|
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: 1568.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 1 MLFGFFRTLFRVLFRIRVTGDTQALYGERVLITPNHVSFLDGVLLALFLPVRPVFAVYSSISEKWYMRWLKPLIDFVPLD 80
Cdd:PRK08043 1 MLFSFFRNLFRVLYRVRVTGDTQALKGERVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQQWYMRWLKPYIDFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 81 PTKPMMIKHLVRLIGQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSQATVVPLRIDGAELTFFSRLKGLVKQRLFPKI 160
Cdd:PRK08043 81 PTKPMAIKHLVRLVEQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 161 TLHILPPTSLPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAQYRYGAKKNCVEDINFTPDTYRKLLTK 240
Cdd:PRK08043 161 TLHILPPTQLPMPDAPRARDRRKLAGEMLHQIMMEARMAVRPRETLYEALLSAQYRYGAGKPCIEDVNFTPDSYRKLLKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 241 TLFVGRILEKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKGKLWH 320
Cdd:PRK08043 241 TLFVGRILEKYSVEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 321 LPEQLTQVRWVFLEDLKADVTTADKLWIFAHLLMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTI 400
Cdd:PRK08043 321 LPEQLTQVRWVYLEDLKDDVTTADKLWIFAHLLMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 401 ADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFFR 480
Cdd:PRK08043 401 ADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFAR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 481 VRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAVPGIEDGGRLQLKG 560
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQGGRLQLKG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 561 PNVMNGYLRVENPGVLEAPTAENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEK 640
Cdd:PRK08043 561 PNIMNGYLRVEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDK 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937565178 641 MHATVVKSDASKGEALVLFTTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPDFVTLKGMVEEAEQQN 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: 952.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 5 FFRTLFRVLFRIRVTG--DTQALyGERVLITPNHVSFLDGVLLALFLPVRPVFAVYSSISEKWymrWLKP---LIDFVPL 79
Cdd:PRK06814 430 IFSILFRAFYRVEVKGleNLQKA-GKKAVIAANHVSFLDGPLLAAYLPEEPTFAIDTDIAKAW---WVKPflkLAKALPV 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 80 DPTKPMMIKHLVRLIGQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSQATVVPLRIDGAELTFFSRLKGLVKQRLFPK 159
Cdd:PRK06814 506 DPTNPMATRTLIKEVQKGEKLVIFPEGRITVTGSLMKIYDGPGMIADKAGAMVVPVRIDGLQFTHFSRLKNQVRRKWFPK 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 160 ITLHILPPTSLPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPR-ETLYESLLSAQYRYGAKKNCVEDINFTPDTYRKLL 238
Cdd:PRK06814 586 VTVTILPPVKLAVDPELKGRERRSAAGAALYDIMSDMMFETSDYdRTLFEALIEAAKIHGFKKLAVEDPVNGPLTYRKLL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 239 TKTLFVGRILEKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKGKL 318
Cdd:PRK06814 666 TGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAFIEKARL 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 319 WHLPEQL-TQVRWVFLEDLKADVTTADKLWIFAHLLMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQI 397
Cdd:PRK06814 746 GPLIEALeFGIRIIYLEDVRAQIGLADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQV 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 398 KTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYD 477
Cdd:PRK06814 826 AARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILFGTDTFLNGYARYAHPYD 905
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 478 FFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAVPGIEDGGRLQ 557
Cdd:PRK06814 906 FRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGIDEGGRLF 985
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 558 LKGPNVMNGYLRVENPGVLEAPtaenvngevETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVS 637
Cdd:PRK06814 986 VRGPNVMLGYLRAENPGVLEPP---------ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELW 1056
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 638 AEKMHATVVKSDASKGEALVLFTTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPDFVTLKGMVEEAEQQ 717
Cdd:PRK06814 1057 PDALHAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAK 1136
|
..
gi 1937565178 718 NA 719
Cdd:PRK06814 1137 PE 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: 688.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 225 EDINFTPDTYRKLLTKTLFVGRILEKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQIN 304
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 305 TIFTSRQFLDKGKLWHLPEQLTQVRWVFLEDLKADVTTADKLWIFAHLLMP------RQAQVKQQPEDDAIILFTSGSEG 378
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPpkwllrIFGVAPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 379 NPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTV 458
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 459 LFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVP-MAAKPGTVGRIL 537
Cdd:cd05909 241 LLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPqSPNKEGTVGRPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 538 PGLDARLLAVPG-----IEDGGRLQLKGPNVMNGYLRVENPGVLeaptaenvngEVETGWYDTGDIVRFDDQGFVQIQGR 612
Cdd:cd05909 321 PGMEVKIVSVETheevpIGEGGLLLVRGPNVMLGYLNEPELTSF----------AFGDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 613 AKRFAKIAGEMVSLEMVETLATAVSAEK-MHATVVKSDASKGEALVLFTTDGELKRDALLRYAREHGIPELAVPRDIRYL 691
Cdd:cd05909 391 LSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQV 470
|
490 500
....*....|....*....|
gi 1937565178 692 KQLPVLGSGKPDFVTLKGMV 711
Cdd:cd05909 471 EEIPLLGTGKPDYVTLKALA 490
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
5-708 |
2.42e-161 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 495.60 E-value: 2.42e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 5 FFRTLFRVLFRIRVTGDTQALYGERVLITPNHVSFLDGVLLALFLPvRPV-FAVYSSISEKWYMRWLKPLIDFVPLDPTK 83
Cdd:PRK08633 418 LLLLLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAASP-RPIrFVMERSIYEKWYLKWFFKLFGVIPISSGG 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 84 PMMIKHLVR-LIGQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSQATVVPLRIDGAELTFFSRLKGlvkqRLFPKITL 162
Cdd:PRK08633 497 SKESLEFIRkALDDGEVVCIFPEGAITRNGQLNEFKRGFELIVKGTDVPIIPFYIRGLWGSIFSRASG----KFLWRWPT 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 163 HILPPTSL----PMPEAPRARDRRKIAGEmLHQIMMEARMAVRPreTLYESLLSAqyrygAKKN----CVEDINFTPDTY 234
Cdd:PRK08633 573 RIPYPVTVafgkPMPAHSTAHEVKQAVFE-LSFDSWKSRKEALP--PLAEAWIDT-----AKRNwsrlAVADSTGGELSY 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 235 RKLLTKTLFVGRILEKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLD 314
Cdd:PRK08633 645 GKALTGALALARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLE 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 315 KGKLWHLPEQLTQ-VRWVFLEDLKADVTTADKLWIF-AHLLMP-----RQAQVKQQPEDDAIILFTSGSEGNPKGVVHSH 387
Cdd:PRK08633 725 KLKNKGFDLELPEnVKVIYLEDLKAKISKVDKLTALlAARLLParllkRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSH 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 388 KSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLG 467
Cdd:PRK08633 805 HNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLR 884
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 468 NYARF--ANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVP----------MAAKPGTVGR 535
Cdd:PRK08633 885 LYLRNkkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaadfkrqTGSKEGSVGM 964
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 536 ILPGLDAR------LLAVPGIEDgGRLQLKGPNVMNGYLRveNPgvleAPTAENVNGEVETGWYDTGDIVRFDDQGFVQI 609
Cdd:PRK08633 965 PLPGVAVRivdpetFEELPPGED-GLILIGGPQVMKGYLG--DP----EKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTI 1037
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 610 QGRAKRFAKIAGEMVSLEMVE-TLATAVSAEKMHATVVK-SDASKGEALVLFTTDGELKRDALLRYAREHGIPELAVPRD 687
Cdd:PRK08633 1038 TDRYSRFAKIGGEMVPLGAVEeELAKALGGEEVVFAVTAvPDEKKGEKLVVLHTCGAEDVEELKRAIKESGLPNLWKPSR 1117
|
730 740
....*....|....*....|.
gi 1937565178 688 IRYLKQLPVLGSGKPDFVTLK 708
Cdd:PRK08633 1118 YFKVEALPLLGSGKLDLKGLK 1138
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
233-717 |
9.95e-96 |
|
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: 303.66 E-value: 9.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTL-FVGRILEKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTsrq 311
Cdd:COG0318 26 TYAELDARARrLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 312 fldkgklwhlpeqltqvrwvfledlkadvttadklwifahllmprqaqvkqqpeddAIILFTSGSEGNPKGVVHSHKSIL 391
Cdd:COG0318 103 --------------------------------------------------------ALILYTSGTTGRPKGVMLTHRNLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 392 ANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSpLHYRIVPELVYDRNCTVLFGTSTF---LGN 468
Cdd:COG0318 127 ANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMlarLLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 469 YARFAnPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINV--PMAAKPGTVGRILPGLDARLLA 546
Cdd:COG0318 206 HPEFA-RYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 547 VPGIE--DG--GRLQLKGPNVMNGYLRveNPgvlEApTAEnvngEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGE 622
Cdd:COG0318 285 EDGRElpPGevGEIVVRGPNVMKGYWN--DP---EA-TAE----AFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 623 MVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTT---DGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGS 699
Cdd:COG0318 355 NVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrpGAELDAEELRAFLRER-LARYKVPRRVEFVDELPRTAS 433
|
490
....*....|....*...
gi 1937565178 700 GKPDFVTLKGMVEEAEQQ 717
Cdd:COG0318 434 GKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
366-703 |
5.00e-78 |
|
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: 253.36 E-value: 5.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 366 DDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYPSPLhYR 445
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFD-PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 446 IVPELVYDRNCTVLFGTSTFLGNYARFAN--PYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSIN 523
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPEsaGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 524 VP--MAAKPGTVGRILPGLDARLLAVPGIEDG----GRLQLKGPNVMNGYLRVEnpgvleaptaENVNGEVETGWYDTGD 597
Cdd:cd04433 159 PPddDARKPGSVGRPVPGVEVRIVDPDGGELPpgeiGELVVRGPSVMKGYWNNP----------EATAAVDEDGWYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 598 IVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKmHATVVKS-DASKGEALVLF---TTDGELKRDALLRY 673
Cdd:cd04433 229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVA-EAAVVGVpDPEWGERVVAVvvlRPGADLDAEELRAH 307
|
330 340 350
....*....|....*....|....*....|
gi 1937565178 674 AREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd04433 308 VRER-LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
233-614 |
1.69e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 219.88 E-value: 1.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRILEKYS-KQGEKIGLMLPNaGISAAVIFGAVSR-GRIPAMMNYTAGVKGLSSAITAAQINTIFTSR 310
Cdd:pfam00501 23 TYRELDERANRLAAGLRALGvGKGDRVAILLPN-SPEWVVAFLACLKaGAVYVPLNPRLPAEELAYILEDSGAKVLITDD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 311 QFLDKGKLWHLPEqLTQVRWVFLEDLKADVTTADKLWIFAHLLMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSI 390
Cdd:pfam00501 102 ALKLEELLEALGK-LEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 391 LANVEQIKTIAD----FTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS--PLHYRIVPELVYDRNCTVLFGTST 464
Cdd:pfam00501 181 VANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGfpALDPAALLELIERYKVTVLYGVPT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 465 FLgNY---ARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPM---AAKPGTVGRILP 538
Cdd:pfam00501 261 LL-NMlleAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLdedLRSLGSVGRPLP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 539 GLDARLLAVPG---IEDG--GRLQLKGPNVMNGYLRveNPgvlEApTAENVngeVETGWYDTGDIVRFDDQGFVQIQGRA 613
Cdd:pfam00501 340 GTEVKIVDDETgepVPPGepGELCVRGPGVMKGYLN--DP---EL-TAEAF---DEDGWYRTGDLGRRDEDGYLEIVGRK 410
|
.
gi 1937565178 614 K 614
Cdd:pfam00501 411 K 411
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
253-701 |
1.02e-63 |
|
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: 219.36 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 253 KQGEKIGLMLPNAGISAAVIFGAVSRGRIPAmmnytagvkglssaitaaQINTIFTSRQfldkgklwhLPEQLT--QVRW 330
Cdd:cd05936 47 QPGDRVALMLPNCPQFPIAYFGALKAGAVVV------------------PLNPLYTPRE---------LEHILNdsGAKA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 331 VFledlkADVTtadklwiFAHLL---MPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIA--DFTA 405
Cdd:cd05936 100 LI-----VAVS-------FTDLLaagAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 406 NDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVyDRNCTVLFGTSTFLGNYARFANP--YDFFRVRY 483
Cdd:cd05936 168 DDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIR-KHRVTIFPGVPTMYIALLNAPEFkkRDFSSLRL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 484 VVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSIN-VPMAAKPGTVGRILPGLDARLLAVPGIE--DG--GRLQL 558
Cdd:cd05936 247 CISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNpLDGPRKPGSIGIPLPGTEVKIVDDDGEElpPGevGELWV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 559 KGPNVMNGYLRveNPgvlEApTAenvngEVET-GWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVS 637
Cdd:cd05936 327 RGPQVMKGYWN--RP---EE-TA-----EAFVdGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHP 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 638 AEKMHATVVKSDASKGEALVLFTT---DGELKRDALLRYAREHgipeLA---VPRDIRYLKQLPVLGSGK 701
Cdd:cd05936 396 AVAEAAVVGVPDPYSGEAVKAFVVlkeGASLTEEEIIAFCREQ----LAgykVPRQVEFRDELPKSAVGK 461
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
197-710 |
8.87e-58 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 205.05 E-value: 8.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 197 RMAVRPRETLYESLLSAQYRYGAKKNCVeDINFTPDTYRKLLTKTLFVGRILEKYSkqGEKIGLMLPNAGISAAVIFGAV 276
Cdd:PRK06334 12 RGKLRSGKTVLESFLKLCSEMTTATVCW-DEQLGKLSYNQVRKAVIALATKVSKYP--DQHIGIMMPASAGAYIAYFATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 277 SRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDK-----GKLWHLPEQLtqvrwVFLEDLKADVTTADKLWIFAH 351
Cdd:PRK06334 89 LSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHlaqthGEDAEYPFSL-----IYMEEVRKELSFWEKCRIGIY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 352 LLMPRQAQVK------QQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGL-TVG 424
Cdd:PRK06334 164 MSIPFEWLMRwfgvsdKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 425 LFtPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYD--FFRVRYVVAGAEKLQDSTRQIWQDK 502
Cdd:PRK06334 244 LF-PLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQEscLPSLRFVVIGGDAFKDSLYQEALKT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 503 F-GLRILEGYGVTECAPVVSINVPMAAKPGT-VGRILPGLDARLLA----VPgIEDG--GRLQLKGPNVMNGYLRvENPG 574
Cdd:PRK06334 323 FpHIQLRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIVSeetkVP-VSSGetGLVLTRGTSLFSGYLG-EDFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 575 vleaptaenvNGEVETG---WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLA----TAVSAEKMHATVVK 647
Cdd:PRK06334 401 ----------QGFVELGgetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILmegfGQNAADHAGPLVVC 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937565178 648 SDASKGEALVLFTTDG-----------ELKRDALLRYAREHgipelavprdirYLKQLPVLGSGKPDFVTLKGM 710
Cdd:PRK06334 471 GLPGEKVRLCLFTTFPtsisevndilkNSKTSSILKISYHH------------QVESIPMLGTGKPDYCSLNAL 532
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
205-701 |
1.55e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 200.90 E-value: 1.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 205 TLYESLLSAQYRYGAKKNCVEDINFTpdTYRKLLTKTLFVGRILEKYS-KQGEKIGLMLPNAG--ISAAviFGAVSRGRI 281
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRL--TYAELNARVRRAAAALAALGiGKGDRVAIWAPNSPhwVIAA--LGALKAGAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 282 PAMMN--YTA----------GVKGlssaitaaqintIFTSRQFLdkGKLWHLPEQLTQVRWVFLEDLKADVTTADKLWIF 349
Cdd:PRK07656 82 VVPLNtrYTAdeaayilargDAKA------------LFVLGLFL--GVDYSATTRLPALEHVVICETEEDDPHTEKMKTF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 350 AHLL---MPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLF 426
Cdd:PRK07656 148 TDFLaagDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 427 TPLLTGAEVFLYP--SPLHyriVPELVYDRNCTVLFGTST---FLGNYARfANPYDFFRVRYVVAGAEKLQDSTRQIWQD 501
Cdd:PRK07656 228 APLMRGATILPLPvfDPDE---VFRLIETERITVLPGPPTmynSLLQHPD-RSAEDLSSLRLAVTGAASMPVALLERFES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 502 KFGLR-ILEGYGVTECAPVVSINVP---MAAKPGTVGRILPGLDARLLAVPGIEDG----GRLQLKGPNVMNGYLRvenp 573
Cdd:PRK07656 304 ELGVDiVLTGYGLSEASGVTTFNRLdddRKTVAGTIGTAIAGVENKIVNELGEEVPvgevGELLVRGPNVMKGYYD---- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 574 gvLEAPTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlatAVSAEkmHATVVKS----- 648
Cdd:PRK07656 380 --DPEATAAAIDAD---GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVE----EVLYE--HPAVAEAavigv 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 649 -DASKGE---ALVLFTTDGELKRDALLRYAREHgipeLA---VPRDIRYLKQLPVLGSGK 701
Cdd:PRK07656 449 pDERLGEvgkAYVVLKPGAELTEEELIAYCREH----LAkykVPRSIEFLDELPKNATGK 504
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
321-708 |
1.80e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 195.41 E-value: 1.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 321 LPEQLTQVR-WVFLEDlkADVTTADKLWIFAHLLMPRQAQVKQQP---EDD-AIILFTSGSEGNPKGVVHSHKSILANVE 395
Cdd:PRK06187 120 ILPQLPTVRtVIVEGD--GPAAPLAPEVGEYEELLAAASDTFDFPdidENDaAAMLYTSGTTGHPKGVVLSHRNLFLHSL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 396 QIKTIADFTANDRFMSALPLFHSFGLTVGlFTPLLTGAEVfLYPSPLHYRIVPELVYDRNCTVLFGTST---FLGNYARf 472
Cdd:PRK06187 198 AVCAWLKLSRDDVYLVIVPMFHVHAWGLP-YLALMAGAKQ-VIPRRFDPENLLDLIETERVTFFFAVPTiwqMLLKAPR- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 473 ANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVP------MAAKPGTVGRILPGLDARLL- 545
Cdd:PRK06187 275 AYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPedqlpgQWTKRRSAGRPLPGVEARIVd 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 546 ----AVP-GIEDGGRLQLKGPNVMNGYLRvenpgvLEAPTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA 620
Cdd:PRK06187 355 ddgdELPpDGGEVGEIIVRGPWLMQGYWN------RPEATAETIDG----GWLHTGDVGYIDEDGYLYITDRIKDVIISG 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 621 GEMV-SLEMVETLAT--AVsAEkmhATVV-KSDASKGE---ALVLFTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQ 693
Cdd:PRK06187 425 GENIyPRELEDALYGhpAV-AE---VAVIgVPDEKWGErpvAVVVLKPGATLDAKELRAFLRGR-LAKFKLPKRIAFVDE 499
|
410
....*....|....*
gi 1937565178 694 LPVLGSGKPDFVTLK 708
Cdd:PRK06187 500 LPRTSVGKILKRVLR 514
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
364-681 |
2.85e-50 |
|
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: 182.02 E-value: 2.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSP-- 441
Cdd:cd05907 86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAet 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 -------LHYRI---VP---ELVYDRNCTVLfgTSTFLGNYARFANpydFFRVRYVVAGAEKLQDSTRQIWQdKFGLRIL 508
Cdd:cd05907 166 llddlseVRPTVflaVPrvwEKVYAAIKVKA--VPGLKRKLFDLAV---GGRLRFAASGGAPLPAELLHFFR-ALGIPVY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 509 EGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARllavpgIEDGGRLQLKGPNVMNGYLRveNPgvleAPTAENVngeV 588
Cdd:cd05907 240 EGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVR------IADDGEILVRGPNVMLGYYK--NP----EATAEAL---D 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 589 ETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA-GEMVSLEMVETLAT---AVSaekmHATVVKSDASKGEALVlfttdgE 664
Cdd:cd05907 305 ADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKaspLIS----QAVVIGDGRPFLVALI------V 374
|
330
....*....|....*..
gi 1937565178 665 LKRDALLRYAREHGIPE 681
Cdd:cd05907 375 PDPEALEAWAEEHGIAY 391
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
224-701 |
1.95e-49 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 180.49 E-value: 1.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 224 VEDINFTPDTYRKLLTKTLFVGRILEKY-SKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQ 302
Cdd:cd05911 3 IDADTGKELTYAQLRTLSRRLAAGLRKLgLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 303 INTIFTSRQFLDK----GKLWHlpeqlTQVRWVFLEDLKADVTTADKLW-IFAHLLMPRQAQVKQQPEDD-AIILFTSGS 376
Cdd:cd05911 83 PKVIFTDPDGLEKvkeaAKELG-----PKDKIIVLDDKPDGVLSIEDLLsPTLGEEDEDLPPPLKDGKDDtAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 377 EGNPKGVVHSHKSILANVEQIKTI--ADFTANDRFMSALPLFHSFGLTVGLFTPLLtGAEVFLYPSPlHYRIVPELVYDR 454
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFlyGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKF-DSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 455 NCTVLFGTST---FLGNYARFaNPYDFFRVRYVVAGA----EKLQDSTRQIWQDKfglRILEGYGVTECAPVVSINVPMA 527
Cdd:cd05911 236 KITFLYLVPPiaaALAKSPLL-DKYDLSSLRVILSGGaplsKELQELLAKRFPNA---TIKQGYGMTETGGILTVNPDGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 528 AKPGTVGRILPGLDARLLAVPGIEDGGR-----LQLKGPNVMNGYLRveNPgvlEApTAENVngeVETGWYDTGDIVRFD 602
Cdd:cd05911 312 DKPGSVGRLLPNVEAKIVDDDGKDSLGPnepgeICVRGPQVMKGYYN--NP---EA-TKETF---DEDGWLHTGDIGYFD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 603 DQGFVQIQGRAKRFAKIAGEMVS---LEMVetLAT--------------AVSAEKMHATVVKSDASKgealvlfTTDGEL 665
Cdd:cd05911 383 EDGYLYIVDRKKELIKYKGFQVApaeLEAV--LLEhpgvadaavigipdEVSGELPRAYVVRKPGEK-------LTEKEV 453
|
490 500 510
....*....|....*....|....*....|....*....
gi 1937565178 666 KR---DALLRYAREHGipelavprDIRYLKQLPVLGSGK 701
Cdd:cd05911 454 KDyvaKKVASYKQLRG--------GVVFVDEIPKSASGK 484
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
366-695 |
1.69e-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: 174.02 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 366 DDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsPLHYR 445
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP-KFDPK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 446 IVPELVYDRNCTVLFGTSTFlgnYARFANPYDFF-------------RVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYG 512
Cdd:cd05941 169 EVAISRLMPSITVFMGVPTI---YTRLLQYYEAHftdpqfaraaaaeRLRLMVSGSAALPVPTLEEWEAITGHTLLERYG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 513 VTECapVVSINVPMAA--KPGTVGRILPGLDARLL----AVPGIEDG-GRLQLKGPNVMNGYLRveNPgvlEApTAENVn 585
Cdd:cd05941 246 MTEI--GMALSNPLDGerRPGTVGMPLPGVQARIVdeetGEPLPRGEvGEIQVRGPSVFKEYWN--KP---EA-TKEEF- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 586 geVETGWYDTGDIVRFDDQGFVQIQGRAK-RFAKIAGEMVS-LEMVETLAT-------AVSA-------EKMHATVVKSD 649
Cdd:cd05941 317 --TDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSaLEIERVLLAhpgvsecAVIGvpdpdwgERVVAVVVLRA 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1937565178 650 AskGEALVLfttdgelkrDALLRYAREHGIPeLAVPRDIRYLKQLP 695
Cdd:cd05941 395 G--AAALSL---------EELKEWAKQRLAP-YKRPRRLILVDELP 428
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
253-680 |
2.22e-46 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 174.52 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 253 KQGEKIGLMLPN--------AGISAAvifGAVSrgripammnytagVkGLSSAITAAQI---------NTIFTSRQF-LD 314
Cdd:COG1022 63 KPGDRVAILSDNrpewviadLAILAA---GAVT-------------V-PIYPTSSAEEVayilndsgaKVLFVEDQEqLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 315 KgkLWHLPEQLTQVRWVFLEDLKA-----DVTTADKL------WIFAHLLMPRQAQVKqqPEDDAIILFTSGSEGNPKGV 383
Cdd:COG1022 126 K--LLEVRDELPSLRHIVVLDPRGlrddpRLLSLDELlalgreVADPAELEARRAAVK--PDDLATIIYTSGTTGRPKGV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 384 VHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTpLLTGAEVFLYPSP------L-----HYRI-VP--- 448
Cdd:COG1022 202 MLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAESPdtlaedLrevkpTFMLaVPrvw 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 449 ELVYDR--------------------------NCTVLFGTSTFLGNYARFAnpydFF--------------RVRYVVAGA 488
Cdd:COG1022 281 EKVYAGiqakaeeagglkrklfrwalavgrryARARLAGKSPSLLLRLKHA----LAdklvfsklrealggRLRFAVSGG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 489 EKLQDSTrqiwqDKF----GLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARllavpgIEDGGRLQLKGPNVM 564
Cdd:COG1022 357 AALGPEL-----ARFfralGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVK------IAEDGEILVRGPNVM 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 565 NGYLRveNPgvlEApTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA-GEMVSLEMVETLATA---VSaek 640
Cdd:COG1022 426 KGYYK--NP---EA-TAEAFDAD---GWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKAsplIE--- 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1937565178 641 mHATVVksdaskGE------ALVlfttdgELKRDALLRYAREHGIP 680
Cdd:COG1022 494 -QAVVV------GDgrpflaALI------VPDFEALGEWAEENGLP 526
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
364-703 |
2.80e-46 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 168.43 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPSPLH 443
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHV-VLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 444 YR---IVPE---LVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECA 517
Cdd:cd05944 80 YRnpgLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 518 PVVSINVP-MAAKPGTVGRILPGLDARLLavpgIEDG-GRLQLK--GPNVMNGYlrVENPGVLEAPTAE--NVNGEVETG 591
Cdd:cd05944 160 CLVAVNPPdGPKRPGSVGLRLPYARVRIK----VLDGvGRLLRDcaPDEVGEIC--VAGPGVFGGYLYTegNKNAFVADG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 592 WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELKRD 668
Cdd:cd05944 234 WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGElpvAYVQLKPGAVVEEE 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 1937565178 669 ALLRYAREHgIPE-LAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd05944 314 ELLAWARDH-VPErAAVPKHIEVLEELPVTAVGKVF 348
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
365-701 |
5.96e-46 |
|
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: 169.71 E-value: 5.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSILANVeqIKTIADFTAN--DRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPl 442
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNA--VNALAALDLGpdDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKF- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 443 hyriVPELVYDR----NCTVLFGTST---FLGNYARFANpYDFFRVRYVVAGAEKLQDSTRQIWQDkFGLRILEGYGVTE 515
Cdd:cd17631 175 ----DPETVLDLierhRVTSFFLVPTmiqALLQHPRFAT-TDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 516 CAPVVSINVP--MAAKPGTVGRILPGLDARLLAvpgiEDG--------GRLQLKGPNVMNGYLRvenpgvLEAPTAENVN 585
Cdd:cd17631 249 TSPGVTFLSPedHRRKLGSAGRPVFFVEVRIVD----PDGrevppgevGEIVVRGPHVMAGYWN------RPEATAAAFR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 586 GevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTD 662
Cdd:cd17631 319 D----GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEavvAVVVPRPG 394
|
330 340 350
....*....|....*....|....*....|....*....
gi 1937565178 663 GELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd17631 395 AELDEDELIAHCRER-LARYKIPKSVEFVDALPRNATGK 432
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-708 |
6.09e-46 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 170.31 E-value: 6.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 255 GEKIGLMLPN----AGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFtsrqfLDKGKLWHLPEQLTQVR- 329
Cdd:cd05922 18 GERVVLILPNrftyIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVL-----ADAGAADRLRDALPASPd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 330 ---WVFLEDLKADVTTADklwifAHLLmprqaqvkqQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTAN 406
Cdd:cd05922 93 pgtVLDADGIRAARASAP-----AHEV---------SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 407 DRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFA-NPYDFFRVRYVV 485
Cdd:cd05922 159 DRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGfDPAKLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 486 AGAEKLQDSTRQIWQDKF-GLRILEGYGVTECAPVVSINVP--MAAKPGTVGRILPGL------DARLLAVPGIEdgGRL 556
Cdd:cd05922 238 QAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPerILEKPGSIGLAIPGGefeildDDGTPTPPGEP--GEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 557 QLKGPNVMNGYLRvenpgvleAPTAENVNGEVETGWYdTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAv 636
Cdd:cd05922 316 VHRGPNVMKGYWN--------DPPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS- 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937565178 637 SAEKMHATVVKSDASKGEALVLFTT-DGELKRDALLRYAREHGiPELAVPRDIRYLKQLPVLGSGKPDFVTLK 708
Cdd:cd05922 386 IGLIIEAAAVGLPDPLGEKLALFVTaPDKIDPKDVLRSLAERL-PPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
253-701 |
5.66e-44 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 166.83 E-value: 5.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 253 KQGEKIGLMLPNagISAAVIF-------GAVSrgrIPAMMNYTAgvKGLSSAITAAQINTIFTSRQFLDKGKLWHLPEQL 325
Cdd:COG0365 62 KKGDRVAIYLPN--IPEAVIAmlacariGAVH---SPVFPGFGA--EALADRIEDAEAKVLITADGGLRGGKVIDLKEKV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 326 TQVR--------WVFLEDLKADVTTADKLWIfaHLLMPRQAQ----VKQQPEDDAIILFTSGSEGNPKGVVHSHKSILAN 393
Cdd:COG0365 135 DEALeelpslehVIVVGRTGADVPMEGDLDW--DELLAAASAefepEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 394 VE-QIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY---PSPLHYRIVPELVYDRNCTVLFGTST----F 465
Cdd:COG0365 213 AAtTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYegrPDFPDPGRLWELIEKYGVTVFFTAPTairaL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 466 LGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTE-CAPVVSINVPMAAKPGTVGRILPGLDARL 544
Cdd:COG0365 293 MKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTEtGGIFISNLPGLPVKPGSMGKPVPGYDVAV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 545 LAvpgiEDG--------GRLQLKG--PNVMNGYLRveNPgvlEApTAENVNGEVEtGWYDTGDIVRFDDQGFVQIQGRAK 614
Cdd:COG0365 373 VD----EDGnpvppgeeGELVIKGpwPGMFRGYWN--DP---ER-YRETYFGRFP-GWYRTGDGARRDEDGYFWILGRSD 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 615 RFAKIAGEMVS-LEMVETLAT--AVsAEkmhATVV-KSDASKGEALVLF-------TTDGELKRDaLLRYAREHgIPELA 683
Cdd:COG0365 442 DVINVSGHRIGtAEIESALVShpAV-AE---AAVVgVPDEIRGQVVKAFvvlkpgvEPSDELAKE-LQAHVREE-LGPYA 515
|
490
....*....|....*...
