKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd17644 443 SAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
194-444 |
2.84e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 103.44 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 194 PEDVVALPFSSGTTGLPKGVMLTHKglvtSVAQQVD------GENPNlyfNRDdvilcvLPMFHIYALNSIMLcslrvGA 267
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTHG----MFEAQIEalredyGIEPG---EID------LPTFPLFALFGPAL-----GM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 268 TILImPKFEIT--------LLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKFP 339
Cdd:PRK09274 235 TSVI-PDMDPTrpatvdpaKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 340 N-AKLGQGYGMTEAGPVLAMS----LGFAKEPFPVKSGAC-GTVVRNAEMKILDPDTGD--------SLPRNKPGEICIR 405
Cdd:PRK09274 314 PdAEILTPYGATEALPISSIEsreiLFATRAATDNGAGICvGRPVDGVEVRIIAISDAPipewddalRLATGEIGEIVVA 393
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15232507 406 GNQIMKGYLNDPLAT--ASTIDKDG--WLHTGDVGFIDDDDEL 444
Cdd:PRK09274 394 GPMVTRSYYNRPEATrlAKIPDGQGdvWHRMGDLGYLDAQGRL 436
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
75-553 |
4.88e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.78 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 75 KLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISK--QAKASAAKLIVTQSRyVDK---I 149
Cdd:PRK05857 53 GLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERfcQITDPAAALVAPGSK-MASsavP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 150 KNLQNDGVLIVTTDSDAIPENClrfseltQSEEPRVDSIPEkISPEDVVALPFSSGTTGLPKGVMLTHKGL--VTSVAQQ 227
Cdd:PRK05857 132 EALHSIPVIAVDIAAVTRESEH-------SLDAASLAGNAD-QGSEDPLAMIFTSGTTGEPKAVLLANRTFfaVPDILQK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 228 --------VDGENpnlyfnrddvILCVLPMFHIYALNSIMLCSLRVGATIlimPKFEITLLLEQIQRC-KVTVAMVVPPI 298
Cdd:PRK05857 204 eglnwvtwVVGET----------TYSPLPATHIGGLWWILTCLMHGGLCV---TGGENTTSLLEILTTnAVATTCLVPTL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 299 VLAIAKSPETEKYDLSSVRMVKSGAAplgkeleDAISA--KFPNA---KLGQGYGMTEAGpVLAMSLGFAKEPFP-VKSG 372
Cdd:PRK05857 271 LSKLVSELKSANATVPSLRLVGYGGS-------RAIAAdvRFIEAtgvRTAQVYGLSETG-CTALCLPTDDGSIVkIEAG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 373 ACGTVVRNAEMKILDPDTGD-SLPRNKP----GEICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIV 447
Cdd:PRK05857 343 AVGRPYPGVDVYLAATDGIGpTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 448 DRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED-EIKQFVS----KQVVFYK 522
Cdd:PRK05857 422 GRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAArALKHTIAarfrRESEPMA 501
|
490 500 510
....*....|....*....|....*....|.
gi 15232507 523 RINKVFFTDSIPKAPSGKILRKDLRARLaNG 553
Cdd:PRK05857 502 RPSTIVIVTDIPRTQSGKVMRASLAAAA-TA 531
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-546 |
6.42e-23 |
|
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: 101.77 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 195 EDVVALPFSSGTTGLPKGVMLTHKGLvtsvAQQVDGENPNLYFNRDDVILCVLPMFHIYA----LNSIM-----LCSLRV 265
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTF----AAQIDALRQLYGIRPGEVDLATFPLFALFGpalgLTSVIpdmdpTRPARA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 266 GATILIMPkfeitllleqIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVRMVKSGAAPLGKELEDAISAKF-PNAKLG 344
Cdd:cd05910 161 DPQKLVGA----------IRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsDEAEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 345 QGYGMTEAGPVLAMS---LGFAKEPFPVK-SGAC-GTVVRNAEMKILDPDTGD--------SLPRNKPGEICIRGNQIMK 411
Cdd:cd05910 231 TPYGATEALPVSSIGsreLLATTTAATSGgAGTCvGRPIPGVRVRIIEIDDEPiaewddtlELPRGEIGEITVTGPTVTP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 412 GYLNDPLATASTIDKDG----WLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEE 487
Cdd:cd05910 311 TYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKP 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232507 488 dAGEVPVAFVVRSKDSNISEDEIKQ---FVSKQVVFYKRINKVFFTDSIPKAP--SGKILRKDL 546
Cdd:cd05910 391 -GCQLPVLCVEPLPGTITPRARLEQelrALAKDYPHTQRIGRFLIHPSFPVDIrhNAKIFREKL 453
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
59-553 |
7.28e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 102.53 E-value: 7.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 59 PTGEV--YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSAnpF--FTPAEISKQAKAS 134
Cdd:PRK00174 92 DPGDSrkITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV--FggFSAEALADRIIDA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 135 AAKLIVT---QSR---------YVDK-IKNLQN-DGVLIVTTDSDAIPENCLR---FSELTQSEEPRVDsiPEKISPEDV 197
Cdd:PRK00174 170 GAKLVITadeGVRggkpiplkaNVDEaLANCPSvEKVIVVRRTGGDVDWVEGRdlwWHELVAGASDECE--PEPMDAEDP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 198 VALPFSSGTTGLPKGVM-----------LTHK-----------------GLVTSvaqqvdgenpnlyfnrddvilcvlpm 249
Cdd:PRK00174 248 LFILYTSGSTGKPKGVLhttggylvyaaMTMKyvfdykdgdvywctadvGWVTG-------------------------- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 250 fHIYalnsIMLCSLRVGATILImpkFEITL-------LLEQIQRCKVTVAMVVPPIVLAIAKSPET--EKYDLSSVRMVK 320
Cdd:PRK00174 302 -HSY----IVYGPLANGATTLM---FEGVPnypdpgrFWEVIDKHKVTIFYTAPTAIRALMKEGDEhpKKYDLSSLRLLG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 321 SGAAPLGkeledaisakfPNA------KLGQG-------YGMTEAGpvlamslGFAKEPFP----VKSGACGTVVRNAEM 383
Cdd:PRK00174 374 SVGEPIN-----------PEAwewyykVVGGErcpivdtWWQTETG-------GIMITPLPgatpLKPGSATRPLPGIQP 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 384 KILDpDTGDSLPRNKPGEICIRgnqimkgylnDPL-ATASTIDKD-------------GWLHTGDVGFIDDDDELFIVDR 449
Cdd:PRK00174 436 AVVD-EEGNPLEGGEGGNLVIK----------DPWpGMMRTIYGDherfvktyfstfkGMYFTGDGARRDEDGYYWITGR 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 450 LKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISED---EIKQFVSKQVVFYKRINK 526
Cdd:PRK00174 505 VDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRKEIGPIAKPDV 584
|
570 580
....*....|....*....|....*..
