|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1-718 |
0e+00 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 1568.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 1 MLFGFFRNLFRVLFRVRVTGDVSALQGERVLITPNHVSFIDGILLALFLPIRPVFAVYTSISQQWYMRWLTPLIDFVPLD 80
Cdd:PRK08043 1 MLFSFFRNLFRVLYRVRVTGDTQALKGERVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQQWYMRWLKPYIDFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 81 PTKPMSIKHLVRLVEQGRPVVIFPEGRISTTGSLMKIYDGAGFVAAKSGATVVPVRIEGAELSRFSRLKGLVKQRFFPRI 160
Cdd:PRK08043 81 PTKPMAIKHLVRLVEQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 161 RLHILPPTQLPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAKYRFGAGKNCIEDINFTPDSYRKLLTK 240
Cdd:PRK08043 161 TLHILPPTQLPMPDAPRARDRRKLAGEMLHQIMMEARMAVRPRETLYEALLSAQYRYGAGKPCIEDVNFTPDSYRKLLKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 241 TLFVARILEKYSTEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDKGKLWH 320
Cdd:PRK08043 241 TLFVGRILEKYSVEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 321 LPEQLTQVRWVYLEDLKADVTFSDKLWIFSHLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTI 400
Cdd:PRK08043 321 LPEQLTQVRWVYLEDLKDDVTTADKLWIFAHLLMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 401 ADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFHR 480
Cdd:PRK08043 401 ADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFAR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 481 LRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVPGIEDGGRLQLKG 560
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQGGRLQLKG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 561 PNIMSGYLRVEKPGVLEVPTAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADK 640
Cdd:PRK08043 561 PNIMNGYLRVEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDK 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 641 MHATAIKSDASKGEALVLFTTDSELTREKLQQYARAHGVPELAVPRDIRHLKQLPLLGSGKPDFVTLKSWVDEPEKQH 718
Cdd:PRK08043 641 QHATAIKSDASKGEALVLFTTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQHD 718
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
5-719 |
0e+00 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 947.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 5 FFRNLFRVLFRVRVTGdVSALQ--GERVLITPNHVSFIDGILLALFLPIRPVFAVYTSISQQWYMRWLTPLIDFVPLDPT 82
Cdd:PRK06814 430 IFSILFRAFYRVEVKG-LENLQkaGKKAVIAANHVSFLDGPLLAAYLPEEPTFAIDTDIAKAWWVKPFLKLAKALPVDPT 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 83 KPMSIKHLVRLVEQGRPVVIFPEGRISTTGSLMKIYDGAGFVAAKSGATVVPVRIEGAELSRFSRLKGLVKQRFFPRIRL 162
Cdd:PRK06814 509 NPMATRTLIKEVQKGEKLVIFPEGRITVTGSLMKIYDGPGMIADKAGAMVVPVRIDGLQFTHFSRLKNQVRRKWFPKVTV 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 163 HILPPTQLPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPR-ETLYESLLAAKYRFGAGKNCIEDINFTPDSYRKLLTKT 241
Cdd:PRK06814 589 TILPPVKLAVDPELKGRERRSAAGAALYDIMSDMMFETSDYdRTLFEALIEAAKIHGFKKLAVEDPVNGPLTYRKLLTGA 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 242 LFVARILEKYSTEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDKGKLWHL 321
Cdd:PRK06814 669 FVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAFIEKARLGPL 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 322 PEQL-TQVRWVYLEDLKADVTFSDKLWIFSHLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTI 400
Cdd:PRK06814 749 IEALeFGIRIIYLEDVRAQIGLADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAAR 828
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 401 ADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFHR 480
Cdd:PRK06814 829 IDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILFGTDTFLNGYARYAHPYDFRS 908
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 481 LRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVPGIEDGGRLQLKG 560
Cdd:PRK06814 909 LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGIDEGGRLFVRG 988
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 561 PNIMSGYLRVEKPGVLEVPtaenaqgeiERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADK 640
Cdd:PRK06814 989 PNVMLGYLRAENPGVLEPP---------ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDA 1059
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124149 641 MHATAIKSDASKGEALVLFTTDSELTREKLQQYARAHGVPELAVPRDIRHLKQLPLLGSGKPDFVTLKSWVDEPEKQHE 719
Cdd:PRK06814 1060 LHAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPE 1138
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
225-711 |
0e+00 |
|
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: 704.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 225 EDINFTPDSYRKLLTKTLFVARILEKYSTEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIK 304
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 305 TIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTFSDKLWIFSHLLAPH------LAQVKQQPEDAAVILFTSGSEG 378
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPPkwllriFGVAPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 379 HPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTV 458
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 459 LFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVP-MAAKSGTVGRIL 537
Cdd:cd05909 241 LLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPqSPNKEGTVGRPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 538 PGMDARLLAVPG-----IEDGGRLQLKGPNIMSGYLRVEKPGVLevptaenaqgEIERGWYDTGDIVRFDENGFVQIQGR 612
Cdd:cd05909 321 PGMEVKIVSVETheevpIGEGGLLLVRGPNVMLGYLNEPELTSF----------AFGDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 613 AKRFAKIAGEMVSLEMVEQLALAVSA-DKMHATAIKSDASKGEALVLFTTDSELTREKLQQYARAHGVPELAVPRDIRHL 691
Cdd:cd05909 391 LSRFAKIAGEMVSLEAIEDILSEILPeDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQV 470
|
490 500
....*....|....*....|
gi 489124149 692 KQLPLLGSGKPDFVTLKSWV 711
Cdd:cd05909 471 EEIPLLGTGKPDYVTLKALA 490
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
9-709 |
9.10e-165 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 504.46 E-value: 9.10e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 9 LFRVLFRVRVTGDVSALQGERVLITPNHVSFIDGILLALFLPiRPV-FAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSI 87
Cdd:PRK08633 422 LMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAASP-RPIrFVMERSIYEKWYLKWFFKLFGVIPISSGGSKES 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 88 KHLVR-LVEQGRPVVIFPEGRISTTGSLMKIYDGAGFVAAKSGATVVPVRIEGAELSRFSRLKGlvkqRFFPRIRLHILP 166
Cdd:PRK08633 501 LEFIRkALDDGEVVCIFPEGAITRNGQLNEFKRGFELIVKGTDVPIIPFYIRGLWGSIFSRASG----KFLWRWPTRIPY 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 167 PTQL----PMPEAPRARDRRKIAGEmLHQIMMEARMAVRPreTLYESLL-AAKYRFGagKNCIEDINFTPDSYRKLLTKT 241
Cdd:PRK08633 577 PVTVafgkPMPAHSTAHEVKQAVFE-LSFDSWKSRKEALP--PLAEAWIdTAKRNWS--RLAVADSTGGELSYGKALTGA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 242 LFVARILEKYSTEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDKGKLWHL 321
Cdd:PRK08633 652 LALARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGF 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 322 PEQLTQ-VRWVYLEDLKADVTFSDKLWIF-------SHLLAPHLAQvKQQPEDAAVILFTSGSEGHPKGVVHSHKSILAN 393
Cdd:PRK08633 732 DLELPEnVKVIYLEDLKAKISKVDKLTALlaarllpARLLKRLYGP-TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 394 VEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARF- 472
Cdd:PRK08633 811 IEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNk 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 473 -AHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVP----------MAAKSGTVGRILPGMD 541
Cdd:PRK08633 891 kLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaadfkrqTGSKEGSVGMPLPGVA 970
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 542 AR------LLAVPGIEDgGRLQLKGPNIMSGYL-RVEKpgvlevpTAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAK 614
Cdd:PRK08633 971 VRivdpetFEELPPGED-GLILIGGPQVMKGYLgDPEK-------TAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYS 1042
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 615 RFAKIAGEMVSLEMVE---QLALAVSADKMHATAIkSDASKGEALVLFTTDSELTREKLQQYARAHGVPELAVPRDIRHL 691
Cdd:PRK08633 1043 RFAKIGGEMVPLGAVEeelAKALGGEEVVFAVTAV-PDEKKGEKLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKV 1121
|
730
....*....|....*...
gi 489124149 692 KQLPLLGSGKPDFVTLKS 709
Cdd:PRK08633 1122 EALPLLGSGKLDLKGLKE 1139
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
233-717 |
8.26e-100 |
|
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: 314.44 E-value: 8.26e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARIL-EKYSTEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTsrq 311
Cdd:COG0318 26 TYAELDARARRLAAALrALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 312 fldkgklwhlpeqltqvrwvyledlkadvtfsdklwifshllaphlaqvkqqpedaAVILFTSGSEGHPKGVVHSHKSIL 391
Cdd:COG0318 103 --------------------------------------------------------ALILYTSGTTGRPKGVMLTHRNLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 392 ANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSpLHYRIVPELVYDRNCTVLFGTSTFLGNYAR 471
Cdd:COG0318 127 ANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 472 F--AHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINV--PMAAKSGTVGRILPGMDARLLAV 547
Cdd:COG0318 206 HpeFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVDE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 548 PGIE--DG--GRLQLKGPNIMSGYLRveKPgvlevptAENAQgEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEM 623
Cdd:COG0318 286 DGRElpPGevGEIVVRGPNVMKGYWN--DP-------EATAE-AFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGEN 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 624 VSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTT---DSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSG 700
Cdd:COG0318 356 VYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrpGAELDAEELRAFLRER-LARYKVPRRVEFVDELPRTASG 434
|
490
....*....|....*..
gi 489124149 701 KPDFVTLKSWVDEPEKQ 717
Cdd:COG0318 435 KIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
366-703 |
2.50e-81 |
|
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: 262.22 E-value: 2.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYPSPLhYR 445
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFD-PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 446 IVPELVYDRNCTVLFGTSTFLGNYARFA--HPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSIN 523
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPesAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 524 VP--MAAKSGTVGRILPGMDARLLAVPGIEDG----GRLQLKGPNIMSGYLRVEkpgvlevptaENAQGEIERGWYDTGD 597
Cdd:cd04433 159 PPddDARKPGSVGRPVPGVEVRIVDPDGGELPpgeiGELVVRGPSVMKGYWNNP----------EATAAVDEDGWYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 598 IVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKmHATAIKS-DASKGEALVLF---TTDSELTREKLQQY 673
Cdd:cd04433 229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVA-EAAVVGVpDPEWGERVVAVvvlRPGADLDAEELRAH 307
|
330 340 350
....*....|....*....|....*....|
gi 489124149 674 ARAHGVPeLAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd04433 308 VRERLAP-YKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
206-701 |
6.49e-69 |
|
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: 233.61 E-value: 6.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 206 LYESLLAAKYRFGAGKNCIEDINFTpdSYRKLLTKTLFVARILEKYSTE-GERIGLMLPNAGISAAVIFGAIARRRIPAM 284
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKL--TYRELDALAEAFAAGLQNLGVQpGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 285 MN--YTAgvKGLTSAITASEIKTIFTSRQFLDKGKLWHLPEQLTQVRwvyledlkadvtfsdklwifshllaphlaqvkq 362
Cdd:cd05936 79 LNplYTP--RELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALT--------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 qPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIA--DFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
Cdd:cd05936 124 -PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 PLHYRIVPELVyDRNCTVLFGTSTFLGNYARFAHP--YDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAP 518
Cdd:cd05936 203 FRPIGVLKEIR-KHRVTIFPGVPTMYIALLNAPEFkkRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSIN-VPMAAKSGTVGRILPGMDARLLAVPGIE--DG--GRLQLKGPNIMSGYLRveKPgvlevptAENAQGEIErGWY 593
Cdd:cd05936 282 VVAVNpLDGPRKPGSIGIPLPGTEVKIVDDDGEElpPGevGELWVRGPQVMKGYWN--RP-------EETAEAFVD-GWL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 594 DTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAIK-SDASKGEALVLFTT---DSELTREK 669
Cdd:cd05936 352 RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEE-VLYEHPAVAEAAVVGvPDPYSGEAVKAFVVlkeGASLTEEE 430
|
490 500 510
....*....|....*....|....*....|....*
gi 489124149 670 LQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGK 701
Cdd:cd05936 431 IIAFCREQ----LAgykVPRQVEFRDELPKSAVGK 461
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
233-614 |
9.54e-68 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 228.74 E-value: 9.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYSTE-GERIGLMLPNaGISAAVIFGAIARRR-IPAMMNYTAGVKGLTSAITASEIKTIFTSR 310
Cdd:pfam00501 23 TYRELDERANRLAAGLRALGVGkGDRVAILLPN-SPEWVVAFLACLKAGaVYVPLNPRLPAEELAYILEDSGAKVLITDD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 311 QFLDKGKLWHLPEqLTQVRWVYLEDLKADVTFSDKLWIFSHLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSI 390
Cdd:pfam00501 102 ALKLEELLEALGK-LEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 391 LANVEQIKTIAD----FTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS--PLHYRIVPELVYDRNCTVLFGTST 464
Cdd:pfam00501 181 VANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGfpALDPAALLELIERYKVTVLYGVPT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 465 FLgNY---ARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVPM---AAKSGTVGRILP 538
Cdd:pfam00501 261 LL-NMlleAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLdedLRSLGSVGRPLP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 539 GMDARLLAVPG---IEDG--GRLQLKGPNIMSGYLRveKPGvlevptaENAQGEIERGWYDTGDIVRFDENGFVQIQGRA 613
Cdd:pfam00501 340 GTEVKIVDDETgepVPPGepGELCVRGPGVMKGYLN--DPE-------LTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRK 410
|
.
gi 489124149 614 K 614
Cdd:pfam00501 411 K 411
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
197-709 |
1.70e-63 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 220.84 E-value: 1.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 197 RMAVRPRETLYESLLAAKYRFGAGKNCIeDINFTPDSYRKLLTKTLFVARILEKYSteGERIGLMLPNAGISAAVIFGAI 276
Cdd:PRK06334 12 RGKLRSGKTVLESFLKLCSEMTTATVCW-DEQLGKLSYNQVRKAVIALATKVSKYP--DQHIGIMMPASAGAYIAYFATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 277 ARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDK-----GKLWHLPEQLtqvrwVYLEDLKADVTFSDKLWIFSH 351
Cdd:PRK06334 89 LSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHlaqthGEDAEYPFSL-----IYMEEVRKELSFWEKCRIGIY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 352 LLAPHLAQVK------QQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGL-TVG 424
Cdd:PRK06334 164 MSIPFEWLMRwfgvsdKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 425 LFtPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFAHPYD--FHRLRYVVAGAEKLQDSTKQLWQEK 502
Cdd:PRK06334 244 LF-PLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQEscLPSLRFVVIGGDAFKDSLYQEALKT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 503 FGLRVL-EGYGVTECAPVVSINVPMAAK-SGTVGRILPGMDARLLA----VPgIEDG--GRLQLKGPNIMSGYLRvEKPG 574
Cdd:PRK06334 323 FPHIQLrQGYGTTECSPVITINTVNSPKhESCVGMPIRGMDVLIVSeetkVP-VSSGetGLVLTRGTSLFSGYLG-EDFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 575 vlevptaenaQGEIERG---WYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALA--VSADKMHATAIKSD 649
Cdd:PRK06334 401 ----------QGFVELGgetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfGQNAADHAGPLVVC 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489124149 650 ASKGEA--LVLFTTDSELTRE--KLQQYARAHGVPELAVprdIRHLKQLPLLGSGKPDFVTLKS 709
Cdd:PRK06334 471 GLPGEKvrLCLFTTFPTSISEvnDILKNSKTSSILKISY---HHQVESIPMLGTGKPDYCSLNA 531
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
205-701 |
7.16e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 204.75 E-value: 7.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 205 TLYESLLAAKYRFGAGKNCIEDINFTpdSYRKLLTKTLFVARILEKYSTE-GERIGLMLPNagiSAAVIFGAIArrripA 283
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRL--TYAELNARVRRAAAALAALGIGkGDRVAIWAPN---SPHWVIAALG-----A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 284 MMnytAG--VKGLTSAITASEI---------KTIFTSRQFLdkGKLWHLPEQLTQVRWVYLEDLKADVTFSDKLWIFSHL 352
Cdd:PRK07656 76 LK---AGavVVPLNTRYTADEAayilargdaKALFVLGLFL--GVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 353 LAPH---LAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPL 429
Cdd:PRK07656 151 LAAGdpaERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 430 LTGAEVFLYP--SPLHyriVPELVYDRNCTVLFGTST---FLGNYARfAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFG 504
Cdd:PRK07656 231 MRGATILPLPvfDPDE---VFRLIETERITVLPGPPTmynSLLQHPD-RSAEDLSSLRLAVTGAASMPVALLERFESELG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 505 LR-VLEGYGVTECAPVVSINVP---MAAKSGTVGRILPGMDARLLAVPGIEDG----GRLQLKGPNIMSGYLRvekpgvL 576
Cdd:PRK07656 307 VDiVLTGYGLSEASGVTTFNRLdddRKTVAGTIGTAIAGVENKIVNELGEEVPvgevGELLVRGPNVMKGYYD------D 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 577 EVPTAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE-- 654
Cdd:PRK07656 381 PEATAAAIDAD---GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEvg 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489124149 655 -ALVLFTTDSELTREKLQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGK 701
Cdd:PRK07656 458 kAYVVLKPGAELTEEELIAYCREH----LAkykVPRSIEFLDELPKNATGK 504
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
321-709 |
3.37e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 200.41 E-value: 3.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 321 LPEQLTQVR-WVYLEDlkADVTFSDKLWI-FSHLLA---PHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVE 395
Cdd:PRK06187 120 ILPQLPTVRtVIVEGD--GPAAPLAPEVGeYEELLAaasDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 396 QIKTIADFTADDRFMSALPLFHSFGLTVGlFTPLLTGAEVfLYPSPLHYRIVPELVYDRNCTVLFGTST---FLGNYARf 472
Cdd:PRK06187 198 AVCAWLKLSRDDVYLVIVPMFHVHAWGLP-YLALMAGAKQ-VIPRRFDPENLLDLIETERVTFFFAVPTiwqMLLKAPR- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 473 AHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVP------MAAKSGTVGRILPGMDARLL- 545
Cdd:PRK06187 275 AYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPedqlpgQWTKRRSAGRPLPGVEARIVd 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 546 ----AVP-GIEDGGRLQLKGPNIMSGYLRVEKpgvlevPTAENaqgeIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA 620
Cdd:PRK06187 355 ddgdELPpDGGEVGEIIVRGPWLMQGYWNRPE------ATAET----IDGGWLHTGDVGYIDEDGYLYITDRIKDVIISG 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 621 GEMV-SLEMVEQLAL--AVSAdkmhATAI-KSDASKGE---ALVLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQ 693
Cdd:PRK06187 425 GENIyPRELEDALYGhpAVAE----VAVIgVPDEKWGErpvAVVVLKPGATLDAKELRAFLRGR-LAKFKLPKRIAFVDE 499
|
410
....*....|....*.
gi 489124149 694 LPLLGSGKPDFVTLKS 709
Cdd:PRK06187 500 LPRTSVGKILKRVLRE 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
224-701 |
5.37e-52 |
|
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: 187.81 E-value: 5.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 224 IEDINFTPDSYRKLLTKTLFVARILEKY-STEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASE 302
Cdd:cd05911 3 IDADTGKELTYAQLRTLSRRLAAGLRKLgLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 303 IKTIFTSRQFLDKgkLWHLPEQLTQVRWVY-LEDLKADVTFSDKLWiFSHLLAPHLAQVKQQ---PEDAAVILFTSGSEG 378
Cdd:cd05911 83 PKVIFTDPDGLEK--VKEAAKELGPKDKIIvLDDKPDGVLSIEDLL-SPTLGEEDEDLPPPLkdgKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 379 HPKGVVHSHKSILANVEQIKTI--ADFTADDRFMSALPLFHSFGLTVGLFTPLLtGAEVFLYPSPlHYRIVPELVYDRNC 456
Cdd:cd05911 160 LPKGVCLSHRNLIANLSQVQTFlyGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKF-DSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 457 TVLFGTST---FLGNYARFAhPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGL-RVLEGYGVTECAPVVSINVPMAAKSGT 532
Cdd:cd05911 238 TFLYLVPPiaaALAKSPLLD-KYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 533 VGRILPGMDARLLAVPGIEDGGR-----LQLKGPNIMSGYLRVEKpgvlevptaENAQGEIERGWYDTGDIVRFDENGFV 607
Cdd:cd05911 317 VGRLLPNVEAKIVDDDGKDSLGPnepgeICVRGPQVMKGYYNNPE---------ATKETFDEDGWLHTGDIGYFDEDGYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 608 QIQGRAKRFAKIAGEMVSLEMVEQLALavSADKMHATAI--KSDASKGE---ALVLFTTDSELTREKLQQYARAHgvpeL 682
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLL--EHPGVADAAVigIPDEVSGElprAYVVRKPGEKLTEKEVKDYVAKK----V 461
|
490 500
....*....|....*....|....*.
gi 489124149 683 AvprDIRHL-------KQLPLLGSGK 701
Cdd:cd05911 462 A---SYKQLrggvvfvDEIPKSASGK 484
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
327-630 |
4.78e-51 |
|
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: 184.34 E-value: 4.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 327 QVRWVyLEDLKADVTFSDKlwifshllaphlaqvkqqPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTAD 406
Cdd:cd05907 68 QIAYI-LNDSEAKALFVED------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 407 DRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSP---------LHYRI---VP---ELVYDRNCTVLfgTSTFLGNYAR 471
Cdd:cd05907 129 DRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAetllddlseVRPTVflaVPrvwEKVYAAIKVKA--VPGLKRKLFD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 472 FAHpydFHRLRYVVAGAEKLQDSTkQLWQEKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARllavpgIE 551
Cdd:cd05907 207 LAV---GGRLRFAASGGAPLPAEL-LHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVR------IA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 552 DGGRLQLKGPNIMSGYLRvekpgvLEVPTAENAqgeIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GEMVSLEMVE 630
Cdd:cd05907 277 DDGEILVRGPNVMLGYYK------NPEATAEAL---DADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIE 347
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
365-701 |
1.57e-47 |
|
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: 173.95 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhy 444
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKF--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 445 riVPELVYDR----NCTVLFGTSTFLgnYARFAHP----YDFHRLRYVVAGAEKLQDSTKQLWQEkFGLRVLEGYGVTEC 516
Cdd:cd17631 175 --DPETVLDLierhRVTSFFLVPTMI--QALLQHPrfatTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTET 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 517 APVVSINVP--MAAKSGTVGRILPGMDARLLAVPG--IEDG--GRLQLKGPNIMSGYLRvekpgvLEVPTAENAQGeier 590
Cdd:cd17631 250 SPGVTFLSPedHRRKLGSAGRPVFFVEVRIVDPDGreVPPGevGEIVVRGPHVMAGYWN------RPEATAAAFRD---- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 591 GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSELTR 667
Cdd:cd17631 320 GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEavvAVVVPRPGAELDE 399
|
330 340 350
....*....|....*....|....*....|....*..
gi 489124149 668 EKLqqyaRAHGVPELA---VPRDIRHLKQLPLLGSGK 701
Cdd:cd17631 400 DEL----IAHCRERLArykIPKSVEFVDALPRNATGK 432
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
366-614 |
3.18e-47 |
|
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: 173.24 E-value: 3.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsPLHYR 445
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP-KFDPK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 446 IVPELVYDRNCTVLFGTSTFlgnYARFAHPYDFH-------------RLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYG 512
Cdd:cd05941 169 EVAISRLMPSITVFMGVPTI---YTRLLQYYEAHftdpqfaraaaaeRLRLMVSGSAALPVPTLEEWEAITGHTLLERYG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 513 VTECapVVSINVPMAA--KSGTVGRILPGMDARLL----AVPGIEDG-GRLQLKGPNIMSGYLRveKPGVlevpTAENAQ 585
Cdd:cd05941 246 MTEI--GMALSNPLDGerRPGTVGMPLPGVQARIVdeetGEPLPRGEvGEIQVRGPSVFKEYWN--KPEA----TKEEFT 317
|
250 260
....*....|....*....|....*....
gi 489124149 586 GEierGWYDTGDIVRFDENGFVQIQGRAK 614
Cdd:cd05941 318 DD---GWFKTGDLGVVDEDGYYWILGRSS 343
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
255-701 |
1.46e-46 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 174.14 E-value: 1.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 255 GERIGLMLPNagISAAVIF-------GAIArrrIPAMMNYTAgvKGLTSAITASEIKTIFTSRQFLDKGKLWHLPEQLTQ 327
Cdd:COG0365 64 GDRVAIYLPN--IPEAVIAmlacariGAVH---SPVFPGFGA--EALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 328 VR--------WVYLEDLKADVTFSDKLWiFSHLLA---PHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVE- 395
Cdd:COG0365 137 ALeelpslehVIVVGRTGADVPMEGDLD-WDELLAaasAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAt 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 396 QIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY---PSPLHYRIVPELVYDRNCTVLFGTST----FLGN 468
Cdd:COG0365 216 TAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYegrPDFPDPGRLWELIEKYGVTVFFTAPTairaLMKA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 469 YARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE-CAPVVSINVPMAAKSGTVGRILPGMDARLLAv 547
Cdd:COG0365 296 GDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTEtGGIFISNLPGLPVKPGSMGKPVPGYDVAVVD- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 548 pgiEDG--------GRLQLKG--PNIMSGYLR-VEKpgvlevpTAENAQGEIErGWYDTGDIVRFDENGFVQIQGRAKRF 616
Cdd:COG0365 375 ---EDGnpvppgeeGELVIKGpwPGMFRGYWNdPER-------YRETYFGRFP-GWYRTGDGARRDEDGYFWILGRSDDV 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 617 AKIAGEMVS-LEMVEQLAL--AVsADkmhATAI-KSDASKGEALVLF------TTDSELTREKLQQYARAHgVPELAVPR 686
Cdd:COG0365 444 INVSGHRIGtAEIESALVShpAV-AE---AAVVgVPDEIRGQVVKAFvvlkpgVEPSDELAKELQAHVREE-LGPYAYPR 518
|
490
....*....|....*
gi 489124149 687 DIRHLKQLPLLGSGK 701
Cdd:COG0365 519 EIEFVDELPKTRSGK 533
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
353-701 |
7.88e-46 |
|
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: 171.01 E-value: 7.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 353 LAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQ-IKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLT 431
Cdd:cd05959 151 EAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELyARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 432 GAEVFLYPSplhyRIVPELVYDR----NCTVLFGTSTFlgnYARF-----AHPYDFHRLRYVVAGAEKLQDSTKQLWQEK 502
Cdd:cd05959 231 GATTVLMPE----RPTPAAVFKRirryRPTVFFGVPTL---YAAMlaapnLPSRDLSSLRLCVSAGEALPAEVGERWKAR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 503 FGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVPG--IEDG--GRLQLKGPNIMSGYL-RVEKpgvle 577
Cdd:cd05959 304 FGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGgdVADGepGELYVRGPSSATMYWnNRDK----- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 578 vpTAENAQGEiergWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAIKSDASKG---- 653
Cdd:cd05959 379 --TRDTFQGE----WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVES-ALVQHPAVLEAAVVGVEDEDGltkp 451
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489124149 654 EALVLF---TTDSELTREKLQQYARAhGVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05959 452 KAFVVLrpgYEDSEALEEELKEFVKD-RLAPYKYPRWIVFVDELPKTATGK 501
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-708 |
2.20e-45 |
|
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: 168.77 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 255 GERIGLMLPN----AGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFtsrqfLDKGKLWHLPEQLTQVrw 330
Cdd:cd05922 18 GERVVLILPNrftyIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVL-----ADAGAADRLRDALPAS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 331 vYLEDLKADVtfsDKLWIFSHLLAPHlaqvKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFM 410
Cdd:cd05922 91 -PDPGTVLDA---DGIRAARASAPAH----EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 411 SALPLFHSFGLTVgLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFA-HPYDFHRLRYVVAGAE 489
Cdd:cd05922 163 TVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGfDPAKLPSLRYLTQAGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 490 KLQDSTKQLWQEKF-GLRVLEGYGVTECAPVVSINVP--MAAKSGTVGRILPGM------DARLLAVPGIEdgGRLQLKG 560
Cdd:cd05922 242 RLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPerILEKPGSIGLAIPGGefeildDDGTPTPPGEP--GEIVHRG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 561 PNIMSGYLRVEkpgvlEVPTAENAQGEIERgwydTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADK 640
Cdd:cd05922 320 PNVMKGYWNDP-----PYRRKEGRGGGVLH----TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA-AARSIGLI 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124149 641 MHATAIKSDASKGEALVLFTT-DSELTREKLQQYARAHGvPELAVPRDIRHLKQLPLLGSGKPDFVTLK 708
Cdd:cd05922 390 IEAAAVGLPDPLGEKLALFVTaPDKIDPKDVLRSLAERL-PPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
301-680 |
2.98e-45 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 171.05 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 301 SEIKTIFTSRQF-LDKgkLWHLPEQLTQVRWVYLEDlKADVTFSDKLWIFSHLLA-----PHLAQVKQ-----QPEDAAV 369
Cdd:COG1022 111 SGAKVLFVEDQEqLDK--LLEVRDELPSLRHIVVLD-PRGLRDDPRLLSLDELLAlgrevADPAELEArraavKPDDLAT 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 370 ILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTpLLTGAEVFLYPSP------L- 442
Cdd:COG1022 188 IIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAESPdtlaedLr 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 ----HYRI-VP---ELVYDR--------------------------NCTVLFGTStfLGNYARFAHP-YD---FH----- 479
Cdd:COG1022 267 evkpTFMLaVPrvwEKVYAGiqakaeeagglkrklfrwalavgrryARARLAGKS--PSLLLRLKHAlADklvFSklrea 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 480 ---RLRYVVAGAEKLQDSTkqlwqEKF----GLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARllavpgIED 552
Cdd:COG1022 345 lggRLRFAVSGGAALGPEL-----ARFfralGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVK------IAE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 553 GGRLQLKGPNIMSGYLRveKPGVlevpTAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GEMVS---LEM 628
Cdd:COG1022 414 DGEILVRGPNVMKGYYK--NPEA----TAEAFDAD---GWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVApqpIEN 484
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 489124149 629 -------VEQlALAVSADKMHATAIksdaskgeaLVLfttDseltREKLQQYARAHGVP 680
Cdd:COG1022 485 alkasplIEQ-AVVVGDGRPFLAAL---------IVP---D----FEALGEWAEENGLP 526
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
254-710 |
3.37e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 168.60 E-value: 3.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 254 EGERIGLMLPNAGISAAVIFGAIArRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDKG---KLWHLPEQLTQVRW 330
Cdd:PRK07529 82 PGDVVAFLLPNLPETHFALWGGEA-AGIANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTDiwqKVAEVLAALPELRT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 331 VYLEDLKADVTfSDKLWIFSHLLAPH-------LAQVKQQPEDAAVI-----------LF-TSGSEGHPKGVVHSHKSIL 391
Cdd:PRK07529 161 VVEVDLARYLP-GPKRLAVPLIRRKAharildfDAELARQPGDRLFSgrpigpddvaaYFhTGGTTGMPKLAQHTHGNEV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 392 ANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLyPSPLHYRivPELVYDR--------NCTVLFGTS 463
Cdd:PRK07529 240 ANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVL-ATPQGYR--GPGVIANfwkiveryRINFLSGVP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 464 TFLGnyARFAHP---YDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVPMAA-KSGTVGRILPG 539
Cdd:PRK07529 317 TVYA--ALLQVPvdgHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGErRIGSVGLRLPY 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 540 MDARllAVPGIEDG-----------GRLQLKGPNIMSGYLRVEKpgvlevptaeNAQGEIERGWYDTGDIVRFDENGFVQ 608
Cdd:PRK07529 395 QRVR--VVILDDAGrylrdcavdevGVLCIAGPNVFSGYLEAAH----------NKGLWLEDGWLNTGDLGRIDADGYFW 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 609 IQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAI-KSDASKGE---ALVLFTTDSELTREKLQQYARAHgVPE-LA 683
Cdd:PRK07529 463 LTGRAKDLIIRGGHNIDPAAIEE-ALLRHPAVALAAAVgRPDAHAGElpvAYVQLKPGASATEAELLAFARDH-IAErAA 540
|
490 500
....*....|....*....|....*..