gi 1937565178 684 VPRDIRYLKQLPVLGSGK 701
Cdd:COG0365 516 YPREIEFVDELPKTRSGK 533
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
363-701 |
7.69e-44 |
|
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: 165.23 E-value: 7.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQ-IKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSp 441
Cdd:cd05959 161 HADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELyARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPE- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 lhyRIVPELVYDR----NCTVLFGTSTFLGNYARFANP--YDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTE 515
Cdd:cd05959 240 ---RPTPAAVFKRirryRPTVFFGVPTLYAAMLAAPNLpsRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 516 CAPVVSINVPMAAKPGTVGRILPGLDARLLAVPG--IEDG--GRLQLKGPNVMNGYLrvENPgvleAPTAENVNGEvetg 591
Cdd:cd05959 317 MLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGgdVADGepGELYVRGPSSATMYW--NNR----DKTRDTFQGE---- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 592 WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVS-LEMVETLAT--AVsaekMHATVVKSDASKG----EALVLF---TT 661
Cdd:cd05959 387 WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSpFEVESALVQhpAV----LEAAVVGVEDEDGltkpKAFVVLrpgYE 462
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1937565178 662 DGELKRDALLRYAREhGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05959 463 DSEALEEELKEFVKD-RLAPYKYPRWIVFVDELPKTATGK 501
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
233-708 |
9.25e-43 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 164.36 E-value: 9.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLL-----TKTLF----VGRilekyskqGEKIGLMLPNAGISAAVIFGAVSRGrIPAMMNYTAGVKGLSSAITAAQI 303
Cdd:PRK07529 60 TYAELLadvtrTANLLhslgVGP--------GDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 304 NTIFTSRQFLDKG---KLWHLPEQLTQVRWVFLEDLkADVTTADKLWIFAHLLMPRQAQV-------KQQPEDDAII--- 370
Cdd:PRK07529 131 KVLVTLGPFPGTDiwqKVAEVLAALPELRTVVEVDL-ARYLPGPKRLAVPLIRRKAHARIldfdaelARQPGDRLFSgrp 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 371 --------LF-TSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLyPSP 441
Cdd:PRK07529 210 igpddvaaYFhTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVL-ATP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 LHYRivPELVYDR--------NCTVLFGTSTFLGNYA-RFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYG 512
Cdd:PRK07529 289 QGYR--GPGVIANfwkiveryRINFLSGVPTVYAALLqVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 513 VTECAPVVSINVPMAA-KPGTVGRILPGLDARllAVPGIEDG-----------GRLQLKGPNVMNGYLRVENpgvleapt 580
Cdd:PRK07529 367 LTEATCVSSVNPPDGErRIGSVGLRLPYQRVR--VVILDDAGrylrdcavdevGVLCIAGPNVFSGYLEAAH-------- 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 581 aeNVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVE-TLAT--AVSAEkmhATVVKSDASKGEALV 657
Cdd:PRK07529 437 --NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEeALLRhpAVALA---AAVGRPDAHAGELPV 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937565178 658 LFTtdgELKRDA------LLRYAREHgIPE-LAVPRDIRYLKQLPVLGSGKPDFVTLK 708
Cdd:PRK07529 512 AYV---QLKPGAsateaeLLAFARDH-IAErAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
229-701 |
1.30e-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: 160.32 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 229 FTPD---TYRKLLTKTLFVGRILEKYSKQ-GEKIGLMLPNAGISAAVIFGAVSRGRIPAMmnytagvkglssaitaaqIN 304
Cdd:cd05919 5 YAADrsvTYGQLHDGANRLGSALRNLGVSsGDRVLLLMLDSPELVQLFLGCLARGAIAVV------------------IN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 305 TIFTSRQFLDKGklwhlpeQLTQVRWVFLEDlkadvttadklwifahllmprqaqvkqqpEDDAIILFTSGSEGNPKGVV 384
Cdd:cd05919 67 PLLHPDDYAYIA-------RDCEARLVVTSA-----------------------------DDIAYLLYSSGTTGPPKGVM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 385 HSHKSILANVEQI-KTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTS 463
Cdd:cd05919 111 HAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 464 TFLGNYARFAN--PYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLD 541
Cdd:cd05919 191 TFYANLLDSCAgsPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 542 ARLLAVPG--IEDG--GRLQLKGPNVMNGYLRveNPGVLEAPTAEnvngevetGWYDTGDIVRFDDQGFVQIQGRAKRFA 617
Cdd:cd05919 271 IRLVDEEGhtIPPGeeGDLLVRGPSAAVGYWN--NPEKSRATFNG--------GWYRTGDKFCRDADGWYTHAGRADDML 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 618 KIAGEMVSLEMVETLATAVSAeKMHATVV----KSDASKGEALVL----FTTDGELKRDaLLRYAREHgIPELAVPRDIR 689
Cdd:cd05919 341 KVGGQWVSPVEVESLIIQHPA-VAEAAVVavpeSTGLSRLTAFVVlkspAAPQESLARD-IHRHLLER-LSAHKVPRRIA 417
|
490
....*....|..
gi 1937565178 690 YLKQLPVLGSGK 701
Cdd:cd05919 418 FVDELPRTATGK 429
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
254-614 |
3.77e-40 |
|
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: 154.70 E-value: 3.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 254 QGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKgklwhLPEQLTQVrwVFL 333
Cdd:cd05904 56 KGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEK-----LASLALPV--VLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 334 EDLKADVTTADKLWIFAHLLMPRQAQVKQqpEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIAD--FTANDRFMS 411
Cdd:cd05904 129 DSAEFDSLSFSDLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLC 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 412 ALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyrivpelvydrnctvlFGTSTFLGNYARF------------------- 472
Cdd:cd05904 207 VLPMFHIYGLSSFALGLLRLGATVVVMPR-------------------FDLEELLAAIERYkvthlpvvppivlalvksp 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 473 -ANPYDFFRVRYVVAGAEKLQDSTRQIWQDKF-GLRILEGYGVTECAPVVSINVP---MAAKPGTVGRILPGLDARLLav 547
Cdd:cd05904 268 iVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIV-- 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 548 pGIEDG--------GRLQLKGPNVMNGYLRveNPgvlEApTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAK 614
Cdd:cd05904 346 -DPETGeslppnqtGELWIRGPSIMKGYLN--NP---EA-TAATIDKE---GWLHTGDLCYIDEDGYLFIVDRLK 410
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
364-701 |
5.88e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 155.16 E-value: 5.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQ----IKTIADftANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkawVPGLGD--GPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPlhyriVPELVYD----RNCTVLFGTSTFLGNYARFA--NPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGV 513
Cdd:PRK05605 296 AP-----DIDLILDamkkHPPTWLPGVPPLYEKIAEAAeeRGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 514 TECAPVVSINvPMAA--KPGTVGRILPGLDARL-----LAV---PGIEdgGRLQLKGPNVMNGYLRVEnpgvlEApTAEN 583
Cdd:PRK05605 371 TETSPIIVGN-PMSDdrRPGYVGVPFPDTEVRIvdpedPDEtmpDGEE--GELLVRGPQVFKGYWNRP-----EE-TAKS 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 584 VNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVS-LEMVETLATAVSAEKmhATVV---KSDASKG-EALVL 658
Cdd:PRK05605 442 FLD----GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYpAEVEEVLREHPGVED--AAVVglpREDGSEEvVAAVV 515
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1937565178 659 FTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK05605 516 LEPGAALDPEGLRAYCREH-LTRYKVPRRFYHVDELPRDQLGK 557
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
364-614 |
6.87e-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: 152.98 E-value: 6.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY---PS 440
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLdkiPS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 441 PL-----HYRI-------VPELVYDRNCTVLFGTSTFLGNYARFANP--------------YDFF--RVRYVVAGAEKLq 492
Cdd:cd05914 168 AKiialaFAQVtptlgvpVPLVIEKIFKMDIIPKLTLKKFKFKLAKKinnrkirklafkkvHEAFggNIKEFVIGGAKI- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 493 dsTRQIWQD--KFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAVPGIEDGGRLQLKGPNVMNGYLRv 570
Cdd:cd05914 247 --NPDVEEFlrTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYK- 323
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1937565178 571 eNPgvlEApTAENVNgevETGWYDTGDIVRFDDQGFVQIQGRAK 614
Cdd:cd05914 324 -NP---EA-TAEAFD---KDGWFHTGDLGKIDAEGYLYIRGRKK 359
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
363-703 |
3.17e-39 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 150.76 E-value: 3.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSP 441
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSF--SFDVSVWeIFGALLAGATLVVLPEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 LHYRI--VPELVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKF-GLRILEGYGVTECAP 518
Cdd:cd05930 169 VRKDPeaLADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 519 VVSINV--PMAAKPGTV--GRILPG-----LDARLLAVP-GIEdgGRLQLKGPNVMNGYLRvenpgvLEAPTAE--NVNG 586
Cdd:cd05930 249 DATYYRvpPDDEEDGRVpiGRPIPNtrvyvLDENLRPVPpGVP--GELYIGGAGLARGYLN------RPELTAErfVPNP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 587 EVETGW-YDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTT---D 662
Cdd:cd05930 321 FGPGERmYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVpdeG 400
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1937565178 663 GELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd05930 401 GELDEEELRAHLAER-LPDYMVPSAFVVLDALPLTPNGKVD 440
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
233-703 |
5.58e-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: 148.23 E-value: 5.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTL-FVGRILEKYSKQGEKIGLMLPNaGISAAVIFGAVSRGR-IPAMMN----------YTAGVK-------- 292
Cdd:cd05926 16 TYADLAELVDdLARQLAALGIKKGDRVAIALPN-GLEFVVAFLAAARAGaVVAPLNpaykkaefefYLADLGsklvltpk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 293 -GLSSAITAAQINTIFTSRQFLDKGKLWHLP--EQLTqvrwvFLEDLKADVTTADKlwifahllmprqaqvkQQPEDDAI 369
Cdd:cd05926 95 gELGPASRAASKLGLAILELALDVGVLIRAPsaESLS-----NLLADKKNAKSEGV----------------PLPDDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 370 ILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyrivpe 449
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPR--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 450 lvydrnctvlFGTSTFLGNYARF--------------------ANPYD-FFRVRYVVAGAEKLQDSTRQIWQDKFGLRIL 508
Cdd:cd05926 225 ----------FSASTFWPDVRDYnatwytavptihqillnrpePNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 509 EGYGVTECAPVVSIN--VPMAAKPGTVG-------RILPglDARLLAVPGIEdgGRLQLKGPNVMNGYLrvenpgvlEAP 579
Cdd:cd05926 295 EAYGMTEAAHQMTSNplPPGPRKPGSVGkpvgvevRILD--EDGEILPPGVV--GEICLRGPNVTRGYL--------NNP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 580 TAENVNGEVEtGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLF 659
Cdd:cd05926 363 EANAEAAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1937565178 660 TT---DGELKRDALLRYAREHgipeLA---VPRDIRYLKQLPVLGSGKPD 703
Cdd:cd05926 442 VVlreGASVTEEELRAFCRKH----LAafkVPKKVYFVDELPKTATGKIQ 487
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
366-701 |
7.61e-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: 144.34 E-value: 7.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 366 DDAI-ILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPSP-LH 443
Cdd:cd05917 2 DDVInIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATM-VFPSPsFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 444 YRIVPELVYDRNCTVLFGTST-FLG--NYARFANpYDFFRVRY-VVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPV 519
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTmFIAelEHPDFDK-FDLSSLRTgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 520 V---SINVPMAAKPGTVGRILPGLDARLL-----AVPGIEDGGRLQLKGPNVMNGYLrvENPgvleAPTAENVNGEvetG 591
Cdd:cd05917 160 StqtRTDDSIEKRVNTVGRIMPHTEAKIVdpeggIVPPVGVPGELCIRGYSVMKGYW--NDP----EKTAEAIDGD---G 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 592 WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVS-LEMVETLATAVSAEKMHATVVKsDASKGE---ALVLFTTDGELKR 667
Cdd:cd05917 231 WLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYpREIEEFLHTHPKVSDVQVVGVP-DERYGEevcAWIRLKEGAELTE 309
|
330 340 350
....*....|....*....|....*....|....
gi 1937565178 668 DALLRYAREhGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05917 310 EDIKAYCKG-KIAHYKVPRYVFFVDEFPLTVSGK 342
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
356-701 |
9.95e-37 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 145.58 E-value: 9.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 356 RQAQVKQQ--PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDR---FMSALPLFHSFGLTVG--LFTP 428
Cdd:PRK08974 195 RMQYVKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGkelVVTALPLYHIFALTVNclLFIE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 429 LltGAEVFLYPSPlhyRIVPELVYDRN---CTVLFGTSTF---LGNYARFANpYDFFRVRYVVAGAEKLQDSTRQIWQDK 502
Cdd:PRK08974 275 L--GGQNLLITNP---RDIPGFVKELKkypFTAITGVNTLfnaLLNNEEFQE-LDFSSLKLSVGGGMAVQQAVAERWVKL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 503 FGLRILEGYGVTECAPVVSIN-VPMAAKPGTVGRILPGLDARLL----AVPGIEDGGRLQLKGPNVMNGYLrvENPgvlE 577
Cdd:PRK08974 349 TGQYLLEGYGLTECSPLVSVNpYDLDYYSGSIGLPVPSTEIKLVdddgNEVPPGEPGELWVKGPQVMLGYW--QRP---E 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 578 ApTAEnvngEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAG---------EMVSL--EMVETLA----TAVSAEKMH 642
Cdd:PRK08974 424 A-TDE----VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGfnvypneieDVVMLhpKVLEVAAvgvpSEVSGEAVK 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937565178 643 ATVVKSDASkgealvlfttdgeLKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK08974 499 IFVVKKDPS-------------LTEEELITHCRRH-LTGYKVPKLVEFRDELPKSNVGK 543
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
361-701 |
2.35e-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: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 361 KQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFM-SALPLFHSfGLTVGLFTPLLTGAEVFLYP 439
Cdd:cd05969 85 RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWcTADPGWVT-GTVYGIWAPWLNGVTNVVYE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPLHYRIVPELVYDRNCTVLFGTST----FLGNYARFANPYDFFRVRYVVAGAEKLqDSTRQIW-QDKFGLRILEGYGVT 514
Cdd:cd05969 164 GRFDAESWYGIIERVKVTVWYTAPTairmLMKEGDELARKYDLSSLRFIHSVGEPL-NPEAIRWgMEVFGVPIHDTWWQT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 515 ECAPVVSINVP-MAAKPGTVGRILPGLDARLLAVPG--IEDG--GRLQLKG--PNVMNGYLRVEnpgvleaptaENVNGE 587
Cdd:cd05969 243 ETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVDENGneLPPGtkGILALKPgwPSMFRGIWNDE----------ERYKNS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 588 VETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTT------ 661
Cdd:cd05969 313 FIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfe 392
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1937565178 662 -DGELKRDaLLRYAReHGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05969 393 pSDELKEE-IINFVR-QKLGAHVAPREIEFVDNLPKTRSGK 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
364-703 |
1.40e-35 |
|
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: 140.07 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFlypspl 442
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPF--SFDLSVmDLYPALASGATLV------ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 443 hyrIVPELVYD-----------RNCTVLFGTSTFL------GNYARFANPydffRVRYVVAGAEKLQDSTRQIWQDKF-G 504
Cdd:cd05945 168 ---PVPRDATAdpkqlfrflaeHGITVWVSTPSFAamcllsPTFTPESLP----SLRHFLFCGEVLPHKTARALQQRFpD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 505 LRILEGYGVTEC-APVVSINVP----MAAKPGTVGRILPGLDARLLAvpgiEDG--------GRLQLKGPNVMNGYLRVE 571
Cdd:cd05945 241 ARIYNTYGPTEAtVAVTYIEVTpevlDGYDRLPIGYAKPGAKLVILD----EDGrpvppgekGELVISGPSVSKGYLNNP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 572 NpgvleaPTAENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDAS 651
Cdd:cd05945 317 E------KTAAAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGE 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 652 KGEALVLFTTDGELKRDALLRYAREH---GIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd05945 391 KVTELIAFVVPKPGAEAGLTKAIKAElaeRLPPYMIPRRFVYLDELPLNANGKID 445
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
365-701 |
1.59e-35 |
|
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: 139.78 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhy 444
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGP--- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 445 RIVPELVYDR----NCTVLFGTSTFlgnYARFANP----YDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTEC 516
Cdd:cd05972 158 RFDAERILELleryGVTSFCGPPTA---YRMLIKQdlssYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 517 APVVSINVPMAAKPGTVGRILPGLDARLL------AVPGIEDGGRLQLKGPNVMNGYLRVenpgvlEAPTAENVNGevet 590
Cdd:cd05972 235 GLTVGNFPDMPVKPGSMGRPTPGYDVAIIdddgreLPPGEEGDIAIKLPPPGLFLGYVGD------PEKTEASIRG---- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 591 GWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFtTDGELKR 667
Cdd:cd05972 305 DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEvvkAFVVL-TSGYEPS 383
|
330 340 350
....*....|....*....|....*....|....*..
gi 1937565178 668 DALLRYAREHGIPELA---VPRDIRYLKQLPVLGSGK 701
Cdd:cd05972 384 EELAEELQGHVKKVLApykYPREIEFVEELPKTISGK 420
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
338-614 |
4.50e-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: 139.03 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 338 ADVTTADKLWIFAHLLmPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFH 417
Cdd:cd17640 62 SDSSVEELLYILNHSE-SVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 418 SFGLTVGLFTPLLTGAEVFLYPSPL---------HYRI-VPEL-------VYD------RNCTVLFGTSTFLGNyarfan 474
Cdd:cd17640 141 SYERSAEYFIFACGCSQAYTSIRTLkddlkrvkpHYIVsVPRLweslysgIQKqvskssPIKQFLFLFFLSGGI------ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 475 pydffrVRYVVAGAEKLQDSTrqiwqDKF----GLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAV--- 547
Cdd:cd17640 215 ------FKFGISGGGALPPHV-----DTFfeaiGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPegn 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937565178 548 ----PGIEdgGRLQLKGPNVMNGYLRveNPgvleAPTAENVNgevETGWYDTGDIVRFDDQGFVQIQGRAK 614
Cdd:cd17640 284 vvlpPGEK--GIVWVRGPQVMKGYYK--NP----EATSKVLD---SDGWFNTGDLGWLTCGGELVLTGRAK 343
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
356-701 |
4.64e-35 |
|
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: 138.67 E-value: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 356 RQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEV 435
Cdd:cd05903 84 RQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 FLYpSPLHYRIVPELVYDRNCTVLFGTSTFLG---NYARFANPyDFFRVR-YVVAGAEKLQDSTRQIWQdKFGLRILEGY 511
Cdd:cd05903 164 VLQ-DIWDPDKALALMREHGVTFMMGATPFLTdllNAVEEAGE-PLSRLRtFVCGGATVPRSLARRAAE-LLGAKVCSAY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 512 GVTECA-PVVSINVPMAAKP-GTVGRILPGL------DARLLAVPGIEdgGRLQLKGPNVMNGYLRvenpgvleapTAEN 583
Cdd:cd05903 241 GSTECPgAVTSITPAPEDRRlYTDGRPLPGVeikvvdDTGATLAPGVE--GELLSRGPSVFLGYLD----------RPDL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 584 VNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE--ALVLFTT 661
Cdd:cd05903 309 TADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGEraCAVVVTK 388
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1937565178 662 DG-ELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05903 389 SGaLLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGK 429
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
366-701 |
9.72e-35 |
|
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: 134.94 E-value: 9.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 366 DDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVflYP-SPLHY 444
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATV--VPvAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 445 RIVPELVYDRNCTVLFGTST----FLGNYARfaNPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLR-ILEGYGVTECapv 519
Cdd:cd17638 79 DAILEAIERERITVLPGPPTlfqsLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEA--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 520 vsiNVPMAAKPG--------TVGRILPGLDARllavpgIEDGGRLQLKGPNVMNGYLrvENPgvleAPTAENVNgevETG 591
Cdd:cd17638 154 ---GVATMCRPGddaetvatTCGRACPGFEVR------IADDGEVLVRGYNVMQGYL--DDP----EATAEAID---ADG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 592 WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELKRD 668
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEvgkAFVVARPGVTLTEE 295
|
330 340 350
....*....|....*....|....*....|...
gi 1937565178 669 ALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd17638 296 DVIAWCRER-LANYKVPRFVRFLDELPRNASGK 327
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
355-614 |
2.80e-34 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 137.31 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
Cdd:PRK07514 146 DDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGAS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 435 VFLYPsplhyRIVPELVYDR--NCTVLFGTSTFlgnYARF-ANPyDFFR-----VRYVVAGAEKLQDSTRQIWQDKFGLR 506
Cdd:PRK07514 226 MIFLP-----KFDPDAVLALmpRATVMMGVPTF---YTRLlQEP-RLTReaaahMRLFISGSAPLLAETHREFQERTGHA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 507 ILEGYGVTECAPVVSiNvPMAAK--PGTVGRILPGLDARllaVPGIEDG--------GRLQLKGPNVMNGYLRvenpgvl 576
Cdd:PRK07514 297 ILERYGMTETNMNTS-N-PYDGErrAGTVGFPLPGVSLR---VTDPETGaelppgeiGMIEVKGPNVFKGYWR------- 364
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1937565178 577 eAP--TAENVNgevETGWYDTGDIVRFDDQGFVQIQGRAK 614
Cdd:PRK07514 365 -MPekTAEEFR---ADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PlsC |
COG0204 |
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ... |
1-204 |
3.72e-34 |
|
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: 129.74 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 1 MLFGFFRTLFRVL-FRIRVTGDTQALYGERVLITPNHVSFLDGVLLALFLPVRPVFAVYSSISEKWYMRWLKPLIDFVPL 79
Cdd:COG0204 15 LVRLWARLLLRLLgVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKIPLLGWLLRALGAIPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 80 DPTKPM----MIKHLVRLIGQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSQATVVPLRIDGAELTFFsrlKGLVKQR 155
Cdd:COG0204 95 DRSKRRaalrALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGAARLALEAGVPIVPVAIDGTERALP---KGFLPRP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937565178 156 lfPKITLHILPPTSlpmPEAPRARDRRKIAgEMLHQIMMEARMAVRPRE 204
Cdd:COG0204 172 --GKVTVRIGPPID---PSDLEGEDRRELA-ERLRAAIEALLAELRAEA 214
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
365-701 |
4.71e-34 |
|
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: 135.30 E-value: 4.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSPLHY 444
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM-ARWDR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 445 RIVPELVYDRNCTVLFGTSTF---LGNYARFANpYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVS 521
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMlvdLLATPEFKT-RDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 522 INVPMAAKPGTVGRILPGLDARLLAvpgIEDG--------GRLQLKGPNVMNGYLRVENpgvleaptaENVNGEVETG-- 591
Cdd:cd05935 242 TNPPLRPKLQCLGIP*FGVDARVID---IETGrelppnevGEIVVRGPQIFKGYWNRPE---------ETEESFIEIKgr 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 592 -WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTD--GEL 665
Cdd:cd05935 310 rFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEevkAFIVLRPEyrGKV 389
|
330 340 350
....*....|....*....|....*....|....*.
gi 1937565178 666 KRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05935 390 TEEDIIEWAREQ-MAAYKYPREVEFVDELPRSASGK 424
|
|
| LPLAT_AGPAT-like |
cd07989 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ... |
6-188 |
5.62e-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: 128.16 E-value: 5.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 6 FRTLFRVL-FRIRVTGDTQALYGERVLITPNHVSFLDGVLLALFLPVRPVFAVYSSISEKWYMRWLKPLIDFVPLDPTKP 84
Cdd:cd07989 1 LRLLLRLLgVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 85 M----MIKHLVRLIGQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSQATVVPLRIDGAELTFFSRLKGlvkqRLFPKI 160
Cdd:cd07989 81 RsareALREAIEALKEGESVVIFPEGTRSRDGELLPFKSGAFRLAKEAGVPIVPVAISGTWGSLPKGKKL----PRPGRV 156
|
170 180
....*....|....*....|....*...
gi 1937565178 161 TLHILPPTSLPmPEAPRARDRRKIAGEM 188
Cdd:cd07989 157 TVRIGEPIPPE-GLELAEEDRKELREKV 183
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
364-681 |
1.66e-33 |
|
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: 135.04 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKT-IADF-TANDRFMSALPLFHSF-----------GLTVGLFTP-- 428
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrVPELlGPDDRYLAYLPLAHIFelaaenvclyrGGTIGYGSPrt 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 429 -------------------LLTG-AEVF----------LYPSPLHYRIVPELVYD-RNCTVLFGTSTFLGNYARFANPYD 477
Cdd:cd17639 167 ltdkskrgckgdltefkptLMVGvPAIWdtirkgvlakLNPMGGLKRTLFWTAYQsKLKALKEGPGTPLLDELVFKKVRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 478 FF--RVRYVVAGAEKLQDSTrQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAVPgiEDG-- 553
Cdd:cd17639 247 ALggRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWE--EGGys 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 554 -------GRLQLKGPNVMNGYLRveNPGVleapTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA-GEMVS 625
Cdd:cd17639 324 tdkppprGEILIRGPNVFKGYYK--NPEK----TKEAFDGD---GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIA 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 626 LEMVETLATAVSAEKMHATVVKSDASKGEALVLfTTDGELKrdallRYAREHGIPE 681
Cdd:cd17639 395 LEKLESIYRSNPLVNNICVYADPDKSYPVAIVV-PNEKHLT-----KLAEKHGVIN 444
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
368-708 |
2.23e-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: 130.91 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 368 AIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVgLFTPLLTGAEVFL---------- 437
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLlernqalaed 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 438 --YPSPLHYRIVP-ELVYdrnctVLfgtstflgnyARFANPYDFFRVRYVVAGAEKL-QDSTRQIwqDKFGLRILEGYGV 513
Cdd:cd17630 82 laPPGVTHVSLVPtQLQR-----LL----------DSGQGPAALKSLRAVLLGGAPIpPELLERA--ADRGIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 514 TECAPVVSINVPMAAKPGTVGRILPGldARLlavpGIEDGGRLQLKGPNVMNGYLRvenpGVLEAPTAENvngevetGWY 593
Cdd:cd17630 145 TETASQVATKRPDGFGRGGVGVLLPG--REL----RIVEDGEIWVGGASLAMGYLR----GQLVPEFNED-------GWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 594 DTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLF-TTDGELKRDALLR 672
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAViVGRGPADPAELRA 287
|
330 340 350
....*....|....*....|....*....|....*.
gi 1937565178 673 YAREHgIPELAVPRDIRYLKQLPVLGSGKPDFVTLK 708
Cdd:cd17630 288 WLKDK-LARFKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
357-638 |
1.07e-32 |
|
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: 130.85 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 357 QAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTV-GLFTPLLTGAEV 435
Cdd:TIGR01733 112 PPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASL--SFDASVeEIFGALLAGATL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 FLYPSPLHYRIVPE---LVYDRNCTVLFGTSTFLGNYARfANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFG-LRILEGY 511
Cdd:TIGR01733 190 VVPPEDEERDDAALlaaLIAEHPVTVLNLTPSLLALLAA-ALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 512 GVTECAPVVSINVPMAAKPG-----TVGRILPG-----LDARLLAVP-GIEdgGRLQLKGPNVMNGYLR---------VE 571
Cdd:TIGR01733 269 GPTETTVWSTATLVDPDDAPrespvPIGRPLANtrlyvLDDDLRPVPvGVV--GELYIGGPGVARGYLNrpeltaerfVP 346
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937565178 572 NPGVleaptaenvnGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSA 638
Cdd:TIGR01733 347 DPFA----------GGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPG 403
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
253-701 |
1.15e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 133.35 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 253 KQGEKIGLMLPNAGISAAVIFGAVSRGRIpammnytagvkglssaitAAQINTIFTSR----QFLDKG--------KLWH 320
Cdd:PRK05677 73 KPGDRIAVQLPNVLQYPVAVFGAMRAGLI------------------VVNTNPLYTARemehQFNDSGakalvclaNMAH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 321 LPEQL---TQVRWVFLEDLkadvttADKLWIFAHLLM-----------PR----QA----------------QVKQQPED 366
Cdd:PRK05677 135 LAEKVlpkTGVKHVIVTEV------ADMLPPLKRLLInavvkhvkkmvPAyhlpQAvkfndalakgagqpvtEANPQADD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 367 DAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTAND---RFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlh 443
Cdd:PRK05677 209 VAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNP-- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 444 yRIVPELVYD---RNCTVLFGTSTF---LGNYARFANpYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECA 517
Cdd:PRK05677 287 -RDLPAMVKElgkWKFSGFVGLNTLfvaLCNNEAFRK-LDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 518 PVVSINVPMAAKPGTVGRILPGLDARLLAVPGIE----DGGRLQLKGPNVMNGYLrvENPGVleapTAENVNGEvetGWY 593
Cdd:PRK05677 365 PVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNElplgEVGELCVKGPQVMKGYW--QRPEA----TDEILDSD---GWL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 594 DTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFT---TDGELKRDAL 670
Cdd:PRK05677 436 KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVvvkPGETLTKEQV 515
|
490 500 510
....*....|....*....|....*....|.