gi 15232507 527 VFFTDSIPKAPSGKILRKDLRArLANG 553
Cdd:PRK00174 585 IQFAPGLPKTRSGKIMRRILRK-IAEG 610
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
42-546 |
1.00e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 101.51 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 42 IFENISEFAAK----PCLINgpTGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIG----A 113
Cdd:PRK04813 4 IIETIEEFAQTqpdfPAYDY--LGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayiP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 114 ITTSanpffTPAE-ISKQAKASAAKLIvtqsryvdkiknlqndgvlIVTTDSDAIPENC--LRFSELTQSEEPRVDSIPE 190
Cdd:PRK04813 82 VDVS-----SPAErIEMIIEVAKPSLI-------------------IATEELPLEILGIpvITLDELKDIFATGNPYDFD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 191 K-ISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVD----GENPNLY----FNRDdvilcvLPMFHIYAlnsimlc 261
Cdd:PRK04813 138 HaVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEdfalPEGPQFLnqapYSFD------LSVMDLYP------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 262 SLRVGATILIMPKFEIT---LLLEQIQRCKVTVAMVVPPIVLAIAKSPE--TEKYDlSSVRMVKSGAApLGKELEDAISA 336
Cdd:PRK04813 205 TLASGGTLVALPKDMTAnfkQLFETLPQLPINVWVSTPSFADMCLLDPSfnEEHLP-NLTHFLFCGEE-LPHKTAKKLLE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 337 KFPNAKLGQGYGMTEAgpVLAMS----------------LGFAKEpfpvksgacgtvvrNAEMKILDpDTGDSLPRNKPG 400
Cdd:PRK04813 283 RFPSATIYNTYGPTEA--TVAVTsieitdemldqykrlpIGYAKP--------------DSPLLIID-EEGTKLPDGEQG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 401 EICIRGNQIMKGYLNDPLATAS---TIDKDGWLHTGDVGFIdDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEIN 477
Cdd:PRK04813 346 EIVISGPSVSKGYLNNPEKTAEaffTFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVE 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232507 478 DVAVVAMKEEDAGEVPVAFVVrSKDSNISED-----EIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:PRK04813 425 SAVVVPYNKDHKVQYLIAYVV-PKEEDFEREfeltkAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-548 |
2.02e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.34 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 33 PNHLPLHDYIFENISEFAAKPCLINGPtgEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIG 112
Cdd:PRK12316 508 PLQRGVHRLFEEQVERTPEAPALAFGE--ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAG 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 113 AITTSANPFFtPAE-ISKQAKASAAKLIVTQSRYVDKIKnlQNDGVLIVTTDSDAIpenclrFSELTQSEEPRVdsipeK 191
Cdd:PRK12316 586 GAYVPLDPEY-PAErLAYMLEDSGVQLLLSQSHLGRKLP--LAAGVQVLDLDRPAA------WLEGYSEENPGT-----E 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 192 ISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSV--AQQVdgenpnlyFNRD--DVILCVLPmFHIYALNSIMLCSLRVGA 267
Cdd:PRK12316 652 LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLcwMQQA--------YGLGvgDTVLQKTP-FSFDVSVWEFFWPLMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 268 TILIMPK---FEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEkyDLSSVRMVKSGAAPLGKELEDAISAKFPNAKLG 344
Cdd:PRK12316 723 RLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 345 QGYGMTEAGPVLAMS--LGFAKEPFPVksgacGTVVRNAEMKILDPDtGDSLPRNKPGEICIRGNQIMKGYLNDPLATAS 422
Cdd:PRK12316 801 NLYGPTEAAIDVTHWtcVEEGGDSVPI-----GRPIANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHGRPGLTAE 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 423 T------IDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKeedaGEVPVAF 496
Cdd:PRK12316 875 RfvpspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGY 950
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15232507 497 VVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRA 548
Cdd:PRK12316 951 VVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
80-543 |
2.38e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 100.97 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 80 LHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTqSRYvdkikNLQNDGVLI 159
Cdd:PTZ00237 109 LLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIIT-TNY-----GILNDEIIT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 160 VTTD-SDAI------PENCL---RFSELTQSEEPRVDSIP------------EKI-----SP--EDV-------VALPFS 203
Cdd:PTZ00237 183 FTPNlKEAIelstfkPSNVItlfRNDITSESDLKKIETIPtipntlswydeiKKIkennqSPfyEYVpvesshpLYILYT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 204 SGTTGLPKGVMLTHK----GLVTSVAQQVDGENPNLYFNRDDVILCVLPMFhIYAlnsimlcSLRVGATI------LIMP 273
Cdd:PTZ00237 263 SGTTGNSKAVVRSNGphlvGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGF-LYG-------SLSLGNTFvmfeggIIKN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 274 KFEITLLLEQIQRCKVTVAMVVPPIVLAIAKS-PETE----KYDLSSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYG 348
Cdd:PTZ00237 335 KHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdPEATiirsKYDLSNLKEIWCGGEVIEESIPEYIENKL-KIKSSRGYG 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 349 MTEAGPVLAMSLGFAKEPFpvksGACGTVVRNAEMKILDPDtGDSLPRNKPGEICIRgnqimkgyLNDPLATASTIDKD- 427
Cdd:PTZ00237 414 QTEIGITYLYCYGHINIPY----NATGVPSIFIKPSILSED-GKELNVNEIGEVAFK--------LPMPPSFATTFYKNd 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 428 -----------GWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVAF 496
Cdd:PTZ00237 481 ekfkqlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGL 560
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15232507 497 VVRSKDSNIS-------EDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILR 543
Cdd:PTZ00237 561 LVLKQDQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
52-542 |
9.70e-22 |
|
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: 99.27 E-value: 9.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 52 KPCLINGPTGEV--YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISK 129
Cdd:cd05943 85 PAAIYAAEDGERteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 130 QAKASAAKLIVTQSRYV---------DKIKNLQnDG-------VLIVTTDSDAIPE-----NCLRFSELtQSEEPRVDSI 188
Cdd:cd05943 165 RFGQIEPKVLFAVDAYTyngkrhdvrEKVAELV-KGlpsllavVVVPYTVAAGQPDlskiaKALTLEDF-LATGAAGELE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 189 PEKISPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGENpNLYFNrdDVIL----CVLPMFHiyalnsIMLCSLR 264