gi 489124149 684 VPRDIRHLKQLPLLGSGKPDFVTLKSW 710
Cdd:PRK07529 541 VPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
364-703 |
5.24e-44 |
|
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: 162.26 E-value: 5.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPSPLH 443
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHV-VLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 444 YR---IVPE---LVYDRNCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECA 517
Cdd:cd05944 80 YRnpgLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 518 PVVSINVPMAAKS-GTVGRILPGMDARLLavpgIEDG-GRLQLK-GPNIMsGYLRVEKPGVLE--VPTAENAQGEIERGW 592
Cdd:cd05944 160 CLVAVNPPDGPKRpGSVGLRLPYARVRIK----VLDGvGRLLRDcAPDEV-GEICVAGPGVFGgyLYTEGNKNAFVADGW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 593 YDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSELTREK 669
Cdd:cd05944 235 LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGElpvAYVQLKPGAVVEEEE 314
|
330 340 350
....*....|....*....|....*....|....*
gi 489124149 670 LQQYARAHgVPE-LAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd05944 315 LLAWARDH-VPErAAVPKHIEVLEELPVTAVGKVF 348
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
365-701 |
2.08e-42 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 159.55 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQI-KTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLH 443
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 444 YRIVPELVYDRNCTVLFGTSTFLGNYARFAH--PYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVS 521
Cdd:cd05919 171 AERVLATLARFRPTVLYGVPTFYANLLDSCAgsPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 522 INVPMAAKSGTVGRILPGMDARLLAVPG--IEDG--GRLQLKGPNIMSGYLRvekpgvlevpTAENAQGEIERGWYDTGD 597
Cdd:cd05919 251 SNRPGAWRLGSTGRPVPGYEIRLVDEEGhtIPPGeeGDLLVRGPSAAVGYWN----------NPEKSRATFNGGWYRTGD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 598 IVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLA---LAVSADKMHATAIKSDASKGEALVLFTTDSElTREKLQQYA 674
Cdd:cd05919 321 KFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIiqhPAVAEAAVVAVPESTGLSRLTAFVVLKSPAA-PQESLARDI 399
|
330 340 350
....*....|....*....|....*....|
gi 489124149 675 RAHGVPELA---VPRDIRHLKQLPLLGSGK 701
Cdd:cd05919 400 HRHLLERLSahkVPRRIAFVDELPRTATGK 429
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
364-698 |
8.32e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 160.55 E-value: 8.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQ----IKTIADftADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkawVPGLGD--GPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SPlhyriVPELVYD----RNCTVLFGTSTFLGNYARFA--HPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGV 513
Cdd:PRK05605 296 AP-----DIDLILDamkkHPPTWLPGVPPLYEKIAEAAeeRGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 514 TECAPVVSINvPMAA--KSGTVGRILPGMDARL-----LAV---PGIEdgGRLQLKGPNIMSGYLRVEkpgvlevptAEN 583
Cdd:PRK05605 371 TETSPIIVGN-PMSDdrRPGYVGVPFPDTEVRIvdpedPDEtmpDGEE--GELLVRGPQVFKGYWNRP---------EET 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 584 AQGeIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAI---KSDASKG-EALVLF 659
Cdd:PRK05605 439 AKS-FLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE-VLREHPGVEDAAVVglpREDGSEEvVAAVVL 516
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489124149 660 TTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLP--LLG 698
Cdd:PRK05605 517 EPGAALDPEGLRAYCREH-LTRYKVPRRFYHVDELPrdQLG 556
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
363-703 |
2.51e-40 |
|
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: 153.84 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSP 441
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSF--SFDVSVWeIFGALLAGATLVVLPEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 LHYRI--VPELVYDRNCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKF-GLRVLEGYGVTECAP 518
Cdd:cd05930 169 VRKDPeaLADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSINV--PMAAKSGTV--GRILPGMDARLL------AVPGIEdgGRLQLKGPNIMSGYLRveKPGvlevPTAENAQGEI 588
Cdd:cd05930 249 DATYYRvpPDDEEDGRVpiGRPIPNTRVYVLdenlrpVPPGVP--GELYIGGAGLARGYLN--RPE----LTAERFVPNP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 589 ERGW---YDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTT---D 662
Cdd:cd05930 321 FGPGermYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVpdeG 400
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489124149 663 SELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd05930 401 GELDEEELRAHLAER-LPDYMVPSAFVVLDALPLTPNGKVD 440
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
364-614 |
3.28e-40 |
|
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: 154.14 E-value: 3.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY---PS 440
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLdkiPS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 PL-----HYRI-------VPELVYDRNCTVLFGTSTFLGNYARFAHPYDFH----------------RLRYVVAGAEKL- 491
Cdd:cd05914 168 AKiialaFAQVtptlgvpVPLVIEKIFKMDIIPKLTLKKFKFKLAKKINNRkirklafkkvheafggNIKEFVIGGAKIn 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 492 QDSTKQLWqeKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVPGIEDGGRLQLKGPNIMSGYLRVE 571
Cdd:cd05914 248 PDVEEFLR--TIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNP 325
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489124149 572 KpgvlevptaENAQGEIERGWYDTGDIVRFDENGFVQIQGRAK 614
Cdd:cd05914 326 E---------ATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKK 359
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
362-701 |
6.21e-39 |
|
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: 149.84 E-value: 6.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSP 441
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ-DI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 LHYRIVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFH--RLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECA-P 518
Cdd:cd05903 169 WDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPlsRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPgA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSINVPMAAKS-GTVGRILPGM------DARLLAVPGIEdgGRLQLKGPNIMSGYLRvekpgvlevpTAENAQGEIERG 591
Cdd:cd05903 249 VTSITPAPEDRRlYTDGRPLPGVeikvvdDTGATLAPGVE--GELLSRGPSVFLGYLD----------RPDLTADAAPEG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 592 WYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSELTRE 668
Cdd:cd05903 317 WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGEracAVVVTKSGALLTFD 396
|
330 340 350
....*....|....*....|....*....|...
gi 489124149 669 KLQQYARAHGVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05903 397 ELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGK 429
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
364-701 |
7.65e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 151.74 E-value: 7.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDR---FMSALPLFHSFGLTVG--LFTPLltGAEVFLY 438
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGkelVVTALPLYHIFALTVNclLFIEL--GGQNLLI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 439 PSPlhyRIVPELVYDRN---CTVLFGTSTF---LGNYARFaHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYG 512
Cdd:PRK08974 283 TNP---RDIPGFVKELKkypFTAITGVNTLfnaLLNNEEF-QELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 513 VTECAPVVSIN-VPMAAKSGTVGRILPGMDARLL----AVPGIEDGGRLQLKGPNIMSGYL-RVEKpgvlevpTAEnaqg 586
Cdd:PRK08974 359 LTECSPLVSVNpYDLDYYSGSIGLPVPSTEIKLVdddgNEVPPGEPGELWVKGPQVMLGYWqRPEA-------TDE---- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 587 EIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQ-LALAVSADKMHATAIKSDASkGEALVLFTT--DS 663
Cdd:PRK08974 428 VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDvVMLHPKVLEVAAVGVPSEVS-GEAVKIFVVkkDP 506
|
330 340 350
....*....|....*....|....*....|....*...
gi 489124149 664 ELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK08974 507 SLTEEELITHCRRH-LTGYKVPKLVEFRDELPKSNVGK 543
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
364-701 |
3.08e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 145.50 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPSP-L 442
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATM-VFPSPsF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 HYRIVPELVYDRNCTVLFGTST-FLgnyARFAHP----YDFHRLRY-VVAGAEKLQDSTKQLwQEKFGLR-VLEGYGVTE 515
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTmFI---AELEHPdfdkFDLSSLRTgIMAGAPCPPELMKRV-IEVMNMKdVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 CAPVV---SINVPMAAKSGTVGRILPGMDARLL-----AVPGIEDGGRLQLKGPNIMSGYLRVEKpgvlevPTAENAQGE 587
Cdd:cd05917 156 TSPVStqtRTDDSIEKRVNTVGRIMPHTEAKIVdpeggIVPPVGVPGELCIRGYSVMKGYWNDPE------KTAEAIDGD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 588 ierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVS-LEMVEQLALAVSADKMHATAIKsDASKGE---ALVLFTTDS 663
Cdd:cd05917 230 ---GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYpREIEEFLHTHPKVSDVQVVGVP-DERYGEevcAWIRLKEGA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489124149 664 ELTREKLQQYAR---AHgvpeLAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05917 306 ELTEEDIKAYCKgkiAH----YKVPRYVFFVDEFPLTVSGK 342
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
260-614 |
3.14e-38 |
|
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: 148.92 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 260 LMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDKgklwhLPEQLTQVrwVYLEDLKAD 339
Cdd:cd05904 62 LLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEK-----LASLALPV--VLLDSAEFD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 340 VTFSDKLWIFSHLLAPHLAQVKQqpEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIAD--FTADDRFMSALPLFH 417
Cdd:cd05904 135 SLSFSDLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 418 SFGLTVGLFTPLLTGAEVFLYPSplhyrivpelvydrnctvlFGTSTFLGNYARF----------------AHP----YD 477
Cdd:cd05904 213 IYGLSSFALGLLRLGATVVVMPR-------------------FDLEELLAAIERYkvthlpvvppivlalvKSPivdkYD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 478 FHRLRYVVAGAEKLQDSTKQLWQEKF-GLRVLEGYGVTECAPVVSINVP---MAAKSGTVGRILPGMDARLLavpGIEDG 553
Cdd:cd05904 274 LSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIV---DPETG 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124149 554 --------GRLQLKGPNIMSGYLRVEKpgvlevptaENAQGEIERGWYDTGDIVRFDENGFVQIQGRAK 614
Cdd:cd05904 351 eslppnqtGELWIRGPSIMKGYLNNPE---------ATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLK 410
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
366-701 |
6.40e-38 |
|
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: 144.18 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVflYP-SPLHY 444
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATV--VPvAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 445 RIVPELVYDRNCTVLFGTSTFLgnYARFAHP----YDFHRLRYVVAGAEKLQDSTKQLWQEKFGLR-VLEGYGVTECApV 519
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLF--QSLLDHPgrkkFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG-V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 520 VSINVP---MAAKSGTVGRILPGMDARllavpgIEDGGRLQLKGPNIMSGYLRVEKpgvlevPTAENAQgeiERGWYDTG 596
Cdd:cd17638 156 ATMCRPgddAETVATTCGRACPGFEVR------IADDGEVLVRGYNVMQGYLDDPE------ATAEAID---ADGWLHTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 597 DIVRFDENGFVQIQGRAKRF----------AKIAGEMVSLEMVEQLA-LAVSADKMhataiksdASKGEALVLFTTDSEL 665
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMyivggfnvypAEVEGALAEHPGVAQVAvIGVPDERM--------GEVGKAFVVARPGVTL 292
|
330 340 350
....*....|....*....|....*....|....*.
gi 489124149 666 TREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd17638 293 TEEDVIAWCRER-LANYKVPRFVRFLDELPRNASGK 327
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
233-703 |
7.01e-38 |
|
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: 147.84 E-value: 7.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKY-STEGERIGLMLPNaGISAAVIFGAIARRRipammnytAGVKGLTSAITASEIKTIF---- 307
Cdd:cd05926 16 TYADLAELVDDLARQLAALgIKKGDRVAIALPN-GLEFVVAFLAAARAG--------AVVAPLNPAYKKAEFEFYLadlg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 308 TSRQFLDKGklWHLPEQ-LTQVRWVYLEDLKADVTFSDKLWIfSHLLAPHLA-------QVKQQPEDAAVILFTSGSEGH 379
Cdd:cd05926 87 SKLVLTPKG--ELGPASrAASKLGLAILELALDVGVLIRAPS-AESLSNLLAdkknaksEGVPLPDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 380 PKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyrivpelvydrnctvl 459
Cdd:cd05926 164 PKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPR------------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 460 FGTSTFLGNYARF--------------------AHPYD-FHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAP 518
Cdd:cd05926 225 FSASTFWPDVRDYnatwytavptihqillnrpePNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSIN--VPMAAKSGTVG-------RILPgmDARLLAVPGIEdgGRLQLKGPNIMSGYLRVEKpgvlevptaENAQGEIE 589
Cdd:cd05926 305 QMTSNplPPGPRKPGSVGkpvgvevRILD--EDGEILPPGVV--GEICLRGPNVTRGYLNNPE---------ANAEAAFK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 590 RGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTT---DSELT 666
Cdd:cd05926 372 DGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlreGASVT 451
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 489124149 667 REKLQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGKPD 703
Cdd:cd05926 452 EEELRAFCRKH----LAafkVPKKVYFVDELPKTATGKIQ 487
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
365-701 |
3.06e-37 |
|
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: 144.79 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhy 444
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGP--- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 445 RIVPELVYDR----NCTVLFGTSTFlgnYARFA----HPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTEC 516
Cdd:cd05972 158 RFDAERILELleryGVTSFCGPPTA---YRMLIkqdlSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 517 APVVSINVPMAAKSGTVGRILPGMDARLL------AVPGIEDGGRLQLKGPNIMSGYLRVEKpgvlevPTAENAQGeier 590
Cdd:cd05972 235 GLTVGNFPDMPVKPGSMGRPTPGYDVAIIdddgreLPPGEEGDIAIKLPPPGLFLGYVGDPE------KTEASIRG---- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 591 GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFT---TDSE 664
Cdd:cd05972 305 DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEvvkAFVVLTsgyEPSE 384
|
330 340 350
....*....|....*....|....*....|....*..
gi 489124149 665 LTREKLQQYARAHGVPElAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05972 385 ELAEELQGHVKKVLAPY-KYPREIEFVEELPKTISGK 420
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
355-710 |
2.44e-36 |
|
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: 142.26 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 355 PHLAQvKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFM-SALPLFHSfGLTVGLFTPLLTGA 433
Cdd:cd05969 80 EELYE-RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWcTADPGWVT-GTVYGIWAPWLNGV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 434 EVFLYPSPLHYRIVPELVYDRNCTVLFGTST----FLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLE 509
Cdd:cd05969 158 TNVVYEGRFDAESWYGIIERVKVTVWYTAPTairmLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 510 GYGVTECAPVVSINVP-MAAKSGTVGRILPGMDARLLAVPG--IEDG--GRLQLKG--PNIMSGYLRVEkpgvlevptaE 582
Cdd:cd05969 238 TWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVDENGneLPPGtkGILALKPgwPSMFRGIWNDE----------E 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 583 NAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTT- 661
Cdd:cd05969 308 RYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISl 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489124149 662 -----DSELTREKLQQYARaHGVPELAVPRDIRHLKQLPLLGSGKPDFVTLKSW 710
Cdd:cd05969 388 kegfePSDELKEEIINFVR-QKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
353-614 |
2.65e-36 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 143.48 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 353 LAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTG 432
Cdd:PRK07514 144 APDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 433 AEVFLYPsplhyRIVPELVYDR--NCTVLFGTSTFlgnYARF-AHPyDFHR-----LRYVVAGAEKLQDSTKQLWQEKFG 504
Cdd:PRK07514 224 ASMIFLP-----KFDPDAVLALmpRATVMMGVPTF---YTRLlQEP-RLTReaaahMRLFISGSAPLLAETHREFQERTG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 505 LRVLEGYGVTECAPVVSiNvPMAAK--SGTVGRILPGMDARllaVPGIEDG--------GRLQLKGPNIMSGYLRV-EKp 573
Cdd:PRK07514 295 HAILERYGMTETNMNTS-N-PYDGErrAGTVGFPLPGVSLR---VTDPETGaelppgeiGMIEVKGPNVFKGYWRMpEK- 368
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489124149 574 gvlevpTAEnaqgEI-ERGWYDTGDIVRFDENGFVQIQGRAK 614
Cdd:PRK07514 369 ------TAE----EFrADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
365-701 |
9.10e-36 |
|
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: 140.31 E-value: 9.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSPLHY 444
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM-ARWDR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 445 RIVPELVYDRNCTVLFGTSTF---LGNYARFAHpYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVS 521
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMlvdLLATPEFKT-RDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 522 INVPMAAKSGTVGRILPGMDARLLAvpgIEDG--------GRLQLKGPNIMSGYLRVEKpgvlevptaENAQGEIE---R 590
Cdd:cd05935 242 TNPPLRPKLQCLGIP*FGVDARVID---IETGrelppnevGEIVVRGPQIFKGYWNRPE---------ETEESFIEikgR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 591 GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTD--SEL 665
Cdd:cd05935 310 RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEevkAFIVLRPEyrGKV 389
|
330 340 350
....*....|....*....|....*....|....*.
gi 489124149 666 TREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05935 390 TEEDIIEWAREQ-MAAYKYPREVEFVDELPRSASGK 424
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
350-701 |
1.13e-35 |
|
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: 139.79 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 350 SHLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVgLFTPL 429
Cdd:cd05912 62 PNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-LMRSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 430 LTGAEVFLYPsplHY--RIVPELVYDRNCTVLFGTSTFLGNY-ARFAHPYDFHrLRYVVAGAEKLQDSTKQLWQEKfGLR 506
Cdd:cd05912 141 IYGMTVYLVD---KFdaEQVLHLINSGKVTIISVVPTMLQRLlEILGEGYPNN-LRCILLGGGPAPKPLLEQCKEK-GIP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 507 VLEGYGVTE-CAPVVSINVPMA-AKSGTVGRILPGMDARLLAVPGIEDG-GRLQLKGPNIMSGYLRVEKPGvlevptaen 583
Cdd:cd05912 216 VYQSYGMTEtCSQIVTLSPEDAlNKIGSAGKPLFPVELKIEDDGQPPYEvGEILLKGPNVTKGYLNRPDAT--------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 584 aQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLF-TTD 662
Cdd:cd05912 287 -EESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFvVSE 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489124149 663 SELTREKLQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGK 701
Cdd:cd05912 366 RPISEEELIAYCSEK----LAkykVPKKIYFVDELPRTASGK 403
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
338-614 |
9.30e-35 |
|
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: 138.26 E-value: 9.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 338 ADVTFSDKLWIFSHLLAPHLAqVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFH 417
Cdd:cd17640 62 SDSSVEELLYILNHSESVALV-VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 418 SFGLTVGLFTPLLTGAEVFLYPSPL---------HYRI-VPEL-------VYD------RNCTVLFGTSTFLGNyarfah 474
Cdd:cd17640 141 SYERSAEYFIFACGCSQAYTSIRTLkddlkrvkpHYIVsVPRLweslysgIQKqvskssPIKQFLFLFFLSGGI------ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 475 pydfhrLRYVVAGAEKLQDSTKQLWqEKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAV------- 547
Cdd:cd17640 215 ------FKFGISGGGALPPHVDTFF-EAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPegnvvlp 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 548 PGIEdgGRLQLKGPNIMSGYLRveKPgvlevptAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAK 614
Cdd:cd17640 288 PGEK--GIVWVRGPQVMKGYYK--NP-------EATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAK 343
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
363-703 |
9.83e-35 |
|
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: 137.82 E-value: 9.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMsalpLFHS--FGLTV-GLFTPLLTGAEVFLYP 439
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSyaFDFSVwEIWGALLHGGRLVVVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 -----SPLHYRivpELVYDRNCTVLFGT-STFLGNYARFAHPY-DFHRLRYVVAGAEKLQDSTKQLWQEKFGL---RVLE 509
Cdd:cd17643 167 yevarSPEDFA---RLLRDEGVTVLNQTpSAFYQLVEAADRDGrDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 510 GYGVTECAPVVSI------NVPMAAKSgTVGRILPG-----MDARLLAVPgieDG--GRLQLKGPNIMSGYLRveKPGVl 576
Cdd:cd17643 244 MYGITETTVHVTFrpldaaDLPAAAAS-PIGRPLPGlrvyvLDADGRPVP---PGvvGELYVSGAGVARGYLG--RPEL- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 577 evpTAE----NAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASK 652
Cdd:cd17643 317 ---TAErfvaNPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPG 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489124149 653 GEALVLFTTD---SELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17643 394 DTRLVAYVVAddgAAADIAELRALLKEL-LPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
364-703 |
1.21e-34 |
|
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: 137.38 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFlypspl 442
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPF--SFDLSVmDLYPALASGATLV------ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 hyrIVPELVYD-----------RNCTVLFGTSTFL------GNYARFAHPydfhRLRYVVAGAEKLQDSTKQLWQEKF-G 504
Cdd:cd05945 168 ---PVPRDATAdpkqlfrflaeHGITVWVSTPSFAamcllsPTFTPESLP----SLRHFLFCGEVLPHKTARALQQRFpD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 505 LRVLEGYGVTEC-APVVSINV--PMAAKSGTV--GRILPGMDARLLAvpgiEDG--------GRLQLKGPNIMSGYLRVE 571
Cdd:cd05945 241 ARIYNTYGPTEAtVAVTYIEVtpEVLDGYDRLpiGYAKPGAKLVILD----EDGrpvppgekGELVISGPSVSKGYLNNP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 572 KpgvlevPTAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDAS 651
Cdd:cd05945 317 E------KTAAAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGE 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 652 KGEALVLFTTDSELTREKLQQYARAH---GVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd05945 391 KVTELIAFVVPKPGAEAGLTKAIKAElaeRLPPYMIPRRFVYLDELPLNANGKID 445
|
|
| LPLAT_AGPAT-like |
cd07989 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ... |
9-188 |
1.96e-34 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.
Pssm-ID: 153251 [Multi-domain] Cd Length: 184 Bit Score: 129.70 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 9 LFRVLFRVRVTGDVSALQGERVLITPNHVSFIDGILLALFLPIRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMS-- 86
Cdd:cd07989 5 LRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNGRSar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 87 --IKHLVRLVEQGRPVVIFPEGRISTTGSLMKIYDGAGFVAAKSGATVVPVRIEGAELSRFSRLKGlvkqRFFPRIRLHI 164
Cdd:cd07989 85 eaLREAIEALKEGESVVIFPEGTRSRDGELLPFKSGAFRLAKEAGVPIVPVAISGTWGSLPKGKKL----PRPGRVTVRI 160
|
170 180
....*....|....*....|....
gi 489124149 165 LPPTQLPmPEAPRARDRRKIAGEM 188
Cdd:cd07989 161 GEPIPPE-GLELAEEDRKELREKV 183
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
254-701 |
5.00e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 137.59 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 254 EGERIGLMLPNAGISAAVIFGAIarrripammnyTAG--VKGLTSAITASEIKtiftsRQFLDKG--------KLWHLPE 323
Cdd:PRK05677 74 PGDRIAVQLPNVLQYPVAVFGAM-----------RAGliVVNTNPLYTAREME-----HQFNDSGakalvclaNMAHLAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 324 QL---TQVRWVYLEDLKADVTFSDKLWIFS---HL--LAP--HLAQ------------------VKQQPEDAAVILFTSG 375
Cdd:PRK05677 138 KVlpkTGVKHVIVTEVADMLPPLKRLLINAvvkHVkkMVPayHLPQavkfndalakgagqpvteANPQADDVAVLQYTGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 376 SEGHPKGVVHSHKSILANVEQIKTIADFTADD---RFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhyRIVPELVY 452
Cdd:PRK05677 218 TTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNP---RDLPAMVK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 453 D---RNCTVLFGTSTF---LGNYARFaHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVPM 526
Cdd:PRK05677 295 ElgkWKFSGFVGLNTLfvaLCNNEAF-RKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQ 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 527 AAKSGTVGRILPGMDARLLAVPGIE----DGGRLQLKGPNIMSGYLrvEKPGVlevpTAENAQGEierGWYDTGDIVRFD 602
Cdd:PRK05677 374 AIQVGTIGIPVPSTLCKVIDDDGNElplgEVGELCVKGPQVMKGYW--QRPEA----TDEILDSD---GWLKTGDIALIQ 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 603 ENGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLAVSADKMHATAIK-SDASKGEALVLFT---TDSELTREKLQQYARAHg 678
Cdd:PRK05677 445 EDGYMRIVDRKKDMILVSGFNVYPNELEDV-LAALPGVLQCAAIGvPDEKSGEAIKVFVvvkPGETLTKEQVMEHMRAN- 522
|
490 500
....*....|....*....|...
gi 489124149 679 VPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK05677 523 LTGYKVPKAVEFRDELPTTNVGK 545
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
233-614 |
5.77e-34 |
|
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: 136.98 E-value: 5.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYSTEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGL--TSAITA-SEIKTIFTS 309
Cdd:cd05931 26 TYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAerLAAILAdAGPRVVLTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 310 RQFLDKGKLWHLPEQLTQVRWVYLEDLKADvtfsdklwifshLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKS 389
Cdd:cd05931 106 AAALAAVRAFAASRPAAGTPRLLVVDLLPD------------TSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 390 ILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSPLHY----RIVPELVYDRNctvlfGTSTF 465
Cdd:cd05931 174 LLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM-SPAAFlrrpLRWLRLISRYR-----ATISA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 466 LGNYArFAH-----------PYDFHRLRYVVAGAEKLQDSTKQLWQEKF---GLR---VLEGYGVTEC----------AP 518
Cdd:cd05931 248 APNFA-YDLcvrrvrdedleGLDLSSWRVALNGAEPVRPATLRRFAEAFapfGFRpeaFRPSYGLAEAtlfvsggppgTG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSINVPMAAKSGTV----------------GRILPGMDARLL-AVPGIE--DG--GRLQLKGPNIMSGYLRveKPGVLE 577
Cdd:cd05931 327 PVVLRVDRDALAGRAvavaaddpaarelvscGRPLPDQEVRIVdPETGRElpDGevGEIWVRGPSVASGYWG--RPEATA 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 489124149 578 VpTAENAQGEIERGWYDTGDIVRFDENGFVqIQGRAK 614
Cdd:cd05931 405 E-TFGALAATDEGGWLRTGDLGFLHDGELY-ITGRLK 439
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
364-701 |
6.99e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 137.01 E-value: 6.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplh 443
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP---- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 444 yR----IVPELVYDRNCTVLFGTST----FLGNyARFAHpYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE 515
Cdd:PRK08314 265 -RwdreAAARLIERYRVTHWTNIPTmvvdFLAS-PGLAE-RDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 CAPVVSINVPMAAKSGTVGRILPGMDARL-----LAVPGIEDGGRLQLKGPNIMSGYLRVEKpgvlevptaENAQGEIER 590
Cdd:PRK08314 342 TMAQTHSNPPDRPKLQCLGIPTFGVDARVidpetLEELPPGEVGEIVVHGPQVFKGYWNRPE---------ATAEAFIEI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 591 G---WYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLalavsadkMHA-TAIK-------SDASKGE---AL 656
Cdd:PRK08314 413 DgkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENL--------LYKhPAIQeacviatPDPRRGEtvkAV 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489124149 657 VLFTTDSE--LTREKLQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGK 701
Cdd:PRK08314 485 VVLRPEARgkTTEEEIIAWAREH----MAaykYPRIVEFVDSLPKSGSGK 530
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
368-711 |
1.03e-33 |
|
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: 132.07 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 368 AVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVgLFTPLLTGAEVFL---------- 437
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLlernqalaed 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 438 --YPSPLHYRIVP-ELVYdrnctVLfgtstflgnyARFAHPYDFHRLRYVVAGAEKL-QDSTKQLwqEKFGLRVLEGYGV 513
Cdd:cd17630 82 laPPGVTHVSLVPtQLQR-----LL----------DSGQGPAALKSLRAVLLGGAPIpPELLERA--ADRGIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 514 TECAPVVSINVPMAAKSGTVGRILPGmdARLlavpGIEDGGRLQLKGPNIMSGYLRvekpGVLEVPTAENaqgeierGWY 593
Cdd:cd17630 145 TETASQVATKRPDGFGRGGVGVLLPG--REL----RIVEDGEIWVGGASLAMGYLR----GQLVPEFNED-------GWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 594 DTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLF-TTDSELTREKLQQ 672
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAViVGRGPADPAELRA 287
|
330 340 350
....*....|....*....|....*....|....*....
gi 489124149 673 YARAHgVPELAVPRDIRHLKQLPLLGSGKPDFVTLKSWV 711
Cdd:cd17630 288 WLKDK-LARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
353-638 |
1.34e-33 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 133.54 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 353 LAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTV-GLFTPLLT 431
Cdd:TIGR01733 108 PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASL--SFDASVeEIFGALLA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 432 GAEVFLYPSPLHYRIVPE---LVYDRNCTVLFGTSTFLGNYARfAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFG-LRV 507
Cdd:TIGR01733 186 GATLVVPPEDEERDDAALlaaLIAEHPVTVLNLTPSLLALLAA-ALPPALASLRLVILGGEALTPALVDRWRARGPgARL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 508 LEGYGVTECAPVVSINVPMAAKSG-----TVGRILPGMDARLLA-----VP-GIEdgGRLQLKGPNIMSGYLrvEKPGVl 576
Cdd:TIGR01733 265 INLYGPTETTVWSTATLVDPDDAPrespvPIGRPLANTRLYVLDddlrpVPvGVV--GELYIGGPGVARGYL--NRPEL- 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 577 evpTAEN-----AQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSA 638
Cdd:TIGR01733 340 ---TAERfvpdpFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPG 403
|
|
| PlsC |
COG0204 |
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ... |
1-204 |
4.53e-33 |
|
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 439974 [Multi-domain] Cd Length: 215 Bit Score: 126.66 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 1 MLFGFFRNLFRVL-FRVRVTGDVSALQGERVLITPNHVSFIDGILLALFLPIRPVFAVYTSISQQWYMRWLTPLIDFVPL 79
Cdd:COG0204 15 LVRLWARLLLRLLgVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKIPLLGWLLRALGAIPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 80 DPTKPM----SIKHLVRLVEQGRPVVIFPEGRISTTGSLMKIYDGAGFVAAKSGATVVPVRIEGAELSRFsrlKGLVKQR 155
Cdd:COG0204 95 DRSKRRaalrALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGAARLALEAGVPIVPVAIDGTERALP---KGFLPRP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489124149 156 ffPRIRLHILPPTQlpmPEAPRARDRRKIAgEMLHQIMMEARMAVRPRE 204
Cdd:COG0204 172 --GKVTVRIGPPID---PSDLEGEDRRELA-ERLRAAIEALLAELRAEA 214
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
360-701 |
6.20e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 134.18 E-value: 6.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 360 VKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADD---------RFMSA-LPLFHSFGLTVGLFTPL 429
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqEVMIApLPLYHIYAFTANCMCMM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 430 LTGAEVFLYPSPlhyRIVPELVYDR---NCTVLFGTSTFLgnYARFAHP----YDFHRLRYVVAGAEKLQDSTKQLWQEK 502
Cdd:PRK12492 282 VSGNHNVLITNP---RDIPGFIKELgkwRFSALLGLNTLF--VALMDHPgfkdLDFSALKLTNSGGTALVKATAERWEQL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 503 FGLRVLEGYGVTECAPVVSINvPMA--AKSGTVGRILPGMDARLLAVPGIE----DGGRLQLKGPNIMSGYLrvEKPGVl 576
Cdd:PRK12492 357 TGCTIVEGYGLTETSPVASTN-PYGelARLGTVGIPVPGTALKVIDDDGNElplgERGELCIKGPQVMKGYW--QQPEA- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 577 evpTAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEAL 656
Cdd:PRK12492 433 ---TAEALDAE---GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAV 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489124149 657 VLFTTDSE--LTREKLQQYARA----HGVPELAVPRDirhlkQLPLLGSGK 701
Cdd:PRK12492 507 KLFVVARDpgLSVEELKAYCKEnftgYKVPKHIVLRD-----SLPMTPVGK 552
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
364-632 |
1.03e-32 |
|
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: 133.49 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANV----EQIKTIADFTADDRFMSALPLFHSF-----------GLTVGLF-- 426
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAHIFervvealflyhGAKIGFYsg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 427 -TPLLTGAEVFLYPS--PLhyriVPEL---VYDRNCTVLFGTST---FLGNYA------------RFAHPY-D---FH-- 479
Cdd:cd05927 193 dIRLLLDDIKALKPTvfPG----VPRVlnrIYDKIFNKVQAKGPlkrKLFNFAlnyklaelrsgvVRASPFwDklvFNki 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 480 ------RLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVP----- 548
Cdd:cd05927 269 kqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPemnyd 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 549 --GIEDGGRLQLKGPNIMSGYLRVEKPgvlevpTAEnaqgEI-ERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GEMV 624
Cdd:cd05927 349 akDPNPRGEVCIRGPNVFSGYYKDPEK------TAE----ALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYV 418
|
....*...
gi 489124149 625 SLEMVEQL 632
Cdd:cd05927 419 APEKIENI 426
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
301-701 |
3.45e-32 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 131.21 E-value: 3.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 301 SEIKTIFTSRQFLDKgkLWHLPEQLTQVR--WVYLEDLKADVTFSDKLWIFSHLLAPH--LAQVKQQPE-DAAVILFTSG 375
Cdd:cd12119 96 AEDRVVFVDRDFLPL--LEAIAPRLPTVEhvVVMTDDAAMPEPAGVGVLAYEELLAAEspEYDWPDFDEnTAAAICYTSG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 376 SEGHPKGVVHSHKSILanveqIKTIADFTAD-------DRFMSALPLFH--SFGLTvglFTPLLTGAEvFLYPSP-LHYR 445
Cdd:cd12119 174 TTGNPKGVVYSHRSLV-----LHAMAALLTDglglsesDVVLPVVPMFHvnAWGLP---YAAAMVGAK-LVLPGPyLDPA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 446 IVPELVYDRNCTVLFGTSTF---LGNYARfAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKfGLRVLEGYGVTECAPVVSI 522
Cdd:cd12119 245 SLAELIEREGVTFAAGVPTVwqgLLDHLE-ANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPLGTV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 523 NVPMAAKSG-----------TVGRILPGMDARLLAVPGIE---DG---GRLQLKGPNIMSGYLRVEkpgvlevptaENAQ 585
Cdd:cd12119 323 ARPPSEHSNlsedeqlalraKQGRPVPGVELRIVDDDGRElpwDGkavGELQVRGPWVTKSYYKND----------EESE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 586 GEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTD 662
Cdd:cd12119 393 ALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErplAVVVLKEG 472
|
410 420 430
....*....|....*....|....*....|....*....