gi 1937565178 671 LRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK05677 516 MEHMRAN-LTGYKVPKAVEFRDELPTTNVGK 545
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
233-701 |
1.35e-32 |
|
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: 133.13 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRILEKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMM---NYTAGVKGLSSAITAAQINTIFTS 309
Cdd:cd05931 26 TYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGRHAERLAAILADAGPRVVLTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 310 RQFLDKGKLWHLPEQLTQVRWVFLEDLKADVTTADklWIFAHLlmprqaqvkqQPEDDAIILFTSGSEGNPKGVVHSHKS 389
Cdd:cd05931 106 AAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAAD--WPPPSP----------DPDDIAYLQYTSGSTGTPKGVVVTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 390 ILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAE-VFLypSPLHY----RIVPELVYDRNctvlfGTST 464
Cdd:cd05931 174 LLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPsVLM--SPAAFlrrpLRWLRLISRYR-----ATIS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 465 FLGNYA-----RFANP-----YDFFRVRYVVAGAEKLQDSTRQIWQDKF---GLR---ILEGYGVTEC----------AP 518
Cdd:cd05931 247 AAPNFAydlcvRRVRDedlegLDLSSWRVALNGAEPVRPATLRRFAEAFapfGFRpeaFRPSYGLAEAtlfvsggppgTG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 519 VVSINVPMAAKPGTV----------------GRILPGLDARLL-AVPGIE--DG--GRLQLKGPNVMNGYLRveNPGVLE 577
Cdd:cd05931 327 PVVLRVDRDALAGRAvavaaddpaarelvscGRPLPDQEVRIVdPETGRElpDGevGEIWVRGPSVASGYWG--RPEATA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 578 ApTAENVNGEVETGWYDTGDI-VRFDDQGFvqIQGRAKRFAKIAGEMVSLEMVE-TLATAVSAEKMHATVVKS-DASKGE 654
Cdd:cd05931 405 E-TFGALAATDEGGWLRTGDLgFLHDGELY--ITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPGCVAAFSvPDDGEE 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937565178 655 ALV----LFTTDGELKRDALL-----RYAREHGIPelavPRDIRYLKQ--LPVLGSGK 701
Cdd:cd05931 482 RLVvvaeVERGADPADLAAIAaairaAVAREHGVA----PADVVLVRPgsIPRTSSGK 535
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
306-701 |
1.42e-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: 132.37 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 306 IFTSRQFLDKgkLWHLPEQLTQVRWVFL--EDLKADVTTADKLWIFAHLLMpRQAQVKQQPEDD----AIILFTSGSEGN 379
Cdd:cd12119 101 VFVDRDFLPL--LEAIAPRLPTVEHVVVmtDDAAMPEPAGVGVLAYEELLA-AESPEYDWPDFDentaAAICYTSGTTGN 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 380 PKGVVHSHKSILANVEQIKTiADFTA---NDRFMSALPLFH--SFGLTvglFTPLLTGAEvFLYPSP-LHYRIVPELVYD 453
Cdd:cd12119 178 PKGVVYSHRSLVLHAMAALL-TDGLGlseSDVVLPVVPMFHvnAWGLP---YAAAMVGAK-LVLPGPyLDPASLAELIER 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 454 RNCTVLFGTSTF---LGNYARfANPYDFFRVRYVVAGAEKLQDSTRQIWQDKfGLRILEGYGVTECAPVVSINVPMAAKP 530
Cdd:cd12119 253 EGVTFAAGVPTVwqgLLDHLE-ANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPLGTVARPPSEHS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 531 G-----------TVGRILPGLDARLLAVPGIE---DG---GRLQLKGPNVMNGYLRveNPGVLEAPTAEnvngevetGWY 593
Cdd:cd12119 331 NlsedeqlalraKQGRPVPGVELRIVDDDGRElpwDGkavGELQVRGPWVTKSYYK--NDEESEALTED--------GWL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 594 DTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELKRDAL 670
Cdd:cd12119 401 RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErplAVVVLKEGATVTAEEL 480
|
410 420 430
....*....|....*....|....*....|.
gi 1937565178 671 LRYAREhGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd12119 481 LEFLAD-KVAKWWLPDDVVFVDEIPKTSTGK 510
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
363-703 |
2.20e-32 |
|
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: 130.89 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMsalpLFHS--FGLTV-GLFTPLLTGAEVFLYP 439
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSyaFDFSVwEIWGALLHGGRLVVVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 -----SPLHYRivpELVYDRNCTVLFGT-STFLGNY-ARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGL---RILE 509
Cdd:cd17643 167 yevarSPEDFA---RLLRDEGVTVLNQTpSAFYQLVeAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 510 GYGVTECAPVVSI------NVPMAAKpGTVGRILPG-----LDARLLAVPgieDG--GRLQLKGPNVMNGYLRveNPGVl 576
Cdd:cd17643 244 MYGITETTVHVTFrpldaaDLPAAAA-SPIGRPLPGlrvyvLDADGRPVP---PGvvGELYVSGAGVARGYLG--RPEL- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 577 eapTAE----NVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASK 652
Cdd:cd17643 317 ---TAErfvaNPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPG 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1937565178 653 GEALVLFTTDGELKRD---ALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17643 394 DTRLVAYVVADDGAAAdiaELRALLKEL-LPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
345-632 |
3.45e-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: 131.95 E-value: 3.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 345 KLWIFAHLL-MPRQAQVKQ---QPEDDAIILFTSGSEGNPKGVVHSHKSILANV----EQIKTIADFTANDRFMSALPLF 416
Cdd:cd05927 90 KVYSLEEFEkLGKKNKVPPpppKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 417 HSF-----------GLTVGLF---TPLLTGAEVFLYPS--PLhyriVPEL---VYDRNCTVLFGTST---FLGNYA---- 470
Cdd:cd05927 170 HIFervvealflyhGAKIGFYsgdIRLLLDDIKALKPTvfPG----VPRVlnrIYDKIFNKVQAKGPlkrKLFNFAlnyk 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 471 --------RFANPY-D--FF---------RVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKP 530
Cdd:cd05927 246 laelrsgvVRASPFwDklVFnkikqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 531 GTVGRILPGLDARLLAVP-------GIEDGGRLQLKGPNVMNGYLRveNPgvlEApTAENVNgevETGWYDTGDIVRFDD 603
Cdd:cd05927 326 GHVGGPLPCAEVKLVDVPemnydakDPNPRGEVCIRGPNVFSGYYK--DP---EK-TAEALD---EDGWLHTGDIGEWLP 396
|
330 340 350
....*....|....*....|....*....|
gi 1937565178 604 QGFVQIQGRAKRFAKIA-GEMVSLEMVETL 632
Cdd:cd05927 397 NGTLKIIDRKKNIFKLSqGEYVAPEKIENI 426
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
364-703 |
6.65e-32 |
|
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: 128.97 E-value: 6.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFL--Y 438
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVA----QVLSIAFDACigeIFSTLCNGGTLVLadP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 439 PSPLHYRIvpelvydRNCTVLFGTSTFLGNYarfaNPYDFFRVRYVVAGAEKLQDSTRQIWqdKFGLRILEGYGVTECAP 518
Cdd:cd17653 180 SDPFAHVA-------RTVDALMSTPSILSTL----SPQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 519 VVSINVPMAAKPGTVGRILPG-----LDARLLAVPgIEDGGRLQLKGPNVMNGYLRvenpgvLEAPTAEN-VNGEVETGW 592
Cdd:cd17653 247 SSTMTELLPGQPVTIGKPIPNstcyiLDADLQPVP-EGVVGEICISGVQVARGYLG------NPALTASKfVPDPFWPGS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 593 --YDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDaskgEALVLFTTDGELKRDAL 670
Cdd:cd17653 320 rmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVN----GRLVAFVTPETVDVDGL 395
|
330 340 350
....*....|....*....|....*....|...
gi 1937565178 671 LRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17653 396 RSELAKH-LPSYAVPDRIIALDSFPLTANGKVD 427
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
364-695 |
8.25e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 129.72 E-value: 8.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGaevflypSPLH 443
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIG-------NRFV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 444 Y--RIVPELV---YDRNCTVLFGTSTFlgnYARFANPYD----FFRVRYVVAGA--------EKLQDSTrqiwqdkfGLR 506
Cdd:PRK07787 200 HtgRPTPEAYaqaLSEGGTLYFGVPTV---WSRIAADPEaaraLRGARLLVSGSaalpvpvfDRLAALT--------GHR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 507 ILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAVPGIE---DG---GRLQLKGPNVMNGYLrvENPgvlEApT 580
Cdd:PRK07787 269 PVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPvphDGetvGELQVRGPTLFDGYL--NRP---DA-T 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 581 AENVNGEvetGWYDTGDIVRFDDQGFVQIQGR-AKRFAKIAGEMVSLEMVET--LATAVSAEkmhATVV-KSDASKGEAL 656
Cdd:PRK07787 343 AAAFTAD---GWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETalLGHPGVRE---AAVVgVPDDDLGQRI 416
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1937565178 657 VLF-TTDGELKRDALLryarEHGIPELAV---PRDIRYLKQLP 695
Cdd:PRK07787 417 VAYvVGADDVAADELI----DFVAQQLSVhkrPREVRFVDALP 455
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
321-701 |
1.26e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 130.08 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 321 LPEQLTQVRWVFLEDLKADVTTADKLwifAHLLMPRQAQVkqQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTI 400
Cdd:PRK08314 151 VPAWLRAEPPLQALAPGGVVAWKEAL---AAGLAPPPHTA--GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 401 ADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplhyR----IVPELVYDRNCTVLFGTSTFLGNYarFANP- 475
Cdd:PRK08314 226 SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP-----RwdreAAARLIERYRVTHWTNIPTMVVDF--LASPg 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 476 ---YDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARL-----LAV 547
Cdd:PRK08314 299 laeRDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVidpetLEE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 548 PGIEDGGRLQLKGPNVMNGYLRveNPgvlEApTAE---NVNGeveTGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMV 624
Cdd:PRK08314 379 LPPGEVGEIVVHGPQVFKGYWN--RP---EA-TAEafiEIDG---KRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKV 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 625 SLEMVETLatavsaekMH-------ATVVKS-DASKGE---ALVLFTTD--GELKRDALLRYAREHgipeLA---VPRDI 688
Cdd:PRK08314 450 WPAEVENL--------LYkhpaiqeACVIATpDPRRGEtvkAVVVLRPEarGKTTEEEIIAWAREH----MAaykYPRIV 517
|
410
....*....|...
gi 1937565178 689 RYLKQLPVLGSGK 701
Cdd:PRK08314 518 EFVDSLPKSGSGK 530
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
360-701 |
1.66e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 126.86 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 360 VKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTAND---------RFMSA-LPLFHSFGLTVGLFTPL 429
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqEVMIApLPLYHIYAFTANCMCMM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 430 LTGAEVFLYPSPlhyRIVPELVYDR---NCTVLFGTSTF---LGNYARFANpYDFFRVRYVVAGAEKLQDSTRQIWQDKF 503
Cdd:PRK12492 282 VSGNHNVLITNP---RDIPGFIKELgkwRFSALLGLNTLfvaLMDHPGFKD-LDFSALKLTNSGGTALVKATAERWEQLT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 504 GLRILEGYGVTECAPVVSINvPMA--AKPGTVGRILPGLDARLLAVPGIE----DGGRLQLKGPNVMNGYLrvENPgvle 577
Cdd:PRK12492 358 GCTIVEGYGLTETSPVASTN-PYGelARLGTVGIPVPGTALKVIDDDGNElplgERGELCIKGPQVMKGYW--QQP---- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 578 APTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALV 657
Cdd:PRK12492 431 EATAEALDAE---GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVK 507
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1937565178 658 LFTT--DGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK12492 508 LFVVarDPGLSVEELKAYCKEN-FTGYKVPKHIVLRDSLPMTPVGK 552
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
233-701 |
2.08e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 125.74 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRIL--EKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSR 310
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLiyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 311 QFLDKgklwhlpeqltqvrwvfLEDLKADVTTADKLWI--FAHLLMPRQAQVKQQPEDDA-IILFTSGSEGNPKGVVHSH 387
Cdd:PRK06839 109 TFQNM-----------------ALSMQKVSYVQRVISItsLKEIEDRKIDNFVEKNESASfIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 388 KSILAN-VEQIKTIaDFTANDRFMSALPLFHSFGltVGLFT-PLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTF 465
Cdd:PRK06839 172 ENMFWNaLNNTFAI-DLTMHDRSIVLLPLFHIGG--IGLFAfPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 466 ---LGNYARFANPyDFFRVRYVVAGAEKLQDSTRQIWQDKfGLRILEGYGVTECAPVVSI--NVPMAAKPGTVGRILPGL 540
Cdd:PRK06839 249 hqaLINCSKFETT-NLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMlsEEDARRKVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 541 DARLLAVPG--IEDG--GRLQLKGPNVMNGYLRVENPgvleapTAENVngevETGWYDTGDIVRFDDQGFVQIQGRAKRF 616
Cdd:PRK06839 327 DYELIDENKnkVEVGevGELLIRGPNVMKEYWNRPDA------TEETI----QDGWLCTGDLARVDEDGFVYIVGRKKEM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 617 AKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFT--------TDGELKRDALLRYARehgipeLAVPRDI 688
Cdd:PRK06839 397 IISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIvkksssvlIEKDVIEHCRLFLAK------YKIPKEI 470
|
490
....*....|...
gi 1937565178 689 RYLKQLPVLGSGK 701
Cdd:PRK06839 471 VFLKELPKNATGK 483
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
356-701 |
2.61e-30 |
|
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: 124.00 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 356 RQAQVKQqpEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVgLFTPLLTGAEV 435
Cdd:cd05912 70 KDSDVKL--DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 FLYPsplHY--RIVPELVYDRNCTVLFGTSTFLGNY-ARFANPYDfFRVRYVVAGAEKLQDSTRQIWQDKfGLRILEGYG 512
Cdd:cd05912 147 YLVD---KFdaEQVLHLINSGKVTIISVVPTMLQRLlEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 513 VTE-CAPVVSINVPMA-AKPGTVGRILPGLDARLLAVPGIEDG-GRLQLKGPNVMNGYLRVENPgvleaptaenvNGEV- 588
Cdd:cd05912 222 MTEtCSQIVTLSPEDAlNKIGSAGKPLFPVELKIEDDGQPPYEvGEILLKGPNVTKGYLNRPDA-----------TEESf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 589 ETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLF-TTDGELKR 667
Cdd:cd05912 291 ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFvVSERPISE 370
|
330 340 350
....*....|....*....|....*....|....*..
gi 1937565178 668 DALLRYAREHgipeLA---VPRDIRYLKQLPVLGSGK 701
Cdd:cd05912 371 EELIAYCSEK----LAkykVPKKIYFVDELPRTASGK 403
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
229-701 |
5.66e-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: 123.36 E-value: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 229 FTPD---TYRKLLTKTLFVGRIL--EKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIpammnyTAGVKGLSSAITAAQI 303
Cdd:cd05958 5 RSPErewTYRDLLALANRIANVLvgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAI------AVATMPLLRPKELAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 304 ntiftsrqfLDKGKLWH--LPEQLTQVrwvfledlkadvttadklwifahllmprqaqvkqqpEDDAIILFTSGSEGNPK 381
Cdd:cd05958 79 ---------LDKARITValCAHALTAS------------------------------------DDICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 382 GVVHSHKSILANVEQI-KTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplhyRIVPELVYD----RNC 456
Cdd:cd05958 114 ATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLE-----EATPDLLLSaiarYKP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 457 TVLFGTST----FLGNyARFANPyDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGT 532
Cdd:cd05958 189 TVLFTAPTayraMLAH-PDAAGP-DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 533 VGRILPGLDARLLAVPG--IEDG--GRLQLKGPNVMNGylrvenpgvLEAPTAENVngeVETGWYDTGDIVRFDDQGFVQ 608
Cdd:cd05958 267 TGKPVPGYEAKVVDDEGnpVPDGtiGRLAVRGPTGCRY---------LADKRQRTY---VQGGWNITGDTYSRDPDGYFR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 609 IQGRAKRFAKIAGEMVS-LEMVETLATAVSAEKMhATVVKSDASKGEALVLFTT--DGELKRDALLRYAREHGIPELA-- 683
Cdd:cd05958 335 HQGRSDDMIVSGGYNIApPEVEDVLLQHPAVAEC-AVVGHPDESRGVVVKAFVVlrPGVIPGPVLARELQDHAKAHIApy 413
|
490
....*....|....*....
gi 1937565178 684 -VPRDIRYLKQLPVLGSGK 701
Cdd:cd05958 414 kYPRAIEFVTELPRTATGK 432
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
353-701 |
8.09e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 124.89 E-value: 8.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 353 LMPRQAQVKQqpeDDAI-ILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLT 431
Cdd:PRK12583 191 LAERQASLDR---DDPInIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 432 GAEVfLYPS----PLhyrIVPELVYDRNCTVLFGTST-FLG--NYARFANpYDFFRVRY-VVAGAEKLQDSTRQIWQDKF 503
Cdd:PRK12583 268 GACL-VYPNeafdPL---ATLQAVEEERCTALYGVPTmFIAelDHPQRGN-FDLSSLRTgIMAGAPCPIEVMRRVMDEMH 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 504 GLRILEGYGVTECAPVV---SINVPMAAKPGTVGRILPGLDARLL----AVPGIEDGGRLQLKGPNVMNGYLrvENPgvl 576
Cdd:PRK12583 343 MAEVQIAYGMTETSPVSlqtTAADDLERRVETVGRTQPHLEVKVVdpdgATVPRGEIGELCTRGYSVMKGYW--NNP--- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 577 EApTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMV-SLEMVETLATavsaekmHATVVK------SD 649
Cdd:PRK12583 418 EA-TAESIDED---GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIyPREIEEFLFT-------HPAVADvqvfgvPD 486
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 650 ASKGE---ALVLFTTDGELKRDALLRYAREhGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK12583 487 EKYGEeivAWVRLHPGHAASEEELREFCKA-RIAHFKVPRYFRFVDEFPMTVTGK 540
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
366-702 |
1.16e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 122.40 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 366 DDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSpLHYR 445
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPR-FSAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 446 IVPELVYDRNCTVLfgtsTFLGNYARF-----ANPYDF-FRVRyVVAGAEKLqDSTRQIWQDKFGLRILEGYGVTECAPV 519
Cdd:cd05934 161 RFWSDVRRYGATVT----NYLGAMLSYllaqpPSPDDRaHRLR-AAYGAPNP-PELHEEFEERFGVRLLEGYGMTETIVG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 520 VSINVPMAAKPGTVGRILPGLDARLL-----AVPgIEDGGRLQLK---GPNVMNGYLRveNPgvleAPTAENVNGevetG 591
Cdd:cd05934 235 VIGPRDEPRRPGSIGRPAPGYEVRIVdddgqELP-AGEPGELVIRglrGWGFFKGYYN--MP----EATAEAMRN----G 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 592 WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELKRD 668
Cdd:cd05934 304 WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDevkAVVVLRPGETLDPE 383
|
330 340 350
....*....|....*....|....*....|....
gi 1937565178 669 ALLRYAREhGIPELAVPRDIRYLKQLPVLGSGKP 702
Cdd:cd05934 384 ELFAFCEG-QLAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
305-701 |
1.63e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 123.70 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 305 TIFTSRQFLDKgkLWHLPEQLTQVRWVFLEDLKADVTTADKLwifAHLLM---PRQAQVKQQPEDDAIILFTSGSEGNPK 381
Cdd:PRK06087 129 TLFKQTRPVDL--ILPLQNQLPQLQQIVGVDKLAPATSSLSL---SQIIAdyePLTTAITTHGDELAAVLFTSGTEGLPK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 382 GVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplHYRIVP--ELVYDRNCTVL 459
Cdd:PRK06087 204 GVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD---IFTPDAclALLEQQRCTCM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 460 FGTSTF---LGNYARfANPYDFFRVR-YVVAGAEKLQDSTRQIWQdkFGLRILEGYGVTECAP--VVSINVPMAAKPGTV 533
Cdd:PRK06087 281 LGATPFiydLLNLLE-KQPADLSALRfFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTESSPhaVVNLDDPLSRFMHTD 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 534 GRILPGL------DARLLAVPGIEdgGRLQLKGPNVMNGYLrvENPGVleapTAENVNGEvetGWYDTGDIVRFDDQGFV 607
Cdd:PRK06087 358 GYAAAGVeikvvdEARKTLPPGCE--GEEASRGPNVFMGYL--DEPEL----TARALDEE---GWYYSGDLCRMDEAGYI 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 608 QIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTTDGE----LKRDALLRYAREHGIPELA 683
Cdd:PRK06087 427 KITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAphhsLTLEEVVAFFSRKRVAKYK 506
|
410
....*....|....*...
gi 1937565178 684 VPRDIRYLKQLPVLGSGK 701
Cdd:PRK06087 507 YPEHIVVIDKLPRTASGK 524
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
364-714 |
4.54e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 122.47 E-value: 4.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLH 443
Cdd:PRK13295 196 PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 444 YRIVpELVYDRNCTVLFGTSTFLGNYARFAN--PYDFFRVR-YVVAGAEKLQDSTRQIWQdKFGLRILEGYGVTECApVV 520
Cdd:PRK13295 276 ARAA-ELIRTEGVTFTMASTPFLTDLTRAVKesGRPVSSLRtFLCAGAPIPGALVERARA-ALGAKIVSAWGMTENG-AV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 521 SINVPMAAKP---GTVGRILPGL-----DARLLAVPGIEDgGRLQLKGPNVMNGYLRvenpgvleaptAENVNGEVETGW 592
Cdd:PRK13295 353 TLTKLDDPDErasTTDGCPLPGVevrvvDADGAPLPAGQI-GRLQVRGCSNFGGYLK-----------RPQLNGTDADGW 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 593 YDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELKRDA 669
Cdd:PRK13295 421 FDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGEracAFVVPRPGQSLDFEE 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1937565178 670 LLRYAREHG-----IPELAVPRDirylkQLPVLGSGKPDFVTLKGMVEEA 714
Cdd:PRK13295 501 MVEFLKAQKvakqyIPERLVVRD-----ALPRTPSGKIQKFRLREMLRGE 545
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
363-701 |
4.99e-28 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 119.21 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFT-----ANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL 437
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTgkleeGCEVVITALPLYHIFALTANGLVFMKIGGCNHL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 438 YPSPLHYR-IVPELVYDRnCTVLFGTSTF---LGNYARFANpYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGV 513
Cdd:PRK08751 286 ISNPRDMPgFVKELKKTR-FTAFTGVNTLfngLLNTPGFDQ-IDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 514 TECAPVVSINvPMAAKP--GTVGRILPGLDA-------RLLAVPGIedgGRLQLKGPNVMNGYLRVENPgvleapTAENV 584
Cdd:PRK08751 364 TETSPAACIN-PLTLKEynGSIGLPIPSTDAcikddagTVLAIGEI---GELCIKGPQVMKGYWKRPEE------TAKVM 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 585 NGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEAL--VLFTTD 662
Cdd:PRK08751 434 DAD---GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVkvVIVKKD 510
|
330 340 350
....*....|....*....|....*....|....*....
gi 1937565178 663 GELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK08751 511 PALTAEDVKAHARAN-LTGYKQPRIIEFRKELPKTNVGK 548
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
233-718 |
7.44e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.98 E-value: 7.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRILEKYS-KQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMN--YT----------AGVK------- 292
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGvEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNplYTereleyqlhdSGAKvilcldl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 293 ---GLSSAITAAQINTIFTSR--QFLDKGKLWHLP-EQLTQVRWVfledLKADVTTADKLWIFAHLLMPRQAQVKQQPED 366
Cdd:PRK06710 131 vfpRVTNVQSATKIEHVIVTRiaDFLPFPKNLLYPfVQKKQSNLV----VKVSESETIHLWNSVEKEVNTGVEVPCDPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 367 D-AIILFTSGSEGNPKGVVHSHKSILAN----VEQIKTIADftANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSp 441
Cdd:PRK06710 207 DlALLQYTGGTTGFPKGVMLTHKNLVSNtlmgVQWLYNCKE--GEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPK- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 LHYRIVPELVYDRNCTVLFGTSTFLgnYARFANP----YDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECA 517
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIY--IALLNSPllkeYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 518 PVVSINVPMAAK-PGTVGRILPGLDARLLAV-------PGieDGGRLQLKGPNVMNGYLRvenpgvleapTAENVNGEVE 589
Cdd:PRK06710 362 PVTHSNFLWEKRvPGSIGVPWPDTEAMIMSLetgealpPG--EIGEIVVKGPQIMKGYWN----------KPEETAAVLQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 590 TGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELK 666
Cdd:PRK06710 430 DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGEtvkAFVVLKEGTECS 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1937565178 667 RDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKpdfVTLKGMVEEAEQQN 718
Cdd:PRK06710 510 EEELNQFARKY-LAAYKVPKVYEFRDELPKTTVGK---ILRRVLIEEEKRKN 557
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
363-712 |
1.75e-27 |
|
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: 116.87 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFM--SAlplfHSFGLTVG-LFTPLLTGAEVFLyP 439
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfAS----YTFDVSILeIFTTLAAGGCLCI-P 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SpLHYRI--VPELVYDRNCTVLFGTSTFlgnyARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKfgLRILEGYGVTECA 517
Cdd:cd05918 179 S-EEDRLndLAGFINRLRVTWAFLTPSV----ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAECT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 518 PVVSINVPMA-AKPGTVGRILPG----LDA----RLLAVPGIedgGRLQLKGPNVMNGYLR---------VENPGVLEAP 579
Cdd:cd05918 252 IAATVSPVVPsTDPRNIGRPLGAtcwvVDPdnhdRLVPIGAV---GELLIEGPILARGYLNdpektaaafIEDPAWLKQE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 580 TAENvNGEVetgwYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVE-TLATAVSAEKMHAT--VVKSDASKGEAL 656
Cdd:cd05918 329 GSGR-GRRL----YRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEhHLRQSLPGAKEVVVevVKPKDGSSSPQL 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 657 VLFTTDGELKRD----------------ALLRYAREH---GIPELAVPRDIRYLKQLPVLGSGKPDFVTLKGMVE 712
Cdd:cd05918 404 VAFVVLDGSSSGsgdgdslflepsdefrALVAELRSKlrqRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
233-710 |
4.09e-27 |
|
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: 116.09 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRILEKYS-KQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQ 311
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGlKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 312 FLDKgkLWHLPEQLTQVRWVFLEDLKADVTTADKLWIFAHLLMPRQAQVKQ-------QPEDDAIILFTSGSEGNPKGVV 384
Cdd:cd17642 126 GLQK--VLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDfkppsfdRDEQVALIMNSSGSTGLPKGVQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 385 HSHKSILANVEQ------IKTIADFTAndrFMSALPLFHSFG-------LTVGLFTPLLTGAEVFLYPSPLH-YRI---- 446
Cdd:cd17642 204 LTHKNIVARFSHardpifGNQIIPDTA---ILTVIPFHHGFGmfttlgyLICGFRVVLMYKFEEELFLRSLQdYKVqsal 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 447 -VPELVydrnctVLFGTSTFLgnyarfaNPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLR-ILEGYGVTECAPVVSINV 524
Cdd:cd17642 281 lVPTLF------AFFAKSTLV-------DKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 525 PMAAKPGTVGRILPGLDARLL-----AVPGIEDGGRLQLKGPNVMNGYlrVENPgvlEApTAENVNgevETGWYDTGDIV 599
Cdd:cd17642 348 EGDDKPGAVGKVVPFFYAKVVdldtgKTLGPNERGELCVKGPMIMKGY--VNNP---EA-TKALID---KDGWLHSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 600 RFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELKRDALLRYARE 676
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGElpaAVVVLEAGKTMTEKEVMDYVAS 498
|
490 500 510
....*....|....*....|....*....|....
gi 1937565178 677 HGIPELAVPRDIRYLKQLPVLGSGKPDFVTLKGM 710
Cdd:cd17642 499 QVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
362-703 |
8.94e-27 |
|
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: 114.00 E-value: 8.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 362 QQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSalplFHSFGLTVG---LFTPLLTGAEVFLY 438
Cdd:cd17649 91 HHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQ----FASFNFDGAheqLLPPLICGACVVLR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 439 PSPL------HYRIVPELvydrNCTVLFGTSTFLGNYARFA---NPYDFFRVRYVVAGAEKLQDSTRQIWQdKFGLRILE 509
Cdd:cd17649 167 PDELwasadeLAEMVREL----GVTVLDLPPAYLQQLAEEAdrtGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 510 GYGVTECapVVSinvPMAAKPGT----------VGRILPG-----LDARLLAVPgieDG--GRLQLKGPNVMNGYLrvEN 572
Cdd:cd17649 242 AYGPTEA--TVT---PLVWKCEAgaaragasmpIGRPLGGrsayiLDADLNPVP---VGvtGELYIGGEGLARGYL--GR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 573 PGVLEAPTAENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKmHATVVKSDASK 652
Cdd:cd17649 312 PELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVR-EAAVVALDGAG 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 653 GEALVLFTTDGELKR----DALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17649 391 GKQLVAYVVLRAAAAqpelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
365-637 |
1.28e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 114.71 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDD-AIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTA-NDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPSPL 442
Cdd:PRK07768 151 EDDlALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHDMGMVGFLTVPMYFGAEL-VKVTPM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 443 HYRIVPeLVYDRNCTVLFGTSTFLGNYA---------RFANP--YDFFRVRYVVAGAEKLQDSTRQIWQD---KFGLR-- 506
Cdd:PRK07768 230 DFLRDP-LLWAELISKYRGTMTAAPNFAyallarrlrRQAKPgaFDLSSLRFALNGAEPIDPADVEDLLDagaRFGLRpe 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 507 -ILEGYGVTECAPVVSIN----------------------VPmAAKPGT-----VGRILPGLDARLLAvpgiEDG----- 553
Cdd:PRK07768 309 aILPAYGMAEATLAVSFSpcgaglvvdevdadllaalrraVP-ATKGNTrrlatLGPPLPGLEVRVVD----EDGqvlpp 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 554 ---GRLQLKGPNVMNGYLRVENPgvleAPTAEnvngevETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
Cdd:PRK07768 384 rgvGVIELRGESVTPGYLTMDGF----IPAQD------ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
....*..
gi 1937565178 631 TLATAVS 637
Cdd:PRK07768 454 RAAARVE 460
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
315-614 |
1.43e-26 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 114.69 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 315 KGKLWHLPEQLTQVRWVFLEDLKADVTTADKLW-------IFAHLLM--PRQAQVKQ-QPEDDAIILFTSGSEGNPKGVV 384
Cdd:cd05906 107 LRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSglpgirvLSIEELLdtAADHDLPQsRPDDLALLMLTSGSTGFPKAVP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 385 HSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLT-VGLFtPLLTGAEVFLYPSPL-------------HYRIvpel 450
Cdd:cd05906 187 LTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVeLHLR-AVYLGCQQVHVPTEEiladplrwldlidRYRV---- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 451 vydrncTVLFGTSTFLGNYARFAN-----PYDFFRVRYVVAGAEKLQDST-RQIWQ--DKFGLR---ILEGYGVTECAPV 519
Cdd:cd05906 262 ------TITWAPNFAFALLNDLLEeiedgTWDLSSLRYLVNAGEAVVAKTiRRLLRllEPYGLPpdaIRPAFGMTETCSG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 520 VSINVPMAAKPGT-------VGRILPGLDARL--LAVPGIEDG--GRLQLKGPNVMNGYLRveNPgvlEAptaenvNGEV 588
Cdd:cd05906 336 VIYSRSFPTYDHSqalefvsLGRPIPGVSMRIvdDEGQLLPEGevGRLQVRGPVVTKGYYN--NP---EA------NAEA 404
|
330 340
....*....|....*....|....*...
gi 1937565178 589 --ETGWYDTGDIVrFDDQGFVQIQGRAK 614
Cdd:cd05906 405 ftEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
364-703 |
1.61e-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: 113.84 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIaDFTANDRFMSALPLfhSF-GLTVGLFTPLLTGAEVFLYPS-- 440
Cdd:cd12117 135 PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPL--AFdASTFEIWGALLNGARLVLAPKgt 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 441 PLHYRIVPELVYDRNCTVLFGTSTFLGNYARfANPYDFFRVRYVVAGAEKLQ-DSTRQIWQDKFGLRILEGYGVTECAPV 519
Cdd:cd12117 212 LLDPDALGALIAEEGVTVLWLTAALFNQLAD-EDPECFAGLRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTTF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 520 VSINV--PMAAKPGTV--GRILPGLDARLL------AVPGIEdgGRLQLKGPNVMNGYLRvenpgvLEAPTAE----NVN 585
Cdd:cd12117 291 TTSHVvtELDEVAGSIpiGRPIANTRVYVLdedgrpVPPGVP--GELYVGGDGLALGYLN------RPALTAErfvaDPF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 586 GEVETgWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTTDGEL 665
Cdd:cd12117 363 GPGER-LYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA 441
|
330 340 350
....*....|....*....|....*....|....*...