Cdd:cd05943 243 FEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHC-DLRPG--DRLFyyttCGWMMWN------WLVSGLA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 265 VGATILIM------PKFEItlLLEQIQRCKVTVAMVVPPIVLAIAKS--PETEKYDLSSVRMVKSGAAPLGKELEDAISA 336
Cdd:cd05943 314 VGATIVLYdgspfyPDTNA--LWDLADEEGITVFGTSAKYLDALEKAglKPAETHDLSSLRTILSTGSPLKPESFDYVYD 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 337 KF-PNAKLGQGYGMTEagpVLAMSLGFAKEpFPVKSGACGTVVRNAEMKILDPDtGDSLpRNKPGE-ICIRGNQIMK-GY 413
Cdd:cd05943 392 HIkPDVLLASISGGTD---IISCFVGGNPL-LPVYRGEIQCRGLGMAVEAFDEE-GKPV-WGEKGElVCTKPFPSMPvGF 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 414 LNDPLAT---ASTIDK-DG-WLHtGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEED 488
Cdd:cd05943 466 WNDPDGSryrAAYFAKyPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKD 544
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232507 489 AGEVPVAFVVRSKDSNISED-------EIKQFVSKQVVfykrINKVFFTDSIPKAPSGKIL 542
Cdd:cd05943 545 GDERVILFVKLREGVELDDElrkrirsTIRSALSPRHV----PAKIIAVPDIPRTLSGKKV 601
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
190-549 |
1.33e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 97.41 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 190 EKISPEDVVALPFSSGTTGLPKGVMLTHkglvTSVAQQVDGENPNLYFNRDDVILCVLPMFHIYALNSIMLCSLRVGATI 269
Cdd:PRK08308 96 VNYLAEEPSLLQYSSGTTGEPKLIRRSW----TEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 270 LIM----PKFeitlLLEQIQRCKVTVAMVVPPIVLAIAK-SPETEKYDlssvRMVKSGAaPLGKELEDAISAKfpNAKLG 344
Cdd:PRK08308 172 VIItnknPKF----ALNILRNTPQHILYAVPLMLHILGRlLPGTFQFH----AVMTSGT-PLPEAWFYKLRER--TTYMM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 345 QGYGMTEAGPV-LAMSLGFAKEpfpvksgaCGTVVRNAEMKIldpdtGDSlpRNKPGEICIRGNQimkgylndplataST 423
Cdd:PRK08308 241 QQYGCSEAGCVsICPDMKSHLD--------LGNPLPHVSVSA-----GSD--ENAPEEIVVKMGD-------------KE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 424 IdkdgwlHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGE-VPVAFvvrSKD 502
Cdd:PRK08308 293 I------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKV---ISH 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15232507 503 SNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRAR 549
Cdd:PRK08308 364 EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELG 410
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
244-547 |
1.18e-20 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 94.68 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 244 LCVLPMFHIYALNSIMLcSLRVGATILIMP---------------KFEITLLLEQIQRckvtvamvvppiVLaiaksPET 308
Cdd:PRK07445 164 FCVLPLYHVSGLMQFMR-SFLTGGKLVILPykrlksgqelppnpsDFFLSLVPTQLQR------------LL-----QLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 309 EKYdLSSVRMVKSGAAPLGKELEDAisAKFPNAKLGQGYGMTE-AGPVLAMSlgfaKEPFPVKSGACGTVVRNAEMKILD 387
Cdd:PRK07445 226 PQW-LAQFRTILLGGAPAWPSLLEQ--ARQLQLRLAPTYGMTEtASQIATLK----PDDFLAGNNSSGQVLPHAQITIPA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 388 PDTGdslprnkpgEICIRGNQIMKGYLNDplatasTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELE 467
Cdd:PRK07445 299 NQTG---------NITIQAQSLALGYYPQ------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 468 SLLIGHPEINDVAVVAMKEEDAGEVPVAFVVrSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PRK07445 364 AAILATGLVQDVCVLGLPDPHWGEVVTAIYV-PKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
193-548 |
4.78e-20 |
|
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: 92.85 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 193 SPEDVVALPFSSGTTGLPKGVMLTHKGLV---TSVAQQVDGENpnlyfNRDDVILcvlpMFHIYALN-SI--MLCSLRVG 266
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrTSLSERYFGRD-----NGDEAVL----FFSNYVFDfFVeqMTLALLNG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 267 ATILIMP---KFEITLLLEQIQRCKVTVAMVVPPIVlaiakspetEKYDLS---SVRMVKSGAAPLGKELEDAISAKFPn 340
Cdd:cd17648 163 QKLVVPPdemRFDPDRFYAYINREKVTYLSGTPSVL---------QQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRFA- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 341 AKLGQGYGMTEAgpvlamSLGFAKEPFPV---KSGACGTVVRNAEMKILDPDTgDSLPRNKPGEICIRGNQIMKGYLNDP 417
Cdd:cd17648 233 GLIINAYGPTET------TVTNHKRFFPGdqrFDKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 418 LATA-------------------STIDKDG----WLHTGDVGFIDDDDelfivdrlkELIKYKGFQVAPAELESLLIGHP 474
Cdd:cd17648 306 ELTAerflpnpfqteqerargrnARLYKTGdlvrWLPSGELEYLGRND---------FQVKIRGQRIEPGEVEAALASYP 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232507 475 EINDVAVVAMKEEDAGEVP-----VAFVVrSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKIlrkDLRA 548
Cdd:cd17648 377 GVRECAVVAKEDASQAQSRiqkylVGYYL-PEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL---DVRA 451
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
65-481 |
9.78e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 92.98 E-value: 9.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAI------TTSANP---FFTPAEIS----KQA 131
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITyvplydTLGANAvefIINHAEVSiafvQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 132 KASAakLIVTQSRYVDKIKNLQNDGVLIVTTDSDA--IPENCLRFSELTQSEEPRVDsIPEKiSPEDVVALPFSSGTTGL 209
Cdd:PLN02861 159 KISS--ILSCLPKCSSNLKTIVSFGDVSSEQKEEAeeLGVSCFSWEEFSLMGSLDCE-LPPK-QKTDICTIMYTSGTTGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 210 PKGVMLTHKGLVTSVAQqVDG--ENPNLYFNRDDVILCVLPMFHIYALNSIMLCsLRVGATILIMpKFEITLLLEQIQRC 287
Cdd:PLN02861 235 PKGVILTNRAIIAEVLS-TDHllKVTDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFW-QGDIRYLMEDVQAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 288 KVTVAMVVPPIVL--------------AIAK-----------------------SPETEKYDLSS--------VRMVKSG 322
Cdd:PLN02861 312 KPTIFCGVPRVYDriytgimqkissggMLRKklfdfaynyklgnlrkglkqeeaSPRLDRLVFDKikeglggrVRLLLSG 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 323 AAPLGKELEDAISAKfPNAKLGQGYGMTEAGPVLAMSLGfakEPFPVkSGACGTVVRNAEMKILD-PDTG-DSLPRNKPG 400
Cdd:PLN02861 392 AAPLPRHVEEFLRVT-SCSVLSQGYGLTESCGGCFTSIA---NVFSM-VGTVGVPMTTIEARLESvPEMGyDALSDVPRG 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 401 EICIRGNQIMKGYLNDPLATASTIdKDGWLHTGDVGFIDDDDELFIVDRLKELIKY-KGFQVAPAELESLLIGHPEINDV 479
Cdd:PLN02861 467 EICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIASI 545
|
..