gi 489124149 663 SELTREKLQQYARAhGVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd12119 473 ATVTAEELLEFLAD-KVAKWWLPDDVVFVDEIPKTSTGK 510
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
364-681 |
6.23e-32 |
|
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: 130.41 E-value: 6.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKT-IADF-TADDRFMSALPLFHSFGLTVgLFTPLLTGAEVFlYPSP 441
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrVPELlGPDDRYLAYLPLAHIFELAA-ENVCLYRGGTIG-YGSP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 --LHYRI------------------VPElVYDR---------NCTVLFGTSTFLGNYAR----FAHPYD--------FH- 479
Cdd:cd17639 165 rtLTDKSkrgckgdltefkptlmvgVPA-IWDTirkgvlaklNPMGGLKRTLFWTAYQSklkaLKEGPGtplldelvFKk 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 480 -------RLRYVVAGAEKLQDSTkQLWQEKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVPgiED 552
Cdd:cd17639 244 vraalggRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWE--EG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 553 G---------GRLQLKGPNIMSGYLRVEkpgvlevptAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GE 622
Cdd:cd17639 321 GystdkppprGEILIRGPNVFKGYYKNP---------EKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGE 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489124149 623 MVSLEMVEQLALAVSADK---MHAtaiKSDASKGEALVLfttdseLTREKLQQYARAHGVPE 681
Cdd:cd17639 392 YIALEKLESIYRSNPLVNnicVYA---DPDKSYPVAIVV------PNEKHLTKLAEKHGVIN 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
366-702 |
1.07e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 128.18 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSpLHYR 445
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPR-FSAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 446 IVPELVYDRNCTVLfgtsTFLGNYARF--AHPYDF----HRLRyVVAGAEKLqDSTKQLWQEKFGLRVLEGYGVTECAPV 519
Cdd:cd05934 161 RFWSDVRRYGATVT----NYLGAMLSYllAQPPSPddraHRLR-AAYGAPNP-PELHEEFEERFGVRLLEGYGMTETIVG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 520 VSINVPMAAKSGTVGRILPGMDARLL-----AVPgIEDGGRLQLK---GPNIMSGYLRVEKPgvlevpTAENAQGeierG 591
Cdd:cd05934 235 VIGPRDEPRRPGSIGRPAPGYEVRIVdddgqELP-AGEPGELVIRglrGWGFFKGYYNMPEA------TAEAMRN----G 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 592 WYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHAT-AIKSDASKGE--ALVLFTTDSELTRE 668
Cdd:cd05934 304 WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVvAVPDEVGEDEvkAVVVLRPGETLDPE 383
|
330 340 350
....*....|....*....|....*....|....
gi 489124149 669 KLQQYARAhGVPELAVPRDIRHLKQLPLLGSGKP 702
Cdd:cd05934 384 ELFAFCEG-QLAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
305-701 |
4.87e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 128.33 E-value: 4.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 305 TIFTSRQFLDKgkLWHLPEQLTQVRWVYLEDLKADVTFSDKLwifSHLLA---PHLAQVKQQPEDAAVILFTSGSEGHPK 381
Cdd:PRK06087 129 TLFKQTRPVDL--ILPLQNQLPQLQQIVGVDKLAPATSSLSL---SQIIAdyePLTTAITTHGDELAAVLFTSGTEGLPK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 382 GVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplHYRIVP--ELVYDRNCTVL 459
Cdd:PRK06087 204 GVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD---IFTPDAclALLEQQRCTCM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 460 FGTSTF---LGNYARfAHPYDFHRLR-YVVAGAEKLQDSTKQLWQekFGLRVLEGYGVTECAP--VVSINVPMAAKSGTV 533
Cdd:PRK06087 281 LGATPFiydLLNLLE-KQPADLSALRfFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTESSPhaVVNLDDPLSRFMHTD 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 534 GRILPGM------DARLLAVPGIEdgGRLQLKGPNIMSGYLrvEKPgvlevptAENAQGEIERGWYDTGDIVRFDENGFV 607
Cdd:PRK06087 358 GYAAAGVeikvvdEARKTLPPGCE--GEEASRGPNVFMGYL--DEP-------ELTARALDEEGWYYSGDLCRMDEAGYI 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 608 QIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTTDSE----LTREKLQQYARAHGVPELA 683
Cdd:PRK06087 427 KITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAphhsLTLEEVVAFFSRKRVAKYK 506
|
410
....*....|....*...
gi 489124149 684 VPRDIRHLKQLPLLGSGK 701
Cdd:PRK06087 507 YPEHIVVIDKLPRTASGK 524
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
233-701 |
1.07e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 127.58 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVAR-ILEKYSTEGERIGLMLPNagiSAAVIFGAIARRRIPAMM---NYTAGVKGLTSAITASEIKTIFT 308
Cdd:PRK12583 47 TWRQLADAVDRLARgLLALGVQPGDRVGIWAPN---CAEWLLTQFATARIGAILvniNPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 309 SRQFldKGKLWH------------------LPEQLTQVRWVYLEDLKAD---VTFSDKLWIFSHLLAPHLAQVKQQ--PE 365
Cdd:PRK12583 124 ADAF--KTSDYHamlqellpglaegqpgalACERLPELRGVVSLAPAPPpgfLAWHELQARGETVSREALAERQASldRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPS----P 441
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACL-VYPNeafdP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 LhyrIVPELVYDRNCTVLFGTST-FLgnyARFAHP----YDFHRLRY-VVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE 515
Cdd:PRK12583 281 L---ATLQAVEEERCTALYGVPTmFI---AELDHPqrgnFDLSSLRTgIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 CAPVV---SINVPMAAKSGTVGRILPGMDARLL----AVPGIEDGGRLQLKGPNIMSGYLRVEKpgvlevPTAENAQGEi 588
Cdd:PRK12583 355 TSPVSlqtTAADDLERRVETVGRTQPHLEVKVVdpdgATVPRGEIGELCTRGYSVMKGYWNNPE------ATAESIDED- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 589 erGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSEL 665
Cdd:PRK12583 428 --GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEeivAWVRLHPGHAA 505
|
490 500 510
....*....|....*....|....*....|....*.
gi 489124149 666 TREKLQQYARAhGVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK12583 506 SEEELREFCKA-RIAHFKVPRYFRFVDEFPMTVTGK 540
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
365-701 |
1.09e-30 |
|
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: 125.67 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQI-KTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplh 443
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLE---- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 444 yRIVPELVYD----RNCTVLFGTSTflGNYARFAHP----YDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE 515
Cdd:cd05958 173 -EATPDLLLSaiarYKPTVLFTAPT--AYRAMLAHPdaagPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 CAPVVSINVPMAAKSGTVGRILPGMDARLLAVPG--IEDG--GRLQLKGPNIMSGYlrvekpgvlevpTAENAQGEIERG 591
Cdd:cd05958 250 MFHIFISARPGDARPGATGKPVPGYEAKVVDDEGnpVPDGtiGRLAVRGPTGCRYL------------ADKRQRTYVQGG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 592 WYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL---AVSADKMHATAIKSDASKGEALVLF---TTDSEL 665
Cdd:cd05958 318 WNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLqhpAVAECAVVGHPDESRGVVVKAFVVLrpgVIPGPV 397
|
330 340 350
....*....|....*....|....*....|....*.
gi 489124149 666 TREKLQQYARAHGVPeLAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05958 398 LARELQDHAKAHIAP-YKYPRAIEFVTELPRTATGK 432
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
233-701 |
1.24e-30 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 127.09 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYSTE-GERIGLMLPNaGISAAVIfgAIARRRIPAMMNYTAGV---KGLTSAITASEIKTIFT 308
Cdd:PRK13295 57 TYRELAALVDRVAVGLARLGVGrGDVVSCQLPN-WWEFTVL--YLACSRIGAVLNPLMPIfreRELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 309 SRQFLD---KGKLWHLPEQLTQVRWVYLEDLKADVTFSDKLWIFSHLLAPHLAQVKQQ----PEDAAVILFTSGSEGHPK 381
Cdd:PRK13295 134 PKTFRGfdhAAMARRLRPELPALRHVVVVGGDGADSFEALLITPAWEQEPDAPAILARlrpgPDDVTQLIYTSGTTGEPK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 382 GVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVpELVYDRNCTVLFG 461
Cdd:PRK13295 214 GVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAA-ELIRTEGVTFTMA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 462 TSTFLGNYARF--AHPYDFHRLR-YVVAGAEKLQDSTKQLWQeKFGLRVLEGYGVTECApVVSINVPMAAK---SGTVGR 535
Cdd:PRK13295 293 STPFLTDLTRAvkESGRPVSSLRtFLCAGAPIPGALVERARA-ALGAKIVSAWGMTENG-AVTLTKLDDPDeraSTTDGC 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 536 ILPGM-----DARLLAVPGIEDgGRLQLKGPNIMSGYLRveKPGVlevpTAENAQgeierGWYDTGDIVRFDENGFVQIQ 610
Cdd:PRK13295 371 PLPGVevrvvDADGAPLPAGQI-GRLQVRGCSNFGGYLK--RPQL----NGTDAD-----GWFDTGDLARIDADGYIRIS 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 611 GRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSELTREKLQQYARAHGV-----PEL 682
Cdd:PRK13295 439 GRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGEracAFVVPRPGQSLDFEEMVEFLKAQKVakqyiPER 518
|
490
....*....|....*....
gi 489124149 683 AVPRDirhlkQLPLLGSGK 701
Cdd:PRK13295 519 LVVRD-----ALPRTPSGK 532
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
365-701 |
1.24e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 126.51 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILAN-VEQIKTIaDFTADDRFMSALPLFHSFGltVGLFT-PLLTGAEVFLYPSPL 442
Cdd:PRK06839 149 SASFIICYTSGTTGKPKGAVLTQENMFWNaLNNTFAI-DLTMHDRSIVLLPLFHIGG--IGLFAfPTLFAGGVIIVPRKF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 HYRIVPELVYDRNCTVLFGTSTF---LGNYARFAHPyDFHRLRYVVAGAEKLQDSTKQLWQEKfGLRVLEGYGVTECAPV 519
Cdd:PRK06839 226 EPTKALSMIEKHKVTVVMGVPTIhqaLINCSKFETT-NLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 520 VSI--NVPMAAKSGTVGRILPGMDARLLAVPG--IEDG--GRLQLKGPNIMSGYLRVEKPgvlevpTAENaqgeIERGWY 593
Cdd:PRK06839 304 VFMlsEEDARRKVGSIGKPVLFCDYELIDENKnkVEVGevGELLIRGPNVMKEYWNRPDA------TEET----IQDGWL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 594 DTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSELTREKL 670
Cdd:PRK06839 374 CTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEipiAFIVKKSSSVLIEKDV 453
|
330 340 350
....*....|....*....|....*....|.
gi 489124149 671 QQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK06839 454 IEHCRLF-LAKYKIPKEIVFLKELPKNATGK 483
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
364-613 |
3.35e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 124.72 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGaevflypSPLH 443
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIG-------NRFV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 444 Y--RIVPELV---YDRNCTVLFGTSTFlgnYARFA----HPYDFHRLRYVVAGA--------EKLQDSTkqlwqekfGLR 506
Cdd:PRK07787 200 HtgRPTPEAYaqaLSEGGTLYFGVPTV---WSRIAadpeAARALRGARLLVSGSaalpvpvfDRLAALT--------GHR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 507 VLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVPGIE---DG---GRLQLKGPNIMSGYLrvEKPGVlevpT 580
Cdd:PRK07787 269 PVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPvphDGetvGELQVRGPTLFDGYL--NRPDA----T 342
|
250 260 270
....*....|....*....|....*....|...
gi 489124149 581 AENAQGEierGWYDTGDIVRFDENGFVQIQGRA 613
Cdd:PRK07787 343 AAAFTAD---GWFRTGDVAVVDPDGMHRIVGRE 372
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
364-709 |
5.91e-30 |
|
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: 123.19 E-value: 5.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFL--Y 438
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVA----QVLSIAFDACigeIFSTLCNGGTLVLadP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 439 PSPLHYRIvpelvydRNCTVLFGTSTFLGNYArfahPYDFHRLRYVVAGAEKLQDSTKQLWqeKFGLRVLEGYGVTECAP 518
Cdd:cd17653 180 SDPFAHVA-------RTVDALMSTPSILSTLS----PQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSINVPMAAKSGTVGRILPG-----MDARLLAVPgIEDGGRLQLKGPNIMSGYLRVEKpgvlevPTAEN-AQGEIERGW 592
Cdd:cd17653 247 SSTMTELLPGQPVTIGKPIPNstcyiLDADLQPVP-EGVVGEICISGVQVARGYLGNPA------LTASKfVPDPFWPGS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 593 --YDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDaskgEALVLFTTDSELTREKL 670
Cdd:cd17653 320 rmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVN----GRLVAFVTPETVDVDGL 395
|
330 340 350
....*....|....*....|....*....|....*....
gi 489124149 671 QQYARAHgVPELAVPRDIRHLKQLPLLGSGKPDFVTLKS 709
Cdd:cd17653 396 RSELAKH-LPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
357-701 |
7.11e-30 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 124.99 E-value: 7.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 357 LAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTAD-----DRFMSALPLFHSFGLTVGLFTPLLT 431
Cdd:PRK08751 200 MPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYHIFALTANGLVFMKI 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 432 GAEVFLYPSPLHYR-IVPELVYDRnCTVLFGTSTF---LGNYARFAHpYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRV 507
Cdd:PRK08751 280 GGCNHLISNPRDMPgFVKELKKTR-FTAFTGVNTLfngLLNTPGFDQ-IDFSSLKMTLGGGMAVQRSVAERWKQVTGLTL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 508 LEGYGVTECAPVVSINvPMAAK--SGTVGRILPGMDA-------RLLAVPGIedgGRLQLKGPNIMSGYLRveKPGvlEV 578
Cdd:PRK08751 358 VEAYGLTETSPAACIN-PLTLKeyNGSIGLPIPSTDAcikddagTVLAIGEI---GELCIKGPQVMKGYWK--RPE--ET 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 579 PTAENAQgeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEAL-- 656
Cdd:PRK08751 430 AKVMDAD-----GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVkv 504
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489124149 657 VLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK08751 505 VIVKKDPALTAEDVKAHARAN-LTGYKQPRIIEFRKELPKTNVGK 548
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
233-703 |
1.97e-29 |
|
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: 123.41 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYS-TEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQ 311
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGlKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 312 FLDKgkLWHLPEQLTQVRWVYLEDLKADVT--FSDKLWIFSHLlAPHLAQVKQQP------EDAAVILFTSGSEGHPKGV 383
Cdd:cd17642 126 GLQK--VLNVQKKLKIIKTIIILDSKEDYKgyQCLYTFITQNL-PPGFNEYDFKPpsfdrdEQVALIMNSSGSTGLPKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 384 VHSHKSILANVEQIKT---IADFTADDRFMSALPLFHSFG-------LTVGLFTPLLTGAEVFLYPSPLH-YRI-----V 447
Cdd:cd17642 203 QLTHKNIVARFSHARDpifGNQIIPDTAILTVIPFHHGFGmfttlgyLICGFRVVLMYKFEEELFLRSLQdYKVqsallV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 448 PELVydrnctVLFGTSTFLGNyarfahpYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLR-VLEGYGVTECAPVVSINVPM 526
Cdd:cd17642 283 PTLF------AFFAKSTLVDK-------YDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 527 AAKSGTVGRILPGMDARLL-----AVPGIEDGGRLQLKGPNIMSGYLRVEKpgvlevptAENAQgEIERGWYDTGDIVRF 601
Cdd:cd17642 350 DDKPGAVGKVVPFFYAKVVdldtgKTLGPNERGELCVKGPMIMKGYVNNPE--------ATKAL-IDKDGWLHSGDIAYY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 602 DENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSELTREKLQQYARAHG 678
Cdd:cd17642 421 DEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGElpaAVVVLEAGKTMTEKEVMDYVASQV 500
|
490 500
....*....|....*....|....*
gi 489124149 679 VPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17642 501 STAKRLRGGVKFVDEVPKGLTGKID 525
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
363-711 |
2.47e-29 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 122.27 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFM--SAlplfHSFGLTVG-LFTPLLTGAEVFLyP 439
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfAS----YTFDVSILeIFTTLAAGGCLCI-P 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SpLHYRI--VPELVYDRNCTVLFGTSTFlgnyARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKfgLRVLEGYGVTECA 517
Cdd:cd05918 179 S-EEDRLndLAGFINRLRVTWAFLTPSV----ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAECT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 518 PVVSINVPMA-AKSGTVGRILPG----MDA----RLLAVPGIedgGRLQLKGPNIMSGYL-RVEKPGVLEVPTAENAQGE 587
Cdd:cd05918 252 IAATVSPVVPsTDPRNIGRPLGAtcwvVDPdnhdRLVPIGAV---GELLIEGPILARGYLnDPEKTAAAFIEDPAWLKQE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 588 IERG---WYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVE---------------------------QLALAVS 637
Cdd:cd05918 329 GSGRgrrLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEhhlrqslpgakevvvevvkpkdgssspQLVAFVV 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489124149 638 ADKMHATAIKSDASKGEALVLFTTDSELTREKLQQYARAHGVPELAVPrdirhLKQLPLLGSGKPDFVTLKSWV 711
Cdd:cd05918 409 LDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSYMVPSVFLP-----LSHLPLTASGKIDRRALRELA 477
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
357-701 |
6.31e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 122.05 E-value: 6.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 357 LAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIAD--FTADDR-----FMSALPLFHSFGLTVGLFTPL 429
Cdd:PRK07059 196 FKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpaFEKKPRpdqlnFVCALPLYHIFALTVCGLLGM 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 430 LTGAEVFLYPSPlhyRIVPELV-----YDRNC----TVLFGTstfLGNYARFaHPYDFHRLRYVVAGAEKLQDSTKQLWQ 500
Cdd:PRK07059 276 RTGGRNILIPNP---RDIPGFIkelkkYQVHIfpavNTLYNA---LLNNPDF-DKLDFSKLIVANGGGMAVQRPVAERWL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 501 EKFGLRVLEGYGVTECAPVVSINVPMAAK-SGTVGRILPGMDARLLAvpgiEDG--------GRLQLKGPNIMSGYLrvE 571
Cdd:PRK07059 349 EMTGCPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSIRD----DDGndlplgepGEICIRGPQVMAGYW--N 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 572 KPgvlevptAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLAlAVSADKMHATAIK-SDA 650
Cdd:PRK07059 423 RP-------DETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV-ASHPGVLEVAAVGvPDE 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489124149 651 SKGEALVLFTT--DSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK07059 495 HSGEAVKLFVVkkDPALTEEDVKAFCKER-LTNYKRPKFVEFRTELPKTNVGK 546
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
364-719 |
3.86e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 119.75 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PE-DAAVILFTSGSEGHPKGVVHSHKSILAN----VEQIKTIADftADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY 438
Cdd:PRK06710 204 PEnDLALLQYTGGTTGFPKGVMLTHKNLVSNtlmgVQWLYNCKE--GEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 439 PSpLHYRIVPELVYDRNCTVLFGTSTFLgnYARFAHP----YDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVT 514
Cdd:PRK06710 282 PK-FDMKMVFEAIKKHKVTLFPGAPTIY--IALLNSPllkeYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 515 ECAPVVSINVPMAAK-SGTVGRILPGMDARLLAV-------PGieDGGRLQLKGPNIMSGYLrvEKPgvlevptaENAQG 586
Cdd:PRK06710 359 ESSPVTHSNFLWEKRvPGSIGVPWPDTEAMIMSLetgealpPG--EIGEIVVKGPQIMKGYW--NKP--------EETAA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 587 EIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDS 663
Cdd:PRK06710 427 VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGEtvkAFVVLKEGT 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489124149 664 ELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKpdfVTLKSWVDEPEKQHE 719
Cdd:PRK06710 507 ECSEEELNQFARKY-LAAYKVPKVYEFRDELPKTTVGK---ILRRVLIEEEKRKNE 558
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
352-637 |
2.20e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 117.02 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 352 LLAPHLAQVKQQPEDAAVIL-FTSGSEGHPKGVVHSHKSILANVEQIKTIADFTAD-DRFMSALPLFHSFGLTVGLFTPL 429
Cdd:PRK07768 138 LLAADPIDPVETGEDDLALMqLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPM 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 430 LTGAEVfLYPSPLHYRIVPeLVYDRNCTVLFGTSTFLGNYA---------RFAHP--YDFHRLRYVVAGAEKLQDSTKQL 498
Cdd:PRK07768 218 YFGAEL-VKVTPMDFLRDP-LLWAELISKYRGTMTAAPNFAyallarrlrRQAKPgaFDLSSLRFALNGAEPIDPADVED 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 499 WQE---KFGLR---VLEGYGVTECAPVVSIN----------------------VPmAAKSGT-----VGRILPGMDARLL 545
Cdd:PRK07768 296 LLDagaRFGLRpeaILPAYGMAEATLAVSFSpcgaglvvdevdadllaalrraVP-ATKGNTrrlatLGPPLPGLEVRVV 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 546 AvpgiEDG--------GRLQLKGPNIMSGYLRVEKPgvleVPTAEnaqgeiERGWYDTGDIVRFDENGFVQIQGRAKRFA 617
Cdd:PRK07768 375 D----EDGqvlpprgvGVIELRGESVTPGYLTMDGF----IPAQD------ADGWLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
330 340
....*....|....*....|
gi 489124149 618 KIAGEMVSLEMVEQLALAVS 637
Cdd:PRK07768 441 IMAGRNIYPTDIERAAARVE 460
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
362-614 |
2.77e-27 |
|
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: 116.61 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLT-VGLFtPLLTGAEVFLYPS 440
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVeLHLR-AVYLGCQQVHVPT 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 PL-------------HYRIvpelvydrnctvlfgTSTFLGNYArFAH-----------PYDFHRLRYVVAGAEKLQDSTK 496
Cdd:cd05906 243 EEiladplrwldlidRYRV---------------TITWAPNFA-FALlndlleeiedgTWDLSSLRYLVNAGEAVVAKTI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 497 QLWQ---EKFGLR---VLEGYGVTE-CAPVVSINVPMAAKSGT------VGRILPGMDARL--LAVPGIEDG--GRLQLK 559
Cdd:cd05906 307 RRLLrllEPYGLPpdaIRPAFGMTEtCSGVIYSRSFPTYDHSQalefvsLGRPIPGVSMRIvdDEGQLLPEGevGRLQVR 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 560 GPNIMSGYLRvekpgvleVPTAeNAQGEIERGWYDTGDIVrFDENGFVQIQGRAK 614
Cdd:cd05906 387 GPVVTKGYYN--------NPEA-NAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
364-703 |
2.80e-26 |
|
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: 113.06 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIaDFTADDRFMSALPLfhSF-GLTVGLFTPLLTGAEVFLYPS-- 440
Cdd:cd12117 135 PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPL--AFdASTFEIWGALLNGARLVLAPKgt 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 PLHYRIVPELVYDRNCTVLFGTSTFLGNYARfAHPYDFHRLRYVVAGAEKLQ-DSTKQLWQEKFGLRVLEGYGVTECAPV 519
Cdd:cd12117 212 LLDPDALGALIAEEGVTVLWLTAALFNQLAD-EDPECFAGLRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTTF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 520 VSINV--PMAAKSGTV--GRILPGMDARLL------AVPGIEdgGRLQLKGPNIMSGYLRveKPGVlevpTAE----NAQ 585
Cdd:cd12117 291 TTSHVvtELDEVAGSIpiGRPIANTRVYVLdedgrpVPPGVP--GELYVGGDGLALGYLN--RPAL----TAErfvaDPF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 586 GEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTT-DSE 664
Cdd:cd12117 363 GPGER-LYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVaEGA 441
|
330 340 350
....*....|....*....|....*....|....*....
gi 489124149 665 LTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd12117 442 LDAAELRAFLRER-LPAYMVPAAFVVLDELPLTANGKVD 479
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
347-703 |
6.27e-26 |
|
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: 111.98 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 347 WIFSHLlAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTVG-L 425
Cdd:cd17646 121 EALAAP-PATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL--SFDVSVWeL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 426 FTPLLTGAEVFLYPSPLH----YriVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQE 501
Cdd:cd17646 198 FWPLVAGARLVVARPGGHrdpaY--LAALIREHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 502 KFGLRVLEGYGVTEcapvVSINVPMAAKSGT-------VGRILPG-----MDARLLAVP-GIedGGRLQLKGPNIMSGYL 568
Cdd:cd17646 276 LPGAELHNLYGPTE----AAIDVTHWPVRGPaetpsvpIGRPVPNtrlyvLDDALRPVPvGV--PGELYLGGVQLARGYL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 569 RveKPGVlevpTAEN------AQGeiERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMH 642
Cdd:cd17646 350 G--RPAL----TAERfvpdpfGPG--SR-MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTH 419
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489124149 643 ATAIKSDASKGEA-----LVLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17646 420 AVVVARAAPAGAArlvgyVVPAAGAAGPDTAALRAHLAER-LPEYMVPAAFVVLDALPLTANGKLD 484
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
362-703 |
6.86e-26 |
|
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: 111.31 E-value: 6.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSalplFHSFGLTVG---LFTPLLTGAEVFLY 438
Cdd:cd17649 91 HHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQ----FASFNFDGAheqLLPPLICGACVVLR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 439 PSPL------HYRIVPELvydrNCTVLFGTSTFLGNYARFA---HPYDFHRLRYVVAGAEKLQDSTKQLWQeKFGLRVLE 509
Cdd:cd17649 167 PDELwasadeLAEMVREL----GVTVLDLPPAYLQQLAEEAdrtGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 510 GYGVTECAPVVSINVP-----MAAKSGTVGRILPG-----MDARLLAVPgieDG--GRLQLKGPNIMSGYLrvEKPGVle 577
Cdd:cd17649 242 AYGPTEATVTPLVWKCeagaaRAGASMPIGRPLGGrsayiLDADLNPVP---VGvtGELYIGGEGLARGYL--GRPEL-- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 578 vpTAEN-----AQGEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKmHATAIKSDASK 652
Cdd:cd17649 315 --TAERfvpdpFGAPGSR-LYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVR-EAAVVALDGAG 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489124149 653 GEALVLF-----TTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17649 391 GKQLVAYvvlraAAAQPELRAQLRTALRAS-LPDYMVPAHLVFLARLPLTPNGKLD 445
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
365-701 |
8.93e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 111.95 E-value: 8.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILAnvEQIKTIA--DFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPl 442
Cdd:PRK08316 171 DDLAQILYTSGTESLPKGAMLTHRALIA--EYVSCIVagDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAP- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 hyriVPELVYDR----NCTVLFGTSTF---LGNYARFAhPYDFHRLRYVVAGA-----EKLQDstkqlWQEKF-GLRVLE 509
Cdd:PRK08316 248 ----DPELILRTieaeRITSFFAPPTVwisLLRHPDFD-TRDLSSLRKGYYGAsimpvEVLKE-----LRERLpGLRFYN 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 510 GYGVTECAPVVSINVP--MAAKSGTVGRILPGMDARLLAVPG--IEDG--GRLQLKGPNIMSGYLRveKPgvleVPTAEN 583
Cdd:PRK08316 318 CYGQTEIAPLATVLGPeeHLRRPGSAGRPVLNVETRVVDDDGndVAPGevGEIVHRSPQLMLGYWD--DP----EKTAEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 584 AQGeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlAL----AVSADKMHATaikSDASKGE---AL 656
Cdd:PRK08316 392 FRG----GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE-ALythpAVAEVAVIGL---PDPKWIEavtAV 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489124149 657 VLFTTDSELTREKLQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGK 701
Cdd:PRK08316 464 VVPKAGATVTEDELIAHCRAR----LAgfkVPKRVIFVDELPRNPSGK 507
|
|
| Acyltransferase |
pfam01553 |
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ... |
15-137 |
2.51e-25 |
|
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.
Pssm-ID: 366704 [Multi-domain] Cd Length: 131 Bit Score: 101.59 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 15 RVRVTGDVSALQGERVLITPNHVSFIDGILLALFLPI---RPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPM----SI 87
Cdd:pfam01553 1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLLSLALYKrgrPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKdaagTL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489124149 88 KHLVRLVEQGRPVVIFPEGRISTTGSLMKIYDGAGFVAAKSGATVVPVRI 137
Cdd:pfam01553 81 EYLVELLREGKLVVIFPEGTRSREGELLPFKKGAFRLAIEAGVPIVPVAI 130
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
366-707 |
3.13e-25 |
|
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: 109.72 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTV-GLFTPLLTGAEVFLYPSPlhy 444
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDP--- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 445 riVPELVY---DR---NCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE--- 515
Cdd:cd05920 217 --SPDAAFpliERegvTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgll 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 CapVVSINVPMAAKSGTVGR-ILPG-----MDARLLAVPGIEDGgRLQLKGPNIMSGYLRVEkpgvlevptAENAQGEIE 589
Cdd:cd05920 295 N--YTRLDDPDEVIIHTQGRpMSPDdeirvVDEEGNPVPPGEEG-ELLTRGPYTIRGYYRAP---------EHNARAFTP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 590 RGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFT--TDSELTR 667
Cdd:cd05920 363 DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVvlRDPPPSA 442
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489124149 668 EKLQQYARAHGVPELAVPRDIRHLKQLPLLGSGKPDFVTL 707
Cdd:cd05920 443 AQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
364-703 |
4.29e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 112.36 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPL 442
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVVAAPGD 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 HYRI--VPELVYDRNCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKL-QDSTKQLWQEKFGLRVLEGYGVTECAPV 519
Cdd:PRK12316 732 HRDPakLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALpADAQEQVFAKLPQAGLYNLYGPTEAAID 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 520 V--SINVPMAAKSGTVGRILPG-----MDARLLAVP-GIEdgGRLQLKGPNIMSGYLRveKPGVlevpTAE----NAQGE 587
Cdd:PRK12316 812 VthWTCVEEGGDSVPIGRPIANlacyiLDANLEPVPvGVL--GELYLAGRGLARGYHG--RPGL----TAErfvpSPFVA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 588 IERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKmHATAIKSDASKGEALVLFTTDSELTR 667
Cdd:PRK12316 884 GER-MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR-EAAVLAVDGKQLVGYVVLESEGGDWR 961
|
330 340 350
....*....|....*....|....*....|....*.
gi 489124149 668 EKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK12316 962 EALKAHLAAS-LPEYMVPAQWLALERLPLTPNGKLD 996
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
356-703 |
1.06e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.20 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 356 HLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTV-GLFTPLLTGAE 434
Cdd:PRK12316 4685 HDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF--SFDGSHeGLYHPLINGAS 4762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 435 VFLYPSPLH--YRIVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQ-DSTKQLWQEKFGLRVLEGY 511
Cdd:PRK12316 4763 VVIRDDSLWdpERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAqASYDLAWRALKPVYLFNGY 4842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 512 GVTECAPVVSI-----NVPMAAKSGTVGRILPGMDARLLAVPG----IEDGGRLQLKGPNIMSGYLrvEKPGVLE---VP 579
Cdd:PRK12316 4843 GPTETTVTVLLwkardGDACGAAYMPIGTPLGNRSGYVLDGQLnplpVGVAGELYLGGEGVARGYL--ERPALTAerfVP 4920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 580 TAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAIKSDASKGEALV-- 657
Cdd:PRK12316 4921 DPFGAPGG---RLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEA-RLREHPAVREAVVIAQEGAVGKQLVgy 4996
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 658 LFTTDSELT---------REKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK12316 4997 VVPQDPALAdadeaqaelRDELKAALRER-LPEYMVPAHLVFLARMPLTPNGKLD 5050
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
372-703 |
1.12e-24 |
|
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: 105.57 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 372 FTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAevFLYPSPLHYRIVPELV 451
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGT--FIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 452 YDRNCTVLFGTSTFLGNYARFAHPYdfHRLRYVVAGAEKLQDSTKQLWQEKF-GLRVLEGYGVTEcAPVVSINVPM-AAK 529
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPE--SKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQeSRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 530 SGTVGRILPGMDARLLAVPGIEDGgRLQLKGPNIMSGYLRVekpgvlevptaenaQGEIERGWYDTGDIVRFDENGFVQI 609
Cdd:cd17633 162 PNSVGRPFPNVEIEIRNADGGEIG-KIFVKSEMVFSGYVRG--------------GFSNPDGWMSVGDIGYVDEEGYLYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 610 QGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQQYARahgvPELA---VPR 686
Cdd:cd17633 227 VGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQLKRFLK----QKLSryeIPK 302
|
330
....*....|....*..