gi 1937565178 666 KRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd12117 442 LDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVD 479
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
323-701 |
5.45e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 113.07 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 323 EQLTQVRWVFLEDlkADVTTADKLWIFAHLLmpRQAQ-----VKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQI 397
Cdd:PRK04319 162 DDLPSLKHVLLVG--EDVEEGPGTLDFNALM--EQASdefdiEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 398 KTIADFTANDRFM-SALPLFHSfGLTVGLFTPLLTGA------EVFlypSPLH-YRIVPELvydrNCTVLFGTST----F 465
Cdd:PRK04319 238 KYVLDLHEDDVYWcTADPGWVT-GTSYGIFAPWLNGAtnvidgGRF---SPERwYRILEDY----KVTVWYTAPTairmL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 466 LGNYARFANPYDFFRVRYVVAGAEKLQDSTrqIW--QDKFGLRILEGYGVTECAPVVSINVP-MAAKPGTVGRILPGLDA 542
Cdd:PRK04319 310 MGAGDDLVKKYDLSSLRHILSVGEPLNPEV--VRwgMKVFGLPIHDNWWMTETGGIMIANYPaMDIKPGSMGKPLPGIEA 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 543 RLLAVPGIEDG----GRLQLKG--PNVMNGYLRveNPgvleaptaENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRF 616
Cdd:PRK04319 388 AIVDDQGNELPpnrmGNLAIKKgwPSMMRGIWN--NP--------EKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDV 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 617 AKIAGEMVSLEMVETLAT---AVsAEkmhATVV-KSDASKGE---ALVL----FTTDGELKRDaLLRYAREhGIPELAVP 685
Cdd:PRK04319 458 IKTSGERVGPFEVESKLMehpAV-AE---AGVIgKPDPVRGEiikAFVAlrpgYEPSEELKEE-IRGFVKK-GLGAHAAP 531
|
410
....*....|....*.
gi 1937565178 686 RDIRYLKQLPVLGSGK 701
Cdd:PRK04319 532 REIEFKDKLPKTRSGK 547
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
360-701 |
8.37e-26 |
|
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: 110.98 E-value: 8.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 360 VKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSF--GLTVGLFTPLLTGAEVFL 437
Cdd:cd05971 83 VTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPADWAWigGLLDVLLPSLYFGVPVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 438 Y-PSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFFRV--RYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVT 514
Cdd:cd05971 163 HrMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVklRAIATGGESLGEELLGWAREQFGVEVNEFYGQT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 515 ECAPVVSIN-VPMAAKPGTVGRILPGLDARLLAVPGIE----DGGRLQLKGPN--VMNGYLRveNPGVLEAPTAenvnge 587
Cdd:cd05971 243 ECNLVIGNCsALFPIKPGSMGKPIPGHRVAIVDDNGTPlppgEVGEIAVELPDpvAFLGYWN--NPSATEKKMA------ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 588 veTGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTT--DGEL 665
Cdd:cd05971 315 --GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnPGET 392
|
330 340 350
....*....|....*....|....*....|....*....
gi 1937565178 666 KRDALLRYAREHGIPELAV---PRDIRYLKQLPVLGSGK 701
Cdd:cd05971 393 PSDALAREIQELVKTRLAAheyPREIEFVNELPRTATGK 431
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
365-701 |
3.15e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 110.41 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSILAnvEQIKTIA--DFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPl 442
Cdd:PRK08316 171 DDLAQILYTSGTESLPKGAMLTHRALIA--EYVSCIVagDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAP- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 443 hyriVPELVYDR----NCTVLFGTSTF---LGNYARFAnPYDFFRVRYVVAGA-----EKLQDstrqiWQDKF-GLRILE 509
Cdd:PRK08316 248 ----DPELILRTieaeRITSFFAPPTVwisLLRHPDFD-TRDLSSLRKGYYGAsimpvEVLKE-----LRERLpGLRFYN 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 510 GYGVTECAPVVSINVP--MAAKPGTVGRilPGL-------DARLLAVPgieDG--GRLQLKGPNVMNGYLRveNPgvleA 578
Cdd:PRK08316 318 CYGQTEIAPLATVLGPeeHLRRPGSAGR--PVLnvetrvvDDDGNDVA---PGevGEIVHRSPQLMLGYWD--DP----E 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 579 PTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMV-SLEMVETLAT--AVSaekmHATVVK-SDASKGE 654
Cdd:PRK08316 387 KTAEAFRG----GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVaSREVEEALYThpAVA----EVAVIGlPDPKWIE 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1937565178 655 ---ALVLFTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK08316 459 avtAVVVPKAGATVTEDELIAHCRAR-LAGFKVPKRVIFVDELPRNPSGK 507
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
368-701 |
5.60e-25 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 110.51 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 368 AIILFTSGSEGNPKGVVHSHKSILANVEQIKTIA-DFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRI 446
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKAlRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 447 VPELVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKF-GLRILEGYGVTECAPVVSINVP 525
Cdd:PRK06060 228 AAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFgGIPILDGIGSTEVGQTFVSNRV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 526 MAAKPGTVGRILPGLDARLLAV------PGIEdgGRLQLKGPNVMNGYLRVENPgVLEaptaenvngevETGWYDTGDIV 599
Cdd:PRK06060 308 DEWRLGTLGRVLPPYEIRVVAPdgttagPGVE--GDLWVRGPAIAKGYWNRPDS-PVA-----------NEGWLDTRDRV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 600 RFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTT-------DGELKRDALLR 672
Cdd:PRK06060 374 CIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVatsgatiDGSVMRDLHRG 453
|
330 340
....*....|....*....|....*....
gi 1937565178 673 YAREhgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK06060 454 LLNR--LSAFKVPHRFAVVDRLPRTPNGK 480
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
253-673 |
2.23e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 107.76 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 253 KQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMN--YTAGvkGLSSAITAAQINTIFTSRQFLDKGKLWHLPEQLTqvrw 330
Cdd:PLN02246 73 RQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANpfYTPA--EIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVT---- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 331 VFLEDLKADVTTAdklwiFAHLLMPRQA---QVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQiktIAD----- 402
Cdd:PLN02246 147 VVTIDDPPEGCLH-----FSELTQADENelpEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQ---QVDgenpn 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 403 --FTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhYRIVP--ELVYDRNCTVlfgtstflgnyARFANP--- 475
Cdd:PLN02246 219 lyFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPK---FEIGAllELIQRHKVTI-----------APFVPPivl 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 476 ----------YDFFRVRYVVAGA----EKLQDSTRqiwqDKFGLRIL-EGYGVTECAPVVSINV-----PMAAKPGTVGR 535
Cdd:PLN02246 285 aiakspvvekYDLSSIRMVLSGAaplgKELEDAFR----AKLPNAVLgQGYGMTEAGPVLAMCLafakePFPVKSGSCGT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 536 ILPGLDARLLAVPGIEDGGRLQ-----LKGPNVMNGYLRveNPgvlEApTAENVNGEvetGWYDTGDIVRFDDQGFVQIQ 610
Cdd:PLN02246 361 VVRNAELKIVDPETGASLPRNQpgeicIRGPQIMKGYLN--DP---EA-TANTIDKD---GWLHTGDIGYIDDDDELFIV 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 611 GRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELKRDALLRY 673
Cdd:PLN02246 432 DRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEvpvAFVVRSNGSEITEDEIKQF 497
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
356-614 |
2.71e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 107.59 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 356 RQAQVKQqpeDDAI-ILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGA- 433
Cdd:PRK08315 192 RQATLDP---DDPInIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGAt 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 434 -----EVFlypSPLHyriVPELVYDRNCTVLFGTST-FLG--NYARFANpYDFFRVRY-VVAGaeklqdST------RQI 498
Cdd:PRK08315 269 mvypgEGF---DPLA---TLAAVEEERCTALYGVPTmFIAelDHPDFAR-FDLSSLRTgIMAG------SPcpievmKRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 499 wQDKFGLR-ILEGYGVTECAPVV---SINVPMAAKPGTVGRILPGLDARLLavpGIEDG--------GRLQLKGPNVMNG 566
Cdd:PRK08315 336 -IDKMHMSeVTIAYGMTETSPVStqtRTDDPLEKRVTTVGRALPHLEVKIV---DPETGetvprgeqGELCTRGYSVMKG 411
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1937565178 567 YLrvENPgvlEApTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAK 614
Cdd:PRK08315 412 YW--NDP---EK-TAEAIDAD---GWMHTGDLAVMDEEGYVNIVGRIK 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
359-703 |
3.91e-24 |
|
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: 106.59 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 359 QVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFL 437
Cdd:cd17646 132 LVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL--SFDVSVWeLFWPLVAGARLVV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 438 YPSPLH----YriVPELVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGV 513
Cdd:cd17646 210 ARPGGHrdpaY--LAALIREHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGP 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 514 TECA-PVVSINVPMAAKPGTV--GRILPG-----LDARLLAVP-GIedGGRLQLKGPNVMNGYLRveNPGVleapTAEN- 583
Cdd:cd17646 288 TEAAiDVTHWPVRGPAETPSVpiGRPVPNtrlyvLDDALRPVPvGV--PGELYLGGVQLARGYLG--RPAL----TAERf 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 584 VNGEVETG--WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETlATAVSAEKMHATVVKSDASKGEA-----L 656
Cdd:cd17646 360 VPDPFGPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTHAVVVARAAPAGAArlvgyV 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1937565178 657 VLFTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17646 439 VPAAGAAGPDTAALRAHLAER-LPEYMVPAAFVVLDALPLTANGKLD 484
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
360-703 |
4.00e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.10 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 360 VKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYP 439
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATLHLLP 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPLHYRivPE----LVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQ-DSTRQIWQDKFGLRILEGYGVT 514
Cdd:PRK12467 730 PDCARD--AEafaaLMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQvDLLARVRALGPGARLINHYGPT 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 515 ECAPVVSI------NVPMAAKPgtVGRILPG-----LDARLLAVPGiEDGGRLQLKGPNVMNGYLRveNPGVleapTAE- 582
Cdd:PRK12467 808 ETTVGVSTyelsdeERDFGNVP--IGQPLANlglyiLDHYLNPVPV-GVVGELYIGGAGLARGYHR--RPAL----TAEr 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 583 ------NVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVsAEKMHATVVKSDASKGEAL 656
Cdd:PRK12467 879 fvpdpfGADGG---RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQ-PGVREAVVLAQPGDAGLQL 954
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 657 VLF--------TTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK12467 955 VAYlvpaavadGAEHQATRDELKAQLRQV-LPDYMVPAHLLLLDSLPLTPNGKLD 1008
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
372-703 |
4.37e-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: 103.64 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 372 FTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAevFLYPSPLHYRIVPELV 451
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGT--FIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 452 YDRNCTVLFGTSTFLGNYARFANPYDffRVRYVVAGAEKLQDST----RQIWQDkfgLRILEGYGVTEcAPVVSINVPM- 526
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPES--KIKSIFSSGQKLFESTkkklKNIFPK---ANLIEFYGTSE-LSFITYNFNQe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 527 AAKPGTVGRILPGLDARLLAVPGIEDgGRLQLKGPNVMNGYLRvenpgvleaptaenVNGEVETGWYDTGDIVRFDDQGF 606
Cdd:cd17633 159 SRPPNSVGRPFPNVEIEIRNADGGEI-GKIFVKSEMVFSGYVR--------------GGFSNPDGWMSVGDIGYVDEEGY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 607 VQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTTDGELKRDALLRYAREHgIPELAVPR 686
Cdd:cd17633 224 LYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQLKRFLKQK-LSRYEIPK 302
|
330
....*....|....*..
gi 1937565178 687 DIRYLKQLPVLGSGKPD 703
Cdd:cd17633 303 KIIFVDSLPYTSSGKIA 319
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
360-701 |
4.41e-24 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 107.03 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 360 VKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIAD--FTANDR-----FMSALPLFHSFGLTVGLFTPLLTG 432
Cdd:PRK07059 199 VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpaFEKKPRpdqlnFVCALPLYHIFALTVCGLLGMRTG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 433 AEVFLYPSPlhyRIVPELV-----YDRNC----TVLFGTstfLGNYARFANpYDFFRVRYVVAGAEKLQDSTRQIWQDKF 503
Cdd:PRK07059 279 GRNILIPNP---RDIPGFIkelkkYQVHIfpavNTLYNA---LLNNPDFDK-LDFSKLIVANGGGMAVQRPVAERWLEMT 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 504 GLRILEGYGVTECAPVVSINVPMAAK-PGTVGRILPGLDARLLAVPGIE----DGGRLQLKGPNVMNGYLrvENPgvlea 578
Cdd:PRK07059 352 GCPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSIRDDDGNDlplgEPGEICIRGPQVMAGYW--NRP----- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 579 ptAENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATavsaekMHATVVKS------DASK 652
Cdd:PRK07059 425 --DETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA------SHPGVLEVaavgvpDEHS 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1937565178 653 GEALVLFTT--DGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK07059 497 GEAVKLFVVkkDPALTEEDVKAFCKER-LTNYKRPKFVEFRTELPKTNVGK 546
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
331-680 |
5.89e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 107.37 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 331 VFLEDLKADVTTAD-KLWIFAHLLM---PRQAQVK-QQPEDD---AIILFTSGSEGNPKGVVHSHKSILANVEQI----- 397
Cdd:PTZ00216 222 IYLDSLPASVDTEGcRLVAWTDVVAkghSAGSHHPlNIPENNddlALIMYTSGTTGDPKGVMHTHGSLTAGILALedrln 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 398 KTIADFTANDRFMSALPLFHSFGLTVglftplltgAEVFLYpsplhyrivpelvydRNCTVLFGTS-TFLGNYAR----- 471
Cdd:PTZ00216 302 DLIGPPEEDETYCSYLPLAHIMEFGV---------TNIFLA---------------RGALIGFGSPrTLTDTFARphgdl 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 472 -------------------------------------------------------------FANPYDFF--RVRYVVAGA 488
Cdd:PTZ00216 358 tefrpvfligvprifdtikkaveaklppvgslkrrvfdhayqsrlralkegkdtpywnekvFSAPRAVLggRVRAMLSGG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 489 EKLQDSTRQIWQDKFGlRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAVPGI------EDGGRLQLKGPN 562
Cdd:PTZ00216 438 GPLSAATQEFVNVVFG-MVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYkhtdtpEPRGEILLRGPF 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 563 VMNGYLRvenpgvLEAPTAENVNgevETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA-GEMVSLEMVETL--ATAVSAE 639
Cdd:PTZ00216 517 LFKGYYK------QEELTREVLD---EDGWFHTGDVGSIAANGTLRIIGRVKALAKNClGEYIALEALEALygQNELVVP 587
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1937565178 640 KMHATVVKSDASKGEALVLftTDGELkrdaLLRYAREHGIP 680
Cdd:PTZ00216 588 NGVCVLVHPARSYICALVL--TDEAK----AMAFAKEHGIE 622
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
372-701 |
1.01e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 105.94 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 372 FTSGSEGNPKGVVHSHKSIL--ANVEQIKTIADFTANDRFMSALPLFH--SFGLTvglFTPLLTGAEVFLyPSP-LHYRI 446
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHvnAWGLP---YSAPLTGAKLVL-PGPdLDGKS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 447 VPELVYDRNCTVLFGTST-FLG--NYARfANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAP---VV 520
Cdd:PRK07008 259 LYELIEAERVTFSAGVPTvWLGllNHMR-EAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPlgtLC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 521 SINVPMAAKPGTV--------GRILPGLDARLLAVPGIE---DG---GRLQLKGPNVMNGYLRVE-NPGVleaptaenvn 585
Cdd:PRK07008 338 KLKWKHSQLPLDEqrkllekqGRVIYGVDMKIVGDDGRElpwDGkafGDLQVRGPWVIDRYFRGDaSPLV---------- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 586 geveTGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE--ALVLFTTDG 663
Cdd:PRK07008 408 ----DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDErpLLVVVKRPG 483
|
330 340 350
....*....|....*....|....*....|....*....
gi 1937565178 664 -ELKRDALLRYArEHGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK07008 484 aEVTREELLAFY-EGKVAKWWIPDDVVFVDAIPHTATGK 521
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
359-703 |
1.02e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 107.74 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 359 QVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFL 437
Cdd:PRK12316 4688 AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF--SFDGSHeGLYHPLINGASVVI 4765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 438 YPSPLH--YRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQ-DSTRQIWQDKFGLRILEGYGVT 514
Cdd:PRK12316 4766 RDDSLWdpERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAqASYDLAWRALKPVYLFNGYGPT 4845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 515 ECAPVVSI-----NVPMAAKPGTVGRILPG-----LDARLLAVPgIEDGGRLQLKGPNVMNGYLrvENPGVLEAPTAENV 584
Cdd:PRK12316 4846 ETTVTVLLwkardGDACGAAYMPIGTPLGNrsgyvLDGQLNPLP-VGVAGELYLGGEGVARGYL--ERPALTAERFVPDP 4922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 585 NGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKmHATVVKSDASKGEALV--LFTTD 662
Cdd:PRK12316 4923 FGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVR-EAVVIAQEGAVGKQLVgyVVPQD 5001
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1937565178 663 GELK---------RDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK12316 5002 PALAdadeaqaelRDELKAALRER-LPEYMVPAHLVFLARMPLTPNGKLD 5050
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
363-701 |
2.16e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 104.84 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSIL---ANVEQIKTIadfTANDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYP 439
Cdd:PRK06155 178 QPGDTAAILYTSGTTGPSKGVCCPHAQFYwwgRNSAEDLEI---GADDVLYTTLPLFHTNALNA-FFQALLAGATYVLEP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPLHYRIVPELVyDRNCTV--LFGT--STFLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQiwqdKFGLRILEGYGVTE 515
Cdd:PRK06155 254 RFSASGFWPAVR-RHGATVtyLLGAmvSILLSQPARESDRAHRVRVALGPGVPAALHAAFRE----RFGVDLLDGYGSTE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 516 CapvvsiNVPMA-----AKPGTVGRILPGLDARLL-----AVPGIEDGGRLqlkgpnvmngyLRVENPGVLEAPTAENVN 585
Cdd:PRK06155 329 T------NFVIAvthgsQRPGSMGRLAPGFEARVVdehdqELPDGEPGELL-----------LRADEPFAFATGYFGMPE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 586 GEVETG---WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVE-TLATAVSAEKMHATVVKSDASKGE-ALVLFT 660
Cdd:PRK06155 392 KTVEAWrnlWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEqVLLSHPAVAAAAVFPVPSELGEDEvMAAVVL 471
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1937565178 661 TDGE-LKRDALLRYArEHGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK06155 472 RDGTaLEPVALVRHC-EPRLAYFAVPRYVEFVAALPKTENGK 512
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
233-701 |
3.12e-23 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 104.58 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKT-LFVGRILEKYSKQGEKIGLMLPNAGiSAAVIFGAVSR-GRIPAMMNYTAGVKGLSSAITAAQINTIFTSR 310
Cdd:cd17634 86 SYRELHREVcRFAGTLLDLGVKKGDRVAIYMPMIP-EAAVAMLACARiGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 311 QFLDKGKLWHLPE--------QLTQVRWVFLED-LKADVTTADKLWIFAHLLM----PRQAQVKQQPEDDAIILFTSGSE 377
Cdd:cd17634 165 GGVRAGRSVPLKKnvddalnpNVTSVEHVIVLKrTGSDIDWQEGRDLWWRDLIakasPEHQPEAMNAEDPLFILYTSGTT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 378 GNPKGVVHSHKS-ILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY------PSPLHYRivpEL 450
Cdd:cd17634 245 GKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYegvpnwPTPARMW---QV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 451 VYDRNCTVLFGTSTFLGNYARfANP-----YDFFRVRYVVAGAEKLQ-DSTRQIWQ--DKFGLRILEGYGVTE----CAP 518
Cdd:cd17634 322 VDKHGVNILYTAPTAIRALMA-AGDdaiegTDRSSLRILGSVGEPINpEAYEWYWKkiGKEKCPVVDTWWQTEtggfMIT 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 519 VVSINVPMaaKPGTVGRILPG-----LDARLLAVPGIEDGG-RLQLKGPNVMNGYLRvenpgvlEAPTAENVNGEVETGW 592
Cdd:cd17634 401 PLPGAIEL--KAGSATRPVFGvqpavVDNEGHPQPGGTEGNlVITDPWPGQTRTLFG-------DHERFEQTYFSTFKGM 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 593 YDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFT------TDGELK 666
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVvlnhgvEPSPEL 551
|
490 500 510
....*....|....*....|....*....|....*
gi 1937565178 667 RDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd17634 552 YAELRNWVRKE-IGPLATPDVVHWVDSLPKTRSGK 585
|
|
| Acyltransferase |
pfam01553 |
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ... |
15-137 |
4.49e-23 |
|
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: 95.04 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 15 RIRVTGDTQALYGERVLITPNHVSFLDGVLLALFLP---VRPVFAVYSSISEKWYMRWLKPLIDFVPLDPTKPM----MI 87
Cdd:pfam01553 1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLLSLALYkrgRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKdaagTL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1937565178 88 KHLVRLIGQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSQATVVPLRI 137
Cdd:pfam01553 81 EYLVELLREGKLVVIFPEGTRSREGELLPFKKGAFRLAIEAGVPIVPVAI 130
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
355-676 |
5.27e-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: 103.32 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
Cdd:cd05932 127 PLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 435 VFLYPS------------PLHYRIVPEL-------VYDR----NCTVLFGTStFLGNYAR--FANPYDFFRVRYVVAGAE 489
Cdd:cd05932 207 VAFAESldtfvedvqrarPTLFFSVPRLwtkfqqgVQDKipqqKLNLLLKIP-VVNSLVKrkVLKGLGLDQCRLAGCGSA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 490 KLQDSTRQiWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARllavpgIEDGGRLQLKGPNVMNGYLR 569
Cdd:cd05932 286 PVPPALLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVR------ISEDGEILVRSPALMMGYYK 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 570 veNPgvlEApTAENVNgevETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA-GEMVSLEMVET-LATAVSAEKMhaTVVK 647
Cdd:cd05932 359 --DP---EA-TAEAFT---ADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENkLAEHDRVEMV--CVIG 427
|
330 340
....*....|....*....|....*....
gi 1937565178 648 SDASKGEALVLFTTDGELKRDALLRYARE 676
Cdd:cd05932 428 SGLPAPLALVVLSEEARLRADAFARAELE 456
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
369-703 |
7.50e-23 |
|
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: 100.42 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 369 IILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypSPLHYRIVP 448
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVM--EKFDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 449 ELVYDRNCTVLFGTSTFLGNY--ARFANPYDFFRVRYvVAGAEKLQdsTRQIWQDKFGLRILEGYGVTECAPVVSINvPM 526
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLldAAEKSGVDLSSLRH-VLGLDAPE--TIQRFEETTGATFWSLYGQTETSGLVTLS-PY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 527 AAKPGTVGRILPGLDARLL-----AVPGIEDgGRLQLKGPNVMNGYLRvenpgvLEAPTAENVNGevetGWYDTGDIVRF 601
Cdd:cd17637 158 RERPGSAGRPGPLVRVRIVddndrPVPAGET-GEIVVRGPLVFQGYWN------LPELTAYTFRN----GWHHTGDLGRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 602 DDQGFVQIQGR--AKRFAKIAGEMVSLEMVEtlATAVSAEKMHATVV--KSDASKGEAL--VLFTTDGE-LKRDALLRYA 674
Cdd:cd17637 227 DEDGYLWYAGRkpEKELIKPGGENVYPAEVE--KVILEHPAIAEVCVigVPDPKWGEGIkaVCVLKPGAtLTADELIEFV 304
|
330 340
....*....|....*....|....*....
gi 1937565178 675 REHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17637 305 GSR-IARYKKPRYVVFVEALPKTADGSID 332
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
363-703 |
8.53e-23 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 104.55 E-value: 8.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSP 441
Cdd:COG1020 615 TPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASL--SFDASVWeIFGALLSGATLVLAPPE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 LHY---RIVpELVYDRNCTVLFGTSTFLGNYARFANPyDFFRVRYVVAGAEKLQDSTRQIWQDKF-GLRILEGYGVTECA 517
Cdd:COG1020 693 ARRdpaALA-ELLARHRVTVLNLTPSLLRALLDAAPE-ALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETT 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 518 PVVSINVPMAAKPG----TVGRILPG-----LDARLLAVP-GIEdgGRLQLKGPNVMNGYLRveNPGVleapTAE----- 582
Cdd:COG1020 771 VDSTYYEVTPPDADggsvPIGRPIANtrvyvLDAHLQPVPvGVP--GELYIGGAGLARGYLN--RPEL----TAErfvad 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 583 --NVNGEVetgWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLF- 659
Cdd:COG1020 843 pfGFPGAR---LYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYv 919
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1937565178 660 -TTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:COG1020 920 vPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLD 964
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
364-703 |
2.27e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.50 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPL 442
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVVAAPGD 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 443 HYRI--VPELVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKL-QDSTRQIWQDKFGLRILEGYGVTECAPV 519
Cdd:PRK12316 732 HRDPakLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALpADAQEQVFAKLPQAGLYNLYGPTEAAID 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 520 VSINVPMAAKPGTV--GRILPG-----LDARLLAVP-GIEdgGRLQLKGPNVMNGYLRveNPGVleapTAEN------VN 585
Cdd:PRK12316 812 VTHWTCVEEGGDSVpiGRPIANlacyiLDANLEPVPvGVL--GELYLAGRGLARGYHG--RPGL----TAERfvpspfVA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 586 GEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKmHATVVKSDASKGEALVLFTTDGEL 665
Cdd:PRK12316 884 GE---RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR-EAAVLAVDGKQLVGYVVLESEGGD 959
|
330 340 350
....*....|....*....|....*....|....*...
gi 1937565178 666 KRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK12316 960 WREALKAHLAAS-LPEYMVPAQWLALERLPLTPNGKLD 996
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
364-703 |
3.17e-22 |
|
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: 100.17 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRfmSALPLFHS--FGLTVGLFTPLLTGAEVFLYPSP 441
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGD--EAVLFFSNyvFDFFVEQMTLALLNGQKLVVPPD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 lHYRIVPELVYD----RNCTVLFGTSTFLgnyarfaNPYDFFR---VRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVT 514
Cdd:cd17648 171 -EMRFDPDRFYAyinrEKVTYLSGTPSVL-------QQYDLARlphLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 515 ECApVVSINVPM---AAKPGTVGRILPG-----LDARLLAVPgIEDGGRLQLKGPNVMNGYLR---------VENPGVLE 577
Cdd:cd17648 243 ETT-VTNHKRFFpgdQRFDKSLGRPVRNtkcyvLNDAMKRVP-VGAVGELYLGGDGVARGYLNrpeltaerfLPNPFQTE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 578 APTAENVNGEVetgwYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEA-- 655
Cdd:cd17648 321 QERARGRNARL----YKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSri 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1937565178 656 ---LV-LFTTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17648 397 qkyLVgYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLD 448
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
360-703 |
8.19e-22 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 99.34 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 360 VKQQPEDDAIILFTSGSEGNPKGVVHSHKSiLANVEQiktiadftANDRFMSALP-----LFHSFGLTVG---LFTPLLT 431
Cdd:cd17651 131 PALDADDLAYVIYTSGSTGRPKGVVMPHRS-LANLVA--------WQARASSLGPgartlQFAGLGFDVSvqeIFSTLCA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 432 GAEVFLYPSplHYRIVPE----LVYDRNCTVLFGTSTFLGNYARFANPYDFF--RVRYVVAGAEKLQDS--TRQIWQDKF 503
Cdd:cd17651 202 GATLVLPPE--EVRTDPPalaaWLDEQRISRVFLPTVALRALAEHGRPLGVRlaALRYLLTGGEQLVLTedLREFCAGLP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 504 GLRILEGYGVTECAPVVSINVPMAAK----PGTVGRILPG-----LDARLLAVP-GIEdgGRLQLKGPNVMNGYLRveNP 573
Cdd:cd17651 280 GLRLHNHYGPTETHVVTALSLPGDPAawpaPPPIGRPIDNtrvyvLDAALRPVPpGVP--GELYIGGAGLARGYLN--RP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 574 GVleapTAEN-VNGEVETG--WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDA 650
Cdd:cd17651 356 EL----TAERfVPDPFVPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDR 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 651 SKGEALVLFTTDGELKRD--ALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17651 432 PGEKRLVAYVVGDPEAPVdaAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLD 486
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
243-715 |
1.25e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 99.35 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 243 FVGRILEKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKGKLwHLP 322
Cdd:PRK06178 71 FAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQ-VRA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 323 EqlTQVRWVF---------------LEDLKADVTTADKLWI--FAHLLMPRQAQVKQQPEDDAI--ILFTSGSEGNPKGV 383
Cdd:PRK06178 150 E--TSLRHVIvtsladvlpaeptlpLPDSLRAPRLAAAGAIdlLPALRACTAPVPLPPPALDALaaLNYTGGTTGMPKGC 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 384 VHSHKSIlanveqIKTIADFTA-------NDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP--SPL-------HYRIV 447
Cdd:PRK06178 228 EHTQRDM------VYTAAAAYAvavvggeDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLArwDAVafmaaveRYRVT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 448 pelvydrNCTVLFGTSTFLGNYARFANpYDFFRVRYV--VAGAEKLQDSTRQIWQDKFGLRILEG-YGVTECAPVVSINV 524
Cdd:PRK06178 302 -------RTVMLVDNAVELMDHPRFAE-YDLSSLRQVrvVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 525 PMA-------AKPGTVGRILPGLD--------ARLLAVpGIEdgGRLQLKGPNVMNGYLRveNPgvlEApTAENVNGeve 589
Cdd:PRK06178 374 GFQdddfdllSQPVFVGLPVPGTEfkicdfetGELLPL-GAE--GEIVVRTPSLLKGYWN--KP---EA-TAEALRD--- 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 590 tGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTT---DGELK 666
Cdd:PRK06178 442 -GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlkpGADLT 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1937565178 667 RDALLRYAREHgIPELAVPrDIRYLKQLPVLGSGKPDFVTLKGMVEEAE 715
Cdd:PRK06178 521 AAALQAWCREN-MAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
320-703 |
1.35e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 320 HLPEQLTQVRWVFLEDLKADVttadkLWIFAhllmPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKT 399
Cdd:PRK12467 3201 HLLEQLPAPAGDTALTLDRLD-----LNGYS----ENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAE 3271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 400 IADFTANDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPL-----HYRivpeLVYDRNCTVLFGTSTFLGNYARFA 473
Cdd:PRK12467 3272 AYELDANDRVLLFMSF--SFDGAQeRFLWTLICGGCLVVRDNDLwdpeeLWQ----AIHAHRISIACFPPAYLQQFAEDA 3345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 474 NPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRIL-EGYGVTECAPVVSI-NVPMAAKPGT----VGRILPG-----LDA 542
Cdd:PRK12467 3346 GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLtNGYGPTEAVVTVTLwKCGGDAVCEApyapIGRPVAGrsiyvLDG 3425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 543 RLLAVP-GIedGGRLQLKGPNVMNGYLRveNPGVleapTAE-------NVNGEvetGWYDTGDIVRFDDQGFVQIQGRAK 614
Cdd:PRK12467 3426 QLNPVPvGV--AGELYIGGVGLARGYHQ--RPSL----TAErfvadpfSGSGG---RLYRTGDLARYRADGVIEYLGRID 3494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 615 RFAKIAGEMVSLEMVETLATAVSAEKmHATVVKSDASKGEALVLFTTDGELKRD--ALLRYAREHGIPELAVPRDIRYLK 692
Cdd:PRK12467 3495 HQVKIRGFRIELGEIEARLLQHPSVR-EAVVLARDGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLLVLA 3573
|
410
....*....|.