gi 15232507 480 AV 481
Cdd:PLN02861 546 WV 547
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
65-546 |
1.67e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 92.80 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSR 144
Cdd:PRK10252 485 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTAD 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 145 YVDKIKNLQNDGVLIVttdsdaipenclrfseltQSEEPRVDSIPEKIS-PEDVVALPFSSGTTGLPKGVMLTHKGLVts 223
Cdd:PRK10252 565 QLPRFADVPDLTSLCY------------------NAPLAPQGAAPLQLSqPHHTAYIIFTSGSTGRPKGVMVGQTAIV-- 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 224 vaqqvdgenpnlyfNR------------DDVILCVLPmfhiyalnsimlCS-----------LRVGATiLIMPKFEI--- 277
Cdd:PRK10252 625 --------------NRllwmqnhypltaDDVVLQKTP------------CSfdvsvweffwpFIAGAK-LVMAEPEAhrd 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 278 -TLLLEQIQRCKVTVAMVVPPIVLAI--AKSPETEKYDLSSVRMV-KSGAApLGKELEDAISAKFpNAKLGQGYGMTEAG 353
Cdd:PRK10252 678 pLAMQQFFAEYGVTTTHFVPSMLAAFvaSLTPEGARQSCASLRQVfCSGEA-LPADLCREWQQLT-GAPLHNLYGPTEAA 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 354 PVLAMSLGFAKEPFPVKSGAC--GTVVRNAEMKILDpDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTIDKDGWL- 430
Cdd:PRK10252 756 VDVSWYPAFGEELAAVRGSSVpiGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAp 834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 431 -----HTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVP------VAFVVR 499
Cdd:PRK10252 835 germyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGgdarqlVGYLVS 914
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15232507 500 SKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDL 546
Cdd:PRK10252 915 QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
65-509 |
2.37e-19 |
|
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: 91.75 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLH-NLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTsanPFftpaeiskQAKASAAKL--IVT 141
Cdd:cd17632 69 TYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSV---PL--------QAGASAAQLapILA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 142 QSR---------YVDKIKNLQNDG-----VLI------VTTDSDA------------IPENCLRFSELTQSEEPRVDSIP 189
Cdd:cd17632 138 ETEprllavsaeHLDLAVEAVLEGgtpprLVVfdhrpeVDAHRAAlesarerlaavgIPVTTLTLIAVRGRDLPPAPLFR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 190 EKISPEDVVALPFSSGTTGLPKGVMLTHKgLVTSVAQQVDGENPNlyFNRDDVILCVLPMFHIYALNSImLCSLRVGATI 269
Cdd:cd17632 218 PEPDDDPLALLIYTSGSTGTPKGAMYTER-LVATFWLKVSSIQDI--RPPASITLNFMPMSHIAGRISL-YGTLARGGTA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 270 LIMPKFEITLLLEQIQRCKVTVAMVVPPI--------------VLAIAKSPET----------EKYDLSSVRMVKSGAAP 325
Cdd:cd17632 294 YFAAASDMSTLFDDLALVRPTELFLVPRVcdmlfqryqaeldrRSVAGADAETlaervkaelrERVLGGRLLAAVCGSAP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 326 LGKELEDAISAKFpNAKLGQGYGMTEAGPVLAmsLGFAKEPfPVksgacgtvvrnAEMKILD-PDTG----DS-LPRnkp 399
Cdd:cd17632 374 LSAEMKAFMESLL-DLDLHDGYGSTEAGAVIL--DGVIVRP-PV-----------LDYKLVDvPELGyfrtDRpHPR--- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 400 GEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKY-KGFQVAPAELESLLIGHPEIND 478
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQ 515
|
490 500 510
....*....|....*....|....*....|.