gi 489124149 687 DIRHLKQLPLLGSGKPD 703
Cdd:cd17633 303 KIIFVDSLPYTSSGKIA 319
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
255-673 |
1.49e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 108.53 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 255 GERIGLMLPNAGISAAVIFGAIARRRIPAMMN--YTAGvkGLTSAITASEIKTIFTSRQFLDKGKLWHLPEQLTqvrwVY 332
Cdd:PLN02246 75 GDVVMLLLPNCPEFVLAFLGASRRGAVTTTANpfYTPA--EIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVT----VV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 333 LEDLKADVTFSdklwiFSHLLAP---HLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQiktIAD------- 402
Cdd:PLN02246 149 TIDDPPEGCLH-----FSELTQAdenELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQ---QVDgenpnly 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 403 FTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhYRIVP--ELVYDRNCTVlfgtstflgnyARFAHP----- 475
Cdd:PLN02246 221 FHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPK---FEIGAllELIQRHKVTI-----------APFVPPivlai 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 476 --------YDFHRLRYVVAGA----EKLQDSTK-QLWQEKFGlrvlEGYGVTECAPVVSINV-----PMAAKSGTVGRIL 537
Cdd:PLN02246 287 akspvvekYDLSSIRMVLSGAaplgKELEDAFRaKLPNAVLG----QGYGMTEAGPVLAMCLafakePFPVKSGSCGTVV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 538 PGMDARLLAVPGIEDGGRLQ-----LKGPNIMSGYLR-VEKpgvlevpTAENAQGEierGWYDTGDIVRFDENGFVQIQG 611
Cdd:PLN02246 363 RNAELKIVDPETGASLPRNQpgeicIRGPQIMKGYLNdPEA-------TANTIDKD---GWLHTGDIGYIDDDDELFIVD 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 612 RAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSELTREKLQQY 673
Cdd:PLN02246 433 RLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEvpvAFVVRSNGSEITEDEIKQF 497
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
366-638 |
1.93e-24 |
|
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: 105.04 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypSPLHYR 445
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVM--EKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 446 IVPELVYDRNCTVLFGTSTFLGNY--ARFAHPYDFHRLRYvVAGAEKLQdsTKQLWQEKFGLRVLEGYGVTECAPVVSIN 523
Cdd:cd17637 79 EALELIEEEKVTLMGSFPPILSNLldAAEKSGVDLSSLRH-VLGLDAPE--TIQRFEETTGATFWSLYGQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 524 vPMAAKSGTVGRILPGMDARLL-----AVPGIEDgGRLQLKGPNIMSGYLRVEkpgvlevptAENAQgEIERGWYDTGDI 598
Cdd:cd17637 156 -PYRERPGSAGRPGPLVRVRIVddndrPVPAGET-GEIVVRGPLVFQGYWNLP---------ELTAY-TFRNGWHHTGDL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489124149 599 VRFDENGFVQIQGR--AKRFAKIAGEMVSLEMVEQLALAVSA 638
Cdd:cd17637 224 GRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPA 265
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
354-717 |
2.33e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.87 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 354 APHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVgLFTPLLTGA 433
Cdd:PRK12467 645 SGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTE-LFGALASGA 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 434 EVFLYPSPLHYRivPE----LVYDRNCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEK-FGLRVL 508
Cdd:PRK12467 724 TLHLLPPDCARD--AEafaaLMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALgPGARLI 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 509 EGYGVTECAPVVSI----NVPMAAKSGTVGRILPG-----MDARLLAVPGiEDGGRLQLKGPNIMSGYLRveKPGVLE-- 577
Cdd:PRK12467 802 NHYGPTETTVGVSTyelsDEERDFGNVPIGQPLANlglyiLDHYLNPVPV-GVVGELYIGGAGLARGYHR--RPALTAer 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 578 -VPTAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVsADKMHATAIKSDASKGEAL 656
Cdd:PRK12467 879 fVPDPFGADGG---RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQ-PGVREAVVLAQPGDAGLQL 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124149 657 VLF--------TTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPDFVTLKSWVDEPEKQ 717
Cdd:PRK12467 955 VAYlvpaavadGAEHQATRDELKAQLRQV-LPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQA 1022
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
323-710 |
5.84e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 106.90 E-value: 5.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 323 EQLTQVRWVYLEDlkADVTFSDKLWIFSHLLA---PHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKT 399
Cdd:PRK04319 162 DDLPSLKHVLLVG--EDVEEGPGTLDFNALMEqasDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKY 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 400 IADFTADDRFM-SALPLFHSfGLTVGLFTPLLTGA------EVFlypSPLH-YRIVPELvydrNCTVLFGTST----FLG 467
Cdd:PRK04319 240 VLDLHEDDVYWcTADPGWVT-GTSYGIFAPWLNGAtnvidgGRF---SPERwYRILEDY----KVTVWYTAPTairmLMG 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 468 NYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVP-MAAKSGTVGRILPGMDARLLA 546
Cdd:PRK04319 312 AGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPaMDIKPGSMGKPLPGIEAAIVD 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 547 VPGIEDG----GRLQLKG--PNIMSGYLRVEkpgvlevptaENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA 620
Cdd:PRK04319 392 DQGNELPpnrmGNLAIKKgwPSMMRGIWNNP----------EKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 621 GEMV-SLE----MVEQLALAvsadkmHATAI-KSDASKGE---ALVL----FTTDSELtREKLQQYAR----AHgvpelA 683
Cdd:PRK04319 462 GERVgPFEveskLMEHPAVA------EAGVIgKPDPVRGEiikAFVAlrpgYEPSEEL-KEEIRGFVKkglgAH-----A 529
|
410 420
....*....|....*....|....*..
gi 489124149 684 VPRDIRHLKQLPLLGSGKPDFVTLKSW 710
Cdd:PRK04319 530 APREIEFKDKLPKTRSGKIMRRVLKAW 556
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
367-701 |
6.76e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 106.33 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 367 AAVILFTSGSEGHPKGVVHSHKSIL--ANVEQIKTIADFTADDRFMSALPLFH--SFGLTvglFTPLLTGAEVFLyPSP- 441
Cdd:PRK07008 178 ASSLCYTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHvnAWGLP---YSAPLTGAKLVL-PGPd 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 LHYRIVPELVYDRNCTVLFGTST-FLG--NYARfAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAP 518
Cdd:PRK07008 254 LDGKSLYELIEAERVTFSAGVPTvWLGllNHMR-EAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSINVPMAAKSG-----------TVGRILPGMDARLLAVPGIE---DG---GRLQLKGPNIMSGYLRVEkpgvlevpta 581
Cdd:PRK07008 333 LGTLCKLKWKHSQlpldeqrklleKQGRVIYGVDMKIVGDDGRElpwDGkafGDLQVRGPWVIDRYFRGD---------- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 582 enaQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMhATAIKSDASKGEA----LV 657
Cdd:PRK07008 403 ---ASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAE-AACIACAHPKWDErpllVV 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489124149 658 LFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK07008 479 VKRPGAEVTREELLAFYEGK-VAKWWIPDDVVFVDAIPHTATGK 521
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
297-701 |
1.14e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 105.66 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 297 AITASEIKTIFTSRQFLD------------------KGKLWHlpEQLTQVRWV-YLEDLKADVTFSdklwiFSHLLA--- 354
Cdd:PRK08315 110 ALNQSGCKALIAADGFKDsdyvamlyelapelatcePGQLQS--ARLPELRRViFLGDEKHPGMLN-----FDELLAlgr 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 355 ----PHLAQVKQ--QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTP 428
Cdd:PRK08315 183 avddAELAARQAtlDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLAC 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 429 LLTGA------EVFlypSPLHyriVPELVYDRNCTVLFGTST-FLgnyARFAHP----YDFHRLRY-VVAGaeklqdST- 495
Cdd:PRK08315 263 VTHGAtmvypgEGF---DPLA---TLAAVEEERCTALYGVPTmFI---AELDHPdfarFDLSSLRTgIMAG------SPc 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 496 -----KQLwQEKFGLR-VLEGYGVTECAPVV---SINVPMAAKSGTVGRILPGMDARLLavpGIEDG--------GRLQL 558
Cdd:PRK08315 328 pievmKRV-IDKMHMSeVTIAYGMTETSPVStqtRTDDPLEKRVTTVGRALPHLEVKIV---DPETGetvprgeqGELCT 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 559 KGPNIMSGYLR-VEKpgvlevpTAEnaqgEIER-GWYDTGDIVRFDENGFVQIQGRAK----RfakiAGEMVS-LEMVEQ 631
Cdd:PRK08315 404 RGYSVMKGYWNdPEK-------TAE----AIDAdGWMHTGDLAVMDEEGYVNIVGRIKdmiiR----GGENIYpREIEEF 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 632 LalavsadkMHATAIKS-------DASKGEALVLFTT---DSELTREKLQQYARAHgvpeLA---VPRDIRHLKQLPLLG 698
Cdd:PRK08315 469 L--------YTHPKIQDvqvvgvpDEKYGEEVCAWIIlrpGATLTEEDVRDFCRGK----IAhykIPRYIRFVDEFPMTV 536
|
...
gi 489124149 699 SGK 701
Cdd:PRK08315 537 TGK 539
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
288-620 |
1.15e-23 |
|
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: 105.24 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 288 TAGVKGLTSAITASEIKTIFTsrqfldkGKLWH-------LPEQLTQVRWVYLEDLKADVTFSDKLwifsHLLAPHLAQV 360
Cdd:cd05932 64 TLNPDTIRYVLEHSESKALFV-------GKLDDwkamapgVPEGLISISLPPPSAANCQYQWDDLI----AQHPPLEERP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 361 KQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
Cdd:cd05932 133 TRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAES 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 ------------PLHYRIVPEL-------VYDR----NCTVLFGTStFLGNYAR--FAHPYDFHRLRYVVAGAEKLQDST 495
Cdd:cd05932 213 ldtfvedvqrarPTLFFSVPRLwtkfqqgVQDKipqqKLNLLLKIP-VVNSLVKrkVLKGLGLDQCRLAGCGSAPVPPAL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 496 kQLWQEKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARllavpgIEDGGRLQLKGPNIMSGYLRVekpgv 575
Cdd:cd05932 292 -LEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVR------ISEDGEILVRSPALMMGYYKD----- 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489124149 576 lEVPTAENAQgeiERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA 620
Cdd:cd05932 360 -PEATAEAFT---ADGFLRTGDKGELDADGNLTITGRVKDIFKTS 400
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
365-701 |
1.45e-23 |
|
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: 102.72 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQI-KTIADFTADDRFMSALPLFHSFGLTVGLfTPLLTGAEVFLYPSPLH 443
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWIL-TCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 444 YRIVPELV--YDRNCTVLFGTS-TFLGNYARFAHPYdFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVV 520
Cdd:cd17635 80 YKSLFKILttNAVTTTCLVPTLlSKLVSELKSANAT-VPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 521 SINVPMAAKS-GTVGRILPGMDARLLAVPGIE----DGGRLQLKGPNIMSGYLrvekpgvlevptaENAQGEIER---GW 592
Cdd:cd17635 159 CLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAgpsaSFGTIWIKSPANMLGYW-------------NNPERTAEVlidGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 593 YDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTTDSELTREKL-- 670
Cdd:cd17635 226 VNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAir 305
|
330 340 350
....*....|....*....|....*....|..
gi 489124149 671 -QQYARAHGVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd17635 306 aLKHTIRRELEPYARPSTIVIVTDIPRTQSGK 337
|
|
| PlsC |
smart00563 |
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ... |
30-140 |
1.52e-23 |
|
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.
Pssm-ID: 214724 [Multi-domain] Cd Length: 118 Bit Score: 96.27 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 30 VLITPNHVSFIDGILLALFLP---IRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKP----MSIKHLVRLVEQGRPVVI 102
Cdd:smart00563 1 ALVVANHQSFLDPLVLSALLPrklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGrkarAALREAVELLKEGEWLLI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 489124149 103 FPEGRISTTGSLMKIYDGAGFVAAKSGATVVPVRIEGA 140
Cdd:smart00563 81 FPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIRGT 118
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
367-646 |
2.07e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 105.50 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 367 AAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIA-DFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYR 445
Cdd:PRK06060 147 LAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKAlRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 446 IVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKF-GLRVLEGYGVTECAPVVSINV 524
Cdd:PRK06060 227 AAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFgGIPILDGIGSTEVGQTFVSNR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 525 PMAAKSGTVGRILPGMDARLLAV------PGIEdgGRLQLKGPNIMSGYLRVEKPgVLEvptaenaqgeiERGWYDTGDI 598
Cdd:PRK06060 307 VDEWRLGTLGRVLPPYEIRVVAPdgttagPGVE--GDLWVRGPAIAKGYWNRPDS-PVA-----------NEGWLDTRDR 372
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489124149 599 VRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlaLAVSADKMHATAI 646
Cdd:PRK06060 373 VCIDSDGWVTYRCRADDTEVIGGVNVDPREVER--LIIEDEAVAEAAV 418
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
333-703 |
2.59e-23 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 106.09 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 333 LEDLKADVTFSDKLWIFSHllAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSA 412
Cdd:COG1020 587 LPELGVPVLALDALALAAE--PATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQF 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 413 LPLfhSFGLTVG-LFTPLLTGAEVFLYPSPLHY---RIVpELVYDRNCTVLFGTSTFLGNYARfAHPYDFHRLRYVVAGA 488
Cdd:COG1020 665 ASL--SFDASVWeIFGALLSGATLVLAPPEARRdpaALA-ELLARHRVTVLNLTPSLLRALLD-AAPEALPSLRLVLVGG 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 489 EKLQDSTKQLWQEKF-GLRVLEGYGVTECAPVVSI----NVPMAAKSGTVGRILPGM-----DARLLAVP-GIEdgGRLQ 557
Cdd:COG1020 741 EALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyevtPPDADGGSVPIGRPIANTrvyvlDAHLQPVPvGVP--GELY 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 558 LKGPNIMSGYLRveKPGVlevpTAE-------NAQGeiERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVE 630
Cdd:COG1020 819 IGGAGLARGYLN--RPEL----TAErfvadpfGFPG--AR-LYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIE 889
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 631 QLALAVSADKMHATAIKSDASKGEALVLF--TTDSELTREKLQQYARAHGVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:COG1020 890 AALLQHPGVREAVVVAREDAPGDKRLVAYvvPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLD 964
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
365-713 |
3.61e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 103.50 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHK----SILANVEQIktiaDFTADDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPs 440
Cdd:PRK03640 141 DEVATIMYTSGTTGKPKGVIQTYGnhwwSAVGSALNL----GLTEDDCWLAAVPIFHISGLSI-LMRSVIYGMRVVLVE- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 plHYRI--VPELVYDRNCTVLFGTSTFL---------GNYarfahPYDFhrlRYVVAGAEKLQDSTKQLWQEKfGLRVLE 509
Cdd:PRK03640 215 --KFDAekINKLLQTGGVTIISVVSTMLqrllerlgeGTY-----PSSF---RCMLLGGGPAPKPLLEQCKEK-GIPVYQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 510 GYGVTE-CAPVVSINvP--MAAKSGTVGRILPGMDARllavpgIEDGGRLQ---------LKGPNIMSGYLRVEKPgvle 577
Cdd:PRK03640 284 SYGMTEtASQIVTLS-PedALTKLGSAGKPLFPCELK------IEKDGVVVppfeegeivVKGPNVTKGYLNREDA---- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 578 vpTAENaqgeIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALV 657
Cdd:PRK03640 353 --TRET----FQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPV 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 658 LF-TTDSELTREKLQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGKPDFVTLKSWVDE 713
Cdd:PRK03640 427 AFvVKSGEVTEEELRHFCEEK----LAkykVPKRFYFVEELPRNASGKLLRHELKQLVEE 482
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
364-710 |
4.12e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 103.35 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP---- 439
Cdd:PRK09088 134 PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNgfep 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 ------------SPLHYRIVPELVydrnctvlfgtstflgnyARF-AHP-YDFHRLRYVVA----GAEKLqdSTKQLWQE 501
Cdd:PRK09088 214 krtlgrlgdpalGITHYFCVPQMA------------------QAFrAQPgFDAAALRHLTAlftgGAPHA--AEDILGWL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 502 KFGLRVLEGYGVTECAPVVSINVP---MAAKSGTVGRILPGMDARLLAVPG--IEDG--GRLQLKGPNIMSGYLRveKPg 574
Cdd:PRK09088 274 DDGIPMVDGFGMSEAGTVFGMSVDcdvIRAKAGAAGIPTPTVQTRVVDDQGndCPAGvpGELLLRGPNLSPGYWR--RP- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 575 vlevptAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEqlalAVSADKMH----ATAIKSDA 650
Cdd:PRK09088 351 ------QATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIE----AVLADHPGirecAVVGMADA 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124149 651 SKGEALVLFTTDSELTREKLQQyARAHGVPELA---VPRDIRHLKQLPLLGSGKPDFVTLKSW 710
Cdd:PRK09088 421 QWGEVGYLAIVPADGAPLDLER-IRSHLSTRLAkykVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
363-701 |
4.65e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 103.68 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSIL---ANVEQIKTIadfTADDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYP 439
Cdd:PRK06155 178 QPGDTAAILYTSGTTGPSKGVCCPHAQFYwwgRNSAEDLEI---GADDVLYTTLPLFHTNALNA-FFQALLAGATYVLEP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SPLHYRIVPELVyDRNCTVLFgtstFLGNY-----ARFAHPYD-FHRLRYVVAGAEKLQDStkQLWQEKFGLRVLEGYGV 513
Cdd:PRK06155 254 RFSASGFWPAVR-RHGATVTY----LLGAMvsillSQPARESDrAHRVRVALGPGVPAALH--AAFRERFGVDLLDGYGS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 514 TECapvvsiNVPMA-----AKSGTVGRILPGMDARLLAVPGIE--DG--GRLQLKGPN---IMSGYLRVEKPGVlevpta 581
Cdd:PRK06155 327 TET------NFVIAvthgsQRPGSMGRLAPGFEARVVDEHDQElpDGepGELLLRADEpfaFATGYFGMPEKTV------ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 582 enaqgEIERG-WYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL---AVSAdkMHATAIKSDASKGE--A 655
Cdd:PRK06155 395 -----EAWRNlWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLshpAVAA--AAVFPVPSELGEDEvmA 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489124149 656 LVLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK06155 468 AVVLRDGTALEPVALVRHCEPR-LAYFAVPRYVEFVAALPKTENGK 512
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
359-703 |
4.69e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 105.63 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 359 QVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDrfmsALPLFHSFGLTV---GLFTPLLTGAEV 435
Cdd:PRK12467 1712 AVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD----VVLQFTSFAFDVsvwELFWPLINGARL 1787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 436 FLYPSPLHYRivPELVYDRNC----TVLFGTST----FLGNYARFAHPYdfhRLRYVVAGAEKLQDSTKQLWQEKFGLRV 507
Cdd:PRK12467 1788 VIAPPGAHRD--PEQLIQLIErqqvTTLHFVPSmlqqLLQMDEQVEHPL---SLRRVVCGGEALEVEALRPWLERLPDTG 1862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 508 L-EGYGVTECA----------------PVVSINVPMAAKSGTVgrilpgMDARLLAVPgIEDGGRLQLKGPNIMSGYLRv 570
Cdd:PRK12467 1863 LfNLYGPTETAvdvthwtcrrkdlegrDSVPIGQPIANLSTYI------LDASLNPVP-IGVAGELYLGGVGLARGYLN- 1934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 571 eKPGVlevpTAE----NAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAI 646
Cdd:PRK12467 1935 -RPAL----TAErfvaDPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEA-RLREQGGVREAVVI 2008
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 647 KSDASKGEALV--LFTTDSELTREKLQQYA-----RAH---GVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK12467 2009 AQDGANGKQLVayVVPTDPGLVDDDEAQVAlrailKNHlkaSLPEYMVPAHLVFLARMPLTPNGKLD 2075
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
233-701 |
1.00e-22 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 103.04 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYST-EGERIGLMLPNagISAAVIfGAIARRRIPAMMNYTAG---VKGLTSAITASEIKTIFT 308
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVkKGDRVAIYMPM--IPEAAV-AMLACARIGAVHSVIFGgfaPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 309 SRQFLDKGKLWHLPE--------QLTQVRWVYLED-LKADVTFSDKLWIFSHLL----APHLAQVKQQPEDAAVILFTSG 375
Cdd:cd17634 163 ADGGVRAGRSVPLKKnvddalnpNVTSVEHVIVLKrTGSDIDWQEGRDLWWRDLiakaSPEHQPEAMNAEDPLFILYTSG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 376 SEGHPKGVVHSHKS-ILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY------PSPLHYRivp 448
Cdd:cd17634 243 TTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYegvpnwPTPARMW--- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 449 ELVYDRNCTVLFGTSTFLGNYARfAHP-----YDFHRLRYVVAGAEKLQDSTKQLWQEKFGLR---VLEGYGVTE----C 516
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMA-AGDdaiegTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTEtggfM 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 517 APVVSINVPMAAKSGTvgRILPGMDARLL------AVPGIEDGGRLQLKGPNIMSGYLRvekpgvlEVPTAENAQGEIER 590
Cdd:cd17634 399 ITPLPGAIELKAGSAT--RPVFGVQPAVVdneghpQPGGTEGNLVITDPWPGQTRTLFG-------DHERFEQTYFSTFK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 591 GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFT------TDSE 664
Cdd:cd17634 470 GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVvlnhgvEPSP 549
|
490 500 510
....*....|....*....|....*....|....*..
gi 489124149 665 LTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd17634 550 ELYAELRNWVRKE-IGPLATPDVVHWVDSLPKTRSGK 585
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
363-703 |
1.12e-22 |
|
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: 101.74 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFLYP 439
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVL----QFASIAFDVAaeeIYVTLLSGATLVLRP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SPLHYRIVPELVY--DRNCTVLFGTSTFLGNYARFAHPYDF---HRLRYVVAGAEKLQDSTKQLWQEKFG--LRVLEGYG 512
Cdd:cd17644 180 EEMRSSLEDFVQYiqQWQLTVLSLPPAYWHLLVLELLLSTIdlpSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 513 VTEC---APVVSINVPMAAKSG--TVGRILPG-----MDARLLAVPgIEDGGRLQLKGPNIMSGYLrvEKPGVlevpTAE 582
Cdd:cd17644 260 PTEAtiaATVCRLTQLTERNITsvPIGRPIANtqvyiLDENLQPVP-VGVPGELHIGGVGLARGYL--NRPEL----TAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 583 N------AQGEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEAL 656
Cdd:cd17644 333 KfishpfNSSESER-LYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489124149 657 VLFT---TDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17644 412 VAYIvphYEESPSTVELRQFLKAK-LPDYMIPSAFVVLEELPLTPNGKID 460
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
360-703 |
3.00e-22 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 100.88 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 360 VKQQPEDAAVILFTSGSEGHPKGVVHSHKSiLANVEQiktiadftADDRFMSALP-----LFHSFGLTVG---LFTPLLT 431
Cdd:cd17651 131 PALDADDLAYVIYTSGSTGRPKGVVMPHRS-LANLVA--------WQARASSLGPgartlQFAGLGFDVSvqeIFSTLCA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 432 GAEVFLYPSplHYRIVPE----LVYDRNCTVLFGTSTFLGNYARFAHPYDFH--RLRYVVAGAEKLQDS--TKQLWQEKF 503
Cdd:cd17651 202 GATLVLPPE--EVRTDPPalaaWLDEQRISRVFLPTVALRALAEHGRPLGVRlaALRYLLTGGEQLVLTedLREFCAGLP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 504 GLRVLEGYGVTECAPVVSINVPmAAKSG-----TVGRILPG-----MDARLLAVP-GIEdgGRLQLKGPNIMSGYLRveK 572
Cdd:cd17651 280 GLRLHNHYGPTETHVVTALSLP-GDPAAwpappPIGRPIDNtrvyvLDAALRPVPpGVP--GELYIGGAGLARGYLN--R 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 573 PGVLEVPTAENAQGEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEqLALAVSADKMHATAIKSDASK 652
Cdd:cd17651 355 PELTAERFVPDPFVPGAR-MYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIE-AALARHPGVREAVVLAREDRP 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 653 GE----ALVLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17651 433 GEkrlvAYVVGDPEAPVDAAELRAALATH-LPEYMVPSAFVLLDALPLTPNGKLD 486
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
360-701 |
3.10e-22 |
|
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: 100.20 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 360 VKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADF--TADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL 437
Cdd:cd05971 83 VTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 438 Y-PSPLHYRIVPELVYDRNCTVLFGTSTFLgNYARFAHPYDFH---RLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGV 513
Cdd:cd05971 163 HrMTKFDPKAALDLMSRYGVTTAFLPPTAL-KMMRQQGEQLKHaqvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 514 TECAPVVSIN-VPMAAKSGTVGRILPGMDARLlavpgIEDGGRLQlkgPNIMSGYLRVEKP------GVLEVPTAENAQg 586
Cdd:cd05971 242 TECNLVIGNCsALFPIKPGSMGKPIPGHRVAI-----VDDNGTPL---PPGEVGEIAVELPdpvaflGYWNNPSATEKK- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 587 eIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEA----LVL---F 659
Cdd:cd05971 313 -MAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIvkafVVLnpgE 391
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489124149 660 TTDSELTREkLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05971 392 TPSDALARE-IQELVKTR-LAAHEYPREIEFVNELPRTATGK 431
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
361-703 |
3.30e-22 |
|
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: 100.24 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 361 KQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADD-RFMSALPLFHSFglTVGLFTPLLTGAeVFLYp 439
Cdd:cd17654 114 IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDiLFLTSPLTFDPS--VVEIFLSLSSGA-TLLI- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SPLHYRIVPELVYD-----RNCTVLFGTSTFLgnyARFAHPYDFHR-------LRYVVAGAEKL-QDSTKQLWQEKF-GL 505
Cdd:cd17654 190 VPTSVKVLPSKLADilfkrHRITVLQATPTLF---RRFGSQSIKSTvlsatssLRVLALGGEPFpSLVILSSWRGKGnRT 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 506 RVLEGYGVTECAPVVSIN-VPMAAKSGTVGRILPGMDARLLAVPGIEDGGRLQLKGPNimSGYLRvekPGVLEVPTAEna 584
Cdd:cd17654 267 RIFNIYGITEVSCWALAYkVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLN--RVCIL---DDEVTVPKGT-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 585 qgeiergWYDTGDIVRFdENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIksdaSKGEALVLFTTdSE 664
Cdd:cd17654 340 -------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTL----SDQQRLIAFIV-GE 406
|
330 340 350
....*....|....*....|....*....|....*....
gi 489124149 665 LTREKLQQYARAHGVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17654 407 SSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVD 445
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
349-703 |
3.39e-22 |
|
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: 100.99 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 349 FSHLLAP--HLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTV-GL 425
Cdd:COG1021 166 LDALLAApaDLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 426 FTPLLTGAEVFL--YPSPLH-------YRI-----VPELVydrnctvlfgtSTFLgNYARfAHPYDFHRLRYVVAGAEKL 491
Cdd:COG1021 246 LGVLYAGGTVVLapDPSPDTafplierERVtvtalVPPLA-----------LLWL-DAAE-RSRYDLSSLRVLQVGGAKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 492 QDSTKQLWQEKFGLRVLEGYGVTE---CapVVSINVPMAAKSGTVGR-ILPGMDARLLAVPGIE--DG--GRLQLKGPNI 563
Cdd:COG1021 313 SPELARRVRPALGCTLQQVFGMAEglvN--YTRLDDPEEVILTTQGRpISPDDEVRIVDEDGNPvpPGevGELLTRGPYT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 564 MSGYLRVEkpgvlevptAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAK----RfakiAGEMVSLEMVEQLALAvsAD 639
Cdd:COG1021 391 IRGYYRAP---------EHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdqinR----GGEKIAAEEVENLLLA--HP 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 640 KMHATAIKS--DASKGEALVLF--TTDSELTREKLQQYARAHGVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:COG1021 456 AVHDAAVVAmpDEYLGERSCAFvvPRGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKID 523
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
320-703 |
1.47e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 320 HLPEQLTQVRWVYLEDLKADVTFSdklwifshlLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKT 399
Cdd:PRK12467 3201 HLLEQLPAPAGDTALTLDRLDLNG---------YSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAE 3271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 400 IADFTADDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPL-----HYRivpeLVYDRNCTVLFGTSTFLGNYARFA 473
Cdd:PRK12467 3272 AYELDANDRVLLFMSF--SFDGAQeRFLWTLICGGCLVVRDNDLwdpeeLWQ----AIHAHRISIACFPPAYLQQFAEDA 3345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 474 HPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVL-EGYGVTECAPVVSI-----NVPMAAKSGTVGRILPG-----MDA 542
Cdd:PRK12467 3346 GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLtNGYGPTEAVVTVTLwkcggDAVCEAPYAPIGRPVAGrsiyvLDG 3425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 543 RLLAVP-GIedGGRLQLKGPNIMSGYLRveKPGVlevpTAEN-----AQGEIERgWYDTGDIVRFDENGFVQIQGRAKRF 616
Cdd:PRK12467 3426 QLNPVPvGV--AGELYIGGVGLARGYHQ--RPSL----TAERfvadpFSGSGGR-LYRTGDLARYRADGVIEYLGRIDHQ 3496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 617 AKIAGEMVSLEMVEQLALAVSADKmHATAIKSDASKGEALVLFTTDSELTREKLQQYAR--AHGVPELAVPRDIRHLKQL 694
Cdd:PRK12467 3497 VKIRGFRIELGEIEARLLQHPSVR-EAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDhlAASLPDYMVPAQLLVLAAM 3575
|
....*....
gi 489124149 695 PLLGSGKPD 703
Cdd:PRK12467 3576 PLGPNGKVD 3584
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
350-701 |
2.93e-21 |
|
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: 97.20 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 350 SHLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPL 429
Cdd:cd05973 73 ARLVVTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 430 LTGAEVFLYPSPLhyriVPELVYDrnCTVLFGTSTFLGNYARF---------AHPYDFHRLRYVVAGAEKLQDSTKQLWQ 500
Cdd:cd05973 153 ALGHPTILLEGGF----SVESTWR--VIERLGVTNLAGSPTAYrllmaagaeVPARPKGRLRRVSSAGEPLTPEVIRWFD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 501 EKFGLRVLEGYGVTECAPVVSINVPMA--AKSGTVGRILPGMDARLLAVPGIEDG----GRLQLKGPN--IM--SGYLRV 570
Cdd:cd05973 227 AALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVLDDDGDELGpgepGRLAIDIANspLMwfRGYQLP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 571 EKPgvlevptaenaqgEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAI-KSD 649
Cdd:cd05973 307 DTP-------------AIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES-ALIEHPAVAEAAVIgVPD 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489124149 650 ASKGEALVLFTTDSELTR------EKLQQYAR----AHgvpelAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05973 373 PERTEVVKAFVVLRGGHEgtpalaDELQLHVKkrlsAH-----AYPRTIHFVDELPKTPSGK 429
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
254-701 |
3.68e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 97.99 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 254 EGERIGLMLPNAgISAAVIF-GAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQflDKGKLWHLPEQLTQVRWVY 332
Cdd:PLN02574 91 QGDVVLLLLPNS-VYFPVIFlAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPE--NVEKLSPLGVPVIGVPENY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 333 LEDLKAdVTFSDKLWIFSHLLAPHLAQVKQQpEDAAVILFTSGSEGHPKGVVHSHKSILANVEqikTIADFTA------- 405
Cdd:PLN02574 168 DFDSKR-IEFPKFYELIKEDFDFVPKPVIKQ-DDVAAIMYSSGTTGASKGVVLTHRNLIAMVE---LFVRFEAsqyeypg 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 406 -DDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP--------------SPLHYRIVPELVydrnctvlfgtsTFLGNYA 470
Cdd:PLN02574 243 sDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRrfdasdmvkvidrfKVTHFPVVPPIL------------MALTKKA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 471 RFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFG-LRVLEGYGVTECAPVVS--INVPMAAKSGTVGRILPGMDARL--- 544
Cdd:PLN02574 311 KGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPhVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVvdw 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 545 ----LAVPGieDGGRLQLKGPNIMSGYLRVEKPGVLEVptaenaqgeIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA 620
Cdd:PLN02574 391 stgcLLPPG--NCGELWIQGPGVMKGYLNNPKATQSTI---------DKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYK 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 621 GEMVSLEMVEqlALAVSADKMHATAIKS--DASKGE---ALVLFTTDSELTREKLQQYARAHGVPELAVpRDIRHLKQLP 695
Cdd:PLN02574 460 GFQIAPADLE--AVLISHPEIIDAAVTAvpDKECGEipvAFVVRRQGSTLSQEAVINYVAKQVAPYKKV-RKVVFVQSIP 536
|
....*.