gi 1937565178 693 QLPVLGSGKPD 703
Cdd:PRK12467 3574 AMPLGPNGKVD 3584
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
334-701 |
1.59e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 98.73 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 334 EDLKADVTTADklwifAHLLMPRQAQvkqQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSAL 413
Cdd:PRK09088 112 EDLAAFIASAD-----ALEPADTPSI---PPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 414 PLFHSFGLTVGLFTPLLTGAEVFLYP----------------SPLHYRIVPELVydrnctvlfgtstflgnyARF-ANP- 475
Cdd:PRK09088 184 PMFHIIGLITSVRPVLAVGGSILVSNgfepkrtlgrlgdpalGITHYFCVPQMA------------------QAFrAQPg 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 476 YDFFRVRYVVA----GAEKLQDSTRQiWQDKfGLRILEGYGVTECAPVVSINVP---MAAKPGTVGRILPGLDARLLAVP 548
Cdd:PRK09088 246 FDAAALRHLTAlftgGAPHAAEDILG-WLDD-GIPMVDGFGMSEAGTVFGMSVDcdvIRAKAGAAGIPTPTVQTRVVDDQ 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 549 G--IEDG--GRLQLKGPNVMNGYLRveNPgvleAPTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMV 624
Cdd:PRK09088 324 GndCPAGvpGELLLRGPNLSPGYWR--RP----QATARAFTGD---GWFRTGDIARRDADGFFWVVDRKKDMFISGGENV 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 625 SLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTTDGElKRDALLRYAREHGIPELA---VPRDIRYLKQLPVLGSGK 701
Cdd:PRK09088 395 YPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD-GAPLDLERIRSHLSTRLAkykVPKHLRLVDALPRTASGK 473
|
|
| PlsC |
smart00563 |
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ... |
30-140 |
1.95e-21 |
|
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: 90.11 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 30 VLITPNHVSFLDGVLLALFLP---VRPVFAVYSSISEKWYMRWLKPLIDFVPLDPTKP----MMIKHLVRLIGQGRPVVI 102
Cdd:smart00563 1 ALVVANHQSFLDPLVLSALLPrklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGrkarAALREAVELLKEGEWLLI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1937565178 103 FPEGRISVTGSLMKIYDGAGFVAAKSQATVVPLRIDGA 140
Cdd:smart00563 81 FPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIRGT 118
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
365-612 |
4.06e-21 |
|
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: 97.15 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFhsfgltvGLFTPLLTGAEV-----FLYP 439
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPALGLTSVipdmdPTRP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPLHYRIVPELVYDRNCTVLFGTSTFLGNYARF--ANPYDFFRVRYVV-AGAE---KLQDSTRQIWQDkfGLRILEGYGV 513
Cdd:cd05910 158 ARADPQKLVGAIRQYGVSIVFGSPALLERVARYcaQHGITLPSLRRVLsAGAPvpiALAARLRKMLSD--EAEILTPYGA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 514 TECAPVVSI---------NVPMAAKPGT-VGRILPGLDARLLAV---PGIEDGGRLQL----------KGPNVMNGYLRV 570
Cdd:cd05910 236 TEALPVSSIgsrellattTAATSGGAGTcVGRPIPGVRVRIIEIddePIAEWDDTLELprgeigeitvTGPTVTPTYVNR 315
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1937565178 571 EnpgvlEAPTAENVNGEVETGWYDTGDIVRFDDQGFVQIQGR 612
Cdd:cd05910 316 P-----VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGR 352
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
363-703 |
6.02e-21 |
|
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: 96.63 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSP 441
Cdd:cd17655 135 KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASI--SFDASVTeIFASLLSGNTLYIVRKE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 LHYRIVPELVY--DRNCTVLFGTSTFLgNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGL--RILEGYGVTECA 517
Cdd:cd17655 213 TVLDGQALTQYirQNRITIIDLTPAHL-KLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 518 PVVSINV--PMAAKPGTV--GRILPG-----LDARLLAVP-GIEdgGRLQLKGPNVMNGYLRvenpgvLEAPTAEN-VNG 586
Cdd:cd17655 292 VDASIYQyePETDQQVSVpiGKPLGNtriyiLDQYGRPQPvGVA--GELYIGGEGVARGYLN------RPELTAEKfVDD 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 587 EVETG--WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEAL-VLFTTDG 663
Cdd:cd17655 364 PFVPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLcAYIVSEK 443
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1937565178 664 ELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17655 444 ELPVAQLREFLARE-LPDYMIPSYFIKLDEIPLTPNGKVD 482
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
365-701 |
9.15e-21 |
|
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: 94.25 E-value: 9.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSILANVEQI-KTIADFTANDRFMSALPLFHSFGLTVGLfTPLLTGAEVFLYPSPLH 443
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWIL-TCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 444 YRIVPELV--YDRNCTVLFGTS-TFLGNYARFANPYdFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVV 520
Cdd:cd17635 80 YKSLFKILttNAVTTTCLVPTLlSKLVSELKSANAT-VPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 521 SINVPMAAKP-GTVGRILPGLDARLLAVPGIE----DGGRLQLKGPNVMNGYLrvENPGVleapTAENVNGevetGWYDT 595
Cdd:cd17635 159 CLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAgpsaSFGTIWIKSPANMLGYW--NNPER----TAEVLID----GWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 596 GDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTTDGELKRDALLRYAR 675
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALK 308
|
330 340
....*....|....*....|....*....
gi 1937565178 676 EHGIPEL---AVPRDIRYLKQLPVLGSGK 701
Cdd:cd17635 309 HTIRRELepyARPSTIVIVTDIPRTQSGK 337
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
359-703 |
1.01e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.11 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 359 QVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPlFHSFGLTVGLFTPLLTGAEVFLY 438
Cdd:PRK12316 3190 AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLA 3268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 439 PSPLHY--RIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQdkFGLRILEGYGVTEC 516
Cdd:PRK12316 3269 GPEDWRdpALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEA 3346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 517 APVVSINVPMAAKPGT--VGRILPG-----LDARLLAVPgIEDGGRLQLKGPNVMNGYLrvENPGVLEAPTAENVNGEVE 589
Cdd:PRK12316 3347 TITVTHWQCVEEGKDAvpIGRPIANracyiLDGSLEPVP-VGALGELYLGGEGLARGYH--NRPGLTAERFVPDPFVPGE 3423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 590 TgWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlATAVSAEKMHATVVKSDASKGEALVLFTTDGELKRDA 669
Cdd:PRK12316 3424 R-LYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE--ARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLRE 3500
|
330 340 350
....*....|....*....|....*....|....
gi 1937565178 670 LLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK12316 3501 ALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLD 3534
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
343-707 |
1.03e-20 |
|
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: 95.86 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 343 ADKLWIFAHLLMPRQAQVKQQpeDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLT 422
Cdd:cd05920 119 PDRHAGFDHRALARELAESIP--EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 423 V-GLFTPLLTGAEVFLYPSPlhyriVPELVY---DR---NCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQDST 495
Cdd:cd05920 197 CpGVLGTLLAGGRVVLAPDP-----SPDAAFpliERegvTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPAL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 496 RQIWQDKFGLRILEGYGVTE---CapVVSINVPMAAKPGTVGR-ILPG-----LDARLLAVPGIEDGgRLQLKGPNVMNG 566
Cdd:cd05920 272 ARRVPPVLGCTLQQVFGMAEgllN--YTRLDDPDEVIIHTQGRpMSPDdeirvVDEEGNPVPPGEEG-ELLTRGPYTIRG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 567 YLRVEnpgvleaptAENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVV 646
Cdd:cd05920 349 YYRAP---------EHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVA 419
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937565178 647 KSDASKGEALVLFT--TDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPDFVTL 707
Cdd:cd05920 420 MPDELLGERSCAFVvlRDPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
359-717 |
1.21e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.11 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 359 QVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDR---FMSalplFHSFGLTVGLFTPLLTGAEV 435
Cdd:PRK12316 2140 AVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCelqFMS----FSFDGAHEQWFHPLLNGARV 2215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 FLYPSPLHyriVPELVYD----RNCTVLFGTSTFLGNYARFA----NPydfFRVRYVVAGAEKL-QDSTRQIWQDKFGLR 506
Cdd:PRK12316 2216 LIRDDELW---DPEQLYDemerHGVTILDFPPVYLQQLAEHAerdgRP---PAVRVYCFGGEAVpAASLRLAWEALRPVY 2289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 507 ILEGYGVTECAPVVSI-----NVPMAAKPGTVGRILPG-----LDARLLAVPgIEDGGRLQLKGPNVMNGYLrvENPGVl 576
Cdd:PRK12316 2290 LFNGYGPTEAVVTPLLwkcrpQDPCGAAYVPIGRALGNrrayiLDADLNLLA-PGMAGELYLGGEGLARGYL--NRPGL- 2365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 577 eapTAE--------NVNGEVetgwYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKmHATVVKS 648
Cdd:PRK12316 2366 ---TAErfvpdpfsASGERL----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVR-EAVVVAQ 2437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937565178 649 DASKGEALVLFTT--DGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPDFVTLKGMVEEAEQQ 717
Cdd:PRK12316 2438 DGASGKQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQ 2508
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
361-703 |
1.63e-20 |
|
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: 95.23 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 361 KQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTAND-RFMSALPLFHSFglTVGLFTPLLTGAeVFLYp 439
Cdd:cd17654 114 IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDiLFLTSPLTFDPS--VVEIFLSLSSGA-TLLI- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPLHYRIVPELVYD-----RNCTVLFGTSTFLgnyARFANPYDFFRV-------RYVVAGAEKL-QDSTRQIWQDKF-GL 505
Cdd:cd17654 190 VPTSVKVLPSKLADilfkrHRITVLQATPTLF---RRFGSQSIKSTVlsatsslRVLALGGEPFpSLVILSSWRGKGnRT 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 506 RILEGYGVTECAPVVSIN-VPMAAKPGTVGRILPGLDARLLAVPGIEDGGRLQLKGPNvmngylRVenpGVLEAPtaenv 584
Cdd:cd17654 267 RIFNIYGITEVSCWALAYkVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLN------RV---CILDDE----- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 585 NGEVETGWYDTGDIVRFDDqGFVQIQGRAKRFAKIAGEMVSLEMVETlaTAVSAEKMHATVVKsdASKGEALVLFTTdGE 664
Cdd:cd17654 333 VTVPKGTMRATGDFVTVKD-GELFFLGRKDSQIKRRGKRINLDLIQQ--VIESCLGVESCAVT--LSDQQRLIAFIV-GE 406
|
330 340 350
....*....|....*....|....*....|....*....
gi 1937565178 665 LKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17654 407 SSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVD 445
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
279-716 |
1.78e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 95.64 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 279 GRIPAMMNYTAGVKGLSSAITAAQiNTIFTsrqfLDKG-KLWHLPEQLTQ---VRW-VFLEDLK-------ADVTTADKL 346
Cdd:PLN02860 81 GGIVAPLNYRWSFEEAKSAMLLVR-PVMLV----TDETcSSWYEELQNDRlpsLMWqVFLESPSssvfiflNSFLTTEML 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 347 WifAHLLMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLf 426
Cdd:PLN02860 156 K--QRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 427 TPLLTGAEVFLYPSpLHYRIVPELVYDRNCTVLFGTSTFLGN---YARFANPYDFFR-VRYVVAGA----EKLQDSTRQI 498
Cdd:PLN02860 233 AMLMVGACHVLLPK-FDAKAALQAIKQHNVTSMITVPAMMADlisLTRKSMTWKVFPsVRKILNGGgslsSRLLPDAKKL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 499 WQDKfglRILEGYGVTE-CAPV--VSINVPMAAKP----GTVGRILPGLDARLLAV------PGIEDG---------GRL 556
Cdd:PLN02860 312 FPNA---KLFSAYGMTEaCSSLtfMTLHDPTLESPkqtlQTVNQTKSSSVHQPQGVcvgkpaPHVELKigldessrvGRI 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 557 QLKGPNVMNGY--LRVENPGVLeaptaenvngeVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlAT 634
Cdd:PLN02860 389 LTRGPHVMLGYwgQNSETASVL-----------SNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVE--AV 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 635 AVSAEKMHATVVKS--DASKGEALVLFTT--DG---------------ELKRDALLRYAREHGIPELAVPRDI-RYLKQL 694
Cdd:PLN02860 456 LSQHPGVASVVVVGvpDSRLTEMVVACVRlrDGwiwsdnekenakknlTLSSETLRHHCREKNLSRFKIPKLFvQWRKPF 535
|
490 500
....*....|....*....|..
gi 1937565178 695 PVLGSGKPDFVTLKGMVEEAEQ 716
Cdd:PLN02860 536 PLTTTGKIRRDEVRREVLSHLQ 557
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
359-703 |
1.87e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 97.15 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 359 QVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDrfmsALPLFHSFGLTV---GLFTPLLTGAEV 435
Cdd:PRK12467 1712 AVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD----VVLQFTSFAFDVsvwELFWPLINGARL 1787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 FLYPSPLHYRivPELVYDRNC----TVLFGTSTFLGNYARFANPYDFFR-VRYVVAGAEKLQDSTRQIWQDKFGLR-ILE 509
Cdd:PRK12467 1788 VIAPPGAHRD--PEQLIQLIErqqvTTLHFVPSMLQQLLQMDEQVEHPLsLRRVVCGGEALEVEALRPWLERLPDTgLFN 1865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 510 GYGVTECA----------------PVVSINVPMAAKPGTVgrilpgLDARLLAVPgIEDGGRLQLKGPNVMNGYLRveNP 573
Cdd:PRK12467 1866 LYGPTETAvdvthwtcrrkdlegrDSVPIGQPIANLSTYI------LDASLNPVP-IGVAGELYLGGVGLARGYLN--RP 1936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 574 GVleapTAE----NVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVET--LATAVSAEkmhATVVK 647
Cdd:PRK12467 1937 AL----TAErfvaDPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEArlREQGGVRE---AVVIA 2009
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 648 SDASKGEALVLFTT-------DGELKRDALLRYAREH---GIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK12467 2010 QDGANGKQLVAYVVptdpglvDDDEAQVALRAILKNHlkaSLPEYMVPAHLVFLARMPLTPNGKLD 2075
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
355-703 |
2.50e-20 |
|
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: 94.67 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTV-GLFTPLLTGA 433
Cdd:cd12116 116 PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTY--AFDISLlELLLPLLAGA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 434 EVFLYPSPLHY--RIVPELVYDRNCTVLFGTST----FLGNYARFANpydffRVRYVVAG-------AEKLQDSTRQIWQ 500
Cdd:cd12116 194 RVVIAPRETQRdpEALARLIEAHSITVMQATPAtwrmLLDAGWQGRA-----GLTALCGGealppdlAARLLSRVGSLWN 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 501 dkfglrileGYGVTE------CAPVVSinvpmAAKPGTVGRILPG-----LDARLLAVP-GIEdgGRLQLKGPNVMNGYL 568
Cdd:cd12116 269 ---------LYGPTEttiwstAARVTA-----AAGPIPIGRPLANtqvyvLDAALRPVPpGVP--GELYIGGDGVAQGYL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 569 RveNPGVLEAPTAENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKS 648
Cdd:cd12116 333 G--RPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRE 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937565178 649 DASKGE--ALVLFTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd12116 411 DGGDRRlvAYVVLKAGAAPDAAALRAHLRAT-LPAYMVPSAFVRLDALPLTANGKLD 466
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
364-701 |
4.73e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 93.87 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDD-AIILFTSGSEGNPKGVVHSHK----SILANVEQIktiaDFTANDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLY 438
Cdd:PRK03640 139 DLDEvATIMYTSGTTGKPKGVIQTYGnhwwSAVGSALNL----GLTEDDCWLAAVPIFHISGLSI-LMRSVIYGMRVVLV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 439 PsplHYRI--VPELVYDRNCTVLFGTSTFL---------GNYarfanPYDFfrvRYVVAGAEKLQDSTRQIWQDKfGLRI 507
Cdd:PRK03640 214 E---KFDAekINKLLQTGGVTIISVVSTMLqrllerlgeGTY-----PSSF---RCMLLGGGPAPKPLLEQCKEK-GIPV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 508 LEGYGVTE-CAPVVSINvP--MAAKPGTVGRilPGLDARLlavpGIEDGGRLQ---------LKGPNVMNGYLRvenpgv 575
Cdd:PRK03640 282 YQSYGMTEtASQIVTLS-PedALTKLGSAGK--PLFPCEL----KIEKDGVVVppfeegeivVKGPNVTKGYLN------ 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 576 LEAPTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEA 655
Cdd:PRK03640 349 REDATRETFQD----GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQV 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1937565178 656 LVLF-TTDGELKRDALLRYAREHgipeLA---VPRDIRYLKQLPVLGSGK 701
Cdd:PRK03640 425 PVAFvVKSGEVTEEELRHFCEEK----LAkykVPKRFYFVEELPRNASGK 470
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
355-701 |
6.73e-20 |
|
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: 93.71 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
Cdd:cd05970 175 RPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 435 VFLYPsplHYRIVPELVYDRncTVLFGTSTFLG--NYARF-----ANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRI 507
Cdd:cd05970 255 VFVYD---YDKFDPKALLEK--LSKYGVTTFCAppTIYRFliredLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 508 LEGYGVTECapVVSI-NVP-MAAKPGTVGRILPGLDARLL-----AVPGIEDGG---RLQLKGP-NVMNGYLRvenpgvl 576
Cdd:cd05970 330 MEGFGQTET--TLTIaTFPwMEPKPGSMGKPAPGYEIDLIdregrSCEAGEEGEiviRTSKGKPvGLFGGYYK------- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 577 eapTAENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlatavSAEKMHATVVKS------DA 650
Cdd:cd05970 401 ---DAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE------SALIQHPAVLECavtgvpDP 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937565178 651 SKGEA----LVL---FTTDGELKRDaLLRYAREHGIPELAvPRDIRYLKQLPVLGSGK 701
Cdd:cd05970 472 IRGQVvkatIVLakgYEPSEELKKE-LQDHVKKVTAPYKY-PRIVEFVDELPKTISGK 527
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
357-630 |
6.75e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 94.40 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 357 QAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFH-----------SFGLTVGL 425
Cdd:PLN02736 213 QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyervnqivmlHYGVAVGF 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 426 FT----PLLTGAEVFlypSPLHYRIVPEL---VYDRnCTVLFGTSTFLG--------NYARFA-----NPYDFF------ 479
Cdd:PLN02736 293 YQgdnlKLMDDLAAL---RPTIFCSVPRLynrIYDG-ITNAVKESGGLKerlfnaayNAKKQAlengkNPSPMWdrlvfn 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 480 --------RVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAVPGI- 550
Cdd:PLN02736 369 kikaklggRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMn 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 551 ---EDG----GRLQLKGPNVMNGYLRVenpgvlEAPTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA-GE 622
Cdd:PLN02736 449 ytsEDQpyprGEICVRGPIIFKGYYKD------EVQTREVIDED---GWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGE 519
|
....*...
gi 1937565178 623 MVSLEMVE 630
Cdd:PLN02736 520 YIAPEKIE 527
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
366-703 |
8.85e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.41 E-value: 8.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 366 DDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsPLHYR 445
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLL---PARGR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 446 IVPELVYD--RNCTVLFGTST------FLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECA 517
Cdd:PRK05852 254 FSAHTFWDdiKAVGATWYTAVptihqiLLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 518 -PVVSINVPMA-------AKPGTVGRIlPGLDARLLAVPGIEDG----GRLQLKGPNVMNGYLrvENPGVleapTAENVN 585
Cdd:PRK05852 334 hQVTTTQIEGIgqtenpvVSTGLVGRS-TGAQIRIVGSDGLPLPagavGEVWLRGTTVVRGYL--GDPTI----TAANFT 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 586 geveTGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTD 662
Cdd:PRK05852 407 ----DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEavaAVIVPRES 482
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1937565178 663 GELKRDALLRYAREhGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK05852 483 APPTAEELVQFCRE-RLAAFEIPASFQEASGLPHTAKGSLD 522
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
365-701 |
1.55e-19 |
|
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: 92.36 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIIL-FTSGSEGNPKGVVHSHKSilANVEQIKTIADFTANDR--FMSALPLFHSFGLTVGLFTPLLTGAEVFL--YP 439
Cdd:cd12118 132 EWDPIALnYTSGTTGRPKGVVYHHRG--AYLNALANILEWEMKQHpvYLWTLPMFHCNGWCFPWTVAAVGGTNVCLrkVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPLHYRivpeLVYDRNCTVLFGTSTFLGNYA----RFANPYDFfRVRYVVAGA-------EKLQdstrqiwqdKFGLRIL 508
Cdd:cd12118 210 AKAIYD----LIEKHKVTHFCGAPTVLNMLAnappSDARPLPH-RVHVMTAGApppaavlAKME---------ELGFDVT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 509 EGYGVTECAPVVSINV--------P------MAAKPGTVGRILPGLDAR----LLAVPGieDG---GRLQLKGPNVMNGY 567
Cdd:cd12118 276 HVYGLTETYGPATVCAwkpewdelPteerarLKARQGVRYVGLEEVDVLdpetMKPVPR--DGktiGEIVFRGNIVMKGY 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 568 LRveNPgvlEApTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVK 647
Cdd:cd12118 354 LK--NP---EA-TAEAFRG----GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVAR 423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937565178 648 SDASKGEALVLFTT---DGELKRDALLRYAREHgIPELAVPRDIRYLkQLPVLGSGK 701
Cdd:cd12118 424 PDEKWGEVPCAFVElkeGAKVTEEEIIAFCREH-LAGFMVPKTVVFG-ELPKTSTGK 478
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
350-701 |
1.78e-19 |
|
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: 91.81 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 350 AHLLMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPL 429
Cdd:cd05973 73 ARLVVTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 430 LTGAEVFLYPSPLhyriVPELVYDrnCTVLFGTSTFLGNYARF---------ANPYDFFRVRYVVAGAEKLQDSTRQIWQ 500
Cdd:cd05973 153 ALGHPTILLEGGF----SVESTWR--VIERLGVTNLAGSPTAYrllmaagaeVPARPKGRLRRVSSAGEPLTPEVIRWFD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 501 DKFGLRILEGYGVTECAPVVSiNVPMAAKP---GTVGRILPGLDARLLAVPGIEDG----GRLQLKGPNV----MNGYLR 569
Cdd:cd05973 227 AALGVPIHDHYGQTELGMVLA-NHHALEHPvhaGSAGRAMPGWRVAVLDDDGDELGpgepGRLAIDIANSplmwFRGYQL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 570 VENPgvleaptaenvngEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSD 649
Cdd:cd05973 306 PDTP-------------AIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPD 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937565178 650 ASKGEALVLFT-----TDG------ELKRDALLRYAREhgipelAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05973 373 PERTEVVKAFVvlrggHEGtpaladELQLHVKKRLSAH------AYPRTIHFVDELPKTPSGK 429
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
363-703 |
2.06e-19 |
|
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: 91.73 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFLYP 439
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVL----QFASIAFDVAaeeIYVTLLSGATLVLRP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPLHYRIVPELVY--DRNCTVLFGTSTFL------GNYARFANPYdffRVRYVVAGAEKLQDSTRQIWQDKFGLRI--LE 509
Cdd:cd17644 180 EEMRSSLEDFVQYiqQWQLTVLSLPPAYWhllvleLLLSTIDLPS---SLRLVIVGGEAVQPELVRQWQKNVGNFIqlIN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 510 GYGVTEC---APVVSINVPMAAKPG--TVGRILPG-----LDARLLAVPgIEDGGRLQLKGPNVMNGYL-RVEnpgvlea 578
Cdd:cd17644 257 VYGPTEAtiaATVCRLTQLTERNITsvPIGRPIANtqvyiLDENLQPVP-VGVPGELHIGGVGLARGYLnRPE------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 579 PTAENV-----NGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKG 653
Cdd:cd17644 329 LTAEKFishpfNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGN 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1937565178 654 EALVLFTTdGELKRDAL---LRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17644 409 KRLVAYIV-PHYEESPStveLRQFLKAKLPDYMIPSAFVVLEELPLTPNGKID 460
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
328-714 |
3.16e-19 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 91.75 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 328 VRWVF-----LEDLKA--------DVTTAdklwifAHllMPRQAQVKQQP-EDDAIILFTSGSEGNPKGVVHSHKSILAN 393
Cdd:PRK05851 109 VRTVLshgshLERLRAvdssvtvhDLATA------AH--TNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 394 VEQIKTIADFT-ANDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYP------SPLH-----------YRIVPELVYDrn 455
Cdd:PRK05851 181 LRGLNARVGLDaATDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPttafsaSPFRwlswlsdsratLTAAPNFAYN-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 456 ctvlfgtstFLGNYARFANPYDFFRVRYVVAGAEKLQ-DSTRQIWQD--KFGLR---ILEGYGVTECAPVVSINVP---- 525
Cdd:PRK05851 258 ---------LIGKYARRVSDVDLGALRVALNGGEPVDcDGFERFATAmaPFGFDagaAAPSYGLAESTCAVTVPVPgigl 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 526 -----------MAAKPGTVGRILPGLDARLlaVPGIEDG-------GRLQLKGPNVMNGYLRvenpgvlEAPTAENvnge 587
Cdd:PRK05851 329 rvdevttddgsGARRHAVLGNPIPGMEVRI--SPGDGAAgvagreiGEIEIRGASMMSGYLG-------QAPIDPD---- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 588 vetGWYDTGDIVRFDDQGFVqIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVV--KSDASKGEALVLFT----T 661
Cdd:PRK05851 396 ---DWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvgTGEGSARPGLVIAAefrgP 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 662 DGELKRDALL-RYAREHGIpelaVPRDIRYLK--QLPVLGSGKPDFVTLKGMVEEA 714
Cdd:PRK05851 472 DEAGARSEVVqRVASECGV----VPSDVVFVApgSLPRTSSGKLRRLAVKRSLEAA 523
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
253-694 |
1.28e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.93 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 253 KQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKgkLWHLPEQLTQVR--W 330
Cdd:PRK08279 85 GKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEA--FEEARADLARPPrlW 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 331 VFLEDLKADVTTADKLWIFAHLLMPRQAQVKQ--QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDR 408
Cdd:PRK08279 163 VAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSgvTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 409 FMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyrivpelvydrnctvlFGTSTFLGNYARFaNPYDFFRV----RYV 484
Cdd:PRK08279 243 LYCCLPLYHNTGGTVAWSSVLAAGATLALRRK-------------------FSASRFWDDVRRY-RATAFQYIgelcRYL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 485 VAGAEKLQDS------------TRQIW---QDKFGL-RILEGYGVTEcAPVVSINVpmAAKPGTVGRILPGL-------- 540
Cdd:PRK08279 303 LNQPPKPTDRdhrlrlmignglRPDIWdefQQRFGIpRILEFYAASE-GNVGFINV--FNFDGTVGRVPLWLahpyaivk 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 541 ------------DARLLAVPGIEDG---GRLQLKGPnvMNGYLrveNPGVLEAPTAENV--NGEVetgWYDTGDIVRFDD 603
Cdd:PRK08279 380 ydvdtgepvrdaDGRCIKVKPGEVGlliGRITDRGP--FDGYT---DPEASEKKILRDVfkKGDA---WFNTGDLMRDDG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 604 QGFVQIQGRA------KrfakiaGEMVSL-EMVETLATAVSAEkmHATV--VK---SDASKGEALVLFTTDGELKRDALL 671
Cdd:PRK08279 452 FGHAQFVDRLgdtfrwK------GENVATtEVENALSGFPGVE--EAVVygVEvpgTDGRAGMAAIVLADGAEFDLAALA 523
|
490 500
....*....|....*....|...