gi 15232507 479 VAVVAMKEEdagEVPVAFVVRSKDSNISEDE 509
Cdd:cd17632 516 IFVYGNSER---AYLLAVVVPTQDALAGEDT 543
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
465-540 |
4.49e-19 |
|
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: 81.44 E-value: 4.49e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232507 465 ELESLLIGHPEINDVAVVAMKEEDAGEVPVAFVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGK 540
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
65-547 |
6.33e-19 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 90.34 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 65 TYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQS- 143
Cdd:PLN02654 122 TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNa 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 -RYVDKIKNLQN--DGVLIVTTDSDAIPENCLRFS-------ELTQSEEPR----VDSIP--------EKISPEDVVALP 201
Cdd:PLN02654 202 vKRGPKTINLKDivDAALDESAKNGVSVGICLTYEnqlamkrEDTKWQEGRdvwwQDVVPnyptkcevEWVDAEDPLFLL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 202 FSSGTTGLPKGVMLTHKGLV----TSVAQQVDGENPNLYFNRDDvilCVLPMFHIYALNSIMLCslrvGATILImpkFEI 277
Cdd:PLN02654 282 YTSGSTGKPKGVLHTTGGYMvytaTTFKYAFDYKPTDVYWCTAD---CGWITGHSYVTYGPMLN----GATVLV---FEG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 278 TLLLEQIQRC-------KVTVAMVVPPIVLAIAKSPE--TEKYDLSSVRMVKSGAAPLGKE-----LEDAISAKFPnakL 343
Cdd:PLN02654 352 APNYPDSGRCwdivdkyKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLRVLGSVGEPINPSawrwfFNVVGDSRCP---I 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 344 GQGYGMTEAGpvlamslGFAKEP----FPVKSGACGTVVRNAEMKILDpDTGDSLPRNKPGEICIRGN--QIMKGYLNDP 417
Cdd:PLN02654 429 SDTWWQTETG-------GFMITPlpgaWPQKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKKSwpGAFRTLYGDH 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 418 LATASTIDK--DGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVA 495
Cdd:PLN02654 501 ERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYA 580
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15232507 496 FVVRSKDSNISEDEIKQFVS---KQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:PLN02654 581 FVTLVEGVPYSEELRKSLILtvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
61-547 |
3.93e-18 |
|
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: 87.10 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 61 GEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIV 140
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 141 TqsRYVDKIKnlqndgvlivttdsdaipenclrfseLTQSEEPRvdSIPEKiSPEDVVALPFSSGTTGLPKGVMLTHKGL 220
Cdd:cd05939 81 F--NLLDPLL--------------------------TQSSTEPP--SQDDV-NFRDKLFYIYTSGTTGLPKAAVIVHSRY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 221 VTSVAqqvdGENPNLYFNRDDVILCVLPMFHIYAlnSIMLC--SLRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPI 298
Cdd:cd05939 130 YRIAA----GAYYAFGMRPEDVVYDCLPLYHSAG--GIMGVgqALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 299 ---VLAIAKSPETEKYdlsSVRMVksgaapLGKELEDAISAKFPN----AKLGQGYGMTEAGPVLAmslgfakePFPVKS 371
Cdd:cd05939 204 cryLLAQPPSEEEQKH---NVRLA------VGNGLRPQIWEQFVRrfgiPQIGEFYGATEGNSSLV--------NIDNHV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 372 GACGTVVRNAE----MKIL--DPDTGDsLPRNKPGeICIRGN---------QIMK--------GYLNDPlATASTIDKDG 428
Cdd:cd05939 267 GACGFNSRILPsvypIRLIkvDEDTGE-LIRDSDG-LCIPCQpgepgllvgKIIQndplrrfdGYVNEG-ATNKKIARDV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 429 WLHtGDVGFIDDD----DEL---FIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAV----VAMKEEDAGEVPVAFV 497
Cdd:cd05939 344 FKK-GDSAFLSGDvlvmDELgylYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygveVPGVEGRAGMAAIVDP 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15232507 498 VRSKDSNIsedeIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLR 547
Cdd:cd05939 423 ERKVDLDR----FSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
194-548 |
7.68e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.92 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 194 PEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVdgenPNLYFNRDDVILCVLPM-FHIYALNsiMLCSLRVGATILIM 272
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKV----PYLALSEADVIAQTASQsFDISVWQ--FLAAPLFGARVEIV 3941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 273 PK---FEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEkydLSSVR-MVKSGAApLGKELEDAISAKFPNAKLGQGYG 348
Cdd:PRK05691 3942 PNaiaHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQA---LDGLRwMLPTGEA-MPPELARQWLQRYPQIGLVNAYG 4017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 349 MTEAGPVLAMslgfakepFPVKSGAC-------GTVVRNAEMKILDPDTgDSLPRNKPGEICIRGNQIMKGYLNDPLATA 421
Cdd:PRK05691 4018 PAECSDDVAF--------FRVDLASTrgsylpiGSPTDNNRLYLLDEAL-ELVPLGAVGELCVAGTGVGRGYVGDPLRTA 4088
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 422 STIDKDGW-------LHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDvAVVAMKEEDAGEVPV 494
Cdd:PRK05691 4089 LAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLV 4167
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232507 495 AFVVRSkDSNISE----DEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRA 548
Cdd:PRK05691 4168 GYLVPH-QTVLAQgallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPA 4224
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
183-512 |
7.98e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 87.07 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 183 PRVDSIPEKisPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQ---QVDgenpnlyFNRDDVILCVLPMFHIYALNSIM 259
Cdd:PRK08043 355 PRLAQVKQQ--PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQiktIAD-------FTPNDRFMSALPLFHSFGLTVGL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 260 LCSLRVGATILIMPK---FEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPetekYDLSSVRMVKSGAAPLGKELEDAISA 336
Cdd:PRK08043 426 FTPLLTGAEVFLYPSplhYRIVPELVYDRNCTVLFGTSTFLGNYARFANP----YDFARLRYVVAGAEKLQESTKQLWQD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 337 KFpNAKLGQGYGMTEAGPVLAMSLgfakePFPVKSGACGTVVRNAEMKILdpdtgdSLPR-NKPGEICIRGNQIMKGYL- 414
Cdd:PRK08043 502 KF-GLRILEGYGVTECAPVVSINV-----PMAAKPGTVGRILPGMDARLL------SVPGiEQGGRLQLKGPNIMNGYLr 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 415 -------NDPLA-TASTIDKDGWLHTGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIG-HPEINDvAVVAMK 485
Cdd:PRK08043 570 vekpgvlEVPTAeNARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKQH-ATAIKS 648
|
330 340
....*....|....*....|....*..