gi 489124149 696 LLGSGK 701
Cdd:PLN02574 537 KSPAGK 542
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
359-703 |
7.64e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 359 QVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDR---FMSalplFHSFGLTVGLFTPLLTGAEV 435
Cdd:PRK12316 2140 AVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCelqFMS----FSFDGAHEQWFHPLLNGARV 2215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 436 FLYPSPLHyriVPELVYD----RNCTVLFGTSTFLGNYARFAHpYDFHRL---RYVVAGAEKLQDSTKQLWQEKFGLRVL 508
Cdd:PRK12316 2216 LIRDDELW---DPEQLYDemerHGVTILDFPPVYLQQLAEHAE-RDGRPPavrVYCFGGEAVPAASLRLAWEALRPVYLF 2291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 509 EGYGVTECAPVVSI-----NVPMAAKSGTVGRILPG-----MDARLLAVPgIEDGGRLQLKGPNIMSGYLrvEKPGVLE- 577
Cdd:PRK12316 2292 NGYGPTEAVVTPLLwkcrpQDPCGAAYVPIGRALGNrrayiLDADLNLLA-PGMAGELYLGGEGLARGYL--NRPGLTAe 2368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 578 --VPTAENAQGEIergWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKmHATAIKSDASKGEA 655
Cdd:PRK12316 2369 rfVPDPFSASGER---LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVR-EAVVVAQDGASGKQ 2444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489124149 656 LVLFT---TDSELTREKLQQYARAhGVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK12316 2445 LVAYVvpdDAAEDLLAELRAWLAA-RLPAYMVPAHWVVLERLPLNPNGKLD 2494
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
331-632 |
7.74e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 97.35 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 331 VYLEDLKADVTFSD-KLWIFSHLLAPHLAQVKQQP-------EDAAVILFTSGSEGHPKGVVHSHKSILANVEQI----- 397
Cdd:PTZ00216 222 IYLDSLPASVDTEGcRLVAWTDVVAKGHSAGSHHPlnipennDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALedrln 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 398 KTIADFTADDRFMSALPLFHSFGLTVglftplltgAEVFLYpsplhyrivpelvydRNCTVLFGTS-TFLGNYAR----- 471
Cdd:PTZ00216 302 DLIGPPEEDETYCSYLPLAHIMEFGV---------TNIFLA---------------RGALIGFGSPrTLTDTFARphgdl 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 472 ------------------------------------FAHPYD-------------------FH--------RLRYVVAGA 488
Cdd:PTZ00216 358 tefrpvfligvprifdtikkaveaklppvgslkrrvFDHAYQsrlralkegkdtpywnekvFSapravlggRVRAMLSGG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 489 EKLQDSTKQLWQEKFGlRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVPGI------EDGGRLQLKGPN 562
Cdd:PTZ00216 438 GPLSAATQEFVNVVFG-MVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYkhtdtpEPRGEILLRGPF 516
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124149 563 IMSGYLRVEKPgvlevpTAENAqgeIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GEMVSLEMVEQL 632
Cdd:PTZ00216 517 LFKGYYKQEEL------TREVL---DEDGWFHTGDVGSIAANGTLRIIGRVKALAKNClGEYIALEALEAL 578
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
363-703 |
1.50e-20 |
|
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: 95.47 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSP 441
Cdd:cd17655 135 KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASI--SFDASVTeIFASLLSGNTLYIVRKE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 LHYRIVPELVY--DRNCTVLFGTSTFLgNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGL--RVLEGYGVTECA 517
Cdd:cd17655 213 TVLDGQALTQYirQNRITIIDLTPAHL-KLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 518 PVVSINV--PMAAKSGTV--GRILPGM-----DARLLAVP-GIEdgGRLQLKGPNIMSGYL-RVE--KPGVLEVPTAENa 584
Cdd:cd17655 292 VDASIYQyePETDQQVSVpiGKPLGNTriyilDQYGRPQPvGVA--GELYIGGEGVARGYLnRPEltAEKFVDDPFVPG- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 585 qgeiERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEAL-VLFTTDS 663
Cdd:cd17655 369 ----ER-MYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLcAYIVSEK 443
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489124149 664 ELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17655 444 ELPVAQLREFLARE-LPDYMIPSYFIKLDEIPLTPNGKVD 482
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
348-701 |
2.24e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 95.49 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 348 IFSHLLAPHLAQVKQQPE--DAAVILFTSGSEGHPKGVVHSHKSIlanveqIKTIADFTA-------DDRFMSALPLFHS 418
Cdd:PRK06178 190 LLPALRACTAPVPLPPPAldALAALNYTGGTTGMPKGCEHTQRDM------VYTAAAAYAvavvggeDSVFLSFLPEFWI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 419 FGLTVGLFTPLLTGAEVFLYP--SPLHyriVPELVYDRNCTVLFGTstfLGNYAR-FAHP----YDFHRLRYV--VAGAE 489
Cdd:PRK06178 264 AGENFGLLFPLFSGATLVLLArwDAVA---FMAAVERYRVTRTVML---VDNAVElMDHPrfaeYDLSSLRQVrvVSFVK 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 490 KLQDSTKQLWQEKFGLRVLEG-YGVTEC-------------------APV-VSINVPmaaksGTVGRILPGMDARLLAVp 548
Cdd:PRK06178 338 KLNPDYRQRWRALTGSVLAEAaWGMTEThtcdtftagfqdddfdllsQPVfVGLPVP-----GTEFKICDFETGELLPL- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 549 GIEdgGRLQLKGPNIMSGYLRveKPGVlevpTAENaqgeIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEM 628
Cdd:PRK06178 412 GAE--GEIVVRTPSLLKGYWN--KPEA----TAEA----LRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 629 VEQLALAVSADKMHATAIKSDASKGEALVLFTT---DSELTREKLQQYARAH----GVPElavprdIRHLKQLPLLGSGK 701
Cdd:PRK06178 480 VEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlkpGADLTAAALQAWCRENmavyKVPE------IRIVDALPMTATGK 553
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
319-701 |
2.67e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 95.25 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 319 WHLPEQLTQ---VRW-VYLEDLKADVTF-------SDKLWifSHLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSH 387
Cdd:PLN02860 117 WYEELQNDRlpsLMWqVFLESPSSSVFIflnsfltTEMLK--QRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 388 KSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLfTPLLTGAEVFLYPSpLHYRIVPELVYDRNCTVLFGTSTFLG 467
Cdd:PLN02860 195 SALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPK-FDAKAALQAIKQHNVTSMITVPAMMA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 468 N---YARFAHPYD-FHRLRYVVAGA----EKLQDSTKQLWQEKfglRVLEGYGVTE-CA--------------PVVSINV 524
Cdd:PLN02860 273 DlisLTRKSMTWKvFPSVRKILNGGgslsSRLLPDAKKLFPNA---KLFSAYGMTEaCSsltfmtlhdptlesPKQTLQT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 525 PMAAKSGT--------VGRILPGMDARLLAVPGIEDgGRLQLKGPNIMSGY--LRVEKPGVLevpTAEnaqgeierGWYD 594
Cdd:PLN02860 350 VNQTKSSSvhqpqgvcVGKPAPHVELKIGLDESSRV-GRILTRGPHVMLGYwgQNSETASVL---SND--------GWLD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 595 TGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEqlALAVSADKMHATAIKS--DASKGEALVLFT--------TDSE 664
Cdd:PLN02860 418 TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVE--AVLSQHPGVASVVVVGvpDSRLTEMVVACVrlrdgwiwSDNE 495
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489124149 665 ---------LTREKLQQYARAHGVPELAVPRDI-RHLKQLPLLGSGK 701
Cdd:PLN02860 496 kenakknltLSSETLRHHCREKNLSRFKIPKLFvQWRKPFPLTTTGK 542
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
362-635 |
3.05e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 95.23 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPE-DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADF--TADDRFMSALPLFH--SFGLTVGLF---TPL-LTG 432
Cdd:PRK05620 177 ELDEtTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLavTHGESFLCCVPIYHvlSWGVPLAAFmsgTPLvFPG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 433 AEVflypSPLHYRIVPELVYDRnctVLFGTST----FLGNYARfaHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVL 508
Cdd:PRK05620 257 PDL----SAPTLAKIIATAMPR---VAHGVPTlwiqLMVHYLK--NPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVV 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 509 EGYGVTECAPVVSINVPMAAKSGTV--------GRILPGMDARLlavpgIEDG----------GRLQLKGPNIMSGYLRV 570
Cdd:PRK05620 328 HVWGMTETSPVGTVARPPSGVSGEArwayrvsqGRFPASLEYRI-----VNDGqvmestdrneGEIQVRGNWVTASYYHS 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489124149 571 ---EKPGVLEVPTAENAQGEIER----GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALA 635
Cdd:PRK05620 403 pteEGGGAASTFRGEDVEDANDRftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMA 474
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
360-703 |
3.70e-20 |
|
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: 94.26 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 360 VKQQPEDAAVILFTSGSEGHPKGVVHSHKSilanveQIKTIADF------TADDRFMSALPLfhSFGLTV-GLFTPLLTG 432
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRA------ALNTILDInrrfavGPDDRVLALSSL--SFDLSVyDIFGALSAG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 433 AEVFLyPSPLHYRIV---PELVYDRNCTV------LFGtstFLGNYARfAHPYDFHRLRYVVAG----AEKLQDSTKQLW 499
Cdd:cd12114 193 ATLVL-PDEARRRDPahwAELIERHGVTLwnsvpaLLE---MLLDVLE-AAQALLPSLRLVLLSgdwiPLDLPARLRALA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 500 QekfGLRVLEGYGVTEcAPVVSI-----NVPMAAKSGTVGRILPGMDARLLAVPGIE--DG--GRLQLKGPNIMSGYLR- 569
Cdd:cd12114 268 P---DARLISLGGATE-ASIWSIyhpidEVPPDWRSIPYGRPLANQRYRVLDPRGRDcpDWvpGELWIGGRGVALGYLGd 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 570 VEKpgvlevpTAE----NAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATA 645
Cdd:cd12114 344 PEL-------TAArfvtHPDGE---RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEA-ALQAHPGVARAVV 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489124149 646 IKSDASKGEALVLF--------TTDSELTREKLQQYarahgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd12114 413 VVLGDPGGKRLAAFvvpdndgtPIAPDALRAFLAQT-----LPAYMIPSRVIALEALPLTANGKVD 473
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
353-703 |
4.77e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.18 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 353 LAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPlFHSFGLTVGLFTPLLTG 432
Cdd:PRK12316 3184 YAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSG 3262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 433 AEVFLYPSPLHY--RIVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEkfGLRVLEG 510
Cdd:PRK12316 3263 ARVVLAGPEDWRdpALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNL 3340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 511 YGVTECAPVVSINVPMAAKSGT--VGRILPG-----MDARLLAVPgIEDGGRLQLKGPNIMSGYLrvEKPGVLEVPTAEN 583
Cdd:PRK12316 3341 YGPTEATITVTHWQCVEEGKDAvpIGRPIANracyiLDGSLEPVP-VGALGELYLGGEGLARGYH--NRPGLTAERFVPD 3417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 584 AQGEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKmHATAIKSDASKGEALVLFTTDS 663
Cdd:PRK12316 3418 PFVPGER-LYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVR-EAVVLAVDGRQLVAYVVPEDEA 3495
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489124149 664 ELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK12316 3496 GDLREALKAHLKAS-LPEYMVPAHLLFLERMPLTPNGKLD 3534
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
363-630 |
8.11e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 94.01 E-value: 8.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFH-----------SFGLTVGLFT---- 427
Cdd:PLN02736 219 KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyervnqivmlHYGVAVGFYQgdnl 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 428 PLLTGAEVFlypSPLHYRIVPEL---VYDRnCTVLFGTSTFLGNyARFAHPYD--------------------FH----- 479
Cdd:PLN02736 299 KLMDDLAAL---RPTIFCSVPRLynrIYDG-ITNAVKESGGLKE-RLFNAAYNakkqalengknpspmwdrlvFNkikak 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 480 ---RLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVPGI----ED 552
Cdd:PLN02736 374 lggRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMnytsED 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 553 G----GRLQLKGPNIMSGYLRVekpgvlEVPTAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GEMVSLE 627
Cdd:PLN02736 454 QpyprGEICVRGPIIFKGYYKD------EVQTREVIDED---GWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPE 524
|
...
gi 489124149 628 MVE 630
Cdd:PLN02736 525 KIE 527
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
366-703 |
1.40e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.03 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsPLHYR 445
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLL---PARGR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 446 IVPELVYD--RNCTVLFGTST------FLGNYARFAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECA 517
Cdd:PRK05852 254 FSAHTFWDdiKAVGATWYTAVptihqiLLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 518 -PVVSINVPMAAKS-------GTVGRIlPGMDARLLAVPGIEDG----GRLQLKGPNIMSGYLrvEKPGVlevpTAENaq 585
Cdd:PRK05852 334 hQVTTTQIEGIGQTenpvvstGLVGRS-TGAQIRIVGSDGLPLPagavGEVWLRGTTVVRGYL--GDPTI----TAAN-- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 586 geIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLAVSADKMHATAI-KSDASKGE---ALVLFTT 661
Cdd:PRK05852 405 --FTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGV-LASHPNVMEAAVFgVPDQLYGEavaAVIVPRE 481
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489124149 662 DSELTREKLQQYARaHGVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK05852 482 SAPPTAEELVQFCR-ERLAAFEIPASFQEASGLPHTAKGSLD 522
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
255-608 |
1.76e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 93.02 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 255 GERIGLMLPN-----AGISAAVIFGAIArrripAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDKgkLWHLPEQLTQVR 329
Cdd:PRK08279 87 GDVVALLMENrpeylAAWLGLAKLGAVV-----ALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEA--FEEARADLARPP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 330 --WVYLEDLKADVTFSDKLWIFSHLLAPHLAQVKQ--QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTA 405
Cdd:PRK08279 160 rlWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSgvTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 406 DDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPElVYDRNCTvLFGtstFLGNYARF-----AHPYDF-H 479
Cdd:PRK08279 240 DDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDD-VRRYRAT-AFQ---YIGELCRYllnqpPKPTDRdH 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 480 RLRYVV-AGaekLQDSTKQLWQEKFGL-RVLEGYGVTEcAPVVSINVpmAAKSGTVGRIlPGMDARLLAVPGIEDGGRLQ 557
Cdd:PRK08279 315 RLRLMIgNG---LRPDIWDEFQQRFGIpRILEFYAASE-GNVGFINV--FNFDGTVGRV-PLWLAHPYAIVKYDVDTGEP 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 558 LKGPNimsGYLRVEKPGvlEVptAEnAQGEI------------------------ERG--WYDTGDIVRFDENGFVQ 608
Cdd:PRK08279 388 VRDAD---GRCIKVKPG--EV--GL-LIGRItdrgpfdgytdpeasekkilrdvfKKGdaWFNTGDLMRDDGFGHAQ 456
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
364-701 |
1.84e-19 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 92.52 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTAD-DRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYP--- 439
Cdd:PRK05851 151 SGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPtta 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 ---SPLH-----------YRIVPELVYDrnctvlfgtstFLGNYARFAHPYDFHRLRYVVAGAEKLQ-DSTKQLWQE--K 502
Cdd:PRK05851 230 fsaSPFRwlswlsdsratLTAAPNFAYN-----------LIGKYARRVSDVDLGALRVALNGGEPVDcDGFERFATAmaP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 503 FGLR---VLEGYGVTE--CAPVVSI--------NVPMAAKSGT-----VGRILPGMDARLlaVPGIEDG-------GRLQ 557
Cdd:PRK05851 299 FGFDagaAAPSYGLAEstCAVTVPVpgiglrvdEVTTDDGSGArrhavLGNPIPGMEVRI--SPGDGAAgvagreiGEIE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 558 LKGPNIMSGYLrvekpgvlevptaenAQGEIERG-WYDTGDIVRFDENGFVqIQGRAKRFAKIAGEMVSLEMVEQLALAV 636
Cdd:PRK05851 377 IRGASMMSGYL---------------GQAPIDPDdWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQV 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489124149 637 SADKMHA-TAIKSD-ASKGEALVLFT----TDSELTR-EKLQQYARAHGVpelaVPRDIRHLK--QLPLLGSGK 701
Cdd:PRK05851 441 RGVREGAvVAVGTGeGSARPGLVIAAefrgPDEAGARsEVVQRVASECGV----VPSDVVFVApgSLPRTSSGK 510
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
233-719 |
1.99e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 92.15 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYSTEGERIGLMLPNaGISAAVIF-GAiarrripAMMNYTA-------GVKGLTSAITASEIK 304
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKESKNKTIAILLEN-RIEFLQLFaGA-------AMAGWTCvpldikwKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 305 TIFTSRQFLDKgklwhLPEQLTQVrwVYLEDLKADVTFSdklwifshllAPHLAQVKQQPEDAAVILFTSGSEGHPKGVV 384
Cdd:PRK07638 100 MIVTERYKLND-----LPDEEGRV--IEIDEWKRMIEKY----------LPTYAPIENVQNAPFYMGFTSGSTGKPKAFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 385 HSHKSILANVEqiKTIADF--TADDRFMSALPLFHSFGLtVGLFTPLLTGAEVFLYPsplhyRIVPELVYDR----NCTV 458
Cdd:PRK07638 163 RAQQSWLHSFD--CNVHDFhmKREDSVLIAGTLVHSLFL-YGAISTLYVGQTVHLMR-----KFIPNQVLDKleteNISV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 459 LFGTSTFLGNYARFAHPYDfHRLRYVVAGAEKLQDSTKQLwQEKF-GLRVLEGYGVTECApVVSINVP--MAAKSGTVGR 535
Cdd:PRK07638 235 MYTVPTMLESLYKENRVIE-NKMKIISSGAKWEAEAKEKI-KNIFpYAKLYEFYGASELS-FVTALVDeeSERRPNSVGR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 536 ILPGMDARLLAVPGIE----DGGRLQLKGPNIMSGYlrvekpgvleVPTAENAQGEIERGWYDTGDIVRFDENGFVQIQG 611
Cdd:PRK07638 312 PFHNVQVRICNEAGEEvqkgEIGTVYVKSPQFFMGY----------IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 612 RAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTTDSElTREKLQQYARAHgVPELAVPRDIRHL 691
Cdd:PRK07638 382 REKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSA-TKQQLKSFCLQR-LSSFKIPKEWHFV 459
|
490 500
....*....|....*....|....*...
gi 489124149 692 KQLPLLGSGKPDFVTLKSWVDEPEKQHE 719
Cdd:PRK07638 460 DEIPYTNSGKIARMEAKSWIENQEKIYE 487
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
345-659 |
2.39e-19 |
|
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: 91.78 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 345 KLW-IFSHLLAPHL----AQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSF 419
Cdd:cd05908 81 KLNkVWNTLKNPYLiteeEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 420 GLTVGLFTPLLTGAEVFLYPSPLHYRiVPEL----VYDRNCTVL----FGTSTFLGNY-ARFAHPYDFHRLRYVVAGAEK 490
Cdd:cd05908 161 GLIAFHLAPLIAGMNQYLMPTRLFIR-RPILwlkkASEHKATIVsspnFGYKYFLKTLkPEKANDWDLSSIRMILNGAEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 491 L-----QDSTKQLwqEKFGLR---VLEGYGVTECAPVVSI---------------------NVPMAAKSGT-------VG 534
Cdd:cd05908 240 IdyelcHEFLDHM--SKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgePEPEVDKKDSecltfveVG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 535 RILPGMDARLL--AVPGIEDG--GRLQLKGPNIMSGYLRVEKpgvlevptaENAQGEIERGWYDTGDIvRFDENGFVQIQ 610
Cdd:cd05908 318 KPIDETDIRICdeDNKILPDGyiGHIQIRGKNVTPGYYNNPE---------ATAKVFTDDGWLKTGDL-GFIRNGRLVIT 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489124149 611 GRAKRFAKIAGEMVSLEMVEQLAL---AVSADKMHATAIKSDASKGEALVLF 659
Cdd:cd05908 388 GREKDIIFVNGQNVYPHDIERIAEeleGVELGRVVACGVNNSNTRNEEIFCF 439
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
233-701 |
3.77e-19 |
|
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: 91.37 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYST--EGERIGLMLPN---------AGISAAVIFgaiarrrIPAMMNYTAgvKGLTSAITAS 301
Cdd:cd05928 43 SFRELGSLSRKAANVLSGACGlqRGDRVAVILPRvpewwlvnvACIRTGLVF-------IPGTIQLTA--KDILYRLQAS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 302 EIKTIFTSrqfldkgklwhlpEQLTQ-VRWVYLE--DLKADVTFSDKLW--------IFSHLLAPHLAqVKQQPEDAAVI 370
Cdd:cd05928 114 KAKCIVTS-------------DELAPeVDSVASEcpSLKTKLLVSEKSRdgwlnfkeLLNEASTEHHC-VETGSQEPMAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 371 LFTSGSEGHPKGVVHSHKSI-LANVEQIKTIADFTADDRF--MSALPLFHSFGLTVglFTPLLTGAEVFLYPSPlhyRIV 447
Cdd:cd05928 180 YFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMwnTSDTGWIKSAWSSL--FEPWIQGACVFVHHLP---RFD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 448 PELVYDR----NCTVLFGTST-----FLGNYARfahpYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAP 518
Cdd:cd05928 255 PLVILKTlssyPITTFCGAPTvyrmlVQQDLSS----YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSINVPMAAKSGTVGRILPGMDARLLAV------PGIEDGGRLQLKgPN----IMSGYlrVEKPgvleVPTAENAQGEi 588
Cdd:cd05928 331 ICANFKGMKIKPGSMGKASPPYDVQIIDDngnvlpPGTEGDIGIRVK-PIrpfgLFSGY--VDNP----EKTAATIRGD- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 589 ergWYDTGDIVRFDENGFVQIQGRAKRFA-----KIAGEMVSLEMVEQLALAVSAdkmhatAIKS-DASKGE---ALVLF 659
Cdd:cd05928 403 ---FYLTGDRGIMDEDGYFWFMGRADDVInssgyRIGPFEVESALIEHPAVVESA------VVSSpDPIRGEvvkAFVVL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489124149 660 TTD------SELTREkLQQYARAHGVPeLAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05928 474 APQflshdpEQLTKE-LQQHVKSVTAP-YKYPRKVEFVQELPKTVTGK 519
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
364-703 |
5.35e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 90.82 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLtvgLFTP-LLTGAEVFLYPS-- 440
Cdd:PRK06188 167 PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA---FFLPtLLRGGTVIVLAKfd 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 PLHY-RIVPElvydRNCTVLFGTSTFLgnYARFAHP----YDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE 515
Cdd:PRK06188 244 PAEVlRAIEE----QRITATFLVPTMI--YALLDHPdlrtRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 CAPVVSI------NVPMAAKSGTVGRILPGMDARLLAvpgiEDG--------GRLQLKGPNIMSGYLRveKPGVlevpTA 581
Cdd:PRK06188 318 APMVITYlrkrdhDPDDPKRLTSCGRPTPGLRVALLD----EDGrevaqgevGEICVRGPLVMDGYWN--RPEE----TA 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 582 ENAQGeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEAL---VL 658
Cdd:PRK06188 388 EAFRD----GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVtavVV 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489124149 659 FTTDSELTREKLQQYARAH-GVPelAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK06188 464 LRPGAAVDAAELQAHVKERkGSV--HAPKQVDFVDSLPLTALGKPD 507
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
364-703 |
5.40e-19 |
|
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: 90.54 E-value: 5.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIktIADFTADDRFMSALPLFHS--FGLTVGLFTPLLTGAEVFLYPSP 441
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL--SERYFGRDNGDEAVLFFSNyvFDFFVEQMTLALLNGQKLVVPPD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 lHYRIVPELVYD----RNCTVLFGTSTFLGNY--ARFAHpydfhrLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE 515
Cdd:cd17648 171 -EMRFDPDRFYAyinrEKVTYLSGTPSVLQQYdlARLPH------LKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 CApVVSINVPM---AAKSGTVGRILPG-----MDARLLAVPgIEDGGRLQLKGPNIMSGYL-RVEKPGVLEVPTAENAQG 586
Cdd:cd17648 244 TT-VTNHKRFFpgdQRFDKSLGRPVRNtkcyvLNDAMKRVP-VGAVGELYLGGDGVARGYLnRPELTAERFLPNPFQTEQ 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 587 EIERG----WYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEA-----LV 657
Cdd:cd17648 322 ERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqkyLV 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489124149 658 -LFTTDSE-LTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17648 402 gYYLPEPGhVPESDLLSFLRAK-LPRYMVPARLVRLEGIPVTINGKLD 448
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
365-701 |
5.56e-19 |
|
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: 91.02 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplHY 444
Cdd:cd05970 185 EDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYD---YD 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 445 RIVPELVYDRncTVLFGTSTFLG--NYARF-----AHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECA 517
Cdd:cd05970 262 KFDPKALLEK--LSKYGVTTFCAppTIYRFliredLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETT 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 518 PVVSINVPMAAKSGTVGRILPGMDARLL-----AVPGIEDGG---RLQLKGP-NIMSGYLRvekpgvlevpTAENAQGEI 588
Cdd:cd05970 340 LTIATFPWMEPKPGSMGKPAPGYEIDLIdregrSCEAGEEGEiviRTSKGKPvGLFGGYYK----------DAEKTAEVW 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 589 ERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEA----LVL---FTT 661
Cdd:cd05970 410 HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVvkatIVLakgYEP 489
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489124149 662 DSELTREkLQQYARAHGVPELAvPRDIRHLKQLPLLGSGK 701
Cdd:cd05970 490 SEELKKE-LQDHVKKVTAPYKY-PRIVEFVDELPKTISGK 527
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
367-708 |
8.59e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 90.58 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 367 AAVILFTSGSEGHPKGVVHSHKSilaNVEQ--IKTIAD---FTADDRFMSALPLFH--SFGLTvglFTPLLTGAEVFLYP 439
Cdd:PRK06018 179 AAGMCYTSGTTGDPKGVLYSHRS---NVLHalMANNGDalgTSAADTMLPVVPLFHanSWGIA---FSAPSMGTKLVMPG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SPLHYRIVPELVYDRNCTVLFGTST---FLGNYARfAHPYDFHRLRYVVAGAEKLQDSTKQLWQEkFGLRVLEGYGVTEC 516
Cdd:PRK06018 253 AKLDGASVYELLDTEKVTFTAGVPTvwlMLLQYME-KEGLKLPHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEM 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 517 APVvsinvpmaaksGTVGRILPGM-----DARL-------LAVPGIE-------------DG---GRLQLKGPNIMSGYL 568
Cdd:PRK06018 331 SPL-----------GTLAALKPPFsklpgDARLdvlqkqgYPPFGVEmkitddagkelpwDGktfGRLKVRGPAVAAAYY 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 569 RVEkpgvlevptaenaqGEI--ERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlaLAVSADKM-HATA 645
Cdd:PRK06018 400 RVD--------------GEIldDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEN--LAVGHPKVaEAAV 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 646 IKSDASK-GEA---LVLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPDFVTLK 708
Cdd:PRK06018 464 IGVYHPKwDERpllIVQLKPGETATREEILKYMDGK-IAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
233-695 |
9.78e-19 |
|
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: 90.63 E-value: 9.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYSTE-GERIGLMLPnAGISAAVIFGAIARRR---IPAMMNYtaGVKGLTSAITASEIKTIFT 308
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGkGDRVGIYLP-MIPEIVPAFLAVARIGgivVPIFSGF--GKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 309 SRQFLDKGKLWHLPE-------QLTQVRWVYLE-DLKADVTFSDKLWIFSHLL--APHLAQVKQQPEDAAVILFTSGSEG 378
Cdd:cd05968 170 ADGFTRRGREVNLKEeadkacaQCPTVEKVVVVrHLGNDFTPAKGRDLSYDEEkeTAGDGAERTESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 379 HPKGVVHSHKSIlanveQIKTIAD--FTADDRFMSALPLFHSFGLTVG---LFTPLLTGAEVFLYPS----PLHYRIVpE 449
Cdd:cd05968 250 KPKGTVHVHAGF-----PLKAAQDmyFQFDLKPGDLLTWFTDLGWMMGpwlIFGGLILGATMVLYDGapdhPKADRLW-R 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 450 LVYDRNCTVLFGTSTFLGNYARFAHPY----DFHRLRyVVAGAEKLQDSTKQLWqekFGLRVLEGY-------GVTECAP 518
Cdd:cd05968 324 MVEDHEITHLGLSPTLIRALKPRGDAPvnahDLSSLR-VLGSTGEPWNPEPWNW---LFETVGKGRnpiinysGGTEISG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 519 VVSINVPMAA-KSGTVGRILPGMDARLL---AVPGIEDGGRLQLKGP--NIMSGYLRVEKPGVlevptaENAQGEIERGW 592
Cdd:cd05968 400 GILGNVLIKPiKPSSFNGPVPGMKADVLdesGKPARPEVGELVLLAPwpGMTRGFWRDEDRYL------ETYWSRFDNVW 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 593 YDtGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFT------TDSELT 666
Cdd:cd05968 474 VH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVvlkpgvTPTEAL 552
|
490 500 510
....*....|....*....|....*....|
gi 489124149 667 REKLQQYARAH-GVPelAVPRDIRHLKQLP 695
Cdd:cd05968 553 AEELMERVADElGKP--LSPERILFVKDLP 580
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
363-703 |
1.32e-18 |
|
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: 89.15 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRfmSALPLFHSF-GLTVGLFTPLLTGAEVFLYPSP 441
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK--SLVYASFSFdASAWEIFPHLTAGAALHVVPSE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 LHYRIVPelvYDRNCTVLFGTSTFL--GNYARFAHpYDFHRLRYVVAGAEKLQDSTKQlwqekfGLRVLEGYGVTECAPV 519
Cdd:cd17645 180 RRLDLDA---LNDYFNQEGITISFLptGAAEQFMQ-LDNQSLRVLLTGGDKLKKIERK------GYKLVNNYGPTENTVV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 520 V-SINVPMAAKSGTVGRILPGMDARLL----AVPGIEDGGRLQLKGPNIMSGYLRVEKpgvlevPTAE----NAQGEIER 590
Cdd:cd17645 250 AtSFEIDKPYANIPIGKPIDNTRVYILdealQLQPIGVAGELCIAGEGLARGYLNRPE------LTAEkfivHPFVPGER 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 591 gWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLF-TTDSELTREK 669
Cdd:cd17645 324 -MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYvTAPEEIPHEE 402
|
330 340 350
....*....|....*....|....*....|....