gi 1937565178 672 RYAREHgIPELAVPRDIRYLKQL 694
Cdd:PRK08279 524 AHLYER-LPAYAVPLFVRLVPEL 545
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
253-695 |
1.97e-18 |
|
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: 89.47 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 253 KQGEKIGLMLPnAGISAAVIFGAVSR-GRI--PAMMNYtaGVKGLSSAITAAQINTIFTSRQFLDKGKLWHLPE------ 323
Cdd:cd05968 114 GKGDRVGIYLP-MIPEIVPAFLAVARiGGIvvPIFSGF--GKEAAATRLQDAEAKALITADGFTRRGREVNLKEeadkac 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 324 -QLTQVRWVFLE-DLKADVTTADKLWIFAHLLM--PRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSI-LANVEQIK 398
Cdd:cd05968 191 aQCPTVEKVVVVrHLGNDFTPAKGRDLSYDEEKetAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMY 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 399 TIADFTANDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFLYPS----PLHYRIVpELVYDRNCTVLfGTS-----TFL 466
Cdd:cd05968 271 FQFDLKPGDLLT----WFTDLGWMMGpwlIFGGLILGATMVLYDGapdhPKADRLW-RMVEDHEITHL-GLSptlirALK 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 467 GNYARFANPYDFFRVRYVVAGAEKLQ-DSTRQIWQDKFGLR--ILEGYGVTECAPVVSINVPMAA-KPGTVGRILPGLDA 542
Cdd:cd05968 345 PRGDAPVNAHDLSSLRVLGSTGEPWNpEPWNWLFETVGKGRnpIINYSGGTEISGGILGNVLIKPiKPSSFNGPVPGMKA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 543 RLL---AVPGIEDGGRLQLKGP--NVMNGYLRVENPGVleaptaENVNGEVETGWYDtGDIVRFDDQGFVQIQGRAKRFA 617
Cdd:cd05968 425 DVLdesGKPARPEVGELVLLAPwpGMTRGFWRDEDRYL------ETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTI 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 618 KIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLF-------TTDGELKRDALLRYAREHGIPelAVPRDIRY 690
Cdd:cd05968 498 NVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFvvlkpgvTPTEALAEELMERVADELGKP--LSPERILF 575
|
....*
gi 1937565178 691 LKQLP 695
Cdd:cd05968 576 VKDLP 580
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
233-695 |
3.78e-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: 87.95 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTK-TLFVGRILEKYSKQGEKIGLMLPNAgISAAVIFGAVSR-GRIPAMMNYTAGVKGLSSAITAAQINTIFTSr 310
Cdd:cd05923 30 TYSELRARiEAVAARLHARGLRPGQRVAVVLPNS-VEAVIALLALHRlGAVPALINPRLKAAELAELIERGEMTAAVIA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 311 qfLDKGklwhlPEQLTQVRWVFLEDLKADVTTADkLWIFAHLLMPRQaqvkQQPEDDAIILFTSGSEGNPKGVVHSHKSI 390
Cdd:cd05923 108 --VDAQ-----VMDAIFQSGVRVLALSDLVGLGE-PESAGPLIEDPP----REPEQPAFVFYTSGTTGLPKGAVIPQRAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 391 LANVEQIKTIAD--FTANDRFMSALPLFHSFGLtVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTF--- 465
Cdd:cd05923 176 ESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGF-FAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHlda 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 466 LGNYARFAnPYDFFRVRYVV-AGAEKLQDSTRQIWQDKFGlRILEGYGVTEcapVVSINVPMAAKPGTVGRilPGLDARL 544
Cdd:cd05923 255 LAAAAEFA-GLKLSSLRHVTfAGATMPDAVLERVNQHLPG-EKVNIYGTTE---AMNSLYMRDARTGTEMR--PGFFSEV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 545 LAVPgieDGGRLQLKGPNVMNGYLRVENP------GVLEAPTAENVNgeVETGWYDTGDIVRFDDQGFVQIQGRAKRFAK 618
Cdd:cd05923 328 RIVR---IGGSPDEALANGEEGELIVAAAadaaftGYLNQPEATAKK--LQDGWYRTGDVGYVDPSGDVRILGRVDDMII 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937565178 619 IAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFT--TDGELKRDALLRYAREHGIPELAVPRDIRYLKQLP 695
Cdd:cd05923 403 SGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVvpREGTLSADELDQFCRASELADFKRPRRYFFLDELP 481
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
361-659 |
3.95e-18 |
|
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: 87.93 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 361 KQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
Cdd:cd05908 102 CELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 441 PLHYRiVPEL----VYDRNCTVL----FGTSTFLGNY-ARFANPYDFFRVRYVVAGAEKLQDSTRQIWQD---KFGLR-- 506
Cdd:cd05908 182 RLFIR-RPILwlkkASEHKATIVsspnFGYKYFLKTLkPEKANDWDLSSIRMILNGAEPIDYELCHEFLDhmsKYGLKrn 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 507 -ILEGYGVTECApvVSINVPMAAKPGT------------------------------VGRILPGLDARLL--AVPGIEDG 553
Cdd:cd05908 261 aILPVYGLAEAS--VGASLPKAQSPFKtitlgrrhvthgepepevdkkdsecltfveVGKPIDETDIRICdeDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 554 --GRLQLKGPNVMNGYLrvENPgvleaptAENVNGEVETGWYDTGdivrfdDQGFVQ-----IQGRAKRFAKIAGEMVSL 626
Cdd:cd05908 339 yiGHIQIRGKNVTPGYY--NNP-------EATAKVFTDDGWLKTG------DLGFIRngrlvITGREKDIIFVNGQNVYP 403
|
330 340 350
....*....|....*....|....*....|....*.
gi 1937565178 627 EMVETLATAVSAE---KMHATVVKSDASKGEALVLF 659
Cdd:cd05908 404 HDIERIAEELEGVelgRVVACGVNNSNTRNEEIFCF 439
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
253-701 |
5.84e-18 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 87.98 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 253 KQGEKIGLMLPNAgISAAVIFGAV-SRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKGKLWHLPEQLTQVRWV 331
Cdd:PLN02574 90 RQGDVVLLLLPNS-VYFPVIFLAVlSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 332 FlEDLKADVTTADKLWIFAHLLMPRQAqVKQQpeDDAIILFTSGSEGNPKGVVHSHKSILANVEqikTIADFTA------ 405
Cdd:PLN02574 169 F-DSKRIEFPKFYELIKEDFDFVPKPV-IKQD--DVAAIMYSSGTTGASKGVVLTHRNLIAMVE---LFVRFEAsqyeyp 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 406 --NDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP--------------SPLHYRIVPELVydrnctvlfgtsTFLGNY 469
Cdd:PLN02574 242 gsDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRrfdasdmvkvidrfKVTHFPVVPPIL------------MALTKK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 470 ARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFG-LRILEGYGVTECAPVVS--INVPMAAKPGTVGRILPGLDARL-- 544
Cdd:PLN02574 310 AKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPhVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVvd 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 545 -----LAVPGieDGGRLQLKGPNVMNGYLrvenpgVLEAPTAENVngeVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKI 619
Cdd:PLN02574 390 wstgcLLPPG--NCGELWIQGPGVMKGYL------NNPKATQSTI---DKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 620 AG--------EMVSLEMVETLATAVSAekmhatvvKSDASKGE---ALVLFTTDGELKRDALLRYAREHGIPELAVpRDI 688
Cdd:PLN02574 459 KGfqiapadlEAVLISHPEIIDAAVTA--------VPDKECGEipvAFVVRRQGSTLSQEAVINYVAKQVAPYKKV-RKV 529
|
490
....*....|...
gi 1937565178 689 RYLKQLPVLGSGK 701
Cdd:PLN02574 530 VFVQSIPKSPAGK 542
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
363-703 |
7.11e-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: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSalplFHSFGLTVG---LFTPLLTGAEVFLYP 439
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQ----FASPSFDASvweLLMALLAGATLVLAP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SplhYRIVP-----ELVYDRNCTVLFGTSTFLGNYArfanPYDFFRVRYVVAGAEKLQDSTRQIWQDkfGLRILEGYGVT 514
Cdd:cd17652 167 A---EELLPgeplaDLLREHRITHVTLPPAALAALP----PDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 515 ECAPVVSINVPMAAKPG-TVGRILPG-----LDARLLAVPgIEDGGRLQLKGPNVMNGYLRveNPGVleapTAE----NV 584
Cdd:cd17652 238 ETTVCATMAGPLPGGGVpPIGRPVPGtrvyvLDARLRPVP-PGVPGELYIAGAGLARGYLN--RPGL----TAErfvaDP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 585 NGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTT--- 661
Cdd:cd17652 311 FGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVpap 390
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1937565178 662 DGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17652 391 GAAPTAAELRAHLAER-LPGYMVPAAFVVLDALPLTPNGKLD 431
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
364-713 |
9.33e-18 |
|
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: 87.12 E-value: 9.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTV-GLFTPLLTGAEVFL--YPS 440
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTVVLapDPS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 441 PLH-------YRI-----VPELVydrnctvlfgtSTFLgNYARFAnPYDFFRVRYVVAGAEKLQDST-RQIwQDKFGLRI 507
Cdd:COG1021 263 PDTafplierERVtvtalVPPLA-----------LLWL-DAAERS-RYDLSSLRVLQVGGAKLSPELaRRV-RPALGCTL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 508 LEGYGVTE---CapVVSINVPMAAKPGTVGR-ILPGLDARLLAVPGIE--DG--GRLQLKGPNVMNGYLRvenpgvleap 579
Cdd:COG1021 329 QQVFGMAEglvN--YTRLDDPEEVILTTQGRpISPDDEVRIVDEDGNPvpPGevGELLTRGPYTIRGYYR---------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 580 tAENVNGEVET--GWYDTGDIVRFDDQGFVQIQGRAK----RfakiAGEMVSLEMVETLATA---VSaekmHATVVK-SD 649
Cdd:COG1021 397 -APEHNARAFTpdGFYRTGDLVRRTPDGYLVVEGRAKdqinR----GGEKIAAEEVENLLLAhpaVH----DAAVVAmPD 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 650 ASKGEALVLF--TTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPDFVTLKGMVEE 713
Cdd:COG1021 468 EYLGERSCAFvvPRGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
233-716 |
1.18e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 86.37 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRILEKYSKQGEKIGLMLPNaGISAAVIF-GAVSRG--RIPAMMNYTAgvKGLSSAITAAQINTIFTS 309
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKESKNKTIAILLEN-RIEFLQLFaGAAMAGwtCVPLDIKWKQ--DELKERLAISNADMIVTE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 310 RQFLDKgklwhLPEQLTQVrwVFLEDLKADVTTAdklwifahllMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKS 389
Cdd:PRK07638 105 RYKLND-----LPDEEGRV--IEIDEWKRMIEKY----------LPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 390 ILANVEqiKTIADF--TANDRFMSALPLFHSFGLtVGLFTPLLTGAEVFLYPsplhyRIVPELVYDR----NCTVLFGTS 463
Cdd:PRK07638 168 WLHSFD--CNVHDFhmKREDSVLIAGTLVHSLFL-YGAISTLYVGQTVHLMR-----KFIPNQVLDKleteNISVMYTVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 464 TFLGNYARfANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECApVVSINVP--MAAKPGTVGRILPGLD 541
Cdd:PRK07638 240 TMLESLYK-ENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELS-FVTALVDeeSERRPNSVGRPFHNVQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 542 ARLLAVPGIE----DGGRLQLKGPNVMNGYlrvenpgVLEAPTAENVNgevETGWYDTGDIVRFDDQGFVQIQGRAKRFA 617
Cdd:PRK07638 318 VRICNEAGEEvqkgEIGTVYVKSPQFFMGY-------IIGGVLARELN---ADGWMTVRDVGYEDEEGFIYIVGREKNMI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 618 KIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFtTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVL 697
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAI-IKGSATKQQLKSFCLQR-LSSFKIPKEWHFVDEIPYT 465
|
490
....*....|....*....
gi 1937565178 698 GSGKPDFVTLKGMVEEAEQ 716
Cdd:PRK07638 466 NSGKIARMEAKSWIENQEK 484
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
355-703 |
1.78e-17 |
|
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: 85.79 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSilanveQIKTIADF------TANDRFMSALPLfhSFGLTV-GLFT 427
Cdd:cd12114 116 APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRA------ALNTILDInrrfavGPDDRVLALSSL--SFDLSVyDIFG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 428 PLLTGAEVFLyPSPLHYRIV---PELVYDRNCTV------LFGtstFLGNYARfANPYDFFRVRYVVAG----AEKLQDS 494
Cdd:cd12114 188 ALSAGATLVL-PDEARRRDPahwAELIERHGVTLwnsvpaLLE---MLLDVLE-AAQALLPSLRLVLLSgdwiPLDLPAR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 495 TRQIWQDkfgLRILEGYGVTEcAPVVSI-----NVPMAAKPGTVGRILPG-----LDARLLAVPgieDG--GRLQLKGPN 562
Cdd:cd12114 263 LRALAPD---ARLISLGGATE-ASIWSIyhpidEVPPDWRSIPYGRPLANqryrvLDPRGRDCP---DWvpGELWIGGRG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 563 VMNGYLRveNPGVLEAPTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlATAVSAEKMH 642
Cdd:cd12114 336 VALGYLG--DPELTAARFVTHPDGE---RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIE--AALQAHPGVA 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937565178 643 ATVVKSDASKGEA-LVLF-------TTDGElkrDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd12114 409 RAVVVVLGDPGGKrLAAFvvpdndgTPIAP---DALRAFLAQT-LPAYMIPSRVIALEALPLTANGKVD 473
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
363-703 |
1.81e-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: 85.45 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKtiADFTANDR--FMSALPLfhSFGLTV-GLFTPLLTGAEVFLYP 439
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAA--AAFSAEELagVLASTSI--CFDLSVfELFGPLATGGKVVLAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SPLHYRIVPEL--VYDRNcTVLFGTSTFLGNYARFANpydffrVRYVVAGAEKL-QDSTRQIWQDKFGLRILEGYGVTE- 515
Cdd:cd12115 179 NVLALPDLPAAaeVTLIN-TVPSAAAELLRHDALPAS------VRVVNLAGEPLpRDLVQRLYARLQVERVVNLYGPSEd 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 516 -----CAPVVsinvPMAAKPGTVGRILPG-----LDARLLAVPgieDG--GRLQLKGPNVMNGYLRveNPGVleapTAEN 583
Cdd:cd12115 252 ttystVAPVP----PGASGEVSIGRPLANtqayvLDRALQPVP---LGvpGELYIGGAGVARGYLG--RPGL----TAER 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 584 --VNGEVETGW-YDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFT 660
Cdd:cd12115 319 flPDPFGPGARlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYI 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1937565178 661 T---DGELKRDALLRYAReHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd12115 399 VaepGAAGLVEDLRRHLG-TRLPAYMVPSRFVRLDALPLTPNGKID 443
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
364-701 |
2.77e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 85.60 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDD-AIILFTSGSEGNPKGVVHSHKSILAN-VEQIKTIADFTANDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYPSP 441
Cdd:PRK07786 172 PNDSpALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIYPLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 lhyRIVPELVYDrnctVLFG---TSTFLGNY-------ARFANPYDFfRVRYVVAGAEKLQDSTRQIWQDKF-GLRILEG 510
Cdd:PRK07786 251 ---AFDPGQLLD----VLEAekvTGIFLVPAqwqavcaEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFpEAQILAA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 511 YGVTECAPVVSINVPMAA--KPGTVGRILPGLDARLLA-----VPgIEDGGRLQLKGPNVMNGYLRveNPgvleAPTAEN 583
Cdd:PRK07786 323 FGQTEMSPVTCMLLGEDAirKLGSVGKVIPTVAARVVDenmndVP-VGEVGEIVYRAPTLMSGYWN--NP----EATAEA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 584 VNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFT 660
Cdd:PRK07786 396 FAG----GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEvpvAVAAVR 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1937565178 661 TDG---------ELKRDALLRYARehgipelavPRDIRYLKQLPVLGSGK 701
Cdd:PRK07786 472 NDDaaltledlaEFLTDRLARYKH---------PKALEIVDALPRNPAGK 512
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
233-708 |
3.06e-17 |
|
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: 85.10 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRILEKYS-KQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLssaitaaqintiftsrq 311
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGlKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESL----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 312 fldkgklwhlpeqltqvrwvfledlkadvttadklwifAHLLmpRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSIL 391
Cdd:cd05940 68 --------------------------------------AHCL--NVSSAKHLVVDAALYIYTSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 392 --ANVEQIKTIAdfTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVyDRNCTVLfgtsTFLGNY 469
Cdd:cd05940 108 rgGAFFAGSGGA--LPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIR-KYQATIF----QYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 470 ARF-----ANPYD-FFRVRyVVAGAEKLQDstrqIW---QDKFGL-RILEGYGVTECApVVSINVPmaAKPGTVGRILPG 539
Cdd:cd05940 181 CRYllnqpPKPTErKHKVR-MIFGNGLRPD----IWeefKERFGVpRIAEFYAATEGN-SGFINFF--GKPGAIGRNPSL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 540 L----------------------DARLLAVPGIEDG---GRLQLKGPnvMNGYLrveNPGVLEAPTAENV--NGEVetgW 592
Cdd:cd05940 253 LrkvaplalvkydlesgepirdaEGRCIKVPRGEPGlliSRINPLEP--FDGYT---DPAATEKKILRDVfkKGDA---W 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 593 YDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlATAVSAEKMHATVV------KSDASKGEALVLFTTDGELK 666
Cdd:cd05940 325 FNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVA--AVLGAFPGVEEANVygvqvpGTDGRAGMAAIVLQPNEEFD 402
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1937565178 667 RDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPDFVTLK 708
Cdd:cd05940 403 LSALAAHLEKN-LPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
255-635 |
3.06e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 85.60 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 255 GEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQflDKGKLWHLPEQLTQVRWV-FL 333
Cdd:PRK05620 64 DQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR--LAEQLGEILKECPCVRAVvFI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 334 EDLKADVTTAD-----KLWIFAHLLMPRQAQVK--QQPEDDAI-ILFTSGSEGNPKGVVHSHKSILANVEQIKTIADF-- 403
Cdd:PRK05620 142 GPSDADSAAAHmpegiKVYSYEALLDGRSTVYDwpELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLav 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 404 TANDRFMSALPLFH--SFGLTVGLF---TPL-LTGAEVflypSPLHYRIVPELVYDRnctVLFGTST----FLGNYARfa 473
Cdd:PRK05620 222 THGESFLCCVPIYHvlSWGVPLAAFmsgTPLvFPGPDL----SAPTLAKIIATAMPR---VAHGVPTlwiqLMVHYLK-- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 474 NPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTV--------GRILPGLDARLl 545
Cdd:PRK05620 293 NPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEArwayrvsqGRFPASLEYRI- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 546 avpgIEDG----------GRLQLKGPNVMNGYLrvENPGVLEAPTAENVNGE---------VETGWYDTGDIVRFDDQGF 606
Cdd:PRK05620 372 ----VNDGqvmestdrneGEIQVRGNWVTASYY--HSPTEEGGGAASTFRGEdvedandrfTADGWLRTGDVGSVTRDGF 445
|
410 420
....*....|....*....|....*....
gi 1937565178 607 VQIQGRAKRFAKIAGEMVSLEMVETLATA 635
Cdd:PRK05620 446 LTIHDRARDVIRSGGEWIYSAQLENYIMA 474
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
363-605 |
3.76e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.34 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFhsfgltvGLFTPLLTGAEvflypspl 442
Cdd:PRK09274 172 APDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF-------ALFGPALGMTS-------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 443 hyrIVPEL----------------VYDRNCTVLFGTSTFLGNYARF--ANPYDFFRVRYV-VAGA-------EKLqdstR 496
Cdd:PRK09274 237 ---VIPDMdptrpatvdpaklfaaIERYGVTNLFGSPALLERLGRYgeANGIKLPSLRRViSAGApvpiaviERF----R 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 497 QIWQDkfGLRILEGYGVTECAPVVSI--------NVPMAAK-PGT-VGRILPGLDARLLAV-----PGIEDGGRLQ---- 557
Cdd:PRK09274 310 AMLPP--DAEILTPYGATEALPISSIesreilfaTRAATDNgAGIcVGRPVDGVEVRIIAIsdapiPEWDDALRLAtgei 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1937565178 558 ----LKGPNVMNGYlrVENPgvlEApTAENVNGEVETG-WYDTGDIVRFDDQG 605
Cdd:PRK09274 388 geivVAGPMVTRSY--YNRP---EA-TRLAKIPDGQGDvWHRMGDLGYLDAQG 434
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
360-701 |
4.85e-17 |
|
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: 84.82 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 360 VKQQPEDDAIILFTSGSEGNPKGVVHSHKSI-LANVEQIKTIADFTANDRF--MSALPLFHSFGLTVglFTPLLTGAEVF 436
Cdd:cd05928 169 VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMwnTSDTGWIKSAWSSL--FEPWIQGACVF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 437 LYPSPlhyRIVPELVYDR----NCTVLFGTST-----FLGNYARfanpYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRI 507
Cdd:cd05928 247 VHHLP---RFDPLVILKTlssyPITTFCGAPTvyrmlVQQDLSS----YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 508 LEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAV------PGIEDGGRLQLKgPN----VMNGYlrVENPgvle 577
Cdd:cd05928 320 YEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDngnvlpPGTEGDIGIRVK-PIrpfgLFSGY--VDNP---- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 578 APTAENVNGEvetgWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlatavSAEKMHATVVKS------DAS 651
Cdd:cd05928 393 EKTAATIRGD----FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVE------SALIEHPAVVESavvsspDPI 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937565178 652 KGE---ALVLFTTD-GELKRDALLRYAREHGIPELA---VPRDIRYLKQLPVLGSGK 701
Cdd:cd05928 463 RGEvvkAFVVLAPQfLSHDPEQLTKELQQHVKSVTApykYPRKVEFVQELPKTVTGK 519
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
364-708 |
6.56e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 84.42 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIIL-FTSGSEGNPKGVVHSHKSilaNVEQ--IKTIAD---FTANDRFMSALPLFH--SFGLTvglFTPLLTGAEV 435
Cdd:PRK06018 175 DENTAAGMcYTSGTTGDPKGVLYSHRS---NVLHalMANNGDalgTSAADTMLPVVPLFHanSWGIA---FSAPSMGTKL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 FLYPSPLHYRIVPELVYDRNCTVLFGTST---FLGNYARfANPYDFFRVRYVVAGAEKLQDSTRQIWQDkFGLRILEGYG 512
Cdd:PRK06018 249 VMPGAKLDGASVYELLDTEKVTFTAGVPTvwlMLLQYME-KEGLKLPHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 513 VTECAPVvsinvpmaakpGTVGRILPGL-----DARL-------LAVPGIE-------------DG---GRLQLKGPNVM 564
Cdd:PRK06018 327 MTEMSPL-----------GTLAALKPPFsklpgDARLdvlqkqgYPPFGVEmkitddagkelpwDGktfGRLKVRGPAVA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 565 NGYLRVEnpgvleaptaenvnGEV--ETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLatAVSAEKM- 641
Cdd:PRK06018 396 AAYYRVD--------------GEIldDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENL--AVGHPKVa 459
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937565178 642 HATVVKSDASK-GE--ALVLFTTDGE-LKRDALLRYArEHGIPELAVPRDIRYLKQLPVLGSGKPDFVTLK 708
Cdd:PRK06018 460 EAAVIGVYHPKwDErpLLIVQLKPGEtATREEILKYM-DGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
364-607 |
9.31e-17 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 84.16 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQI-KTIADFTAND-RFMSALPLFHSFG--LTVGLF------------- 426
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLaQTFPFLAEEPpVLVDWLPWNHTFGgnHNLGIVlynggtlyiddgk 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 427 -TPLLTG------AEVflypSPLHYRIVP----ELVydrnctvlfgtsTFLGNYARFANpyDFF-RVRYVV-AGA----- 488
Cdd:PRK08180 288 pTPGGFDetlrnlREI----SPTVYFNVPkgweMLV------------PALERDAALRR--RFFsRLKLLFyAGAalsqd 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 489 --EKLQDSTRQIWQDKfgLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLlaVPgieDGGRLQL--KGPNVM 564
Cdd:PRK08180 350 vwDRLDRVAEATCGER--IRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKL--VP---VGGKLEVrvKGPNVT 422
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1937565178 565 NGYLRveNPgvleAPTAENVNgevETGWYDTGDIVRFDD-----QGFV 607
Cdd:PRK08180 423 PGYWR--AP----ELTAEAFD---EEGYYRSGDAVRFVDpadpeRGLM 461
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
363-646 |
1.64e-16 |
|
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: 83.25 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQI-KTIADFTANDRFM-SALPLFHSFGLTVGLFTPLLTGAEVFL--- 437
Cdd:cd05921 163 GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLeQTYPFFGEEPPVLvDWLPWNHTFGGNHNFNLVLYNGGTLYIddg 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 438 YPSPLHYRIVPELVYDRNCTVLF----GTSTFLGNY-------ARFanpydFFRVRYVVAGAEKLQDSTRQIWQD----K 502
Cdd:cd05921 243 KPMPGGFEETLRNLREISPTVYFnvpaGWEMLVAALekdealrRRF-----FKRLKLMFYAGAGLSQDVWDRLQAlavaT 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 503 FGLRI--LEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLlaVPGiedGGRLQ--LKGPNVMNGYLRvenpgvleA 578
Cdd:cd05921 318 VGERIpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL--VPS---GGKYEvrVKGPNVTPGYWR--------Q 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 579 P--TAENVNgevETGWYDTGDIVRFDD-----QGFVqIQGR-AKRFAKIAGEMVSLEMVETLATAVSAEKMHATVV 646
Cdd:cd05921 385 PelTAQAFD---EEGFYCLGDAAKLADpddpaKGLV-FDGRvAEDFKLASGTWVSVGPLRARAVAACAPLVHDAVV 456
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
369-701 |
2.26e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 82.67 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 369 IILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGL-TVGLFTPLltGAEVFLypsplHYRIV 447
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWaHLTLAMAL--GSTVVL-----RRRFD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 448 PE----LVYDRNCTVLFGTSTFLgnyARF-------ANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTEC 516
Cdd:PRK07788 284 PEatleDIAKHKATALVVVPVML---SRIldlgpevLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 517 ApVVSINVP--MAAKPGTVGRILPGLDARLLAvpgiEDGGRLqlkGPNVMnGYLRVENPGVLEAPTAENvNGEVETGWYD 594
Cdd:PRK07788 361 A-FATIATPedLAEAPGTVGRPPKGVTVKILD----ENGNEV---PRGVV-GRIFVGNGFPFEGYTDGR-DKQIIDGLLS 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 595 TGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETL---------ATAVSAE------KMHATVVKSDaskGEAlvlf 659
Cdd:PRK07788 431 SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLlaghpdvveAAVIGVDdeefgqRLRAFVVKAP---GAA---- 503
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1937565178 660 ttdgeLKRDALLRYAREHgipeLA---VPRDIRYLKQLPVLGSGK 701
Cdd:PRK07788 504 -----LDEDAIKDYVRDN----LArykVPRDVVFLDELPRNPTGK 539
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
338-703 |
2.30e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 82.73 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 338 ADVTTADKLWIFAHLLMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFH 417
Cdd:PRK06188 141 GPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 418 SFGLtvgLFTP-LLTGAEVFLYPS--P-------LHYRI-----VPELVY---------DRNC----TVLFGTSTFlgny 469
Cdd:PRK06188 221 AGGA---FFLPtLLRGGTVIVLAKfdPaevlraiEEQRItatflVPTMIYalldhpdlrTRDLssleTVYYGASPM---- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 470 arfaNPydffrVRYVVAGaeklqdstrqiwqDKFGLRILEGYGVTECAPVVSINVP---MAAKPGTV---GRILPGLDAR 543
Cdd:PRK06188 294 ----SP-----VRLAEAI-------------ERFGPIFAQYYGQTEAPMVITYLRKrdhDPDDPKRLtscGRPTPGLRVA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 544 LLAvpgiEDG--------GRLQLKGPNVMNGYLRvenpgvLEAPTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKR 615
Cdd:PRK06188 352 LLD----EDGrevaqgevGEICVRGPLVMDGYWN------RPEETAEAFRD----GWLHTGDVAREDEDGFYYIVDRKKD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 616 FAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE---ALVLFTTDGELKRDALLRYAREHGIPELAvPRDIRYLK 692
Cdd:PRK06188 418 MIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEavtAVVVLRPGAAVDAAELQAHVKERKGSVHA-PKQVDFVD 496
|
410
....*....|.
gi 1937565178 693 QLPVLGSGKPD 703
Cdd:PRK06188 497 SLPLTALGKPD 507
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
361-624 |
2.76e-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: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 361 KQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDR----FMSALPLFHSFGLTVGLFTPLLTGAEV- 435
Cdd:cd05933 146 SQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHIAAQILDIWLPIKVGGQVy 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 FLYPSPLHYRIVPEL-------------VYDR------------------------------NCTVLFGTSTFLGNYaRF 472
Cdd:cd05933 226 FAQPDALKGTLVKTLrevrptafmgvprVWEKiqekmkavgaksgtlkrkiaswakgvgletNLKLMGGESPSPLFY-RL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 473 ANPYDFFRVRYVVA---------GAEKLQDSTRQIWQDkFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDAR 543
Cdd:cd05933 305 AKKLVFKKVRKALGldrcqkfftGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 544 LLAvPGIEDGGRLQLKGPNVMNGYLRvenpgvLEAPTAENVNgevETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA-GE 622
Cdd:cd05933 384 IHN-PDADGIGEICFWGRHVFMGYLN------MEDKTEEAID---EDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGE 453
|
..
gi 1937565178 623 MV 624
Cdd:cd05933 454 NV 455
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
363-703 |
3.18e-16 |
|
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: 81.83 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRfmSALPLFHSF-GLTVGLFTPLLTGAEVFLYPSP 441
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK--SLVYASFSFdASAWEIFPHLTAGAALHVVPSE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 LHYRIVP--ELVYDRNCTVLFGTSTFLGNYARFANPydffRVRYVVAGAEKLQDSTRQiwqdkfGLRILEGYGVTECAPV 519
Cdd:cd17645 180 RRLDLDAlnDYFNQEGITISFLPTGAAEQFMQLDNQ----SLRVLLTGGDKLKKIERK------GYKLVNNYGPTENTVV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 520 VSI--------NVPMaAKPGTVGRILpgLDARLLAVPGIEDGGRLQLKGPNVMNGYLRVENPGVLEAPTAENVNGEvetG 591
Cdd:cd17645 250 ATSfeidkpyaNIPI-GKPIDNTRVY--ILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGE---R 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 592 WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTTDGELKRDALL 671
Cdd:cd17645 324 MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEEL 403
|
330 340 350
....*....|....*....|....*....|..
gi 1937565178 672 RYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17645 404 REWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
368-703 |
5.55e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.91 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 368 AIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLH--- 443
Cdd:PRK05691 1276 AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI--SFDVSVwECFWPLITGCRLVLAGPGEHrdp 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 444 YRIVpELVYDRNCTVLFGTSTFLGNYARFANPYDFFRVRYVVAGAEKLQDSTR-QIWQDKFGLRILEGYGVTECApvvsI 522
Cdd:PRK05691 1354 QRIA-ELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTETA----I 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 523 NVP---MAAKPGT---VGRILPG-----LDARL-LAVPGIedGGRLQLKGPNVMNGYLRveNPGVleapTAE----NVNG 586
Cdd:PRK05691 1429 NVThwqCQAEDGErspIGRPLGNvlcrvLDAELnLLPPGV--AGELCIGGAGLARGYLG--RPAL----TAErfvpDPLG 1500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 587 EVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLFTTDGELK 666
Cdd:PRK05691 1501 EDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQE 1580
|
330 340 350
....*....|....*....|....*....|....*...