gi 15232507 486 EEDAGEvpvAFVVRSKDSNISEDEIKQ 512
Cdd:PRK08043 649 DASKGE---ALVLFTTDSELTREKLQQ 672
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
57-326 |
1.72e-17 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 86.00 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 57 NGPTGEVyTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAA 136
Cdd:PRK03584 109 DGPRREL-SWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 137 KLIVTQSRY----------------VDKIKNLQNdgVLIV----TTDSDAIPENCLRFSELTQSEEPrvdsipekiSPED 196
Cdd:PRK03584 188 KVLIAVDGYryggkafdrrakvaelRAALPSLEH--VVVVpylgPAAAAAALPGALLWEDFLAPAEA---------AELE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 197 VVALPF--------SSGTTGLPK-------GVMLTHkglVTSVAQQVDgenpnlyFNRDDVilcvlpmFHIYALNSIM-- 259
Cdd:PRK03584 257 FEPVPFdhplwilySSGTTGLPKcivhghgGILLEH---LKELGLHCD-------LGPGDR-------FFWYTTCGWMmw 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232507 260 ---LCSLRVGATILIM------PKFEItlLLEQIQRCKVTVAMVVPPIVLAIAKS---PeTEKYDLSSVRMVKSGAAPL 326
Cdd:PRK03584 320 nwlVSGLLVGATLVLYdgspfyPDPNV--LWDLAAEEGVTVFGTSAKYLDACEKAglvP-GETHDLSALRTIGSTGSPL 395
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
195-551 |
2.45e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 83.56 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 195 EDVVALPFS-SGTTGLPKGVMLTHKGLVTS---VAQQVDGENPnlyfnrddvILCVLPMFHIYALnSIMLCSLRVGATIL 270
Cdd:PRK07824 34 DDDVALVVAtSGTTGTPKGAMLTAAALTASadaTHDRLGGPGQ---------WLLALPAHHIAGL-QVLVRSVIAGSEPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 271 IMP---KFEITLLLEQIQRCK---VTVAMVvpPIVLAIA-KSPE-TEKydLSSVRMVKSGAAPLGKEleDAISAKFPNAK 342
Cdd:PRK07824 104 ELDvsaGFDPTALPRAVAELGggrRYTSLV--PMQLAKAlDDPAaTAA--LAELDAVLVGGGPAPAP--VLDAAAAAGIN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 343 LGQGYGMTEAgpvlamslgfakepfpvkSGAC---GTVVRNAEMKILDpdtgdslprnkpGEICIRGNQIMKGYLN---- 415
Cdd:PRK07824 178 VVRTYGMSET------------------SGGCvydGVPLDGVRVRVED------------GRIALGGPTLAKGYRNpvdp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 416 DPLAtastidKDGWLHTGDVGFIDDDdELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAGEVPVA 495
Cdd:PRK07824 228 DPFA------EPGWFRTDDLGALDDG-VLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15232507 496 FVVRSKDSNISEDEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRARLA 551
Cdd:PRK07824 301 AVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFA 356
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
172-550 |
3.68e-17 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 84.43 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 172 LRFSELTQSEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVMLTHKGL---VTSVAQQVDGENPNlyfnrdDVILCVLP 248
Cdd:PRK05851 129 VTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVlsnLRGLNARVGLDAAT------DVGCSWLP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 249 MFHIYALnSIMLCSLRVGATILIMPK--FEITLL--LEQIQRCKVTvaMVVPPIVL--AIAK-SPETEKYDLSSVRMVKS 321
Cdd:PRK05851 203 LYHDMGL-AFLLTAALAGAPLWLAPTtaFSASPFrwLSWLSDSRAT--LTAAPNFAynLIGKyARRVSDVDLGALRVALN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 322 GAAPL---GKELEDAISAKF---PNAkLGQGYGMTEAG-----PVLAMSLGFAKEPFPVKSGA-----CGTVVRNAEMKI 385
Cdd:PRK05851 280 GGEPVdcdGFERFATAMAPFgfdAGA-AAPSYGLAESTcavtvPVPGIGLRVDEVTTDDGSGArrhavLGNPIPGMEVRI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 386 LDPDTGDSLPRNKPGEICIRGNQIMKGYLNDPlatasTIDKDGWLHTGDVGFIDDDdELFIVDRLKELIKYKGFQVAPAE 465
Cdd:PRK05851 359 SPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDG-GLVVCGRAKELITVAGRNIFPTE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 466 LESLLIGHPEINDVAVVAMKEEDAGEVP---VAFVVRSKDSNISEDEIKQFVSKQ-------VVFYKrinkvffTDSIPK 535
Cdd:PRK05851 433 IERVAAQVRGVREGAVVAVGTGEGSARPglvIAAEFRGPDEAGARSEVVQRVASEcgvvpsdVVFVA-------PGSLPR 505
|
410
....*....|....*
gi 15232507 536 APSGKILRKDLRARL 550
Cdd:PRK05851 506 TSSGKLRRLAVKRSL 520
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
189-476 |
8.69e-17 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 82.50 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 189 PEKI-SPEDVVALPF---------------------------SSGTTGLPKGVMLTHKGL---VTSVAQqvdgenpNLY- 236
Cdd:COG1541 49 PDDIkSLEDLAKLPFttkedlrdnypfglfavpleeivrihaSSGTTGKPTVVGYTRKDLdrwAELFAR-------SLRa 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 237 --FNRDDVILCVLP--------MFHiYALNsimlcslRVGATILIMPKFEITLLLEQIQRCKVTVAMVVPPIVLAIAKSP 306
Cdd:COG1541 122 agVRPGDRVQNAFGyglftgglGLH-YGAE-------RLGATVIPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 307 ETEKYDL--SSVRMVKSGAAPLGKELEDAISAKFpNAKLGQGYGMTEAGPVLAMSlgfakepfpvksgaC----GTVVRN 380
Cdd:COG1541 194 EEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERW-GIKAYDIYGLTEVGPGVAYE--------------CeaqdGLHIWE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 381 AE--MKILDPDTGDSLPRNKPGEICIrgnqimkgylndplataSTIDKDGW----LHTGDVGFIDDDDE---------LF 445
Cdd:COG1541 259 DHflVEIIDPETGEPVPEGEEGELVV-----------------TTLTKEAMplirYRTGDLTRLLPEPCpcgrthpriGR 321
|
330 340 350
....*....|....*....|....*....|.