gi 489124149 670 LQQYARaHGVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17645 403 LREWLK-NDLPDYMIPTYFVHLKALPLTANGKVD 435
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
233-695 |
1.56e-18 |
|
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: 89.49 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTK-TLFVARILEKYSTEGERIGLMLPNAgISAAVIFGAIAR-RRIPAMMNYTAGVKGLTSAITASEIKTIFTSr 310
Cdd:cd05923 30 TYSELRARiEAVAARLHARGLRPGQRVAVVLPNS-VEAVIALLALHRlGAVPALINPRLKAAELAELIERGEMTAAVIA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 311 qfLDKGklwhlPEQLTQVRWVYLEDLKADVTfSDKLWIFSHLLAPHlaqvKQQPEDAAVILFTSGSEGHPKGVVHSHKSI 390
Cdd:cd05923 108 --VDAQ-----VMDAIFQSGVRVLALSDLVG-LGEPESAGPLIEDP----PREPEQPAFVFYTSGTTGLPKGAVIPQRAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 391 LANVEQIKTIAD--FTADDRFMSALPLFHSFGLtVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTF--- 465
Cdd:cd05923 176 ESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGF-FAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHlda 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 466 LGNYARFAhPYDFHRLRYVV-AGAEKLQDSTKQLWQEKFGLRVlEGYGVTEcapVVSINVPMAAKSGTVGRilPGMDARL 544
Cdd:cd05923 255 LAAAAEFA-GLKLSSLRHVTfAGATMPDAVLERVNQHLPGEKV-NIYGTTE---AMNSLYMRDARTGTEMR--PGFFSEV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 545 LAVPgieDGGRLQLKGPNIMSGYLRVEKP------GVLEVPTAENAQgeIERGWYDTGDIVRFDENGFVQIQGRAKRFAK 618
Cdd:cd05923 328 RIVR---IGGSPDEALANGEEGELIVAAAadaaftGYLNQPEATAKK--LQDGWYRTGDVGYVDPSGDVRILGRVDDMII 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 619 IAGEMVSLEMVEQ-LALAVSADKMHATAIKsDASKGEALVLFTTDSE--LTREKLQQYARAHGVPELAVPRDIRHLKQLP 695
Cdd:cd05923 403 SGGENIHPSEIERvLSRHPGVTEVVVIGVA-DERWGQSVTACVVPREgtLSADELDQFCRASELADFKRPRRYFFLDELP 481
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
364-701 |
1.95e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 89.45 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDA-AVILFTSGSEGHPKGVVHSHKSILAN-VEQIKTIADFTADDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYPSP 441
Cdd:PRK07786 172 PNDSpALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIYPLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 lhyRIVPELVYDrnctVLFG---TSTFLGNY-------ARFAHPYDFhRLRYVVAGAEKLQDSTKQLWQEKF-GLRVLEG 510
Cdd:PRK07786 251 ---AFDPGQLLD----VLEAekvTGIFLVPAqwqavcaEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFpEAQILAA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 511 YGVTECAPVVSINVPMAA--KSGTVGRILPGMDARLLA-----VPgIEDGGRLQLKGPNIMSGYLRVEKPgvlevpTAEN 583
Cdd:PRK07786 323 FGQTEMSPVTCMLLGEDAirKLGSVGKVIPTVAARVVDenmndVP-VGEVGEIVYRAPTLMSGYWNNPEA------TAEA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 584 AQGeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAI-KSDASKGEA----LVL 658
Cdd:PRK07786 396 FAG----GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVEN-VLASHPDIVEVAVIgRADEKWGEVpvavAAV 470
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489124149 659 FTTDSELTREKLQQY-----AR-AHgvpelavPRDIRHLKQLPLLGSGK 701
Cdd:PRK07786 471 RNDDAALTLEDLAEFltdrlARyKH-------PKALEIVDALPRNPAGK 512
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
363-703 |
2.06e-18 |
|
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: 88.68 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANV---EQIKTIADFTADDRFMSALplfhSFGLTVGLFT-PLLTGAEvfLY 438
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAhawRREYELDSFPVRLLQMASF----SFDVFAGDFArSLLNGGT--LV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 439 PSPLHYRIVPELVYD----RNCTVLFGTSTFLGNYARFA--HPYDFHRLRYVVAGAEKLQDSTKQLWQEKFG--LRVLEG 510
Cdd:cd17650 165 ICPDEVKLDPAALYDlilkSRITLMESTPALIRPVMAYVyrNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGqgMRIINS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 511 YGVTEC-----------APVVSI-NVPmaaksgtVGRILPGM-----DARLLAVP-GIedGGRLQLKGPNIMSGYLrvEK 572
Cdd:cd17650 245 YGVTEAtidstyyeegrDPLGDSaNVP-------IGRPLPNTamyvlDERLQPQPvGV--AGELYIGGAGVARGYL--NR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 573 PGVLEVPTAENAQGEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDAsK 652
Cdd:cd17650 314 PELTAERFVENPFAPGER-MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-G 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 653 GEA-LVLF-----TTDSELTREKLQQYarahgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17650 392 GEArLCAYvvaaaTLNTAELRAFLAKE-----LPSYMIPSYYVQLDALPLTPNGKVD 443
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
364-701 |
2.61e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 88.83 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGL-TVGLFTPLltGAEVFlypspL 442
Cdd:PRK07788 206 PKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWaHLTLAMAL--GSTVV-----L 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 HYRIVPE----LVYDRNCTVLFGTSTFLgnyAR-FAHP------YDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGY 511
Cdd:PRK07788 279 RRRFDPEatleDIAKHKATALVVVPVML---SRiLDLGpevlakYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLY 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 512 GVTECApVVSINVP--MAAKSGTVGRILPGMDARLLAvpgiEDG--------GRLQLKGPNIMSGYLRVEKPgvlevpta 581
Cdd:PRK07788 356 GSTEVA-FATIATPedLAEAPGTVGRPPKGVTVKILD----ENGnevprgvvGRIFVGNGFPFEGYTDGRDK-------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 582 enaqgEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLAVSADKMHATAIK-SDASKGE---ALV 657
Cdd:PRK07788 423 -----QIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDL-LAGHPDVVEAAVIGvDDEEFGQrlrAFV 496
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 489124149 658 LFTTDSELTREKLQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGK 701
Cdd:PRK07788 497 VKAPGAALDEDAIKDYVRDN----LArykVPRDVVFLDELPRNPTGK 539
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
365-690 |
2.74e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 88.29 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFhsfgltvGLFTPLLTGAEV-----FLYP 439
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPALGLTSVipdmdPTRP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SPLHYRIVPELVYDRNCTVLFGTSTFLGNYARF--AHPYDFHRLRYVV-AGAE---KLQDSTKQLWQEkfGLRVLEGYGV 513
Cdd:cd05910 158 ARADPQKLVGAIRQYGVSIVFGSPALLERVARYcaQHGITLPSLRRVLsAGAPvpiALAARLRKMLSD--EAEILTPYGA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 514 TECAPVVSI---------NVPMAAKSGT-VGRILPGMDARLLAV---PGIEDGGRLQL----------KGPNIMSGYL-R 569
Cdd:cd05910 236 TEALPVSSIgsrellattTAATSGGAGTcVGRPIPGVRVRIIEIddePIAEWDDTLELprgeigeitvTGPTVTPTYVnR 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 570 VEKPGVLEVPTaenaqgEIERGWYDTGDIVRFDENGFVQIQGR-AKRFAKIAGEMVSlEMVEqlALAVSADKMHATAIKS 648
Cdd:cd05910 316 PVATALAKIDD------NSEGFWHRMGDLGYLDDEGRLWFCGRkAHRVITTGGTLYT-EPVE--RVFNTHPGVRRSALVG 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 649 DASKG--------EALVLFTTDSELTREKLQQYARAH----GVPEL----AVPRDIRH 690
Cdd:cd05910 387 VGKPGcqlpvlcvEPLPGTITPRARLEQELRALAKDYphtqRIGRFlihpSFPVDIRH 444
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
278-637 |
3.65e-18 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 89.02 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 278 RRRIPAMMNYTA-GVKGLTSAITASEIKTIFTSRQFLDKgkLWHLPEQLTQV-RWVYLEDLKADVTFSDKL---WI---F 349
Cdd:PLN02387 153 RQNITVVTIYASlGEEALCHSLNETEVTTVICDSKQLKK--LIDISSQLETVkRVIYMDDEGVDSDSSLSGssnWTvssF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 350 SHL--------LAPHLAQvkqqPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTI-ADFTADDRFMSALPLFHSF- 419
Cdd:PLN02387 231 SEVeklgkenpVDPDLPS----PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVvPKLGKNDVYLAYLPLAHILe 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 420 ----------GLTVGLFTPL-LT-----------GAEVFLYPSPLhyRIVP-------------------------ELVY 452
Cdd:PLN02387 307 laaesvmaavGAAIGYGSPLtLTdtsnkikkgtkGDASALKPTLM--TAVPaildrvrdgvrkkvdakgglakklfDIAY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 453 DRNCTVLFGtsTFLGNYARFAHPYDF-----------HRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE-CAPvv 520
Cdd:PLN02387 385 KRRLAAIEG--SWFGAWGLEKLLWDAlvfkkiravlgGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTEtCAG-- 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 521 sinvpmAAKS----GTVGRILPGMDARLLAVPGIEDGGRLQ-----------LKGPNIMSGYLRVEKpgvlevPTAENAQ 585
Cdd:PLN02387 461 ------ATFSewddTSVGRVGPPLPCCYVKLVSWEEGGYLIsdkpmprgeivIGGPSVTLGYFKNQE------KTDEVYK 528
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 586 GEiERG--WYDTGDIVRFDENGFVQIQGRAKRFAKI-AGEMVSLEMVEQlALAVS 637
Cdd:PLN02387 529 VD-ERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLqHGEYVSLGKVEA-ALSVS 581
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
363-703 |
5.73e-18 |
|
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: 86.92 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSalplFHSFGLTVG---LFTPLLTGAEVFLYP 439
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQ----FASPSFDASvweLLMALLAGATLVLAP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SplhYRIVP-----ELVYDRNCTVLFGTSTFLGNYArfahPYDFHRLRYVVAGAEKLQDSTKQLWQEkfGLRVLEGYGVT 514
Cdd:cd17652 167 A---EELLPgeplaDLLREHRITHVTLPPAALAALP----PDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 515 ECAPVVSINVPMAAKSG-TVGRILPG-----MDARLLAVPgIEDGGRLQLKGPNIMSGYLRveKPGVlevpTAE----NA 584
Cdd:cd17652 238 ETTVCATMAGPLPGGGVpPIGRPVPGtrvyvLDARLRPVP-PGVPGELYIAGAGLARGYLN--RPGL----TAErfvaDP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 585 QGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTT--- 661
Cdd:cd17652 311 FGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVpap 390
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489124149 662 DSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17652 391 GAAPTAAELRAHLAER-LPGYMVPAAFVVLDALPLTPNGKLD 431
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
332-702 |
7.88e-18 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 87.37 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 332 YLEDLKADVTFSDKLWIFSH-----LLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIA-DFTA 405
Cdd:PRK09192 138 LLPWVNEATHGNPLLHVLSHawfkaLPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlKVRP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 406 DDRFMSALPLFHSFGLtVGLF-TPLLTGAEVFLYPS------PLHYRivpELVYDRNCTVLFgTSTF-------LGNYAR 471
Cdd:PRK09192 218 GDRCVSWLPFYHDMGL-VGFLlTPVATQLSVDYLPTrdfarrPLQWL---DLISRNRGTISY-SPPFgyelcarRVNSKD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 472 FAHpYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLR------VLEGYGVTECAPVVS----------------------IN 523
Cdd:PRK09192 293 LAE-LDLSCWRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEATLAVSfsplgsgivveevdrdrleyqgKA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 524 VPMAAKSGTV------GRILPGMDARLLAVPGIEDG----GRLQLKGPNIMSGYLRVEkpgvlevptaENAQGEIERGWY 593
Cdd:PRK09192 372 VAPGAETRRVrtfvncGKALPGHEIEIRNEAGMPLPervvGHICVRGPSLMSGYFRDE----------ESQDVLAADGWL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 594 DTGDIvRFDENGFVQIQGRAKRFAKIAGEMV---SLE-MVEQLALAVSADkmhATAIKSDASKGEALVLF----TTDSEl 665
Cdd:PRK09192 442 DTGDL-GYLLDGYLYITGRAKDLIIINGRNIwpqDIEwIAEQEPELRSGD---AAAFSIAQENGEKIVLLvqcrISDEE- 516
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 489124149 666 TREKLQQYA-----RAHGVP---ELAVPRdirhlkQLPLLGSGKP 702
Cdd:PRK09192 517 RRGQLIHALaalvrSEFGVEaavELVPPH------SLPRTSSGKL 555
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
362-701 |
9.47e-18 |
|
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: 86.97 E-value: 9.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPED---AAVILFTSGSEGHPKGVVHSHKSilANVEQIKTIADFTADDR--FMSALPLFHSFGLTVGLFTPLLTGAEVF 436
Cdd:cd12118 127 IPPADewdPIALNYTSGTTGRPKGVVYHHRG--AYLNALANILEWEMKQHpvYLWTLPMFHCNGWCFPWTVAAVGGTNVC 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 437 L--YPSPLHYRivpeLVYDRNCTVLFGTSTFLGNYARFAH----PYDfHRLRYVVAGAEKLQDSTKQLwqEKFGLRVLEG 510
Cdd:cd12118 205 LrkVDAKAIYD----LIEKHKVTHFCGAPTVLNMLANAPPsdarPLP-HRVHVMTAGAPPPAAVLAKM--EELGFDVTHV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 511 YGVTECAPVVSINV--------PMAAKSGTVGR------ILPGMDAR----LLAVPGieDG---GRLQLKGPNIMSGYLR 569
Cdd:cd12118 278 YGLTETYGPATVCAwkpewdelPTEERARLKARqgvryvGLEEVDVLdpetMKPVPR--DGktiGEIVFRGNIVMKGYLK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 570 VEKpgvlevPTAENAQGeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSD 649
Cdd:cd12118 356 NPE------ATAEAFRG----GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPD 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 650 ASKGEALVLFTT---DSELTREKLQQYARAHgVPELAVPRDIrHLKQLPLLGSGK 701
Cdd:cd12118 426 EKWGEVPCAFVElkeGAKVTEEEIIAFCREH-LAGFMVPKTV-VFGELPKTSTGK 478
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
314-601 |
1.08e-17 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 87.10 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 314 DKGKLWHLPEQLTQvRWVYLEDLKAdvtFSDKL----------------------WIFSHLLA-PHLAQV-----KQQPE 365
Cdd:cd05921 90 DLAKLKHLFELLKP-GLVFAQDAAP---FARALaaifplgtplvvsrnavagrgaISFAELAAtPPTAAVdaafaAVGPD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQI-KTIADFTADDRFM-SALPLFHSFGLTVGLFTPLLTGAEVFL---YPS 440
Cdd:cd05921 166 TVAKFLFTSGSTGLPKAVINTQRMLCANQAMLeQTYPFFGEEPPVLvDWLPWNHTFGGNHNFNLVLYNGGTLYIddgKPM 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 PLHYRIVPELVYDRNCTVLF----GTSTFLGNY-------ARFahpydFHRLRYVVAGAEKLQ----DSTKQLWQEKFGL 505
Cdd:cd05921 246 PGGFEETLRNLREISPTVYFnvpaGWEMLVAALekdealrRRF-----FKRLKLMFYAGAGLSqdvwDRLQALAVATVGE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 506 RV--LEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLlaVPGiedGGRLQ--LKGPNIMSGYLRVEKpgvlevpta 581
Cdd:cd05921 321 RIpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL--VPS---GGKYEvrVKGPNVTPGYWRQPE--------- 386
|
330 340
....*....|....*....|
gi 489124149 582 ENAQGEIERGWYDTGDIVRF 601
Cdd:cd05921 387 LTAQAFDEEGFYCLGDAAKL 406
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
350-701 |
1.64e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 86.09 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 350 SHLLAPHLA---QVKQQPEDAAVILFTSGSEGHPKGVVHSHKSI-LANVEQIKTIAdFTADDRFMSALPLFHsfgltVGL 425
Cdd:PRK06145 131 RRLAQGGLEippQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLhWKSIDHVIALG-LTASERLLVVGPLYH-----VGA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 426 FTplLTGAEVFLYPSPL--HYRIVPELVY-----DRNCTVLFG---TSTFLGNYARFAhpYDFHRLRYVVAGAEKLQDST 495
Cdd:PRK06145 205 FD--LPGIAVLWVGGTLriHREFDPEAVLaaierHRLTCAWMApvmLSRVLTVPDRDR--FDLDSLAWCIGGGEKTPESR 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 496 KQLWQEKF-GLRVLEGYGVTEcapVVSINVPMAA-----KSGTVGRILPGM-------DARLLAvPGIEdgGRLQLKGPN 562
Cdd:PRK06145 281 IRDFTRVFtRARYIDAYGLTE---TCSGDTLMEAgreieKIGSTGRALAHVeiriadgAGRWLP-PNMK--GEICMRGPK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 563 IMSGYLRV-EKpgvlevpTAENAQGeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKM 641
Cdd:PRK06145 355 VTKGYWKDpEK-------TAEAFYG----DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAE 423
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124149 642 HATAIKSDASKGE---ALVLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK06145 424 AAVIGVHDDRWGEritAVVVLNPGATLTLEALDRHCRQR-LASFKVPRQLKVRDELPRNPSGK 485
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
320-703 |
2.41e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.15 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 320 HLPEQLTQVRWVY---LEDLKADVtfsdklWIFS----HLLAPHLAQVkqqpedaaviLFTSGSEGHPKGVVHSHKSILA 392
Cdd:PRK05691 1237 HLLERLPQAEGVSaiaLDSLHLDS------WPSQapglHLHGDNLAYV----------IYTSGSTGQPKGVGNTHAALAE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 393 NVEQIKTIADFTADDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLH---YRIVpELVYDRNCTVLFGTSTFLGN 468
Cdd:PRK05691 1301 RLQWMQATYALDDSDVLMQKAPI--SFDVSVwECFWPLITGCRLVLAGPGEHrdpQRIA-ELVQQYGVTTLHFVPPLLQL 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 469 YARFAHPYDFHRLRYVVAGAEKLQDSTKQlwqekfglRVLE---------GYGVTECApvvsINVP---MAAKSGT---V 533
Cdd:PRK05691 1378 FIDEPLAAACTSLRRLFSGGEALPAELRN--------RVLQrlpqvqlhnRYGPTETA----INVThwqCQAEDGErspI 1445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 534 GRILPGMDARLL------AVPGIedGGRLQLKGPNIMSGYLRveKPGVlevpTAE----NAQGEIERGWYDTGDIVRFDE 603
Cdd:PRK05691 1446 GRPLGNVLCRVLdaelnlLPPGV--AGELCIGGAGLARGYLG--RPAL----TAErfvpDPLGEDGARLYRTGDRARWNA 1517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 604 NGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEALVLFTTD--SELTREKLQQyARAHGVPE 681
Cdd:PRK05691 1518 DGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEagQEAEAERLKA-ALAAELPE 1596
|
410 420
....*....|....*....|..
gi 489124149 682 LAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK05691 1597 YMVPAQLIRLDQMPLGPSGKLD 1618
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
363-703 |
2.45e-17 |
|
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: 85.06 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKtiADFTADDR--FMSALPLfhSFGLTV-GLFTPLLTGAEVFLYP 439
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAA--AAFSAEELagVLASTSI--CFDLSVfELFGPLATGGKVVLAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SPLHYRIVPelvydRNCTVlfgtsTFLGNYARFAHPYDFHR-----LRYVVAGAEKL-QDSTKQLWQEKFGLRVLEGYGV 513
Cdd:cd12115 179 NVLALPDLP-----AAAEV-----TLINTVPSAAAELLRHDalpasVRVVNLAGEPLpRDLVQRLYARLQVERVVNLYGP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 514 TE------CAPVVsinvPMAAKSGTVGRILPG-----MDARLLAVPgieDG--GRLQLKGPNIMSGYLRveKPGVlevpT 580
Cdd:cd12115 249 SEdttystVAPVP----PGASGEVSIGRPLANtqayvLDRALQPVP---LGvpGELYIGGAGVARGYLG--RPGL----T 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 581 AE----NAQGEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEAL 656
Cdd:cd12115 316 AErflpDPFGPGAR-LYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRL 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489124149 657 VLFTT---DSELTREKLQQYARaHGVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd12115 395 VAYIVaepGAAGLVEDLRRHLG-TRLPAYMVPSRFVRLDALPLTPNGKID 443
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
353-703 |
3.26e-17 |
|
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: 85.04 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 353 LAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTV-GLFTPLLT 431
Cdd:cd12116 114 AAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTY--AFDISLlELLLPLLA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 432 GAEVFLYPSPLHY--RIVPELVYDRNCTVLFGTST----FLGnyarfAHPYDFHRLRYVVAG-------AEKLQDSTKQL 498
Cdd:cd12116 192 GARVVIAPRETQRdpEALARLIEAHSITVMQATPAtwrmLLD-----AGWQGRAGLTALCGGealppdlAARLLSRVGSL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 499 WQEkfglrvlegYGVTE------CAPVVSinvpmAAKSGTVGRILPG-----MDARLLAVP-GIEdgGRLQLKGPNIMSG 566
Cdd:cd12116 267 WNL---------YGPTEttiwstAARVTA-----AAGPIPIGRPLANtqvyvLDAALRPVPpGVP--GELYIGGDGVAQG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 567 YLRveKPGVL-EVPTAENAQGEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVE-QLALAVSADKMHAT 644
Cdd:cd12116 331 YLG--RPALTaERFVPDPFAGPGSR-LYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEaALAAHPGVAQAAVV 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 645 AIKSDASKG-EALVLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd12116 408 VREDGGDRRlVAYVVLKAGAAPDAAALRAHLRAT-LPAYMVPSAFVRLDALPLTANGKLD 466
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
363-605 |
4.17e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 84.95 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFhsfgltvGLFTPLLTGAEvflypspl 442
Cdd:PRK09274 172 APDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF-------ALFGPALGMTS-------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 hyrIVPEL----------------VYDRNCTVLFGTSTFLGNYARF--AHPYDFHRLRYV-VAGAEklqdSTKQLWqEKF 503
Cdd:PRK09274 237 ---VIPDMdptrpatvdpaklfaaIERYGVTNLFGSPALLERLGRYgeANGIKLPSLRRViSAGAP----VPIAVI-ERF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 504 ------GLRVLEGYGVTECAPVVSI--------NVPMAAK-SGT-VGRILPGMDARLLAV-----PGIEDGGRLQ----- 557
Cdd:PRK09274 309 ramlppDAEILTPYGATEALPISSIesreilfaTRAATDNgAGIcVGRPVDGVEVRIIAIsdapiPEWDDALRLAtgeig 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 558 ---LKGPNIMSGYLRvekpgvlevPTAENAQGEIERG----WYDTGDIVRFDENG 605
Cdd:PRK09274 389 eivVAGPMVTRSYYN---------RPEATRLAKIPDGqgdvWHRMGDLGYLDAQG 434
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
349-703 |
4.28e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 86.25 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 349 FSHLLAPHLAQVKQ--QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLfhSFGLTV-GL 425
Cdd:PRK10252 580 YNAPLAPQGAAPLQlsQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPC--SFDVSVwEF 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 426 FTPLLTGAEVFLYPSPLH------------YRI-----VPELVydrnctvlfgtSTFLGNYARFAHPYDFHRLRYVVAGA 488
Cdd:PRK10252 658 FWPFIAGAKLVMAEPEAHrdplamqqffaeYGVttthfVPSML-----------AAFVASLTPEGARQSCASLRQVFCSG 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 489 EKLQDSTKQLWQEKFGLRVLEGYGVTECA--------------PVVSINVPMAAKSGTVG-RILpgmDARLLAVP-GIed 552
Cdd:PRK10252 727 EALPADLCREWQQLTGAPLHNLYGPTEAAvdvswypafgeelaAVRGSSVPIGYPVWNTGlRIL---DARMRPVPpGV-- 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 553 GGRLQLKGPNIMSGYLrvEKPGVlevpTAEN------AQGeiERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGE---- 622
Cdd:PRK10252 802 AGDLYLTGIQLAQGYL--GRPDL----TASRfiadpfAPG--ER-MYRTGDVARWLDDGAVEYLGRSDDQLKIRGQriel 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 623 ------MVSLEMVEQlALAVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQQYARAhGVPELAVPRDIRHLKQLPL 696
Cdd:PRK10252 873 geidraMQALPDVEQ-AVTHACVINQAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRE-RLPPHMVPVVLLQLDQLPL 950
|
....*..
gi 489124149 697 LGSGKPD 703
Cdd:PRK10252 951 SANGKLD 957
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
364-601 |
1.71e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 83.39 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQI-KTIADFTADD-RFMSALPLFHSFG----LTVGLF----------- 426
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLaQTFPFLAEEPpVLVDWLPWNHTFGgnhnLGIVLYnggtlyiddgk 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 427 -TPLLTG------AEVflypSPLHYRIVP----ELVydrnctvlfgtsTFLGNYARFAHPYdFHRLRYVV-AGA------ 488
Cdd:PRK08180 288 pTPGGFDetlrnlREI----SPTVYFNVPkgweMLV------------PALERDAALRRRF-FSRLKLLFyAGAalsqdv 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 489 -EKLQDSTKQLWQEKfgLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLlaVPgieDGGRLQL--KGPNIMS 565
Cdd:PRK08180 351 wDRLDRVAEATCGER--IRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKL--VP---VGGKLEVrvKGPNVTP 423
|
250 260 270
....*....|....*....|....*....|....*...
gi 489124149 566 GYLRvekpgvlevptAENAQGEI--ERGWYDTGDIVRF 601
Cdd:PRK08180 424 GYWR-----------APELTAEAfdEEGYYRSGDAVRF 450
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
361-624 |
2.58e-16 |
|
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: 82.79 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 361 KQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADF-TADDR---FMSALPLFHSFGLTVGLFTPLLTGAEV- 435
Cdd:cd05933 146 SQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLrPATVGqesVVSYLPLSHIAAQILDIWLPIKVGGQVy 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 436 FLYPSPLHYRIVPEL-------------VYDR---NCTVLFGTSTFL----GNYARFA--------------HPYDFHRL 481
Cdd:cd05933 226 FAQPDALKGTLVKTLrevrptafmgvprVWEKiqeKMKAVGAKSGTLkrkiASWAKGVgletnlklmggespSPLFYRLA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 482 RYVV-----------------AGAEKLQDSTKQLWQeKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARL 544
Cdd:cd05933 306 KKLVfkkvrkalgldrcqkffTGAAPISRETLEFFL-SLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKI 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 545 LAvPGIEDGGRLQLKGPNIMSGYLRvekpgvLEVPTAENAQgeiERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GEM 623
Cdd:cd05933 385 HN-PDADGIGEICFWGRHVFMGYLN------MEDKTEEAID---EDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGEN 454
|
.
gi 489124149 624 V 624
Cdd:cd05933 455 V 455
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
370-701 |
3.10e-16 |
|
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: 82.75 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 370 ILFTSGSEGHPKGVV-----HShksiLANVEQIKTIADFTADDRFMSALPLfhsfGLTVG----LFTPLLTGAEVFLY-- 438
Cdd:cd05967 235 ILYTSGTTGKPKGVVrdnggHA----VALNWSMRNIYGIKPGDVWWAASDV----GWVVGhsyiVYGPLLHGATTVLYeg 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 439 -----PSPLHY-RIVPElvYDRNCtvLFGTSTFL---------GNYARfahPYDFHRLRYVVAGAEKLQDSTKQLWQEKF 503
Cdd:cd05967 307 kpvgtPDPGAFwRVIEK--YQVNA--LFTAPTAIrairkedpdGKYIK---KYDLSSLRTLFLAGERLDPPTLEWAENTL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 504 GLRVLEGYGVTECAPVVSIN----VPMAAKSGTVGRILPGMDARLLAvpgiEDGGRLqlkGPNIMsGYLRVE---KPGVL 576
Cdd:cd05967 380 GVPVIDHWWQTETGWPITANpvglEPLPIKAGSPGKPVPGYQVQVLD----EDGEPV---GPNEL-GNIVIKlplPPGCL 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 577 evPTAENAQGEIE-------RGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSD 649
Cdd:cd05967 452 --LTLWKNDERFKklylskfPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRD 529
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489124149 650 ASKGE---ALVLFTTDSELTREKLQQYARAHgVPE----LAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05967 530 ELKGQvplGLVVLKEGVKITAEELEKELVAL-VREqigpVAAFRLVIFVKRLPKTRSGK 587
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
321-613 |
7.37e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 80.69 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 321 LPEQLTQVrwvYLEDLKADVTFSDK-------LWIFSHLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILAN 393
Cdd:PRK09029 87 LPQPLLEE---LLPSLTLDFALVLEgentfsaLTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 394 VEQIKTIADFTADDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPS-PL--------HYRIVPE-----LVYDRNCTVL 459
Cdd:PRK09029 164 AEGVLSLMPFTAQDSWLLSLPLFHVSGQGI-VWRWLYAGATLVVRDKqPLeqalagctHASLVPTqlwrlLDNRSEPLSL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 460 fgTSTFLGnyarfahpydfhrlryvvaGAEKLQDSTKQLwqEKFGLRVLEGYGVTECAPVVsinvpmAAK----SGTVGR 535
Cdd:PRK09029 243 --KAVLLG-------------------GAAIPVELTEQA--EQQGIRCWCGYGLTEMASTV------CAKradgLAGVGS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 536 ILPGMDARLlavpgieDGGRLQLKGPNIMSGYLRvekpgvlevptaenaQGEI-----ERGWYDTGDIVRFDeNGFVQIQ 610
Cdd:PRK09029 294 PLPGREVKL-------VDGEIWLRGASLALGYWR---------------QGQLvplvnDEGWFATRDRGEWQ-NGELTIL 350
|
...
gi 489124149 611 GRA 613
Cdd:PRK09029 351 GRL 353
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
363-703 |
2.10e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.98 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSalplFHSFGL---TVGLFTPLLTGAEVFLYP 439
Cdd:PRK05691 2331 LPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELH----FYSINFdaaSERLLVPLLCGARVVLRA 2406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 S-PLHYRIVPELVYDRNCTVLFGTSTFLGNYARF-AHPYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVL-EGYGVTEC 516
Cdd:PRK05691 2407 QgQWGAEEICQLIREQQVSILGFTPSYGSQLAQWlAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTET 2486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 517 A--PVVSI---NVPMAAKSGTVGRILPG-----MDARLLAVP--GIedgGRLQLKGPNIMSGYLRveKPGVLE---VPTA 581
Cdd:PRK05691 2487 VvmPLACLapeQLEEGAASVPIGRVVGArvayiLDADLALVPqgAT---GELYVGGAGLAQGYHD--RPGLTAerfVADP 2561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 582 ENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAvSADKMHATAIKSDASKGEALV--LF 659
Cdd:PRK05691 2562 FAADGG---RLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE-HPAVREAVVLALDTPSGKQLAgyLV 2637
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489124149 660 TTDSELT-------REKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK05691 2638 SAVAGQDdeaqaalREALKAHLKQQ-LPDYMVPAHLILLDSLPLTANGKLD 2687
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
365-704 |
4.69e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 77.42 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSI---LANVEQIKTIADFTADD-----------RFMSALPLFHSFGLTVGlFTPLL 430
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTPSEDahkaaaaaagtVMFPAPPLMHGTGSWTA-FGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 431 TGAEVFLYPSPLHYRIVPELVYDRNCTVLfgtsTFLGN-YAR-------FAHPYDFHRLRYVVAGAEKLQDSTKQLWQEK 502
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSM----TIVGDaMARplidalrDAGPYDLSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 503 FGLRVL-EGYGVTEC-APVVSINVPMAAKSGTVGRILPGM-----DARLLAvPGIEDGGRLQLKGpNIMSGYLRVEKPGV 575
Cdd:cd05924 158 VPNITLvDAFGSSETgFTGSGHSAGSGPETGPFTRANPDTvvlddDGRVVP-PGSGGVGWIARRG-HIPLGYYGDEAKTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 576 LEVPTAENAQgeiergWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAI-KSDASKGE 654
Cdd:cd05924 236 ETFPEVDGVR------YAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEE-ALKSHPAVYDVLVVgRPDERWGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489124149 655 ---ALVLFTTDSELTREKLQQYARahgvPELA---VPRDIRHLKQLPLLGSGKPDF 704
Cdd:cd05924 309 evvAVVQLREGAGVDLEELREHCR----TRIArykLPKQVVFVDEIERSPAGKADY 360
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
254-701 |
5.80e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 78.26 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 254 EGERIGLMLPNagiSAAVIFGAIARRRIPA---MMNYTAGVKGLTSAITASEIKTIFTSRQF---LDKGkLWHLPEQLTQ 327
Cdd:PRK13382 92 EPRVVGIMCRN---HRGFVEALLAANRIGAdilLLNTSFAGPALAEVVTREGVDTVIYDEEFsatVDRA-LADCPQATRI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 328 VRWVyleDLKADVTFSDklwifshLLAPHLAQ-VKQQPEDAAVILFTSGSEGHPKGVVHSHKsilANVEQIKTIADFT-- 404
Cdd:PRK13382 168 VAWT---DEDHDLTVEV-------LIAAHAGQrPEPTGRKGRVILLTSGTTGTPKGARRSGP---GGIGTLKAILDRTpw 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 405 -ADDRFMSALPLFHSFGLTVGLFTPLLTGAEVflypspLHYRIVPE----LVyDRN-----CTVLFGTSTFLGNYARFAH 474
Cdd:PRK13382 235 rAEEPTVIVAPMFHAWGFSQLVLAASLACTIV------TRRRFDPEatldLI-DRHratglAVVPVMFDRIMDLPAEVRN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 475 PYDFHRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTEcAPVVSINVP--MAAKSGTVGRILPGMDARLLAVPGIE- 551
Cdd:PRK13382 308 RYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE-AGMIATATPadLRAAPDTAGRPAEGTEIRILDQDFREv 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 552 -DG--GRLQLKGPNIMSGYlrveKPGvlevptaenAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEM 628
Cdd:PRK13382 387 pTGevGTIFVRNDTQFDGY----TSG---------STKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIE 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 629 VEQlALAVSADKMHATAIKSDASK-GEAL---VLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK13382 454 VEK-TLATHPDVAEAAVIGVDDEQyGQRLaafVVLKPGASATPETLKQHVRDN-LANYKVPRDIVVLDELPRGATGK 528
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
233-701 |
6.51e-15 |
|
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: 78.37 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEK-YSTEGERIGLMLPNagISAAVIFG-AIARrrIPAMMNYT-AG--VKGLTSAITASEIKTIF 307
Cdd:cd05966 86 TYRELLREVCRFANVLKSlGVKKGDRVAIYMPM--IPELVIAMlACAR--IGAVHSVVfAGfsAESLADRINDAQCKLVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 308 TSRQFLDKGKLWHLP-------EQLTQVRWVY-LEDLKADVTFSDK--LWiFSHLLA---PHLAQVKQQPEDAAVILFTS 374
Cdd:cd05966 162 TADGGYRGGKVIPLKeivdealEKCPSVEKVLvVKRTGGEVPMTEGrdLW-WHDLMAkqsPECEPEWMDSEDPLFILYTS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 375 GSEGHPKGVVHSHKSILANVEQ-IKTIADFTADDRFMSALPLF----HSFGLtvglFTPLLTGAEVFLY---PSPLHYRI 446
Cdd:cd05966 241 GSTGKPKGVVHTTGGYLLYAATtFKYVFDYHPDDIYWCTADIGwitgHSYIV----YGPLANGATTVMFegtPTYPDPGR 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 447 VPELVYDRNCTVLFGTSTFLGNYARF--AHP--YDFHRLR-----------------YVVAGAEKLQ--DStkqLWQEKF 503
Cdd:cd05966 317 YWDIVEKHKVTIFYTAPTAIRALMKFgdEWVkkHDLSSLRvlgsvgepinpeawmwyYEVIGKERCPivDT---WWQTET 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 504 GlrvleGYGVTeCAPVVsinVPMaaKSGTVGRILPGMDARLLAvpgiEDGGrlQLKGPNimSGYLRVEK--PGVLEvpta 581
Cdd:cd05966 394 G-----GIMIT-PLPGA---TPL--KPGSATRPFFGIEPAILD----EEGN--EVEGEV--EGYLVIKRpwPGMAR---- 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 582 eNAQGEIER----------GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALaVSADKMHATAI--KSD 649
Cdd:cd05966 451 -TIYGDHERyedtyfskfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVES-AL-VAHPAVAEAAVvgRPH 527
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 650 ASKGEALVLFTT--DSELTREKLQQYARAHgVPE----LAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05966 528 DIKGEAIYAFVTlkDGEEPSDELRKELRKH-VRKeigpIATPDKIQFVPGLPKTRSGK 584
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
233-709 |
6.55e-15 |
|
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: 77.78 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYS-TEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKtiftsrq 311
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGlKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAK------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 312 fldkgklwhlpeqltqvrwvyledlkadvtfsdklwifsHLLAphlaqvkqqpeDAAVILFTSGSEGHPKGVVHSHKSIL 391
Cdd:cd05940 78 ---------------------------------------HLVV-----------DAALYIYTSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 392 --ANVEQIKTIAdfTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVyDRNCTVLfgtsTFLGNY 469
Cdd:cd05940 108 rgGAFFAGSGGA--LPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIR-KYQATIF----QYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 470 ARF-----AHPYDF-HRLRYVVAGAekLQDSTKQLWQEKFGL-RVLEGYGVTECApVVSINVPmaAKSGTVGRI--LPGM 540
Cdd:cd05940 181 CRYllnqpPKPTERkHKVRMIFGNG--LRPDIWEEFKERFGVpRIAEFYAATEGN-SGFINFF--GKPGAIGRNpsLLRK 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 541 DARLLAVPGIEDGGRLqLKGPNimsGYLR---VEKPGVL--EVPTAENAQGEI--------------ERG--WYDTGDIV 599
Cdd:cd05940 256 VAPLALVKYDLESGEP-IRDAE---GRCIkvpRGEPGLLisRINPLEPFDGYTdpaatekkilrdvfKKGdaWFNTGDLM 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 600 RFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAI-----KSDASKGEALVLFTTDSELTREKLQQYA 674
Cdd:cd05940 332 RLDGEGFWYFVDRLGDTFRWKGENVSTTEVAA-VLGAFPGVEEANVYgvqvpGTDGRAGMAAIVLQPNEEFDLSALAAHL 410
|
490 500 510
....*....|....*....|....*....|....*
gi 489124149 675 RAHgVPELAVPRDIRHLKQLPLLGSGKPDFVTLKS 709
Cdd:cd05940 411 EKN-LPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
364-715 |
6.92e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 78.14 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSIL----ANVEQIktiaDFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
Cdd:PRK13388 149 AMDPFMLIFTSGTTGAPKAVRCSHGRLAfagrALTERF----GLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SplhyrivpelvydrnctvlFGTSTFLGNYARFAHPYdFHR----LRYVVAGAEKLQDSTKQL---------------WQ 500
Cdd:PRK13388 225 K-------------------FSASGFLDDVRRYGATY-FNYvgkpLAYILATPERPDDADNPLrvafgneasprdiaeFS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 501 EKFGLRVLEGYGVTECApvVSINVPMAAKSGTVGRILPGM------DARLLAVPGIEDGGRL-----------QLKGPNI 563
Cdd:PRK13388 285 RRFGCQVEDGYGSSEGA--VIVVREPGTPPGSIGRGAPGVaiynpeTLTECAVARFDAHGALlnadeaigelvNTAGAGF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 564 MSGYLRvekpgvlevptAENAQGE-IERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL---AVSAD 639
Cdd:PRK13388 363 FEGYYN-----------NPEATAErMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLrhpAINRV 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 640 KMHATaikSDASKGE---ALVLFTTDSELTREKLQQYARAHgvPEL---AVPRDIRHLKQLPLLGSGK---PDFVTLKSW 710
Cdd:PRK13388 432 AVYAV---PDERVGDqvmAALVLRDGATFDPDAFAAFLAAQ--PDLgtkAWPRYVRIAADLPSTATNKvlkRELIAQGWA 506
|
....*
gi 489124149 711 VDEPE 715
Cdd:PRK13388 507 TGDPV 511
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
361-630 |
1.42e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 77.57 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 361 KQQPEDAAVILFTSGSEGHPKGVVHSHKSILANV---EQIKTIAD--FTADDRFMSALPLFHSFGLTVGLFTpLLTGAEV 435
Cdd:PLN02861 216 PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDrvATEEDSYFSYLPLAHVYDQVIETYC-ISKGASI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 436 FLYPSPLHYRI-------------VPElVYDRNCTVLFGTSTFLGNYAR----FAHPYDFH------------------- 479
Cdd:PLN02861 295 GFWQGDIRYLMedvqalkptifcgVPR-VYDRIYTGIMQKISSGGMLRKklfdFAYNYKLGnlrkglkqeeasprldrlv 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 480 ----------RLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE-CAPVVSINVPMAAKSGTVGRILPGMDARLLAVP 548
Cdd:PLN02861 374 fdkikeglggRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLESVP 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 549 giEDG---------GRLQLKGPNIMSGYLRveKPGVLEVPTAEnaqgeierGWYDTGDIVRFDENGFVQIQGRAKRFAKI 619
Cdd:PLN02861 454 --EMGydalsdvprGEICLRGNTLFSGYHK--RQDLTEEVLID--------GWFHTGDIGEWQPNGAMKIIDRKKNIFKL 521
|
330
....*....|..