gi 1937565178 667 RDAL-LRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK05691 1581 AEAErLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLD 1618
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
363-703 |
1.01e-15 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 80.20 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANV---EQIKTIADFTANDRFMSALplfhSFGLTVGLFT-PLLTGAEvfLY 438
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAhawRREYELDSFPVRLLQMASF----SFDVFAGDFArSLLNGGT--LV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 439 PSPLHYRIVPELVYD----RNCTVLFGTSTFLGNYARFA--NPYDFFRVRYVVAGAEKLQDSTRQIWQDKFG--LRILEG 510
Cdd:cd17650 165 ICPDEVKLDPAALYDlilkSRITLMESTPALIRPVMAYVyrNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGqgMRIINS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 511 YGVTEC-----------APVVSI-NVPmaakpgtVGRILPG-----LDARLLAVP-GIedGGRLQLKGPNVMNGYLR--- 569
Cdd:cd17650 245 YGVTEAtidstyyeegrDPLGDSaNVP-------IGRPLPNtamyvLDERLQPQPvGV--AGELYIGGAGVARGYLNrpe 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 570 ------VENPGVleapTAENVngevetgwYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHA 643
Cdd:cd17650 316 ltaerfVENPFA----PGERM--------YRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAV 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937565178 644 TVVKSDAsKGEA-LVLFTTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17650 384 VAVREDK-GGEArLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
351-701 |
1.72e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 79.93 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 351 HLLMPRQAQVKqqPEDDAIILFTSGSEGNPKGVVHSHKSI-LANVEQIKTIAdFTANDRFMSALPLFHsfgltVGLFTpl 429
Cdd:PRK06145 137 GLEIPPQAAVA--PTDLVRLMYTSGTTDRPKGVMHSYGNLhWKSIDHVIALG-LTASERLLVVGPLYH-----VGAFD-- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 430 LTGAEVFLYPSPL--HYRIVPELVY-----DRNCTVLFG---TSTFLGNYARFAnpYDFFRVRYVVAGAEKLQDSTRQIW 499
Cdd:PRK06145 207 LPGIAVLWVGGTLriHREFDPEAVLaaierHRLTCAWMApvmLSRVLTVPDRDR--FDLDSLAWCIGGGEKTPESRIRDF 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 500 QDKF-GLRILEGYGVTEcapVVSINVPMAA-----KPGTVGRILPGL-------DARLLAvPGIEdgGRLQLKGPNVMNG 566
Cdd:PRK06145 285 TRVFtRARYIDAYGLTE---TCSGDTLMEAgreieKIGSTGRALAHVeiriadgAGRWLP-PNMK--GEICMRGPKVTKG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 567 YLRVENPgvleapTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVV 646
Cdd:PRK06145 359 YWKDPEK------TAEAFYG----DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIG 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937565178 647 KSDASKGE---ALVLFTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK06145 429 VHDDRWGEritAVVVLNPGATLTLEALDRHCRQR-LASFKVPRQLKVRDELPRNPSGK 485
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
364-701 |
1.83e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 80.07 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSIL----ANVEQIktiaDFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
Cdd:PRK13388 149 AMDPFMLIFTSGTTGAPKAVRCSHGRLAfagrALTERF----GLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 SplhyrivpelvydrnctvlFGTSTFLGNYARFANPYdFFRV----RYVVAGAEKLQD-------------STRQI--WQ 500
Cdd:PRK13388 225 K-------------------FSASGFLDDVRRYGATY-FNYVgkplAYILATPERPDDadnplrvafgneaSPRDIaeFS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 501 DKFGLRILEGYGVTECApvVSINVPMAAKPGTVGRILPGL------DARLLAVPGIEDGGRL-----------QLKGPNV 563
Cdd:PRK13388 285 RRFGCQVEDGYGSSEGA--VIVVREPGTPPGSIGRGAPGVaiynpeTLTECAVARFDAHGALlnadeaigelvNTAGAGF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 564 MNGYLRveNPgvleAPTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETL--------ATA 635
Cdd:PRK13388 363 FEGYYN--NP----EATAERMRH----GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERIllrhpainRVA 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937565178 636 VSA--------EKMHATVVKSDASkgealvlfttdgeLKRDALLRYAREHgiPEL---AVPRDIRYLKQLPVLGSGK 701
Cdd:PRK13388 433 VYAvpdervgdQVMAALVLRDGAT-------------FDPDAFAAFLAAQ--PDLgtkAWPRYVRIAADLPSTATNK 494
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
340-703 |
2.17e-15 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 80.47 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 340 VTTADKLWIFAHL-----------LMPRQAQVKQ--QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTAN 406
Cdd:PRK10252 560 ITTADQLPRFADVpdltslcynapLAPQGAAPLQlsQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTAD 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 407 DRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLH------------YRI-----VPELVydrnctvlfgtSTFLGN 468
Cdd:PRK10252 640 DVVLQKTPC--SFDVSVwEFFWPFIAGAKLVMAEPEAHrdplamqqffaeYGVttthfVPSML-----------AAFVAS 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 469 YARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVS---------INVPMAAKP------GTV 533
Cdd:PRK10252 707 LTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSwypafgeelAAVRGSSVPigypvwNTG 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 534 GRIlpgLDARLLAVP-GIedGGRLQLKGPNVMNGYLrvENPGVleapTAEN------VNGEvetGWYDTGDIVRFDDQGF 606
Cdd:PRK10252 787 LRI---LDARMRPVPpGV--AGDLYLTGIQLAQGYL--GRPDL----TASRfiadpfAPGE---RMYRTGDVARWLDDGA 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 607 VQIQGRAKRFAKIAGEMVSLEMVET-------LATAVSaekmHATVVKSDASKG---EALVLFTTDGE---LKRDALLRY 673
Cdd:PRK10252 853 VEYLGRSDDQLKIRGQRIELGEIDRamqalpdVEQAVT----HACVINQAAATGgdaRQLVGYLVSQSglpLDTSALQAQ 928
|
410 420 430
....*....|....*....|....*....|
gi 1937565178 674 AREhGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK10252 929 LRE-RLPPHMVPVVLLQLDQLPLSANGKLD 957
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
233-701 |
3.14e-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: 79.53 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRILEK-YSKQGEKIGLMLPN-----------AGISA--AVIFGAVSrgripammnytagVKGLSSAI 298
Cdd:cd05966 86 TYRELLREVCRFANVLKSlGVKKGDRVAIYMPMipelviamlacARIGAvhSVVFAGFS-------------AESLADRI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 299 TAAQINTIFTSRQFLDKGKLWHLP-------EQLTQVRWVF-LEDLKADVTTADKLWIFAHLLMPRQAQ----VKQQPED 366
Cdd:cd05966 153 NDAQCKLVITADGGYRGGKVIPLKeivdealEKCPSVEKVLvVKRTGGEVPMTEGRDLWWHDLMAKQSPecepEWMDSED 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 367 DAIILFTSGSEGNPKGVVHSHKSILANVEQ-IKTIADFTANDRFMSALPLF----HSFGLtvglFTPLLTGAEVFLY--- 438
Cdd:cd05966 233 PLFILYTSGSTGKPKGVVHTTGGYLLYAATtFKYVFDYHPDDIYWCTADIGwitgHSYIV----YGPLANGATTVMFegt 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 439 PSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFAN----PYDFFRVR-----------------YVVAGAEKLQ--DSt 495
Cdd:cd05966 309 PTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDewvkKHDLSSLRvlgsvgepinpeawmwyYEVIGKERCPivDT- 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 496 rqIWQDKFGlrileGYGVTeCAPVVsinVPMaaKPGTVGRILPGLDARLLAvpgiEDGGRLqlkgPNVMNGYLRVENP-- 573
Cdd:cd05966 388 --WWQTETG-----GIMIT-PLPGA---TPL--KPGSATRPFFGIEPAILD----EEGNEV----EGEVEGYLVIKRPwp 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 574 ----GVLEAPTA-ENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKS 648
Cdd:cd05966 447 gmarTIYGDHERyEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRP 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937565178 649 DASKGEALVLFTT--DGELKRDAL---LRYAREHGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05966 527 HDIKGEAIYAFVTlkDGEEPSDELrkeLRKHVRKEIGPIATPDKIQFVPGLPKTRSGK 584
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
197-701 |
5.37e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 78.50 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 197 RMAVRPRETLYESLLSAQYRYGAKKNCVEDINFTpdTYRKLLTKTLFVGRILEKYS-KQGEKIGLMLPNAGISAAVIFGA 275
Cdd:PRK13383 28 REASRGGTNPYTLLAVTAARWPGRTAIIDDDGAL--SYRELQRATESLARRLTRDGvAPGRAVGVMCRNGRGFVTAVFAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 276 VSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKgklwhlpeqltqvrwvfLEDLKADVTTADKLWIFAHLLMP 355
Cdd:PRK13383 106 GLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAER-----------------IAGADDAVAVIDPATAGAEESGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 356 RQAQVKQqpedDAIILFTSGSEGNPKGVVHSHKsILANVEQIKTIADFT---ANDRFMSALPLFHSFG-----LTVGLFT 427
Cdd:PRK13383 169 RPAVAAP----GRIVLLTSGTTGKPKGVPRAPQ-LRSAVGVWVTILDRTrlrTGSRISVAMPMFHGLGlgmlmLTIALGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 428 PLLT----GAEVFLYPSPLH----YRIVPelvydrnctVLFGTSTFLGNYARFANPYDFFRVryVVAGAEKLQDSTRQIW 499
Cdd:PRK13383 244 TVLThrhfDAEAALAQASLHradaFTAVP---------VVLARILELPPRVRARNPLPQLRV--VMSSGDRLDPTLGQRF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 500 QDKFGLRILEGYGVTECApVVSINVPMAAK--PGTVGRILPGLDARLLavpgiEDGGRLQlkGPNVMNgylRVENPGVLE 577
Cdd:PRK13383 313 MDTYGDILYNGYGSTEVG-IGALATPADLRdaPETVGKPVAGCPVRIL-----DRNNRPV--GPRVTG---RIFVGGELA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 578 APTAENVNGE-VETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEAL 656
Cdd:PRK13383 382 GTRYTDGGGKaVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRL 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1937565178 657 VLFTT---DGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK13383 462 AAFVVlhpGSGVDAAQLRDYLKDR-VSRFEQPRDINIVSSIPRNPTGK 508
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
254-701 |
7.22e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 77.88 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 254 QGEKIGLMLPNagiSAAVIFGAVSRGRIPA---MMNYTAGVKGLSSAITAAQINTIFTSRQF---LDKGkLWHLPEQLTQ 327
Cdd:PRK13382 92 EPRVVGIMCRN---HRGFVEALLAANRIGAdilLLNTSFAGPALAEVVTREGVDTVIYDEEFsatVDRA-LADCPQATRI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 328 VRWVfleDLKADVTTaDKLwIFAHLlmprQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKsilANVEQIKTIADFT--- 404
Cdd:PRK13382 168 VAWT---DEDHDLTV-EVL-IAAHA----GQRPEPTGRKGRVILLTSGTTGTPKGARRSGP---GGIGTLKAILDRTpwr 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 405 ANDRFMSALPLFHSFGLTVGLFTPLLTGAEVflypspLHYRIVPE----LVyDRN-----CTVLFGTSTFLGNYARFANP 475
Cdd:PRK13382 236 AEEPTVIVAPMFHAWGFSQLVLAASLACTIV------TRRRFDPEatldLI-DRHratglAVVPVMFDRIMDLPAEVRNR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 476 YDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTEcAPVVSINVP--MAAKPGTVGRILPGLDARLLAvpgiEDG 553
Cdd:PRK13382 309 YSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE-AGMIATATPadLRAAPDTAGRPAEGTEIRILD----QDF 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 554 GRLqlkgPNVMNGYLRVENPGVLEAPTAeNVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMV-SLEMVETL 632
Cdd:PRK13382 384 REV----PTGEVGTIFVRNDTQFDGYTS-GSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVyPIEVEKTL 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 633 ATavSAEKMHATVVKSDASK-GEALVLF--------TTDGELK---RDALLRYArehgipelaVPRDIRYLKQLPVLGSG 700
Cdd:PRK13382 459 AT--HPDVAEAAVIGVDDEQyGQRLAAFvvlkpgasATPETLKqhvRDNLANYK---------VPRDIVVLDELPRGATG 527
|
.
gi 1937565178 701 K 701
Cdd:PRK13382 528 K 528
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
364-630 |
9.55e-15 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 77.85 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTI-ADFTANDRFMSALPLFHSF-----------GLTVGLFTPL-L 430
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVvPKLGKNDVYLAYLPLAHILelaaesvmaavGAAIGYGSPLtL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 431 T-----------GAEVFLYPSPLhyRIVP-------------------------ELVYDRNCTVLFGtsTFLGNYARFAN 474
Cdd:PLN02387 329 TdtsnkikkgtkGDASALKPTLM--TAVPaildrvrdgvrkkvdakgglakklfDIAYKRRLAAIEG--SWFGAWGLEKL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 475 PYDFF-----------RVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTE-CApvvsinvpmaakPGT--------VG 534
Cdd:PLN02387 405 LWDALvfkkiravlggRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTEtCA------------GATfsewddtsVG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 535 RILPGLDARLLAVPGIEDGGRLQ-----------LKGPNVMNGYLRveNpgvlEAPTAE--NVNgEVETGWYDTGDIVRF 601
Cdd:PLN02387 473 RVGPPLPCCYVKLVSWEEGGYLIsdkpmprgeivIGGPSVTLGYFK--N----QEKTDEvyKVD-ERGMRWFYTGDIGQF 545
|
330 340 350
....*....|....*....|....*....|
gi 1937565178 602 DDQGFVQIQGRAKRFAKI-AGEMVSLEMVE 630
Cdd:PLN02387 546 HPDGCLEIIDRKKDIVKLqHGEYVSLGKVE 575
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
365-704 |
1.26e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 75.88 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSI---------LANVEQIKT--IADFTAND---RFMSALPLFHSFGLTVGlFTPLL 430
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIfrmlmggadFGTGEFTPSedAHKAAAAAagtVMFPAPPLMHGTGSWTA-FGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 431 TGAEVFLYPSPLHYRIVPELVYDRNCTVLfgtsTFLGN-YAR-------FANPYDFFRVRYVVAGAEKLQDSTRQIWQD- 501
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSM----TIVGDaMARplidalrDAGPYDLSSLFAISSGGALLSPEVKQGLLEl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 502 KFGLRILEGYGVTEC-APVVSINVPMAAKPGTVGRILPGL-----DARLLAvPGIEDGGRLQLKGpNVMNGYLRVenpgv 575
Cdd:cd05924 158 VPNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANPDTvvlddDGRVVP-PGSGGVGWIARRG-HIPLGYYGD----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 576 lEAPTAEN---VNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlatavSAEKMHATV------- 645
Cdd:cd05924 231 -EAKTAETfpeVDGV---RYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVE------EALKSHPAVydvlvvg 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937565178 646 VKSD--ASKGEALVLFTTDGELKRDALlryaREHGIPELA---VPRDIRYLKQLPVLGSGKPDF 704
Cdd:cd05924 301 RPDErwGQEVVAVVQLREGAGVDLEEL----REHCRTRIArykLPKQVVFVDEIERSPAGKADY 360
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
363-703 |
3.54e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 76.75 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSalplFHSFGL---TVGLFTPLLTGAEVFLYP 439
Cdd:PRK05691 2331 LPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELH----FYSINFdaaSERLLVPLLCGARVVLRA 2406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 S-PLHYRIVPELVYDRNCTVLFGTSTFLGNYARF-ANPYDFFRVRYVVAGAEKLQ----DSTRQIWQDKFglrILEGYGV 513
Cdd:PRK05691 2407 QgQWGAEEICQLIREQQVSILGFTPSYGSQLAQWlAGQGEQLPVRMCITGGEALTgehlQRIRQAFAPQL---FFNAYGP 2483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 514 TECA--PVVSInVPMAAKPGT----VGRILPG-----LDARLLAVP--GIedgGRLQLKGPNVMNGYLRveNPGVleapT 580
Cdd:PRK05691 2484 TETVvmPLACL-APEQLEEGAasvpIGRVVGArvayiLDADLALVPqgAT---GELYVGGAGLAQGYHD--RPGL----T 2553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 581 AENVNGE---VETG-WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKmHATVVKSDASKGEAL 656
Cdd:PRK05691 2554 AERFVADpfaADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVR-EAVVLALDTPSGKQL 2632
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 657 VLFTTDGELK---------RDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK05691 2633 AGYLVSAVAGqddeaqaalREALKAHLKQQ-LPDYMVPAHLILLDSLPLTANGKLD 2687
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
329-701 |
4.41e-14 |
|
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: 75.81 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 329 RWVFLEDLKADVTTADKLWIFAHllmprqaqvkqqpeDDAIILFTSGSEGNPKGVV-----HShksiLANVEQIKTIADF 403
Cdd:cd05967 208 RDLDWSELLAKAEPVDCVPVAAT--------------DPLYILYTSGTTGKPKGVVrdnggHA----VALNWSMRNIYGI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 404 TANDRFMSALPLfhsfGLTVG----LFTPLLTGAEVFLY-------PSPLHY-RIVPElvYDRNCtvLFGTSTFL----- 466
Cdd:cd05967 270 KPGDVWWAASDV----GWVVGhsyiVYGPLLHGATTVLYegkpvgtPDPGAFwRVIEK--YQVNA--LFTAPTAIrairk 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 467 ----GNYARfanPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSIN----VPMAAKPGTVGRILP 538
Cdd:cd05967 342 edpdGKYIK---KYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANpvglEPLPIKAGSPGKPVP 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 539 GLDARLLAvpgiEDGGRLqlkGPNVMnGYLRVE---NPGVLeaPTAENVNGEVET-------GWYDTGDIVRFDDQGFVQ 608
Cdd:cd05967 419 GYQVQVLD----EDGEPV---GPNEL-GNIVIKlplPPGCL--LTLWKNDERFKKlylskfpGYYDTGDAGYKDEDGYLF 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 609 IQGRAKRFAKIAGEMVSL-EMVETLAT--AVsAEKmhATVVKSDASKGE---ALVLFTTDGELKRDALLR----YAREHg 678
Cdd:cd05967 489 IMGRTDDVINVAGHRLSTgEMEESVLShpAV-AEC--AVVGVRDELKGQvplGLVVLKEGVKITAEELEKelvaLVREQ- 564
|
410 420
....*....|....*....|...
gi 1937565178 679 IPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05967 565 IGPVAAFRLVIFVKRLPKTRSGK 587
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
246-614 |
5.22e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 75.43 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 246 RILEKYSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKG-------LSSAITAAQINTIFTSRQFLDkgkl 318
Cdd:PRK09192 65 RLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGresyiaqLRGMLASAQPAAIITPDELLP---- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 319 whlpeqltqvrWVfledlKADVTTADKLWIFAH-LLMPRQAQV----KQQPEDDAIILFTSGSEGNPKGVVHSHKSILAN 393
Cdd:PRK09192 141 -----------WV-----NEATHGNPLLHVLSHaWFKALPEADvalpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMAN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 394 VEQIKTIA-DFTANDRFMSALPLFHSFGLtVGLF-TPLLTGAEVFLYPS------PLHYRivpELVYDRNCTVLFgTSTF 465
Cdd:PRK09192 205 LRAISHDGlKVRPGDRCVSWLPFYHDMGL-VGFLlTPVATQLSVDYLPTrdfarrPLQWL---DLISRNRGTISY-SPPF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 466 lgNY---ARFAN-----PYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLR------ILEGYGVTECAPVVS---------- 521
Cdd:PRK09192 280 --GYelcARRVNskdlaELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEATLAVSfsplgsgivv 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 522 ------------INVPMAAKPGTV------GRILPGLDARLLAVPGIEDG----GRLQLKGPNVMNGYLRVENPG-VLEA 578
Cdd:PRK09192 358 eevdrdrleyqgKAVAPGAETRRVrtfvncGKALPGHEIEIRNEAGMPLPervvGHICVRGPSLMSGYFRDEESQdVLAA 437
|
410 420 430
....*....|....*....|....*....|....*..
gi 1937565178 579 ptaenvngeveTGWYDTGDI-VRFDdqGFVQIQGRAK 614
Cdd:PRK09192 438 -----------DGWLDTGDLgYLLD--GYLYITGRAK 461
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
363-701 |
6.28e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.06 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIIL-FTSGSEGNPKGVVHSHKSilANVEQIKTIADFTAN--DRFMSALPLFHSFGLTVGLFTPLLTGAEVFL-- 437
Cdd:PLN03102 183 QDEHDPISLnYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGtcPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMrh 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 438 YPSPLHYRIVpEL--VYDRNCT------VLFGTSTflgNYARFANPydffrVRYVVAGAEKLQDSTRQIwqDKFGLRILE 509
Cdd:PLN03102 261 VTAPEIYKNI-EMhnVTHMCCVptvfniLLKGNSL---DLSPRSGP-----VHVLTGGSPPPAALVKKV--QRLGFQVMH 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 510 GYGVTEC-APVV-------------SINVPMAAKPGTVGRILPGLDAR----LLAVPgiEDG---GRLQLKGPNVMNGYL 568
Cdd:PLN03102 330 AYGLTEAtGPVLfcewqdewnrlpeNQQMELKARQGVSILGLADVDVKnketQESVP--RDGktmGEIVIKGSSIMKGYL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 569 RveNPgvleAPTAEnvngEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVE--------TLATAVSA-- 638
Cdd:PLN03102 408 K--NP----KATSE----AFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVEnvlykypkVLETAVVAmp 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 639 -----EKMHATVV--KSDASKGEALVLFTTDgelKRDaLLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PLN03102 478 hptwgETPCAFVVleKGETTKEDRVDKLVTR---ERD-LIEYCREN-LPHFMCPRKVVFLQELPKNGNGK 542
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
321-613 |
1.68e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 73.37 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 321 LPEQLTQVrwvFLEDLKAD--VTTADKLWIFA-----HLLMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILAN 393
Cdd:PRK09029 87 LPQPLLEE---LLPSLTLDfaLVLEGENTFSAltslhLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 394 VEQIKTIADFTANDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPS-PL--------HYRIVPE-----LVYDRNCTVL 459
Cdd:PRK09029 164 AEGVLSLMPFTAQDSWLLSLPLFHVSGQGI-VWRWLYAGATLVVRDKqPLeqalagctHASLVPTqlwrlLDNRSEPLSL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 460 fgTSTFLGnyarfanpydffrvryvvaGAEKLQDSTRQIWQdkFGLRILEGYGVTECAPVVsinvpmAAKP----GTVGR 535
Cdd:PRK09029 243 --KAVLLG-------------------GAAIPVELTEQAEQ--QGIRCWCGYGLTEMASTV------CAKRadglAGVGS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 536 ILPGLDARLlavpgieDGGRLQLKGPNVMNGYLRvenpgvleaptaenvNGEV-----ETGWYDTGDIVRFDDqGFVQIQ 610
Cdd:PRK09029 294 PLPGREVKL-------VDGEIWLRGASLALGYWR---------------QGQLvplvnDEGWFATRDRGEWQN-GELTIL 350
|
...
gi 1937565178 611 GRA 613
Cdd:PRK09029 351 GRL 353
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
364-646 |
3.13e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.16 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDR---FMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvSLDWMPWNHTMGGNANFNGLLWGGGTLYIDDG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 441 plhyRIVPELVYD--RNCTVLfgTSTFLGN----YARFANPYD--------FF-RVRYVVAGAEKLQDSTRQIWQD---- 501
Cdd:PRK12582 299 ----KPLPGMFEEtiRNLREI--SPTVYGNvpagYAMLAEAMEkddalrrsFFkNLRLMAYGGATLSDDLYERMQAlavr 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 502 KFGLRIL--EGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLAVpgiEDGGRLQLKGPNVMNGYLRveNPGVleap 579
Cdd:PRK12582 373 TTGHRIPfyTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPV---GDKYEVRVKGPNVTPGYHK--DPEL---- 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937565178 580 TAENVNgevETGWYDTGDIVRFDD-----QGFVqIQGR-AKRFAKIAGEMVSLEMVETLATAVSAEKMHATVV 646
Cdd:PRK12582 444 TAAAFD---EEGFYRLGDAARFVDpddpeKGLI-FDGRvAEDFKLSTGTWVSVGTLRPDAVAACSPVIHDAVV 512
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
205-701 |
4.23e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 72.32 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 205 TLYESLLSAQYRYGAKKNCVEDINFTPDTYRKLLTKTLFVGRILEKYS-KQGEKIGLMLPNAGISAAVIFGAVSRGRIPA 283
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGlRKGQVVVVVLPNVAEYGIVALGIMAAGGVFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 284 MMNYTAGVKGLSSAITAAQINTIFTSRQFLDKGKLWHLP-------EQLTQVRWVFLedLKADVTTADKLwifahllmpR 356
Cdd:PLN02330 109 GANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPvivlgeeKIEGAVNWKEL--LEAADRAGDTS---------D 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 357 QAQVKQQpeDDAIILFTSGSEGNPKGVVHSHKSILANV---------EQIKTIADftandrfMSALPLFHSFGLTVGLFT 427
Cdd:PLN02330 178 NEEILQT--DLCALPFSSGTTGISKGVMLTHRNLVANLcsslfsvgpEMIGQVVT-------LGLIPFFHIYGITGICCA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 428 PLLTGAEV-----FLYPSPLHYRIVPELVYDRNCTVLFgtstflgnYARFANP----YDF--FRVRYVVAGAEKLQDSTR 496
Cdd:PLN02330 249 TLRNKGKVvvmsrFELRTFLNALITQEVSFAPIVPPII--------LNLVKNPiveeFDLskLKLQAIMTAAAPLAPELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 497 QIWQDKF-GLRILEGYGVTE--CAPVVSINVPMA---AKPGTVGRILPGLDARL------LAVPGiEDGGRLQLKGPNVM 564
Cdd:PLN02330 321 TAFEAKFpGVQVQEAYGLTEhsCITLTHGDPEKGhgiAKKNSVGFILPNLEVKFidpdtgRSLPK-NTPGELCVRSQCVM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 565 NGYLRVENPgvleapTAENVNgevETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVS-LEMVETLATAVSAEKMhA 643
Cdd:PLN02330 400 QGYYNNKEE------TDRTID---EDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVApAELEAILLTHPSVEDA-A 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937565178 644 TVVKSDASKGE---ALVLFTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PLN02330 470 VVPLPDEEAGEipaACVVINPKAKESEEDILNFVAAN-VAHYKKVRVVQFVDSIPKSLSGK 529
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
362-638 |
4.85e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 72.36 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 362 QQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTI-----ADFTANDRFMSALPLFHSF-----------GLTVGL 425
Cdd:PLN02614 220 KKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLlksanAALTVKDVYLSYLPLAHIFdrvieecfiqhGAAIGF 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 426 F---TPLLTGAEVFLYPSPlhYRIVPElVYDRNCTVLFGTSTFLGNYARF----ANPYDFF------------------- 479
Cdd:PLN02614 300 WrgdVKLLIEDLGELKPTI--FCAVPR-VLDRVYSGLQKKLSDGGFLKKFvfdsAFSYKFGnmkkgqshveasplcdklv 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 480 ----------RVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTE-CAPVVSINVPMAAKPGTVGRILPGLDARLLAVP 548
Cdd:PLN02614 377 fnkvkqglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVP 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 549 GIE-DG------GRLQLKGPNVMNGYLRvenpgvleaptAENVNGEVET-GWYDTGDIVRFDDQGFVQIQGRAKRFAKIA 620
Cdd:PLN02614 457 EMEyDAlastprGEICIRGKTLFSGYYK-----------REDLTKEVLIdGWLHTGDVGEWQPNGSMKIIDRKKNIFKLS 525
|
330
....*....|....*....
gi 1937565178 621 -GEMVSLEMVETLATAVSA 638
Cdd:PLN02614 526 qGEYVAVENIENIYGEVQA 544
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
356-708 |
1.01e-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: 70.67 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 356 RQAQVKQQPEDDAIIL-FTSGSEGNPKGVVHSHKSI-LANVEQIKTIADFTANDRFMSALPLF--HSFGltvGLFTPLLT 431
Cdd:cd05974 75 YAAVDENTHADDPMLLyFTSGTTSKPKLVEHTHRSYpVGHLSTMYWIGLKPGDVHWNISSPGWakHAWS---CFFAPWNA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 432 GAEVFLYPSP-LHYRIVPELVYDRNCTVLFGTSTFL-----GNYARFANPydffrVRYVVAGAEKLQDSTRQIWQDKFGL 505
Cdd:cd05974 152 GATVFLFNYArFDAKRVLAALVRYGVTTLCAPPTVWrmliqQDLASFDVK-----LREVVGAGEPLNPEVIEQVRRAWGL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 506 RILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLL-AVPGIEDGGRLQL-----KGPNVMNGYlrVENPGvleaP 579
Cdd:cd05974 227 TIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLdPDGAPATEGEVALdlgdtRPVGLMKGY--AGDPD----K 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 580 TAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDA---SKGEAL 656
Cdd:cd05974 301 TAHAMRG----GYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPvrlSVPKAF 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937565178 657 VLFTTDGELKRD---ALLRYAREhgipELAVPRDIRYLK--QLPVLGSGKPDFVTLK 708
Cdd:cd05974 377 IVLRAGYEPSPEtalEIFRFSRE----RLAPYKRIRRLEfaELPKTISGKIRRVELR 429
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
363-632 |
3.52e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 69.84 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIAD-----FTANDRFMSALPLFHSF-----------GLTVG-- 424
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHILdrmieeyffrkGASVGyy 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 425 -------------LFTPLLTGA-EVF--LYP---------SPLHYRIVPELvYDRNCTVLFgtstfLGNYARFANPY-DF 478
Cdd:PLN02430 298 hgdlnalrddlmeLKPTLLAGVpRVFerIHEgiqkalqelNPRRRLIFNAL-YKYKLAWMN-----RGYSHKKASPMaDF 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 479 F-----------RVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAPVVSINVP--MAAKpGTVGRILPGLDARLL 545
Cdd:PLN02430 372 LafrkvkaklggRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPdeMCML-GTVGAPAVYNELRLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 546 AVP-------GIEDGGRLQLKGPNVMNGYLRveNPgvleaptaENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAK 618
Cdd:PLN02430 451 EVPemgydplGEPPRGEICVRGKCLFSGYYK--NP--------ELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIK 520
|
330
....*....|....*
gi 1937565178 619 IA-GEMVSLEMVETL 632
Cdd:PLN02430 521 LSqGEYVALEYLENV 535
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
362-701 |
4.39e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.21 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 362 QQPED--DAIIL-FTSGSEGNPKGVVHSHK-SILANVEQIkTIADFTANDRFMSALPLFH----SFGLTVglftPLLTGA 433
Cdd:PRK08162 176 TLPADewDAIALnYTSGTTGNPKGVVYHHRgAYLNALSNI-LAWGMPKHPVYLWTLPMFHcngwCFPWTV----AARAGT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 434 EVFLYpsplhyRIVPELVYD----RNCTVLFGT----STFLGNYARFANPYDFfRVRYVVAGA---EKLQDSTRQIwqdk 502
Cdd:PRK08162 251 NVCLR------KVDPKLIFDlireHGVTHYCGApivlSALINAPAEWRAGIDH-PVHAMVAGAappAAVIAKMEEI---- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 503 fGLRILEGYGVTECAPVVSIN--------VPMAAKPGTVGR------ILPG---LDARLLA-VPgiEDG---GRLQLKGP 561
Cdd:PRK08162 320 -GFDLTHVYGLTETYGPATVCawqpewdaLPLDERAQLKARqgvrypLQEGvtvLDPDTMQpVP--ADGetiGEIMFRGN 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 562 NVMNGYLRveNPgvlEApTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVS-LEMVETL--ATAVSA 638
Cdd:PRK08162 397 IVMKGYLK--NP---KA-TEEAFAG----GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISsIEVEDVLyrHPAVLV 466
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 639 EkmhATVVKSDASKGE---ALVLFTTDGELKRDALLRYAREHgIPELAVPRDIRYlKQLPVLGSGK 701
Cdd:PRK08162 467 A---AVVAKPDPKWGEvpcAFVELKDGASATEEEIIAHCREH-LAGFKVPKAVVF-GELPKTSTGK 527
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
361-630 |
7.38e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 68.72 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 361 KQQPEDDAIILFTSGSEGNPKGVVHSHKSILANV---EQIKTIAD--FTANDRFMSALPLFHSFGLTVGLFTpLLTGAEV 435
Cdd:PLN02861 216 PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDrvATEEDSYFSYLPLAHVYDQVIETYC-ISKGASI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 FLYPSPLHYRI-------------VPElVYDRNCTVL----------------FGTSTFLGNYARF-----ANPydFF-- 479
Cdd:PLN02861 295 GFWQGDIRYLMedvqalkptifcgVPR-VYDRIYTGImqkissggmlrkklfdFAYNYKLGNLRKGlkqeeASP--RLdr 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 480 ------------RVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTE-CAPVVSINVPMAAKPGTVGRILPGLDARLLA 546
Cdd:PLN02861 372 lvfdkikeglggRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLES 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 547 VPgiEDG---------GRLQLKGPNVMNGYLRveNPGVLEAPTAEnvngevetGWYDTGDIVRFDDQGFVQIQGRAKRFA 617
Cdd:PLN02861 452 VP--EMGydalsdvprGEICLRGNTLFSGYHK--RQDLTEEVLID--------GWFHTGDIGEWQPNGAMKIIDRKKNIF 519
|
330
....*....|....