gi 15232507 446 IVDRLKELIKYKGFQVAPAELESLLIGHPEI 476
Cdd:COG1541 322 ILGRADDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-548 |
9.35e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 84.45 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 33 PNHLPLHDYIFENISEFAAK----PCLINGptGEVYTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAA 108
Cdd:PRK05691 2181 AGEARLDQTLHGLFAAQAARtpqaPALTFA--GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAI 2258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 109 SFIGAITTSANPFFTPAEISKQAKASAAKLIVTQSRYVDKIKNLqndgvlivttdsdaiPENCLRFSelTQSEEPRVDSI 188
Cdd:PRK05691 2259 LKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGEL---------------PAGVARWC--LEDDAAALAAY 2321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 189 PEkiSPEDVVALP-------FSSGTTGLPKGVMLTHKGLVTSVAQQVD--GENPnlyfnrDDvilCVLpmfHIYALN--- 256
Cdd:PRK05691 2322 SD--APLPFLSLPqhqayliYTSGSTGKPKGVVVSHGEIAMHCQAVIErfGMRA------DD---CEL---HFYSINfda 2387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 257 --SIMLCSLRVGATILIMPKF-----EI-TLLLEQiqrcKVTVAMVVPPIVLAIAKSPETEkYDLSSVRMVKSGAAPLGK 328
Cdd:PRK05691 2388 asERLLVPLLCGARVVLRAQGqwgaeEIcQLIREQ----QVSILGFTPSYGSQLAQWLAGQ-GEQLPVRMCITGGEALTG 2462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 329 ELEDAISAKFPNAKLGQGYGMTEAgpvLAMSLG-FAKEPFPVKSGAC--GTVVRNAEMKILDPDTGdSLPRNKPGEICIR 405
Cdd:PRK05691 2463 EHLQRIRQAFAPQLFFNAYGPTET---VVMPLAcLAPEQLEEGAASVpiGRVVGARVAYILDADLA-LVPQGATGELYVG 2538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 406 GNQIMKGYLNDPLATASTIDKDGWLH-------TGDVGFIDDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEIND 478
Cdd:PRK05691 2539 GAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE 2618
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232507 479 VAVVAMKEEdAGEVPVAFVVRSKDSNISE------DEIKQFVSKQVVFYKRINKVFFTDSIPKAPSGKILRKDLRA 548
Cdd:PRK05691 2619 AVVLALDTP-SGKQLAGYLVSAVAGQDDEaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPA 2693
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
62-543 |
3.20e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 81.53 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 62 EVYTYADVHVTSRKLAAGLHNLGVKQhDVVMILLPNSPEVVLTFLAASFIGAIttsANPFFTPA------EISKQAKASA 135
Cdd:PRK05850 34 ETLTWSQLYRRTLNVAEELRRHGSTG-DRAVILAPQGLEYIVAFLGALQAGLI---AVPLSVPQggahdeRVSAVLRDTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 136 AKLIVTQSRYVDKIK------NLQNDGVlIVTTDSdaipenclrfSELTQSEEPRVDSIPekisPEDVVALPFSSGTTGL 209
Cdd:PRK05850 110 PSVVLTTSAVVDDVTeyvapqPGQSAPP-VIEVDL----------LDLDSPRGSDARPRD----LPSTAYLQYTSGSTRT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 210 PKGVMLTHKGLVTSVAQQVDGenpnlYFNRDDVIL-----CV--LPMFH----IYALNSIMLCSLRvgaTILIMPkfeit 278
Cdd:PRK05850 175 PAGVMVSHRNVIANFEQLMSD-----YFGDTGGVPppdttVVswLPFYHdmglVLGVCAPILGGCP---AVLTSP----- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 279 llleqiqrckvtVAMVVPPI--VLAIAKSPET---------------------EKYDLSSVRMVKSGA-----APLGKEL 330
Cdd:PRK05850 242 ------------VAFLQRPArwMQLLASNPHAfsaapnfafelavrktsdddmAGLDLGGVLGIISGServhpATLKRFA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 331 EDAISAKFPNAKLGQGYGMTEA-----------GPVLA------MSLGFAKepfPVKSGAcGT------VVRNAEMKILD 387
Cdd:PRK05850 310 DRFAPFNLRETAIRPSYGLAEAtvyvatrepgqPPESVrfdyekLSAGHAK---RCETGG-GTplvsygSPRSPTVRIVD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 388 PDTGDSLPRNKPGEICIRGNQIMKGYLNDPLATASTID----------KDG-WLHTGDVGFIdDDDELFIVDRLKELIKY 456
Cdd:PRK05850 386 PDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtPEGpWLRTGDLGFI-SEGELFIVGRIKDLLIV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 457 KGFQVAPAELESLLighPEINDVAVVAMK-EEDAGEVPVAFVVRSKDSNISEDEIKQF--VSKQVV-FYKRINKVFFTD- 531
Cdd:PRK05850 465 DGRNHYPDDIEATI---QEITGGRVAAISvPDDGTEKLVAIIELKKRGDSDEEAMDRLrtVKREVTsAISKSHGLSVADl 541
|
570
....*....|....*...
gi 15232507 532 ------SIPKAPSGKILR 543
Cdd:PRK05850 542 vlvapgSIPITTSGKIRR 559
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
57-556 |
5.60e-16 |
|
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: 80.86 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 57 NGPTGEVYTYADVHVTSRKLAAGLHN-LGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEIS------- 128
Cdd:cd05905 8 KGKEATTLTWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGfllgtck 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 129 -KQAKASAA---KLIVTQSRYVDKIKNLQNDGV--LIVTTDsdaIPENcLRFSELTQSEEPRVdsipekiSPEDVVALPF 202
Cdd:cd05905 88 vRVALTVEAclkGLPKKLLKSKTAAEIAKKKGWpkILDFVK---IPKS-KRSKLKKWGPHPPT-------RDGDTAYIEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 203 SSGTTGLPKGVMLTHKGLVT---SVAQQVDgenpnlYFNRDDVILCVLPM----FHIYALNSIMLcslrvGATILIMPKF 275
Cdd:cd05905 157 SFSSDGSLSGVAVSHSSLLAhcrALKEACE------LYESRPLVTVLDFKsglgLWHGCLLSVYS-----GHHTILIPPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 276 EIT----LLLEQIQRCKVTVAMV----VPPIVLAIAKSPETEKY---DLSSVRM-------------VKSGAAPLGKE-- 329
Cdd:cd05905 226 LMKtnplLWLQTLSQYKVRDAYVklrtLHWCLKDLSSTLASLKNrdvNLSSLRMcmvpcenrprissCDSFLKLFQTLgl 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 330 LEDAISAKF---PNAKLG-QGYGMTEAGPVL----AMSLGfakEPFPVKSGA--------CGTVVRNAEMKILDPDTGDS 393
Cdd:cd05905 306 SPRAVSTEFgtrVNPFICwQGTSGPEPSRVYldmrALRHG---VVRLDERDKpnslplqdSGKVLPGAQVAIVNPETKGL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 394 LPRNKPGEICIRGNQIMKGYL-----------NDPLATASTID-KDGWLHTGDVGFI----------DDDDELFIVDRLK 451
Cdd:cd05905 383 CKDGEIGEIWVNSPANASGYFlldgetndtfkVFPSTRLSTGItNNSYARTGLLGFLrptkctdlnvEEHDLLFVVGSID 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 452 ELIKYKGFQVAPAELE-SLLIGHPEINDVAVVamkeeDAGEVPVaFVVRSKDSniSEDEIKQFVSKQVV-----FYKRIN 525
Cdd:cd05905 463 ETLEVRGLRHHPSDIEaTVMRVHPYRGRCAVF-----SITGLVV-VVAEQPPG--SEEEALDLVPLVLNaileeHQVIVD 534
|
570 580 590
....*....|....*....|....*....|...