gi 489124149 620 A-GEMVSLEMVE 630
Cdd:PLN02861 522 SqGEYVAVENLE 533
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
363-632 |
3.04e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 76.39 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 363 QPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIAD-----FTADDRFMSALPLFHSF-----------GLTVG-- 424
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHILdrmieeyffrkGASVGyy 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 425 -------------LFTPLLTGA-EVF--LYP---------SPLHYRIVPELvYDRNCTVLFgtstfLGNYARFAHPY-DF 478
Cdd:PLN02430 298 hgdlnalrddlmeLKPTLLAGVpRVFerIHEgiqkalqelNPRRRLIFNAL-YKYKLAWMN-----RGYSHKKASPMaDF 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 479 -----------HRLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTECAPVVSINVP--MAAkSGTVGRILPGMDARLL 545
Cdd:PLN02430 372 lafrkvkaklgGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPdeMCM-LGTVGAPAVYNELRLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 546 AVP-------GIEDGGRLQLKGPNIMSGYLRvekpgvlevpTAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAK 618
Cdd:PLN02430 451 EVPemgydplGEPPRGEICVRGKCLFSGYYK----------NPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIK 520
|
330
....*....|....*
gi 489124149 619 IA-GEMVSLEMVEQL 632
Cdd:PLN02430 521 LSqGEYVALEYLENV 535
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
349-695 |
3.32e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 75.87 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 349 FSHLLAPHLAQ----VKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVG 424
Cdd:PRK07867 132 WADELAAHRDAeppfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 425 LFTPLLTGAEVFLYPSplhyrivpelvydrnctvlFGTSTFLGNYARFAHPYdFHR----LRYVVAGAEKLQDSTKQL-- 498
Cdd:PRK07867 212 WAVALAAGASIALRRK-------------------FSASGFLPDVRRYGATY-ANYvgkpLSYVLATPERPDDADNPLri 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 499 -------------WQEKFGLRVLEGYGVTECApvVSINVPMAAKSGTVGRILPGM-----DARLLAVPG-IEDGGRLQ-- 557
Cdd:PRK07867 272 vygnegapgdiarFARRFGCVVVDGFGSTEGG--VAITRTPDTPPGALGPLPPGVaivdpDTGTECPPAeDADGRLLNad 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 558 --------LKGPNIMSGYLRvekpgvlevptaeNAQGEIER---GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSL 626
Cdd:PRK07867 350 eaigelvnTAGPGGFEGYYN-------------DPEADAERmrgGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGT 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 627 EMVEQLALavSADKMHATAIKS--DASKGE----ALVLfTTDSELTREKLQQYARAHgvPEL---AVPRDIRHLKQLP 695
Cdd:PRK07867 417 APIERILL--RYPDATEVAVYAvpDPVVGDqvmaALVL-APGAKFDPDAFAEFLAAQ--PDLgpkQWPSYVRVCAELP 489
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
233-708 |
3.89e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 75.49 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKL---LTKT--LFVARILEKysteGERIGLMLPNagiSAAVIF--------GAIArrrIPAMMNYTAGVKGLTsaIT 299
Cdd:PRK08008 39 SYLELneeINRTanLFYSLGIRK----GDKVALHLDN---CPEFIFcwfglakiGAIM---VPINARLLREESAWI--LQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 300 ASEIKTIFTSRQFLD--KGKLWHLPEQLTQVrWVYLEDLKADVTFSDklwiFSHLLAPHLAQVKQQP----EDAAVILFT 373
Cdd:PRK08008 107 NSQASLLVTSAQFYPmyRQIQQEDATPLRHI-CLTRVALPADDGVSS----FTQLKAQQPATLCYAPplstDDTAEILFT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 374 SGSEGHPKGVVHSHKSIL-ANVEQIKTIAdFTADDRFMSALPLFHS-FGLTVGLftPLLT-GA---------------EV 435
Cdd:PRK08008 182 SGTTSRPKGVVITHYNLRfAGYYSAWQCA-LRDDDVYLTVMPAFHIdCQCTAAM--AAFSaGAtfvllekysarafwgQV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 436 FLYPS------PLHYRIV---PELVYDRNctvlfgtstflgnyarfahpydfHRLRYVVAGAEkLQDSTKQLWQEKFGLR 506
Cdd:PRK08008 259 CKYRAtiteciPMMIRTLmvqPPSANDRQ-----------------------HCLREVMFYLN-LSDQEKDAFEERFGVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 507 VLEGYGVTECapVVSI--NVPMAAKS-GTVGRilPGM--DARLLAVPGIE----DGGRLQLK---GPNIMSGYLRVEKpg 574
Cdd:PRK08008 315 LLTSYGMTET--IVGIigDRPGDKRRwPSIGR--PGFcyEAEIRDDHNRPlpagEIGEICIKgvpGKTIFKEYYLDPK-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 575 vlevPTAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLAVSADKMHAT------AIKS 648
Cdd:PRK08008 389 ----ATAKVLEAD---GWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI-IATHPKIQDIVvvgikdSIRD 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 649 DASKgeALVLFTTDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPDFVTLK 708
Cdd:PRK08008 461 EAIK--AFVVLNEGETLSEEEFFAFCEQN-MAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
362-638 |
9.72e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 74.67 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTI-----ADFTADDRFMSALPLFHSF-----------GLTVGL 425
Cdd:PLN02614 220 KKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLlksanAALTVKDVYLSYLPLAHIFdrvieecfiqhGAAIGF 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 426 F---TPLLTGAEVFLYPSPlhYRIVPElVYDRNCTVLFGTSTFLGNYARF----AHPYDFHRL----------------- 481
Cdd:PLN02614 300 WrgdVKLLIEDLGELKPTI--FCAVPR-VLDRVYSGLQKKLSDGGFLKKFvfdsAFSYKFGNMkkgqshveasplcdklv 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 482 ------------RYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE-CAPVVSINVPMAAKSGTVGRILPGMDARLLAVP 548
Cdd:PLN02614 377 fnkvkqglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVP 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 549 GIE-DG------GRLQLKGPNIMSGYLRVEkpgvlevptaENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA- 620
Cdd:PLN02614 457 EMEyDAlastprGEICIRGKTLFSGYYKRE----------DLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSq 526
|
330
....*....|....*...
gi 489124149 621 GEMVSLEMVEQLALAVSA 638
Cdd:PLN02614 527 GEYVAVENIENIYGEVQA 544
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
364-601 |
8.84e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 71.62 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDR---FMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvSLDWMPWNHTMGGNANFNGLLWGGGTLYIDDG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 441 plhyRIVPELVYD--RNCTVLfgTSTFLGN----YARFAHPYD---------FHRLRYVVAGAEKLQDstkQLWQEKFGL 505
Cdd:PRK12582 299 ----KPLPGMFEEtiRNLREI--SPTVYGNvpagYAMLAEAMEkddalrrsfFKNLRLMAYGGATLSD---DLYERMQAL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 506 RVLE---------GYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLAVpgiEDGGRLQLKGPNIMSGYL-RVEKpgv 575
Cdd:PRK12582 370 AVRTtghripfytGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPV---GDKYEVRVKGPNVTPGYHkDPEL--- 443
|
250 260
....*....|....*....|....*.
gi 489124149 576 levptaeNAQGEIERGWYDTGDIVRF 601
Cdd:PRK12582 444 -------TAAAFDEEGFYRLGDAARF 462
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
366-622 |
1.10e-12 |
|
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: 69.64 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 366 DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsplhYR 445
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFV------RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 446 IVPE----LVYDRNCTVLFGTSTFLGNYARF--AHPYDFHRLRYVVAGAEKLQDST--KQLWQEKFGlrvleGYGVTECA 517
Cdd:cd17636 75 VDAEevleLIEAERCTHAFLLPPTIDQIVELnaDGLYDLSSLRSSPAAPEWNDMATvdTSPWGRKPG-----GYGQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 518 PVVSINVPMAAKSGTVGRILPGMDARLLAVPGIE--DG--GRLQLKGPNIMSGYLRveKPGVlevptaeNAQgeieR--- 590
Cdd:cd17636 150 GLATFAALGGGAIGGAGRPSPLVQVRILDEDGREvpDGevGEIVARGPTVMAGYWN--RPEV-------NAR----Rtrg 216
|
250 260 270
....*....|....*....|....*....|..
gi 489124149 591 GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGE 622
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAE 248
|
|
| LPLAT_ACT14924-like |
cd07986 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ... |
7-185 |
1.13e-12 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ACT14924; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Pectobacterium carotovorum subsp. carotovorum PC1 locus ACT14924 putative acyltransferase, and similar proteins.
Pssm-ID: 153248 [Multi-domain] Cd Length: 210 Bit Score: 67.66 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 7 RNLFRVLFRVRVTGDVSALQGERVLITPNH-VSFIDGILLA-LFLPIRPVFAVYTSiSQQWYMRWLTPLidFVPLDPTKP 84
Cdd:cd07986 1 LDALNVQLEVDVSGLENIPKDGPVVIVANHpFGILDGLILAdLLGSVRPDVRILAN-QLLSKIPELRDL--FIPVDPLEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 85 M--------SIKHLVRLVEQGRPVVIFPEGRIST-TGSLMKIYD-----GAGFVAAKSGATVVPVRIEGaelsRFSRLKG 150
Cdd:cd07986 78 RaalaknreSLREALRHLKNGGALIIFPAGRVSTaSPPFGRVSDrpwnpFVARLARKAKAPVVPVYFSG----RNSRLFY 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489124149 151 LVkQRFFPRIRLHILP---------------PTQLPMPEAPRARDRRKIA 185
Cdd:cd07986 154 LA-GLIHPTLRTLLLPrellnkrgktirirvGRPIPPEELARFEDAEELA 202
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
354-701 |
1.19e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 70.88 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 354 APHLAQVKQQPedaAVILFTSGSEGHPKGVVHSHKSI--LANVEQIK-TIADFTADDRFMSALPLFHS----FGLTVGLF 426
Cdd:PRK12406 144 EPYDGPPVPQP---QSMIYTSGTTGHPKGVRRAAPTPeqAAAAEQMRaLIYGLKPGIRALLTGPLYHSapnaYGLRAGRL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 427 tplltGAEVFLYPsplhyRIVPE----LVYDRNCTVLFGTSTF------LGNYARFAhpYDFHRLRYVVAGAEKLQDSTK 496
Cdd:PRK12406 221 -----GGVLVLQP-----RFDPEellqLIERHRITHMHMVPTMfirllkLPEEVRAK--YDVSSLRHVIHAAAPCPADVK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 497 QLWQEKFGLRVLEGYGVTECAPVVSINVPMA-AKSGTVGRILPGMDARLLAvpgiEDGGRLQLKGPnimsGYLRVEKPGV 575
Cdd:PRK12406 289 RAMIEWWGPVIYEYYGSTESGAVTFATSEDAlSHPGTVGKAAPGAELRFVD----EDGRPLPQGEI----GEIYSRIAGN 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 576 LEVpTAEN---AQGEIER-GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSAdkMHATAI--KSD 649
Cdd:PRK12406 361 PDF-TYHNkpeKRAEIDRgGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPG--VHDCAVfgIPD 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 650 ASKGEALVLFT---TDSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK12406 438 AEFGEALMAVVepqPGATLDEADIRAQLKAR-LAGYKVPKHIEIMAELPREDSGK 491
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
365-708 |
1.97e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 69.90 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSI-LANVEQIKTIADFTADDRFMSALPLF--HSFGltvGLFTPLLTGAEVFLYPSP 441
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYpVGHLSTMYWIGLKPGDVHWNISSPGWakHAWS---CFFAPWNAGATVFLFNYA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 -LHYRIVPELVYDRNCTVLFGTSTFL-----GNYARFAHPydfhrLRYVVAGAEKLQDSTKQLWQEKFGLRVLEGYGVTE 515
Cdd:cd05974 162 rFDAKRVLAALVRYGVTTLCAPPTVWrmliqQDLASFDVK-----LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 CAPVVSINVPMAAKSGTVGRILPGMDARLL-AVPGIEDGGRLQL-----KGPNIMSGYlrVEKPGVLevptaenaQGEIE 589
Cdd:cd05974 237 TTALVGNSPGQPVKAGSMGRPLPGYRVALLdPDGAPATEGEVALdlgdtRPVGLMKGY--AGDPDKT--------AHAMR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 590 RGWYDTGDIVRFDENGFVQIQGRAK--------RFAKIAGEMVSLE--MVEQLALAVSADKMHATAIK--------SDAS 651
Cdd:cd05974 307 GGYYRTGDIAMRDEDGYLTYVGRADdvfkssdyRISPFELESVLIEhpAVAEAAVVPSPDPVRLSVPKafivlragYEPS 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489124149 652 KGEALVLFttdsELTREKLQQYARahgvpelavprdIRHLK--QLPLLGSGKPDFVTLK 708
Cdd:cd05974 387 PETALEIF----RFSRERLAPYKR------------IRRLEfaELPKTISGKIRRVELR 429
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
197-701 |
2.23e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 70.03 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 197 RMAVRPRETLYESLLAAKYRFGAGKNCIEDINFTpdSYRKLLTKTLFVARILEKYST-EGERIGLMLPNAG--ISAAVIF 273
Cdd:PRK13383 28 REASRGGTNPYTLLAVTAARWPGRTAIIDDDGAL--SYRELQRATESLARRLTRDGVaPGRAVGVMCRNGRgfVTAVFAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 274 GAIARRRIPAMMNYTAgvKGLTSAITASEIKTIFTSRQFLDKgklwhlpeqltqvrwvyledlkadVTFSDKLWIfshLL 353
Cdd:PRK13383 106 GLLGADVVPISTEFRS--DALAAALRAHHISTVVADNEFAER------------------------IAGADDAVA---VI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 354 APHLAQVKQ---QPEDAA---VILFTSGSEGHPKGVVHSHKsILANVEQIKTIADFT---ADDRFMSALPLFHSFG---- 420
Cdd:PRK13383 157 DPATAGAEEsggRPAVAApgrIVLLTSGTTGKPKGVPRAPQ-LRSAVGVWVTILDRTrlrTGSRISVAMPMFHGLGlgml 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 421 -LTVGLFTPLLT----GAEVFLYPSPLH----YRIVPelvydrnctVLFGTSTFLGNYARFAHPydFHRLRYVVAGAEKL 491
Cdd:PRK13383 236 mLTIALGGTVLThrhfDAEAALAQASLHradaFTAVP---------VVLARILELPPRVRARNP--LPQLRVVMSSGDRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 492 QDSTKQLWQEKFGLRVLEGYGVTECApVVSINVPMAAKSG--TVGRILPGMDARLLAVPGIEDG----GRLQLKGPNIMS 565
Cdd:PRK13383 305 DPTLGQRFMDTYGDILYNGYGSTEVG-IGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGprvtGRIFVGGELAGT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 566 GYLRVEKPGVLEvptaenaqgeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATA 645
Cdd:PRK13383 384 RYTDGGGKAVVD-------------GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVEN-ALAAHPAVADNAV 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 646 IK-SDASKGEALVLFTT---DSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK13383 450 IGvPDERFGHRLAAFVVlhpGSGVDAAQLRDYLKDR-VSRFEQPRDINIVSSIPRNPTGK 508
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
362-701 |
4.93e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 69.28 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPEDAAVILFTSGSEGHPKGVVHSHKSilANVEQIKTIADFTAD--DRFMSALPLFHSFGLTVGLFTPLLTGAEVFL-- 437
Cdd:PLN03102 183 QDEHDPISLNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGtcPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMrh 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 438 YPSPLHYRIVpEL--VYDRNCTVLFGTSTFLGNYARFAHPYDfhRLRYVVAGAEKLQDSTKQLwqEKFGLRVLEGYGVTE 515
Cdd:PLN03102 261 VTAPEIYKNI-EMhnVTHMCCVPTVFNILLKGNSLDLSPRSG--PVHVLTGGSPPPAALVKKV--QRLGFQVMHAYGLTE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 516 C-APVV-------------SINVPMAAKSGTVGRILPGMDAR----LLAVPgiEDG---GRLQLKGPNIMSGYLRVEKPg 574
Cdd:PLN03102 336 AtGPVLfcewqdewnrlpeNQQMELKARQGVSILGLADVDVKnketQESVP--RDGktmGEIVIKGSSIMKGYLKNPKA- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 575 vlevpTAEnaqgEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQ--------LALAVSAdKMHATAI 646
Cdd:PLN03102 413 -----TSE----AFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENvlykypkvLETAVVA-MPHPTWG 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124149 647 KSDAS-----KGEALVLFTTDSELTREK-LQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PLN03102 483 ETPCAfvvleKGETTKEDRVDKLVTRERdLIEYCREN-LPHFMCPRKVVFLQELPKNGNGK 542
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-614 |
2.64e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYSTEGERIGLMLPNAGISAAVIFG-----AIARRRIPAMMNYTAGVKGLTSAITASEIKTIF 307
Cdd:PRK05691 42 SYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGclyagVIAVPAYPPESARRHHQERLLSIIADAEPRLLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 308 TSRQFLDKgklwhlpeqLTQvrwvyLEDLKADvtfSDKLWIFSHLLAPHLAQVKQ----QPEDAAVILFTSGSEGHPKGV 383
Cdd:PRK05691 122 TVADLRDS---------LLQ-----MEELAAA---NAPELLCVDTLDPALAEAWQepalQPDDIAFLQYTSGSTALPKGV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 384 VHSHKSILANVEQIKT--IADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSPLHY--RIV------------ 447
Cdd:PRK05691 185 QVSHGNLVANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-SPAYFleRPLrwleaiseyggt 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 448 ----PELVYdRNCTVLFGTSTFLGnyarfahpYDFHRLRYVVAGAEKLQDSTKQLWQEKF---GLR---VLEGYGVTECA 517
Cdd:PRK05691 264 isggPDFAY-RLCSERVSESALER--------LDLSRWRVAYSGSEPIRQDSLERFAEKFaacGFDpdsFFASYGLAEAT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 518 PVVSinvpmaakSGTVGRILPGM--DARLLAVPGIEDGgrlqlKGPNIMS-GY------LRVEKPGVLEVpTAENAQGEI 588
Cdd:PRK05691 335 LFVS--------GGRRGQGIPALelDAEALARNRAEPG-----TGSVLMScGRsqpghaVLIVDPQSLEV-LGDNRVGEI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489124149 589 --------------------------ERGWYDTGDIvRFDENGFVQIQGRAK 614
Cdd:PRK05691 401 wasgpsiahgywrnpeasaktfvehdGRTWLRTGDL-GFLRDGELFVTGRLK 451
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
349-613 |
4.61e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 65.83 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 349 FSHLLAPHL------AQVKQqpEDAAVILFTSGSEGHPKGVVHSHKS---ILANveqikTIADF----TADDRFMSALPL 415
Cdd:PRK07470 143 YEALVARHLgarvanAAVDH--DDPCWFFFTSGTTGRPKAAVLTHGQmafVITN-----HLADLmpgtTEQDASLVVAPL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 416 FHSFGltVGLFTPLLTGAEVFLYPSPlhyRIVPE----LVYDRNCTVLFGTSTFLGNYARfaHP----YDFHRLRYVV-A 486
Cdd:PRK07470 216 SHGAG--IHQLCQVARGAATVLLPSE---RFDPAevwaLVERHRVTNLFTVPTILKMLVE--HPavdrYDHSSLRYVIyA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 487 GAEKL-QDSTKQLwqEKFGLRVLEGYGVTECAPVVSINVPM--------AAKSGTVGRILPGM-----DARLLAVPGIED 552
Cdd:PRK07470 289 GAPMYrADQKRAL--AKLGKVLVQYFGLGEVTGNITVLPPAlhdaedgpDARIGTCGFERTGMevqiqDDEGRELPPGET 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489124149 553 GgRLQLKGPNIMSGYLRVekpgvlevPTAeNAQGeIERGWYDTGDIVRFDENGFVQIQGRA 613
Cdd:PRK07470 367 G-EICVIGPAVFAGYYNN--------PEA-NAKA-FRDGWFRTGDLGHLDARGFLYITGRA 416
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
254-701 |
5.20e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.77 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 254 EGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDKGKLWHLP-------EQLT 326
Cdd:PLN02330 79 KGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPvivlgeeKIEG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 327 QVRWVYLedLKADVTFSDKLwifshllaphlAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANV---------EQI 397
Cdd:PLN02330 159 AVNWKEL--LEAADRAGDTS-----------DNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLcsslfsvgpEMI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 398 KTIADftaddrfMSALPLFHSFGLT--------------------VGLFTPLLTGAEVFLYPsplhyrIVPELVYD--RN 455
Cdd:PLN02330 226 GQVVT-------LGLIPFFHIYGITgiccatlrnkgkvvvmsrfeLRTFLNALITQEVSFAP------IVPPIILNlvKN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 456 CTVlfgtstflgnyarfaHPYDFHRL--RYVVAGAEKLQDSTKQLWQEKF-GLRVLEGYGVTE--CAPVVSINVPMA--- 527
Cdd:PLN02330 293 PIV---------------EEFDLSKLklQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEhsCITLTHGDPEKGhgi 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 528 AKSGTVGRILPGMDARL------LAVPGiEDGGRLQLKGPNIMSGYLRVEKpgvlevptaENAQGEIERGWYDTGDIVRF 601
Cdd:PLN02330 358 AKKNSVGFILPNLEVKFidpdtgRSLPK-NTPGELCVRSQCVMQGYYNNKE---------ETDRTIDEDGWLHTGDIGYI 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 602 DENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGE---ALVLFTTDSELTREKLQQYArAHG 678
Cdd:PLN02330 428 DDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEipaACVVINPKAKESEEDILNFV-AAN 506
|
490 500
....*....|....*....|...
gi 489124149 679 VPELAVPRDIRHLKQLPLLGSGK 701
Cdd:PLN02330 507 VAHYKKVRVVQFVDSIPKSLSGK 529
|
|
| LPLAT |
cd06551 |
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ... |
5-167 |
5.22e-11 |
|
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).
Pssm-ID: 153244 [Multi-domain] Cd Length: 187 Bit Score: 62.43 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 5 FFRNLFRVLFRVRVTGDVSALQGERVLITPNHVSFIDGILLALFLPIRPVFAVYTSISQQ-----WYMRWLtpliDFVPL 79
Cdd:cd06551 3 YLLLNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLLLERGLRRDVYGLMDEElleryPFFTRL----GAFSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 80 DPTKPMSI-KHLV----RLVEQGRPVVIFPEGRISTTGS-LMKIYDGAGFVAAKSGATVVPVRIEGAelsrfsrlKGLVK 153
Cdd:cd06551 79 DRDSPRSAaKSLKyvarLLSKPGSVVWIFPEGTRTRRDKrPLQFKPGVAHLAEKAGVPIVPVALRYT--------FELFE 150
|
170
....*....|....