gi 15232507 526 KVFFTD--SIPKAPSGKILRKDLRARLANGLMN 556
Cdd:cd05905 535 CVALVPpgSLPKNPLGEKQRMEIRQAFLAGKLH 567
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
170-455 |
7.75e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 77.84 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 170 NCLRFSELTQSEEPRVDSIPEKisPEDVVALPFSSGTTGLPKGVMLTHKGLVTSVAQQVDGE-----NPNLYFNrddvil 244
Cdd:PTZ00342 281 SIILFDDMTKNKTTNYKIQNED--PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSifkkyNPKTHLS------ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 245 cVLPMFHIYALNSIMLCSLRvGATILIMPKfEITLLLEQIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSV--RMVK-- 320
Cdd:PTZ00342 353 -YLPISHIYERVIAYLSFML-GGTINIWSK-DINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLkrFLVKki 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 321 ------SGAAPLGKELEDA--ISAKF-----PN--------AKLG----------------QGYGMTE-AGPVLAMSlgf 362
Cdd:PTZ00342 430 lslrksNNNGGFSKFLEGIthISSKIkdkvnPNlevilnggGKLSpkiaeelsvllnvnyyQGYGLTEtTGPIFVQH--- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 363 AKEPFPVKSGacGTVVRNAEMKILDPDT---GDSLPRnkpGEICIRGNQIMKGYLNDPLATASTIDKDGWLHTGDVGFID 439
Cdd:PTZ00342 507 ADDNNTESIG--GPISPNTKYKVRTWETykaTDTLPK---GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQIN 581
|
330
....*....|....*.
gi 15232507 440 DDDELFIVDRLKELIK 455
Cdd:PTZ00342 582 KNGSLTFLDRSKGLVK 597
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
202-546 |
1.27e-08 |
|
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: 57.48 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 202 FSSGTTGLPKGVMLTHKGLV---TSVAQQVDGENPNLYFnrddviLCVLPMFHIYALNSIMlcSLRVGATILIMP---KF 275
Cdd:cd17654 125 HTSGTTGTPKIVAVPHKCILpniQHFRSLFNITSEDILF------LTSPLTFDPSVVEIFL--SLSSGATLLIVPtsvKV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 276 EITLLLEQI-QRCKVTVAMVVPPIV--LAIAKSPETEKYDLSSVRMVKSGAAPLGKELED-AISAKFPNAKLGQGYGMTE 351
Cdd:cd17654 197 LPSKLADILfKRHRITVLQATPTLFrrFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILsSWRGKGNRTRIFNIYGITE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 352 agpVLAMSLGF----AKEPFPVKSGACGTVVRNAEMkildpdTGDSLPRNKPGEICIRGNqIMKGYLNDPLATastidkd 427
Cdd:cd17654 277 ---VSCWALAYkvpeEDSPVQLGSPLLGTVIEVRDQ------NGSEGTGQVFLGGLNRVC-ILDDEVTVPKGT------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 428 gWLHTGDVGFIdDDDELFIVDRLKELIKYKGFQVAPAELESLLIGHPEINDVAVVAMKEEDAgevpVAFVV-RSKDSNIS 506
Cdd:cd17654 340 -MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL----IAFIVgESSSSRIH 413
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15232507 507 EDEIKQFVSKQVVfykrINKVFFTDSIPKAPSGKILRKDL 546
Cdd:cd17654 414 KELQLTLLSSHAI----PDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
77-317 |
2.12e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 53.93 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 77 AAGLHNLGVKQHDVVMILLPNSPEVVLTFLAASFIGAITTSANPFFTPAEISKQAKASAAKLIVTQ-------------S 143
Cdd:PLN03052 222 ANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQdvivrggksiplyS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 144 RYVDKiknlQNDGVLIVTTDSDAIPENcLR--------FSELTQSEEPRVDSIPEKISPEDVVALPFSSGTTGLPKGVML 215
Cdd:PLN03052 302 RVVEA----KAPKAIVLPADGKSVRVK-LRegdmswddFLARANGLRRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPW 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 216 THkglVTSVAQQVDGEnPNLYFNRDDVIlC--------VLPMFhIYAlnsimlcSLRVGATILI---------MPKFeit 278
Cdd:PLN03052 377 TQ---LTPLRAAADAW-AHLDIRKGDIV-CwptnlgwmMGPWL-VYA-------SLLNGATLALyngsplgrgFAKF--- 440
|
250 260 270
....*....|....*....|....*....|....*....
gi 15232507 279 llleqIQRCKVTVAMVVPPIVLAIAKSPETEKYDLSSVR 317
Cdd:PLN03052 441 -----VQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIR 474
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
37-220 |
1.18e-06 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 51.60 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 37 PLHDYIFENISEFAAKPCLINGPTGEV-------YTYADVHVTSRKLAAGLHNLGVKQHDVVMILLPNSPEVVLTFLAAS 109
Cdd:TIGR03443 237 AIHDIFADNAEKHPDRTCVVETPSFLDpssktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232507 110 FIGAITTSANPFFTPAeisKQ------AK-------ASAAKLIVTQSRYVDK----------IKnLQNDGVLiVTTDSDA 166
Cdd:TIGR03443 317 KAGATFSVIDPAYPPA---RQtiylsvAKpraliviEKAGTLDQLVRDYIDKelelrteipaLA-LQDDGSL-VGGSLEG 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15232507 167 IPENCLRFSELTQSEEPRV----DSIPekispedvvALPFSSGTTGLPKGVMLTHKGL 220
Cdd:TIGR03443 392 GETDVLAPYQALKDTPTGVvvgpDSNP---------TLSFTSGSEGIPKGVLGRHFSL 440
|
|
| |