gi 489124149 154 QrfFPRIRLHILPP 167
Cdd:cd06551 151 Q--FPEIFVRIGPP 162
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
350-703 |
8.82e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 64.30 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 350 SHLLAPHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANveqiktiADFTAD-----DRFMSALPLFHSFGLTVg 424
Cdd:PRK07824 20 AALLRDALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTAS-------ADATHDrlggpGQWLLALPAHHIAGLQV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 425 LFTPLLTGAE-VFLYPS-----PLHYRIVPELVYDRNCTVLfgTSTFLGNYARfaHPYDFHRLR----YVVAGA---EKL 491
Cdd:PRK07824 92 LVRSVIAGSEpVELDVSagfdpTALPRAVAELGGGRRYTSL--VPMQLAKALD--DPAATAALAeldaVLVGGGpapAPV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 492 QDSTKQLwqekfGLRVLEGYGVTECApvvsinvpmaakSGTV--GRILPGMDARLlavpgieDGGRLQLKGPNIMSGYLR 569
Cdd:PRK07824 168 LDAAAAA-----GINVVRTYGMSETS------------GGCVydGVPLDGVRVRV-------EDGRIALGGPTLAKGYRN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 570 VEKPGvlevPTAENaqgeierGWYDTGDIVRFDeNGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSD 649
Cdd:PRK07824 224 PVDPD----PFAEP-------GWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPD 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 650 ASKGEALVLFTTDSELTREKLQQYaRAHGVPEL---AVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK07824 292 DRLGQRVVAAVVGDGGPAPTLEAL-RAHVARTLdrtAAPRELHVVDELPRRGIGKVD 347
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
362-432 |
1.06e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 64.96 E-value: 1.06e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489124149 362 QQPEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIktIADFTADD--------RFMSALPLFHSFGLTVGLFTPLLTG 432
Cdd:PRK05850 157 RDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQL--MSDYFGDTggvpppdtTVVSWLPFYHDMGLVLGVCAPILGG 233
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
375-711 |
1.46e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 64.24 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 375 GSEGHPKGVVHSHK----SILANVEqiktIADFTADDRFMSALPLFHSFGLT----VGLFtplLTGAEVFLY--PSPL-- 442
Cdd:PRK10946 192 GSTGTPKLIPRTHNdyyySVRRSVE----ICGFTPQTRYLCALPAAHNYPMSspgaLGVF---LAGGTVVLApdPSATlc 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 -----HYRI-----VPELVydrnctvlfgtSTFLGNYARFAHPYDFHRLRYVVAGAEKLQDSTK---------QLwQEKF 503
Cdd:PRK10946 265 fplieKHQVnvtalVPPAV-----------SLWLQAIAEGGSRAQLASLKLLQVGGARLSETLArripaelgcQL-QQVF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 504 GLRvlEG---YGVTECAPVVSINvpmaaksgTVGR-ILPGMDARLLAvpgiEDG--------GRLQLKGPNIMSGYLRve 571
Cdd:PRK10946 333 GMA--EGlvnYTRLDDSDERIFT--------TQGRpMSPDDEVWVAD----ADGnplpqgevGRLMTRGPYTFRGYYK-- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 572 KPgvlevptAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAvSADKMHAtAIKS--D 649
Cdd:PRK10946 397 SP-------QHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLR-HPAVIHA-ALVSmeD 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124149 650 ASKGEALVLF-TTDSELTREKLQQYARAHGVPELAVPRDIRHLKQLPLLGSGKPDFVTLKSWV 711
Cdd:PRK10946 468 ELMGEKSCAFlVVKEPLKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
354-701 |
1.85e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 63.87 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 354 APHLAQVKQQP----EDAAVILFTSGSEGHPKGVVHSHKSILA--NVEQIKTIA--DFTADDRFMSALPLFHSFGLTvGL 425
Cdd:PRK05857 154 SLDAASLAGNAdqgsEDPLAMIFTSGTTGEPKAVLLANRTFFAvpDILQKEGLNwvTWVVGETTYSPLPATHIGGLW-WI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 426 FTPLL------TGAEvflypsplHYRIVPELVYDR--NCTVLFGTS-TFLGNYARFAhPYDFHRLRYVVAGAEKLQDSTK 496
Cdd:PRK05857 233 LTCLMhgglcvTGGE--------NTTSLLEILTTNavATTCLVPTLlSKLVSELKSA-NATVPSLRLVGYGGSRAIAADV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 497 QlWQEKFGLRVLEGYGVTE------CAPVVSINVPmAAKSGTVGRILPGMDARLLAV----PGIEDG------GRLQLKG 560
Cdd:PRK05857 304 R-FIEATGVRTAQVYGLSEtgctalCLPTDDGSIV-KIEAGAVGRPYPGVDVYLAATdgigPTAPGAgpsasfGTLWIKS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 561 PNIMSGYLRvekpgvlevpTAENAQGEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADK 640
Cdd:PRK05857 382 PANMLGYWN----------NPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVR 451
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 641 MHATAIKSDASKGE----ALVLFTTDSELTREKLQQYARAHGVPE---LAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK05857 452 EAACYEIPDEEFGAlvglAVVASAELDESAARALKHTIAARFRREsepMARPSTIVIVTDIPRTQSGK 519
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
258-701 |
6.44e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 62.06 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 258 IGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITASEIKTIFTSRQFLDKGKlwhlpEQLTqvrwvYLEDLK 337
Cdd:cd05915 52 VATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVE-----AIRG-----ELKTVQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 338 ADVTFSDKLWIFSHLLA---PHLAQVKQQPE-DAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDR--FMS 411
Cdd:cd05915 122 HFVVMDEKAPEGYLAYEealGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKdvVLP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 412 ALPLFHSFGLTVgLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYA--RFAHPYDFHRLRYVVAGAE 489
Cdd:cd05915 202 VVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALAdyLESTGHRLKTLRRLVVGGS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 490 KLQDSTKQLwqEKFG-LRVLEGYGVTECAPVVSI--------------NVPMAAKSGT--VGRILPGMDARLLAVPgiED 552
Cdd:cd05915 281 AAPRSLIAR--FERMgVEVRQGYGLTETSPVVVQnfvkshleslseeeKLTLKAKTGLpiPLVRLRVADEEGRPVP--KD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 553 GGRLQ---LKGPNIMSGYLRVEkpgvlEVPTAENAQGeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMV 629
Cdd:cd05915 357 GKALGevqLKGPWITGGYYGNE-----EATRSALTPD----GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDL 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489124149 630 EQLALAVSADKMHATAIKSDASKGEALVLFT--TDSELTREKLQQYARAHGVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:cd05915 428 ENALMGHPKVKEAAVVAIPHPKWQERPLAVVvpRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGK 501
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
365-703 |
9.06e-10 |
|
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: 61.72 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKtiaDFTADDRFMSALPlFHSFGLTVG---LFTPLLTGAEVFLYPSP 441
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER---EKTNINFSDKVLQ-FATCSFDVCyqeIFSTLLSGGTLYIIREE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 442 LHyRIVPEL---VYDRNCTVLFGTSTFL---GNYARFAHPYdFHRLRYVVAGAEKLQDStkQLWQEKF---GLRVLEGYG 512
Cdd:cd17656 204 TK-RDVEQLfdlVKRHNIEVVFLPVAFLkfiFSEREFINRF-PTCVKHIITAGEQLVIT--NEFKEMLhehNVHLHNHYG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 513 VTECAPVVSINV---------PMAAKSGTVGRILPGMDARLLAVPGIEdgGRLQLKGPNIMSGYLRVEKPgvlevpTAE- 582
Cdd:cd17656 280 PSETHVVTTYTInpeaeipelPPIGKPISNTWIYILDQEQQLQPQGIV--GELYISGASVARGYLNRQEL------TAEk 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 583 ---NAQGEIERgWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASKGEAL-VL 658
Cdd:cd17656 352 ffpDPFDPNER-MYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLcAY 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489124149 659 FTTDSELTREKLQQYArAHGVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:cd17656 431 FVMEQELNISQLREYL-AKQLPEYMIPSFFVPLDQLPLTPNGKVD 474
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
364-689 |
9.18e-10 |
|
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: 61.68 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLH 443
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 444 YRIVPElVYDRNCTVLfgtsTFLGNYARF-----AHPYD-FHRLRyvVAGAEKLQDSTKQLWQEKFGLRVL-EGYGVTEc 516
Cdd:cd05937 166 SQFWKD-VRDSGATII----QYVGELCRYllstpPSPYDrDHKVR--VAWGNGLRPDIWERFRERFNVPEIgEFYAATE- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 517 APVVSIN-------VPMAAKSGTVGRILPGMDARLLAV-------------------PGIEDG---GRLQLKGPNIMSGY 567
Cdd:cd05937 238 GVFALTNhnvgdfgAGAIGHHGLIRRWKFENQVVLVKMdpetddpirdpktgfcvraPVGEPGemlGRVPFKNREAFQGY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 568 LRVEKPGVLEVPTAENAQGEIergWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLAVSADKMHA---- 643
Cdd:cd05937 318 LHNEDATESKLVRDVFRKGDI---YFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADV-LGAHPDIAEAnvyg 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489124149 644 -TAIKSDASKGEALVLFTTDS----ELTREKLQQYARAhGVPELAVPRDIR 689
Cdd:cd05937 394 vKVPGHDGRAGCAAITLEESSavptEFTKSLLASLARK-NLPSYAVPLFLR 443
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
370-709 |
1.38e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 61.05 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 370 ILFTSGSEGHPKGVVHSHKSI---------LANVEQIKT---IADFTADD---RFMSALPLFHSFGLTvGLFTPLLTGAE 434
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIfrvllggrdFATGEPIEDeeeLAKRAAAGpgmRRFPAPPLMHGAGQW-AAFAALFSGQT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 435 VFLYPSP-LHYRIVPELVYDRNCTVLFgtstFLGN-YAR-------FAHPYDFHRLRYVVAGAEKLQDSTKQLWQEKF-G 504
Cdd:PRK07798 247 VVLLPDVrFDADEVWRTIEREKVNVIT----IVGDaMARplldaleARGPYDLSSLFAIASGGALFSPSVKEALLELLpN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 505 LRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARLLA------VPGIEDGGRLQLKGPnIMSGYLRVEKPGVLEV 578
Cdd:PRK07798 323 VVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDedgnpvEPGSGEIGWIARRGH-IPLGYYKDPEKTAETF 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 579 PTAENAQgeiergWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALAVSADKMHATAIKSDASK-GE--- 654
Cdd:PRK07798 402 PTIDGVR------YAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEE-ALKAHPDVADALVVGVPDERwGQevv 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 655 ALVLFTTDSELTREKLQQYARAHgvpeLA---VPRDIRHLKQLPLLGSGKPDFVTLKS 709
Cdd:PRK07798 475 AVVQLREGARPDLAELRAHCRSS----LAgykVPRAIWFVDEVQRSPAGKADYRWAKE 528
|
|
| AGP_acyltrn |
TIGR00530 |
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ... |
14-135 |
2.06e-09 |
|
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129621 [Multi-domain] Cd Length: 130 Bit Score: 56.20 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 14 FRVRVTGDVSALQGERVLITPNHVSFIDGILLALFLPIRPVFAVYTSISQQWYMRWLTPLIDFVPLD--PTKPM--SIKH 89
Cdd:TIGR00530 2 LKVEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFIDreNIRAIatALKA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489124149 90 LVRLVEQGRPVVIFPEGRISTTGSLMKIYDGAGFVAAKSGATVVPV 135
Cdd:TIGR00530 82 AIEVLKQGRSIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVPILPV 127
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
362-701 |
2.36e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 60.35 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPED---AAVILFTSGSEGHPKGVVHSHK-SILANVEQIkTIADFTADDRFMSALPLFH----SFGLTVglftPLLTGA 433
Cdd:PRK08162 176 TLPADewdAIALNYTSGTTGNPKGVVYHHRgAYLNALSNI-LAWGMPKHPVYLWTLPMFHcngwCFPWTV----AARAGT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 434 EVFLYpsplhyRIVPELVYD----RNCTVLFGT----STFLGNYARFAHPYDfHRLRYVVAGA-------EKLqdstkql 498
Cdd:PRK08162 251 NVCLR------KVDPKLIFDlireHGVTHYCGApivlSALINAPAEWRAGID-HPVHAMVAGAappaaviAKM------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 499 wqEKFGLRVLEGYGVTECAPVVSIN--------VPMAAKSGTVGR------ILPG---MDARLLA-VPgiEDG---GRLQ 557
Cdd:PRK08162 317 --EEIGFDLTHVYGLTETYGPATVCawqpewdaLPLDERAQLKARqgvrypLQEGvtvLDPDTMQpVP--ADGetiGEIM 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 558 LKGPNIMSGYLRVEKPgvlevpTAENAQGeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQ------ 631
Cdd:PRK08162 393 FRGNIVMKGYLKNPKA------TEEAFAG----GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDvlyrhp 462
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 632 --LALAVSAdkmhataiKSDASKGE---ALVLFTTDSELTREKLQQYARAHgvpeLA---VPRDIRhLKQLPLLGSGK 701
Cdd:PRK08162 463 avLVAAVVA--------KPDPKWGEvpcAFVELKDGASATEEEIIAHCREH----LAgfkVPKAVV-FGELPKTSTGK 527
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
364-630 |
3.06e-09 |
|
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: 60.13 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPL--FHSFGLTVGlfTPLLTGAEV------ 435
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwIGEQMYSVG--QALVCGFIVnfpeep 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 436 --------------FLYP------------------SPLH---YRIVPELVYDRNCTVLFGTSTFLGNYARFAHPY---- 476
Cdd:cd17641 235 etmmedlreigptfVLLPprvwegiaadvrarmmdaTPFKrfmFELGMKLGLRALDRGKRGRPVSLWLRLASWLADallf 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 477 -------DFHRLRYVVAGAEKLQDSTKQLWQeKFGLRVLEGYGVTECAPVVSINVPMAAKSGTVGRILPGMDARllavpg 549
Cdd:cd17641 315 rplrdrlGFSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVR------ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 550 IEDGGRLQLKGPNIMSGYLRVEKPgvlevpTAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GEMVSLEM 628
Cdd:cd17641 388 IDEVGEILVRSPGVFVGYYKNPEA------TAEDFDED---GWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQF 458
|
..
gi 489124149 629 VE 630
Cdd:cd17641 459 IE 460
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
354-703 |
8.64e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.41 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 354 APHLAQVKQQPEDAAVILFTSGSEGHPKGVVHSHKSILANveQIKTIADFTADDRFMSALPLFHSFGLTVGLF--TPLLt 431
Cdd:PRK05691 3858 ASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNN--QLSKVPYLALSEADVIAQTASQSFDISVWQFlaAPLF- 3934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 432 GAEVFLYPSPL--HYRIVPELVYDRNCTVLFGT-STFLGNYARFAHPYDfhRLRYVVAGAEKLQDSTKQLWQEKF-GLRV 507
Cdd:PRK05691 3935 GARVEIVPNAIahDPQGLLAHVQAQGITVLESVpSLIQGMLAEDRQALD--GLRWMLPTGEAMPPELARQWLQRYpQIGL 4012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 508 LEGYGVTECAPVVSI-NVPMAAKSGTVGRI--------LPGMDARLLAVPgIEDGGRLQLKGPNIMSGYL-RVEKPGVLE 577
Cdd:PRK05691 4013 VNAYGPAECSDDVAFfRVDLASTRGSYLPIgsptdnnrLYLLDEALELVP-LGAVGELCVAGTGVGRGYVgDPLRTALAF 4091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 578 VPTAENAQGEierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAIKSDASkGEALV 657
Cdd:PRK05691 4092 VPHPFGAPGE---RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVN-GKHLV 4167
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489124149 658 -------LFTTDSELtREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK05691 4168 gylvphqTVLAQGAL-LERIKQRLRAE-LPDYMVPLHWLWLDRLPLNANGKLD 4218
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
230-632 |
1.42e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 57.83 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 230 TPDSYRKLLTKTLFVARILEKYST-EGERIGLMLPNAgISAAVIFGAIAR----------------------RRIPAMMN 286
Cdd:PRK06164 34 RPLSRAELRALVDRLAAWLAAQGVrRGDRVAVWLPNC-IEWVVLFLACARlgatviavntryrshevahilgRGRARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 287 YTAGVKGLTSAITASEIKtiftsrqfldkgklwhlPEQLTQVRWVYLEDLKADVT----FSDKLWIFS-HLLAPHLA-QV 360
Cdd:PRK06164 113 VWPGFKGIDFAAILAAVP-----------------PDALPPLRAIAVVDDAADATpapaPGARVQLFAlPDPAPPAAaGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 361 KQQPEDAAVILFT-SGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYP 439
Cdd:PRK06164 176 RAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFS-TLLGALAGGAPLVCEP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 SPLHYRIVpELVYDRNCTVLFGTSTFLGNYARFA-HPYDFHRLRYV--VAGAEKLQDSTKQLWQEKFGLRVLegYGVTEC 516
Cdd:PRK06164 255 VFDAARTA-RALRRHRVTHTFGNDEMLRRILDTAgERADFPSARLFgfASFAPALGELAALARARGVPLTGL--YGSSEV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 517 APVVSINvPMAAKSGTvgRILPGmdaRLLAVPGIE-------------DG--GRLQLKGPNIMSGYLrvEKPgvlevpta 581
Cdd:PRK06164 332 QALVALQ-PATDPVSV--RIEGG---GRPASPEARvrardpqdgallpDGesGEIEIRAPSLMRGYL--DNP-------- 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489124149 582 ENAQGEIER-GWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQL 632
Cdd:PRK06164 396 DATARALTDdGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHA 447
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
321-703 |
2.18e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 57.21 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 321 LPEQLTQVRWVYLEDLKaDVTFSDKLWIFSHllaphlaQVKQqpEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIktI 400
Cdd:PRK04813 109 LPLEILGIPVITLDELK-DIFATGNPYDFDH-------AVKG--DDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWM--L 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 401 ADF-TADDRFMSALPLFhSFGLTV-GLFTPLLTGAEVFLYPSPLHYRivPELVYDR----NCTVLFGTSTF------LGN 468
Cdd:PRK04813 177 EDFaLPEGPQFLNQAPY-SFDLSVmDLYPTLASGGTLVALPKDMTAN--FKQLFETlpqlPINVWVSTPSFadmcllDPS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 469 YARFAHPydfhRLRYVVAGAEKLQDSTKQLWQEKF-GLRVLEGYGVTEcAPV----VSINVPMAAKSGT--VGRILPGM- 540
Cdd:PRK04813 254 FNEEHLP----NLTHFLFCGEELPHKTAKKLLERFpSATIYNTYGPTE-ATVavtsIEITDEMLDQYKRlpIGYAKPDSp 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 541 ----DARLLAVPGIEDgGRLQLKGPNIMSGYLR-VEKpgvlevpTAEnAQGEIERGW-YDTGDIVRFDeNGFVQIQGRAK 614
Cdd:PRK04813 329 lliiDEEGTKLPDGEQ-GEIVISGPSVSKGYLNnPEK-------TAE-AFFTFDGQPaYHTGDAGYLE-DGLLFYQGRID 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 615 RFAKIAGEMVSLEMVEQlALAVSADKMHATAI-KSDASKGEALV--------LFTTDSELT---REKLQQYarahgVPEL 682
Cdd:PRK04813 399 FQIKLNGYRIELEEIEQ-NLRQSSYVESAVVVpYNKDHKVQYLIayvvpkeeDFEREFELTkaiKKELKER-----LMEY 472
|
410 420
....*....|....*....|.
gi 489124149 683 AVPRDIRHLKQLPLLGSGKPD 703
Cdd:PRK04813 473 MIPRKFIYRDSLPLTPNGKID 493
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
365-621 |
3.00e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 57.05 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 365 EDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPL-- 442
Cdd:PRK07769 180 DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFvr 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 443 -HYRIVPELVYDRNCTVlfGTSTFLGNYArFAH------------PYDFHRLRYVVAGAEKLQDSTKQLWQEKF---GLR 506
Cdd:PRK07769 260 rPGRWIRELARKPGGTG--GTFSAAPNFA-FEHaaarglpkdgepPLDLSNVKGLLNGSEPVSPASMRKFNEAFapyGLP 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 507 ---VLEGYGVTECAPVVSiNVPMAAKSGTV---------GRILPGMDARLLAVPGI----------------------ED 552
Cdd:PRK07769 337 ptaIKPSYGMAEATLFVS-TTPMDEEPTVIyvdrdelnaGRFVEVPADAPNAVAQVsagkvgvsewavivdpetaselPD 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 553 G--GRLQLKGPNIMSGYLrvEKP--------GVLEVPTAEN-AQGEIERG-WYDTGDI-VRFDenGFVQIQGRAKRFAKI 619
Cdd:PRK07769 416 GqiGEIWLHGNNIGTGYW--GKPeetaatfqNILKSRLSEShAEGAPDDAlWVRTGDYgVYFD--GELYITGRVKDLVII 491
|
..
gi 489124149 620 AG 621
Cdd:PRK07769 492 DG 493
|
|
| PLN02901 |
PLN02901 |
1-acyl-sn-glycerol-3-phosphate acyltransferase |
35-140 |
3.73e-08 |
|
1-acyl-sn-glycerol-3-phosphate acyltransferase
Pssm-ID: 215488 [Multi-domain] Cd Length: 214 Bit Score: 54.35 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 35 NHVSFIDgiLLALFLPIRPV-FAVYTSISQQWYMRWLTPLIDFVPLDPTKPMS----IKHLVRLVEQGRPVVIFPEGRIS 109
Cdd:PLN02901 57 NHQSFLD--IYTLFHLGRPFkFISKTSIFLIPIIGWAMYMTGHIPLKRMDRRSqlecLKRCMELLKKGASVFFFPEGTRS 134
|
90 100 110
....*....|....*....|....*....|.
gi 489124149 110 TTGSLMKIYDGAGFVAAKSGATVVPVRIEGA 140
Cdd:PLN02901 135 KDGKLAAFKKGAFSVAAKTGVPVVPITLVGT 165
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
333-630 |
8.10e-08 |
|
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: 55.51 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 333 LEDLKADVTFSD-KLWIFSHLLAPHLAQVKQQP-------EDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFT 404
Cdd:cd05939 64 LESLLHCITVSKaKALIFNLLDPLLTQSSTEPPsqddvnfRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 405 ADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVyDRNCTVlfgtSTFLGNYARF--AHPY----DF 478
Cdd:cd05939 144 PEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCV-KYNCTI----VQYIGEICRYllAQPPseeeQK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 479 HRLRYVVAGAEKlqdstKQLWQE---KFGL-RVLEGYGVTEC-APVVSINVPMAAkSGTVGRILPGM-DARLLAVPgiED 552
Cdd:cd05939 219 HNVRLAVGNGLR-----PQIWEQfvrRFGIpQIGEFYGATEGnSSLVNIDNHVGA-CGFNSRILPSVyPIRLIKVD--ED 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 553 GGRLqLKGPNIMSGYLRVEKPGVL------------------EVPTAEN-AQGEIERG--WYDTGDIVRFDENGFVQIQG 611
Cdd:cd05939 291 TGEL-IRDSDGLCIPCQPGEPGLLvgkiiqndplrrfdgyvnEGATNKKiARDVFKKGdsAFLSGDVLVMDELGYLYFKD 369
|
330
....*....|....*....
gi 489124149 612 RAKRFAKIAGEMVSLEMVE 630
Cdd:cd05939 370 RTGDTFRWKGENVSTTEVE 388
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
364-522 |
1.28e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 54.38 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 364 PEDAAVILF-TSGSEGHPKGVVHSHKSILA---NVEQIKTIADFTADDRFMSALplfhSFGLTVGlFTPLLTGAEVflyp 439
Cdd:COG1541 81 PLEEIVRIHaSSGTTGKPTVVGYTRKDLDRwaeLFARSLRAAGVRPGDRVQNAF----GYGLFTG-GLGLHYGAER---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 440 spLHYRIVP----------ELVYDRNCTVLFGTSTF---LGNYARfAHPYDF--HRLRYVVAGAEKLQDSTKQLWQEKFG 504
Cdd:COG1541 152 --LGATVIPagggnterqlRLMQDFGPTVLVGTPSYllyLAEVAE-EEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERWG 228
|
170
....*....|....*...
gi 489124149 505 LRVLEGYGVTECAPVVSI 522
Cdd:COG1541 229 IKAYDIYGLTEVGPGVAY 246
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
270-482 |
5.92e-07 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 52.66 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 270 AVIFGAiarRRIPAMMNYTAGVKGLTSAItaseiKTIFTSRQFLDkgklwHLPEQLTQVRWVYLEDLKADVTFSDKLWI- 348
Cdd:cd05943 179 AYTYNG---KRHDVREKVAELVKGLPSLL-----AVVVVPYTVAA-----GQPDLSKIAKALTLEDFLATGAAGELEFEp 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 349 --FSHLLAphlaqvkqqpedaavILFTSGSEGHPKGVVHSHKSILanVEQIKTIA---DFTADDRFMsalplfhsFGLTV 423
Cdd:cd05943 246 lpFDHPLY---------------ILYSSGTTGLPKCIVHGAGGTL--LQHLKEHIlhcDLRPGDRLF--------YYTTC 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124149 424 G------LFTPLLTGAEVFLYP-SPLHYR--IVPELVYDRNCTVlFGTS-TFLGNYAR----FAHPYDFHRLR 482
Cdd:cd05943 301 GwmmwnwLVSGLAVGATIVLYDgSPFYPDtnALWDLADEEGITV-FGTSaKYLDALEKaglkPAETHDLSSLR 372
|
|
| COG3176 |
COG3176 |
Putative hemolysin [General function prediction only]; |
5-178 |
2.45e-06 |
|
Putative hemolysin [General function prediction only];
Pssm-ID: 442409 Cd Length: 270 Bit Score: 49.65 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 5 FFRNLFRVL-FRVRV-TGDVSAL-QGERVLITPNH-VSFIDGI-LLALFLPIRPVFAVYTS-----ISQQWYmrwlTPLi 74
Cdd:COG3176 45 FLRYVFEELgARLEVpEGDLDRIdADGHLLVVANHpLGILDGLaLLKLVGTVRPDYRILANdlalrIPGGFY----SEL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 75 dFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISTTGSLMkiyD-----GAGFVAAKSGATVVPVRIEGAE------LS 143
Cdd:COG3176 120 -EFPVDPFNLETLKAARRHLLEGGRSCVFPAGRVSGARRVI---DllwsgLAAKLARKAGAPVVPVYFDGRNsglfylFG 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489124149 144 RFSRLKG-------LVKQRFFPrIRLHI---LPPTQLPMPEAPRA 178
Cdd:COG3176 196 SIHPTLRtaalpreLLRKRGHL-IELRVgrpIPPLELDLDLDPAE 239
|
|
| LPLAT_LPCAT1-like |
cd07991 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ... |
6-137 |
3.93e-06 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.
Pssm-ID: 153253 [Multi-domain] Cd Length: 211 Bit Score: 48.37 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 6 FRNLFRVL--FRVRVTGDVSALQGERVLITpNHVSFIDGILLALFLPirpvfavyTSISQQWYMRWLtPLI-------DF 76
Cdd:cd07991 1 ARVLLFAFgfYVIKVHGKPDPPEAPRIIVA-NHTSFIDPLILFSDLF--------PSIVAKKELGKL-PFIgtilralGC 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 77 VPLDPTKPMSIKHLVRLVEQ------GRPVVIFPEGRISTTGSLMKIYDGAgFVAaksGATVVPVRI 137
Cdd:cd07991 71 IFVDRSEPKDRKKVVEEIKEratdpnWPPILIFPEGTTTNGKALIMFKKGA-FEP---GVPVQPVAI 133
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
370-482 |
1.05e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 49.02 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 370 ILFTSGSEGHPKGVVHSHKSILanVEQIKTIA---DFTADDRFMsalplfhsFGLTVG------LFTPLLTGAEVFLYP- 439
Cdd:PRK03584 268 ILYSSGTTGLPKCIVHGHGGIL--LEHLKELGlhcDLGPGDRFF--------WYTTCGwmmwnwLVSGLLVGATLVLYDg 337
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489124149 440 SPLHyrivP------ELVYDRNCTVlFGTS-TFLGNYARF-AHP---YDFHRLR 482
Cdd:PRK03584 338 SPFY----PdpnvlwDLAAEEGVTV-FGTSaKYLDACEKAgLVPgetHDLSALR 386
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
345-439 |
1.68e-05 |
|
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: 48.06 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 345 KLWIFSHLLAPH-----LAQVKQQPEDA--------------AVILFTSGSEGHPKGVVHSHKSILAnVEQIKTIADFTA 405
Cdd:cd05938 105 SVWYLSHTSNTEgvislLDKVDAASDEPvpaslrahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLCGVTA 183
|
90 100 110
....*....|....*....|....*....|....
gi 489124149 406 DDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
Cdd:cd05938 184 DDVIYITLPLYHSSGFLLGIGGCIELGATCVLKP 217
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
647-701 |
6.89e-05 |
|
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: 41.76 E-value: 6.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489124149 647 KSDASKGEALVLFTT---DSELTREKLQQYARAHgVPELAVPRDIRHLKQLPLLGSGK 701
Cdd:pfam13193 20 VPDELKGEAPVAFVVlkpGVELLEEELVAHVREE-LGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
233-432 |
2.34e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.35 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYSTEGERIGLMLPN-----AGISAAVIFGAIArrrIPAMMNYTAG-VKGLTSAITASEIKTI 306
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQVAGPGDRVAILAPQgidyvAGFFAAIKAGTIA---VPLFAPELPGhAERLDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 307 FTS-------RQFLDKgklwhLPeQLTQVRWVYLEDLKADVtfsdklwifSHLLAPhlaqVKQQPEDAAVILFTSGSEGH 379
Cdd:PRK12476 147 LTTtaaaeavEGFLRN-----LP-RLRRPRVIAIDAIPDSA---------GESFVP----VELDTDDVSHLQYTSGSTRP 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489124149 380 PKGVVHSHKSILANVEQ-IKTIADFTADDRFMSALPLFHSFGLTVGLFtPLLTG 432
Cdd:PRK12476 208 PVGVEITHRAVGTNLVQmILSIDLLDRNTHGVSWLPLYHDMGLSMIGF-PAVYG 260
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
233-439 |
3.59e-04 |
|
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: 43.88 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 233 SYRKLLTKTLFVARILEKYST--EGERIGLMLPNAGISAAVIFGA---------IARRRIPAMMNYTAGV----KGLTSA 297
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGlkPGDRVALMYPDPLDFVAAFYGClyagvvpipIEPPDISQQLGFLLGTckvrVALTVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 298 ITASE-IKTIFTSRQ--FLDKGKLWhlPeqltqvRWVYLEDLKADVTFSDKLWIfshllaphlAQVKQQPEDAAVILFTS 374
Cdd:cd05905 96 ACLKGlPKKLLKSKTaaEIAKKKGW--P------KILDFVKIPKSKRSKLKKWG---------PHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 375 GSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIP 223
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
362-701 |
3.99e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 43.68 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 362 QQPED---AAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY 438
Cdd:PLN02479 189 KPPADewqSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNICLR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 439 psplhyRIVPELVYdrNCTVLFGTSTFLG-----NYARFAHPYDF-----HRLRYVVAGAEKLQDSTKQLwqEKFGLRVL 508
Cdd:PLN02479 269 ------QVTAKAIY--SAIANYGVTHFCAapvvlNTIVNAPKSETilplpRVVHVMTAGAAPPPSVLFAM--SEKGFRVT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 509 EGYGVTE-------CA--------PVVSiNVPMAAKSGTVGRILPGMDA----RLLAVPGieDG---GRLQLKGPNIMSG 566
Cdd:PLN02479 339 HTYGLSEtygpstvCAwkpewdslPPEE-QARLNARQGVRYIGLEGLDVvdtkTMKPVPA--DGktmGEIVMRGNMVMKG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 567 YLRVEKPgvlevpTAENAQGeierGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALAVSADKMHATAI 646
Cdd:PLN02479 416 YLKNPKA------NEEAFAN----GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489124149 647 KSDASKGEALVLFTT--------DSELTREKLQQYARAHgVPELAVPRDIRhLKQLPLLGSGK 701
Cdd:PLN02479 486 RPDERWGESPCAFVTlkpgvdksDEAALAEDIMKFCRER-LPAYWVPKSVV-FGPLPKTATGK 546
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
526-701 |
5.89e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 43.21 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 526 MAAKSGTVGRILPGMDARLLAvpgiEDGGrlQLKGPNimSGYLRVEK--PGVLEvptaeNAQGEIER----------GWY 593
Cdd:PRK00174 419 TPLKPGSATRPLPGIQPAVVD----EEGN--PLEGGE--GGNLVIKDpwPGMMR-----TIYGDHERfvktyfstfkGMY 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 594 DTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALaVSADKMHATAI--KSDASKGEALVLFTT--DSELTREK 669
Cdd:PRK00174 486 FTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES-AL-VAHPKVAEAAVvgRPDDIKGQGIYAFVTlkGGEEPSDE 563
|
170 180 190
....*....|....*....|....*....|....*
gi 489124149 670 LQQYARAHGVPE---LAVPRDIRHLKQLPLLGSGK 701
Cdd:PRK00174 564 LRKELRNWVRKEigpIAKPDVIQFAPGLPKTRSGK 598
|
|
| LPLAT_DUF374-like |
cd07983 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: DUF374; ... |
88-190 |
6.41e-04 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: DUF374; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are the uncharacterized DUF374 phospholipid/glycerol acyltransferases and similar proteins.
Pssm-ID: 153245 [Multi-domain] Cd Length: 189 Bit Score: 41.43 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 88 KHLVRLVEQGRPVVIFPEGrisTTGSLMKIYDGAGFVAAKSGATVVPVrieGAELSRFSRLKGLVKQRF---FPRIRLHI 164
Cdd:cd07983 88 REMLRALKDGYNIAITPDG---PRGPRYKVKPGVILLARKSGAPIVPV---AIAASRAWRLKSWDRFIIpkpFSRVVIVF 161
|
90 100
....*....|....*....|....*...
gi 489124149 165 LPPTQLP--MPEAPRARDRRKIAGEMLH 190
Cdd:cd07983 162 GEPIHVPpdADEEELEEYRLELEAALNA 189
|
|
| LPLAT_AAK14816-like |
cd07992 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ... |
5-194 |
3.27e-03 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown AAK14816-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized glycerol-3-phosphate acyltransferases such as the Plasmodium falciparum locus AAK14816 putative acyltransferase, and similar proteins.
Pssm-ID: 153254 [Multi-domain] Cd Length: 203 Bit Score: 39.55 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 5 FFRNLFRVLFR-VRVTGDVSALQGERVLITPNHV-SFIDGILLALFLPIRPVFAVYTSISQQWYMRWLTPLIDFVPLDPT 82
Cdd:cd07992 4 LSRVILRIYFRrITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPVYRP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 83 K------------PMSIKHLVRLVEQGRPVVIFPEGrISTTGS-LMKIYDGAG---FVAAKSGAT---VVPVriegaels 143
Cdd:cd07992 84 KdlarggigkisnAAVFDAVGEALKAGGAIGIFPEG-GSHDRPrLLPLKAGAArmaLEALEAGQKdvkIVPV-------- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489124149 144 rfsrlkGLV---KQRFFPRIRLHILPPTQL-PMPEAPRARDRRKIAGEMLHQIMM 194
Cdd:cd07992 155 ------GLNyedKSRFRSRVLVEFGKPISVsAFEEAEASRDVEKKLINQLEAELE 203
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
364-437 |
4.08e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 40.19 E-value: 4.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489124149 364 PEDAAVILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTADDRFMSALPLFHSfGLTVGLFTPLLTGAEVFL 437
Cdd:cd17647 108 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHD-PIQRDMFTPLFLGAQLLV 180
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
358-701 |
4.15e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 40.32 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 358 AQVKQQPEDAAV------------ILFTSGSEGHPKGV---VHSHKSILANveQIKTIADFTADDRFMSAlplfHSFGLT 422
Cdd:PRK10524 214 ATLRAQHLGARVpvewlesnepsyILYTSGTTGKPKGVqrdTGGYAVALAT--SMDTIFGGKAGETFFCA----SDIGWV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 423 VG----LFTPLLTGAEVFLY------PSPlhyRIVPELVYDRNCTVLFGTST---FLGNY-ARFAHPYDFHRLRYVVAGA 488
Cdd:PRK10524 288 VGhsyiVYAPLLAGMATIMYeglptrPDA---GIWWRIVEKYKVNRMFSAPTairVLKKQdPALLRKHDLSSLRALFLAG 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 489 EKLQDSTKQLWQEKFGLRVLEGYGVTECA-PVVSIN---VPMAAKSGTVGRILPGMDARLLAvpgiEDGGrlQLKGPNiM 564
Cdd:PRK10524 365 EPLDEPTASWISEALGVPVIDNYWQTETGwPILAIArgvEDRPTRLGSPGVPMYGYNVKLLN----EVTG--EPCGPN-E 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 565 SGYLRVE---KPGVLEVPTAENAQ------GEIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQlALA 635
Cdd:PRK10524 438 KGVLVIEgplPPGCMQTVWGDDDRfvktywSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEE-SIS 516
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489124149 636 VSADKMHATAIK-SDASKGEALVLF-------TTDSELTREKLQQYARAHGVPEL---AVPRDIRHLKQLPLLGSGK 701
Cdd:PRK10524 517 SHPAVAEVAVVGvKDALKGQVAVAFvvpkdsdSLADREARLALEKEIMALVDSQLgavARPARVWFVSALPKTRSGK 593
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
365-386 |
4.97e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 40.12 E-value: 4.97e-03
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
554-632 |
9.35e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 39.32 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489124149 554 GRLQLKGPNIMSGYLrvekpgvLEVPTAENAQgeIERGWYDTGDIVRFDENGFVQIQGRAKRFAKIA-GEMVSLEMVEQL 632
Cdd:PTZ00342 542 GELLIKSDSIFSGYF-------LEKEQTKNAF--TEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSqGEYIETDMLNNL 612
|
|
| |