gi 1937565178 618 KIA-GEMVSLEMVE 630
Cdd:PLN02861 520 KLSqGEYVAVENLE 533
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
258-701 |
9.48e-12 |
|
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: 67.84 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 258 IGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKGKlwhlpEQLTqvrwvFLEDLK 337
Cdd:cd05915 52 VATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVE-----AIRG-----ELKTVQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 338 ADVTTADKLWIFAHLLM---PRQAQVKQQPEDDAIIL-FTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDR--FMS 411
Cdd:cd05915 122 HFVVMDEKAPEGYLAYEealGEEADPVRVPERAACGMaYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKdvVLP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 412 ALPLFHSFGLTVgLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGnyaRFANPYDFFRVRY-----VVA 486
Cdd:cd05915 202 VVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWL---ALADYLESTGHRLktlrrLVV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 487 GAEKLQDSTRQIwqDKFG-LRILEGYGVTECAPVVSI--------------NVPMAAKPGT--VGRILPGLDARLLAVPg 549
Cdd:cd05915 278 GGSAAPRSLIAR--FERMgVEVRQGYGLTETSPVVVQnfvkshleslseeeKLTLKAKTGLpiPLVRLRVADEEGRPVP- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 550 iEDGGRLQ---LKGPNVMNGYLRVEnpgvlEAPTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSL 626
Cdd:cd05915 355 -KDGKALGevqLKGPWITGGYYGNE-----EATRSALTPD----GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISS 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937565178 627 EMVETLATAVSAEKMHATVVKSDASKGEALVLFT--TDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05915 425 VDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvpRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGK 501
|
|
| LPLAT |
cd06551 |
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ... |
5-171 |
1.85e-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: 63.59 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 5 FFRTLFRVLFRIRVTGDTQALYGERVLITPNHVSFLDGVLLALFLPVRPVFAVYSSISE-----KWYMRWLKplidFVPL 79
Cdd:cd06551 3 YLLLNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLLLERGLRRDVYGLMDEellerYPFFTRLG----AFSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 80 DPTKPMMI----KHLVRLI-GQGRPVVIFPEGRIS-VTGSLMKIYDGAGFVAAKSQATVVPLridgaeltFFSRLKGLVK 153
Cdd:cd06551 79 DRDSPRSAakslKYVARLLsKPGSVVWIFPEGTRTrRDKRPLQFKPGVAHLAEKAGVPIVPV--------ALRYTFELFE 150
|
170
....*....|....*...
gi 1937565178 154 QrlFPKITLHILPPTSLP 171
Cdd:cd06551 151 Q--FPEIFVRIGPPIPYA 166
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
355-432 |
5.42e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 65.73 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPEDDAIIL-FTSGSEGNPKGVVHSHKSILANVEQIktIADF--------TANDRFMSALPLFHSFGLTVGL 425
Cdd:PRK05850 149 PRGSDARPRDLPSTAYLqYTSGSTRTPAGVMVSHRNVIANFEQL--MSDYfgdtggvpPPDTTVVSWLPFYHDMGLVLGV 226
|
....*..
gi 1937565178 426 FTPLLTG 432
Cdd:PRK05850 227 CAPILGG 233
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
258-622 |
5.55e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 65.47 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 258 IGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSRQFLDKgklwhLPEQLTQVRWVfledlk 337
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAEL-----LDGLDPGVRVI------ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 338 aDVTT---ADKLWIFAHLLMPRQAQvkqQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALP 414
Cdd:PRK07867 126 -NVDSpawADELAAHRDAEPPFRVA---DPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 415 LFHSFGLTVGLFTPLLTGAEVFLYPSplhyrivpelvydrnctvlFGTSTFLGNYARFANPYDFF---RVRYVVAGAEKL 491
Cdd:PRK07867 202 LFHSNAVMAGWAVALAAGASIALRRK-------------------FSASGFLPDVRRYGATYANYvgkPLSYVLATPERP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 492 QD-------------STRQI--WQDKFGLRILEGYGVTECApvVSINVPMAAKPGTVGRILPGL-----DARLLAVPG-I 550
Cdd:PRK07867 263 DDadnplrivygnegAPGDIarFARRFGCVVVDGFGSTEGG--VAITRTPDTPPGALGPLPPGVaivdpDTGTECPPAeD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 551 EDGGRLQ----------LKGPNVMNGYLRveNPgvlEApTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA 620
Cdd:PRK07867 341 ADGRLLNadeaigelvnTAGPGGFEGYYN--DP---EA-DAERMRG----GVYWSGDLAYRDADGYAYFAGRLGDWMRVD 410
|
..
gi 1937565178 621 GE 622
Cdd:PRK07867 411 GE 412
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
355-701 |
1.04e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 64.64 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPE---DDAI-ILFTSGSEGNPKGVVHSHKSILA--NVEQIKTIA--DFTANDRFMSALPLFHSFGLTvGLF 426
Cdd:PRK05857 155 LDAASLAGNADqgsEDPLaMIFTSGTTGEPKAVLLANRTFFAvpDILQKEGLNwvTWVVGETTYSPLPATHIGGLW-WIL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 427 TPLL------TGAEvflypsplHYRIVPELVYDR--NCTVLFGTS-TFLGNYARFANPyDFFRVRYVVAGAeklqdsTRQ 497
Cdd:PRK05857 234 TCLMhgglcvTGGE--------NTTSLLEILTTNavATTCLVPTLlSKLVSELKSANA-TVPSLRLVGYGG------SRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 498 IWQD-KF----GLRILEGYGVTE------CAPVVSINVPmAAKPGTVGRILPGLDARLLAV----PGIEDG------GRL 556
Cdd:PRK05857 299 IAADvRFieatGVRTAQVYGLSEtgctalCLPTDDGSIV-KIEAGAVGRPYPGVDVYLAATdgigPTAPGAgpsasfGTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 557 QLKGPNVMNGYLrvENPgvleaptaENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAV 636
Cdd:PRK05857 378 WIKSPANMLGYW--NNP--------ERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGV 447
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937565178 637 SAEKMHATVVKSDASKGEAL---VLFTTD------GELKRDALLRYAREHgiPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK05857 448 SGVREAACYEIPDEEFGALVglaVVASAEldesaaRALKHTIAARFRRES--EPMARPSTIVIVTDIPRTQSGK 519
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
321-713 |
1.37e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 64.15 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 321 LPEQLTQVRWVFLEDLKaDVTTADKLWIFAHllmprqaQVKQqpEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTI 400
Cdd:PRK04813 109 LPLEILGIPVITLDELK-DIFATGNPYDFDH-------AVKG--DDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLED 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 401 ADFTANDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLHYRivPELVYDR----NCTVLFGTSTF---------- 465
Cdd:PRK04813 179 FALPEGPQFLNQAPY--SFDLSVmDLYPTLASGGTLVALPKDMTAN--FKQLFETlpqlPINVWVSTPSFadmclldpsf 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 466 ----LGNYARFanpydFFrvryvvAGaEKLQDSTRQIWQDKF-GLRILEGYGVTE-CAPVVSINV-----------PMA- 527
Cdd:PRK04813 255 neehLPNLTHF-----LF------CG-EELPHKTAKKLLERFpSATIYNTYGPTEaTVAVTSIEItdemldqykrlPIGy 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 528 AKPGTVGRIlpgLDARLLAVPGIEDgGRLQLKGPNVMNGYLrvENPgvleAPTAENVNGEVETGWYDTGDIVRFDDqGFV 607
Cdd:PRK04813 323 AKPDSPLLI---IDEEGTKLPDGEQ-GEIVISGPSVSKGYL--NNP----EKTAEAFFTFDGQPAYHTGDAGYLED-GLL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 608 QIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALV--LFTTDGELKRDALLRYAREHG----IPE 681
Cdd:PRK04813 392 FYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIayVVPKEEDFEREFELTKAIKKElkerLME 471
|
410 420 430
....*....|....*....|....*....|..
gi 1937565178 682 LAVPRDIRYLKQLPVLGSGKPDfvtLKGMVEE 713
Cdd:PRK04813 472 YMIPRKFIYRDSLPLTPNGKID---RKALIEE 500
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
349-708 |
2.41e-10 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 63.55 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 349 FAHLLMPRQAQVKQQP----EDDAIILFTSGSEGNPKGVVHSHKSIL-ANVEQIKTIAdFTANDRFMSALPLFHS-FGLT 422
Cdd:PRK08008 153 FTQLKAQQPATLCYAPplstDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQCA-LRDDDVYLTVMPAFHIdCQCT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 423 VGLftPLLT-GA---------------EVFLYPS------PLHYRIV---PELVYDRN-C--TVLFgtstflgnyarFAN 474
Cdd:PRK08008 232 AAM--AAFSaGAtfvllekysarafwgQVCKYRAtiteciPMMIRTLmvqPPSANDRQhClrEVMF-----------YLN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 475 pydffrvryvVAGAEKLQDSTRqiwqdkFGLRILEGYGVTECapVVSInvpMAAKPG------TVGRilPGL--DARLLA 546
Cdd:PRK08008 299 ----------LSDQEKDAFEER------FGVRLLTSYGMTET--IVGI---IGDRPGdkrrwpSIGR--PGFcyEAEIRD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 547 VPGIE----DGGRLQLK---GPNVMNGYLrvENPgvlEApTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKI 619
Cdd:PRK08008 356 DHNRPlpagEIGEICIKgvpGKTIFKEYY--LDP---KA-TAKVLEAD---GWLHTGDTGYVDEEGFFYFVDRRCNMIKR 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 620 AGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEAL---VLFTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPV 696
Cdd:PRK08008 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIkafVVLNEGETLSEEEFFAFCEQN-MAKFKVPSYLEIRKDLPR 505
|
410
....*....|..
gi 1937565178 697 LGSGKPDFVTLK 708
Cdd:PRK08008 506 NCSGKIIKKNLK 517
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
365-714 |
2.87e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 63.37 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSI---------LANVEQIKT---IADFTAND---RFMSALPLFHSFGLTvGLFTPL 429
Cdd:PRK07798 163 PDDLYLLYTGGTTGMPKGVMWRQEDIfrvllggrdFATGEPIEDeeeLAKRAAAGpgmRRFPAPPLMHGAGQW-AAFAAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 430 LTGAEVFLYPSP-LHYRIVPELVYDRNCTVLFgtstFLGN-YAR-------FANPYDFFRVRYVVAGAEKLQDSTRQIWQ 500
Cdd:PRK07798 242 FSGQTVVLLPDVrFDADEVWRTIEREKVNVIT----IVGDaMARplldaleARGPYDLSSLFAIASGGALFSPSVKEALL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 501 DKF-GLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARLLA------VPGIEDGGRLQLKGPnVMNGYLRVenp 573
Cdd:PRK07798 318 ELLpNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDedgnpvEPGSGEIGWIARRGH-IPLGYYKD--- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 574 gvlEAPTAEN---VNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlatavSAEKMH-----ATV 645
Cdd:PRK07798 394 ---PEKTAETfptIDGV---RYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVE------EALKAHpdvadALV 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 646 VKSDASK-GE---ALVLFTTDGELKRDALLRYAREHgipeLA---VPRDIRYLKQLPVLGSGKPDFVTLKGMVEEA 714
Cdd:PRK07798 462 VGVPDERwGQevvAVVQLREGARPDLAELRAHCRSS----LAgykVPRAIWFVDEVQRSPAGKADYRWAKEQAAER 533
|
|
| LPLAT_ACT14924-like |
cd07986 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ... |
10-156 |
4.39e-10 |
|
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: 59.95 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 10 FRVLFRIRVTGDTQALYGERVLITPNH-VSFLDGVLLA-LFLPVRPVFAVY-----SSISEkwymrwLKPLidFVPLDPT 82
Cdd:cd07986 4 LNVQLEVDVSGLENIPKDGPVVIVANHpFGILDGLILAdLLGSVRPDVRILanqllSKIPE------LRDL--FIPVDPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 83 KPM--------MIKHLVRLIGQGRPVVIFPEGRISV-TGSLMKIYD-----GAGFVAAKSQATVVPLRIDGAELTFFSRL 148
Cdd:cd07986 76 EGRaalaknreSLREALRHLKNGGALIIFPAGRVSTaSPPFGRVSDrpwnpFVARLARKAKAPVVPVYFSGRNSRLFYLA 155
|
....*...
gi 1937565178 149 kGLVKQRL 156
Cdd:cd07986 156 -GLIHPTL 162
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
366-622 |
6.98e-10 |
|
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: 61.16 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 366 DDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsplhYR 445
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFV------RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 446 IVPE----LVYDRNCTVLFGTSTFLGNYARF--ANPYDFFRVRYVVAGAEKLQDSTrqIWQDKFGlRILEGYGVTECAPV 519
Cdd:cd17636 75 VDAEevleLIEAERCTHAFLLPPTIDQIVELnaDGLYDLSSLRSSPAAPEWNDMAT--VDTSPWG-RKPGGYGQTEVMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 520 VSINVPMAAKPGTVGRILPGLDARLLAVPGIE--DG--GRLQLKGPNVMNGYLRvenpgvleaptAENVNGE-VETGWYD 594
Cdd:cd17636 152 ATFAALGGGAIGGAGRPSPLVQVRILDEDGREvpDGevGEIVARGPTVMAGYWN-----------RPEVNARrTRGGWHH 220
|
250 260
....*....|....*....|....*...
gi 1937565178 595 TGDIVRFDDQGFVQIQGRAKRFAKIAGE 622
Cdd:cd17636 221 TNDLGRREPDGSLSFVGPKTRMIKSGAE 248
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
355-701 |
1.53e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 60.87 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPeddAIILFTSGSEGNPKGVVHSHKSI--LANVEQIK-TIADFTANDRFMSALPLFHS----FGLTVGLFt 427
Cdd:PRK12406 145 PYDGPPVPQP---QSMIYTSGTTGHPKGVRRAAPTPeqAAAAEQMRaLIYGLKPGIRALLTGPLYHSapnaYGLRAGRL- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 428 plltGAEVFLYPsplhyRIVPE----LVYDRNCTVLFGTSTFLGNYARFA----NPYDFFRVRYVVAGAEKLQDSTRQIW 499
Cdd:PRK12406 221 ----GGVLVLQP-----RFDPEellqLIERHRITHMHMVPTMFIRLLKLPeevrAKYDVSSLRHVIHAAAPCPADVKRAM 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 500 QDKFGLRILEGYGVTECAPVVSINVPMA-AKPGTVGRILPGLDARLLAvpgiEDGGRLQLKGPNVMngYLRVE-NPGVle 577
Cdd:PRK12406 292 IEWWGPVIYEYYGSTESGAVTFATSEDAlSHPGTVGKAAPGAELRFVD----EDGRPLPQGEIGEI--YSRIAgNPDF-- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 578 apTAEN---VNGEVE-TGWYDTGDIVRFDDQGFVQIQGRAKRFAkIAGEmVSLEMVETLATAVSAEKMHATVV--KSDAS 651
Cdd:PRK12406 364 --TYHNkpeKRAEIDrGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGG-VNIYPAEIEAVLHAVPGVHDCAVfgIPDAE 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1937565178 652 KGEALVLFT---TDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK12406 440 FGEALMAVVepqPGATLDEADIRAQLKAR-LAGYKVPKHIEIMAELPREDSGK 491
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
363-614 |
2.40e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 363 QPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKT--IADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpS 440
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-S 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 441 PLHY--RIV----------------PELVYdRNCTVLFGTSTFLGnyarfanpYDFFRVRYVVAGAEKLQDSTRQIWQDK 502
Cdd:PRK05691 243 PAYFleRPLrwleaiseyggtisggPDFAY-RLCSERVSESALER--------LDLSRWRVAYSGSEPIRQDSLERFAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 503 F---GLR---ILEGYGVTECAPVVSINVP-------------MA---AKPGT------VGRILPG-----LDARLLAVPG 549
Cdd:PRK05691 314 FaacGFDpdsFFASYGLAEATLFVSGGRRgqgipaleldaeaLArnrAEPGTgsvlmsCGRSQPGhavliVDPQSLEVLG 393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 550 IEDGGRLQLKGPNVMNGYLRveNPgvlEAPTAENVNGEVETgWYDTGDIvRFDDQGFVQIQGRAK 614
Cdd:PRK05691 394 DNRVGEIWASGPSIAHGYWR--NP---EASAKTFVEHDGRT-WLRTGDL-GFLRDGELFVTGRLK 451
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
354-717 |
2.99e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 60.05 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 354 MPRQAQVKQqpEDDAIILFTSGSEGNPKGVVHSHKS---ILANveqikTIADF----TANDRFMSALPLFHSFGltVGLF 426
Cdd:PRK07470 154 RVANAAVDH--DDPCWFFFTSGTTGRPKAAVLTHGQmafVITN-----HLADLmpgtTEQDASLVVAPLSHGAG--IHQL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 427 TPLLTGAEVFLYPSPlhyRIVPE----LVYDRNCTVLFGTSTFLGNYARF--ANPYDFFRVRYVV-AGAEKL-QDSTRQI 498
Cdd:PRK07470 225 CQVARGAATVLLPSE---RFDPAevwaLVERHRVTNLFTVPTILKMLVEHpaVDRYDHSSLRYVIyAGAPMYrADQKRAL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 499 wqDKFGLRILEGYGVTECAPVVSINVPM--------AAKPGTVGRILPG-----LDARLLAVPGIEDGgRLQLKGPNVMN 565
Cdd:PRK07470 302 --AKLGKVLVQYFGLGEVTGNITVLPPAlhdaedgpDARIGTCGFERTGmevqiQDDEGRELPPGETG-EICVIGPAVFA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 566 GYLRveNPgvlEApTAENVNGevetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVEtlatavsaEK--MHA 643
Cdd:PRK07470 379 GYYN--NP---EA-NAKAFRD----GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIE--------EKllTHP 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 644 TVVKS------DASKGE---ALVLFTTDGELKRDALLRYArEHGIPELAVPRDIRYLKQLPVLGSGKpdfVTLKGMVEEA 714
Cdd:PRK07470 441 AVSEVavlgvpDPVWGEvgvAVCVARDGAPVDEAELLAWL-DGKVARYKLPKRFFFWDALPKSGYGK---ITKKMVREEL 516
|
...
gi 1937565178 715 EQQ 717
Cdd:PRK07470 517 EER 519
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
375-714 |
4.51e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 59.62 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 375 GSEGNPKGVVHSHK----SILANVEqiktIADFTANDRFMSALPLFHSFGLT----VGLFtplLTGAEVFLY--PSPL-- 442
Cdd:PRK10946 192 GSTGTPKLIPRTHNdyyySVRRSVE----ICGFTPQTRYLCALPAAHNYPMSspgaLGVF---LAGGTVVLApdPSATlc 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 443 -----HYRI-----VPELVydrnctvlfgtSTFLGNYARFANPYDFFRVRYVVAGAEKLQDST-RQI-------WQDKFG 504
Cdd:PRK10946 265 fplieKHQVnvtalVPPAV-----------SLWLQAIAEGGSRAQLASLKLLQVGGARLSETLaRRIpaelgcqLQQVFG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 505 LRilEG---YGVTECAPVVSINvpmaakpgTVGR-ILPG-----LDARLLAVPgieDG--GRLQLKGPNVMNGYLRvenp 573
Cdd:PRK10946 334 MA--EGlvnYTRLDDSDERIFT--------TQGRpMSPDdevwvADADGNPLP---QGevGRLMTRGPYTFRGYYK---- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 574 gvleAPtAENVNGEVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKG 653
Cdd:PRK10946 397 ----SP-QHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937565178 654 EALVLF-TTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPDFVTLKGMVEEA 714
Cdd:PRK10946 472 EKSCAFlVVKEPLKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASR 533
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
322-700 |
6.08e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 58.99 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 322 PEQLTQVRWVFLEDLKADVTTADklWIFAHLLMPRQ--------AQVKQQPEDDAIILFT-SGSEGNPKGVVHSHKSILA 392
Cdd:PRK06164 131 PDALPPLRAIAVVDDAADATPAP--APGARVQLFALpdpappaaAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLR 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 393 NVEQIKTIADFTANDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYPSPLHYRIVpELVYDRNCTVLFGTSTFLGNYARF 472
Cdd:PRK06164 209 HARAIARAYGYDPGAVLLAALPFCGVFGFS-TLLGALAGGAPLVCEPVFDAARTA-RALRRHRVTHTFGNDEMLRRILDT 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 473 A-NPYDFFRVRYVvaGAEKLQDSTRQI--WQDKFGLRILEGYGVTECAPVVSINvPMA-------------AKPGTVGRI 536
Cdd:PRK06164 287 AgERADFPSARLF--GFASFAPALGELaaLARARGVPLTGLYGSSEVQALVALQ-PATdpvsvriegggrpASPEARVRA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 537 LPGLDARLLAvPGIEdgGRLQLKGPNVMNGYLrvENPgvlEApTAENVNGEvetGWYDTGDI-VRFDDQGFVqIQGRAKR 615
Cdd:PRK06164 364 RDPQDGALLP-DGES--GEIEIRAPSLMRGYL--DNP---DA-TARALTDD---GYFRTGDLgYTRGDGQFV-YQTRMGD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 616 FAKIAGEMVS-LEMVETLAtavSAEKMHATVVKSDASKGEALV---LFTTDGELKRDALLRYAREHGIPELAVPRDIRYL 691
Cdd:PRK06164 431 SLRLGGFLVNpAEIEHALE---ALPGVAAAQVVGATRDGKTVPvafVIPTDGASPDEAGLMAACREALAGFKVPARVQVV 507
|
....*....
gi 1937565178 692 KQLPVLGSG 700
Cdd:PRK06164 508 EAFPVTESA 516
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
364-689 |
7.11e-09 |
|
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: 58.60 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLH 443
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 444 YRIVPElVYDRNCTVLfgtsTFLGNYARF-----ANPYD-FFRVRyvVAGAEKLQDSTRQIWQDKFGLRIL-EGYGVTEc 516
Cdd:cd05937 166 SQFWKD-VRDSGATII----QYVGELCRYllstpPSPYDrDHKVR--VAWGNGLRPDIWERFRERFNVPEIgEFYAATE- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 517 APVVSINvpMAAKPGTVGRI-LPGLDARLLavpgIEDGGRLQLKGPNVMNGYLRVENPGVLEAPTAE------NVNGEVE 589
Cdd:cd05937 238 GVFALTN--HNVGDFGAGAIgHHGLIRRWK----FENQVVLVKMDPETDDPIRDPKTGFCVRAPVGEpgemlgRVPFKNR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 590 TG-------------------------WYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSaeKMHAT 644
Cdd:cd05937 312 EAfqgylhnedatesklvrdvfrkgdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHP--DIAEA 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1937565178 645 VV------KSDASKGEALVLFT---TDGELKRDALLRYAREHGIPELAVPRDIR 689
Cdd:cd05937 390 NVygvkvpGHDGRAGCAAITLEessAVPTEFTKSLLASLARKNLPSYAVPLFLR 443
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
364-630 |
7.39e-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: 58.97 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPL--FHSFGLTVGlfTPLLTGAEV------ 435
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwIGEQMYSVG--QALVCGFIVnfpeep 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 436 --------------FLYP------------------SPLH---YRIVPELVYDRNCTVLFGTSTFLGNYARFA------- 473
Cdd:cd17641 235 etmmedlreigptfVLLPprvwegiaadvrarmmdaTPFKrfmFELGMKLGLRALDRGKRGRPVSLWLRLASWladallf 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 474 ----NPYDFFRVRYVVAGAEKLQDSTRQIWQdKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGLDARllavpg 549
Cdd:cd17641 315 rplrDRLGFSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVR------ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 550 IEDGGRLQLKGPNVMNGYLrvENPgvlEApTAENVNGEvetGWYDTGDIVRFDDQGFVQIQGRAKRFAKIA-GEMVSLEM 628
Cdd:cd17641 388 IDEVGEILVRSPGVFVGYY--KNP---EA-TAEDFDED---GWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQF 458
|
..
gi 1937565178 629 VE 630
Cdd:cd17641 459 IE 460
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
370-701 |
8.14e-09 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 58.54 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 370 ILFTSGSEGNPKGVVHSHKSILANVEQIKTIAD---FTANDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPsplhyRI 446
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALgfgPGADSVYLSPAPLYHAAPFRW-SMTALFMGGTLVLME-----KF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 447 VPE----LV--YDRNCTVLFGT--STFLGNYARFANPYDFFRVRYVVAGAEKLQDSTRQIWQDKFGLRILEGYGVTECAP 518
Cdd:cd05929 204 DPEeflrLIerYRVTFAQFVPTmfVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 519 VVSIN-VPMAAKPGTVGRILPG----LDARLLAVPGIEDGGRLQLKGPnvmnGYLRVENPgvleAPTAENVNgevETGWY 593
Cdd:cd05929 284 LTIINgEEWLTHPGSVGRAVLGkvhiLDEDGNEVPPGEIGEVYFANGP----GFEYTNDP----EKTAAARN---EGGWS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 594 DTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETL---------ATAVSA------EKMHATVVKSD-ASKGEALV 657
Cdd:cd05929 353 TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENAliahpkvldAAVVGVpdeelgQRVHAVVQPAPgADAGTALA 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1937565178 658 lfttdGELK---RDALLRYarehgipelAVPRDIRYLKQLPVLGSGK 701
Cdd:cd05929 433 -----EELIaflRDRLSRY---------KCPRSIEFVAELPRDDTGK 465
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
365-703 |
1.06e-08 |
|
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: 58.25 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKtiaDFTANDRFMSALPlFHSFGLTVG---LFTPLLTGAEVFLYPSP 441
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER---EKTNINFSDKVLQ-FATCSFDVCyqeIFSTLLSGGTLYIIREE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 LHyRIVPEL---VYDRNCTVLFGTSTFL---GNYARFANPYdFFRVRYVVAGAEKLQDStrQIWQDKF---GLRILEGYG 512
Cdd:cd17656 204 TK-RDVEQLfdlVKRHNIEVVFLPVAFLkfiFSEREFINRF-PTCVKHIITAGEQLVIT--NEFKEMLhehNVHLHNHYG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 513 VTECAPVVSINV---------PMAAKPGTVGRILPgLDARLLAVP-GIEdgGRLQLKGPNVMNGYlrVENPGVleapTAE 582
Cdd:cd17656 280 PSETHVVTTYTInpeaeipelPPIGKPISNTWIYI-LDQEQQLQPqGIV--GELYISGASVARGY--LNRQEL----TAE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 583 NVNG---EVETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGEALVLF 659
Cdd:cd17656 351 KFFPdpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAY 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1937565178 660 TTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:cd17656 431 FVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
350-703 |
4.09e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.82 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 350 AHLLmpRQAQVKQQPEDD--AIILFTSGSEGNPKGVVHSHKSILANVEqiKTIADFTANDRFMSALPLFHSFGLTVgLFT 427
Cdd:PRK07824 20 AALL--RDALRVGEPIDDdvALVVATSGTTGTPKGAMLTAAALTASAD--ATHDRLGGPGQWLLALPAHHIAGLQV-LVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 428 PLLTGAE-VFLYPS-----PLHYRIVPELVYDRNCTVLFGTSTF--LGNYARFANPYDFFRVryVVAGA---EKLQDSTR 496
Cdd:PRK07824 95 SVIAGSEpVELDVSagfdpTALPRAVAELGGGRRYTSLVPMQLAkaLDDPAATAALAELDAV--LVGGGpapAPVLDAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 497 QIwqdkfGLRILEGYGVTECAPvvsinvpmaakpGTV--GRILPGLDARLlavpgieDGGRLQLKGPNVMNGYLRVENPG 574
Cdd:PRK07824 173 AA-----GINVVRTYGMSETSG------------GCVydGVPLDGVRVRV-------EDGRIALGGPTLAKGYRNPVDPD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 575 VLeaptaenvngeVETGWYDTGDIVRFDDqGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHATVVKSDASKGE 654
Cdd:PRK07824 229 PF-----------AEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQ 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1937565178 655 ALV--LFTTDGELKRDALLRYAREHGIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK07824 297 RVVaaVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVD 347
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
362-701 |
8.24e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 55.62 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 362 QQPED--DAIIL-FTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY 438
Cdd:PLN02479 189 KPPADewQSIALgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNICLR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 439 psplhyRIVPELVYdrNCTVLFGTSTFLG-----NYARFANPYDFF----RVRYV-VAGAEKLQDSTRQIwqDKFGLRIL 508
Cdd:PLN02479 269 ------QVTAKAIY--SAIANYGVTHFCAapvvlNTIVNAPKSETIlplpRVVHVmTAGAAPPPSVLFAM--SEKGFRVT 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 509 EGYGVTE-------CA--------PVVSiNVPMAAKPGTVGRILPGLDA----RLLAVPGieDG---GRLQLKGPNVMNG 566
Cdd:PLN02479 339 HTYGLSEtygpstvCAwkpewdslPPEE-QARLNARQGVRYIGLEGLDVvdtkTMKPVPA--DGktmGEIVMRGNMVMKG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 567 YLRveNPgvleaptaeNVNGEV-ETGWYDTGDI-VRFDDqGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVSAEKMHAT 644
Cdd:PLN02479 416 YLK--NP---------KANEEAfANGWFHSGDLgVKHPD-GYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASV 483
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 645 VVKSDASKGEALVLFTT--DGELKRDA------LLRYAREHgIPELAVPRDIRYlKQLPVLGSGK 701
Cdd:PLN02479 484 VARPDERWGESPCAFVTlkPGVDKSDEaalaedIMKFCRER-LPAYWVPKSVVF-GPLPKTATGK 546
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
365-530 |
1.29e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 55.12 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 365 EDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPL-- 442
Cdd:PRK07769 180 DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFvr 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 443 -HYRIVPELVYDRNCTVlfGTSTFLGNYArF------------ANPYDFFRVRYVVAGAEKLQDSTRQIWQDKF---GLR 506
Cdd:PRK07769 260 rPGRWIRELARKPGGTG--GTFSAAPNFA-FehaaarglpkdgEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFapyGLP 336
|
170 180
....*....|....*....|....*..
gi 1937565178 507 ---ILEGYGVTECAPVVSiNVPMAAKP 530
Cdd:PRK07769 337 ptaIKPSYGMAEATLFVS-TTPMDEEP 362
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
364-703 |
3.17e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILFTSGSEGNPKGVVHSHKSILANveQIKTIADFTANDRFMSALPLFHSFGLTVGLF--TPLLtGAEVFLYPSP 441
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNN--QLSKVPYLALSEADVIAQTASQSFDISVWQFlaAPLF-GARVEIVPNA 3944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 442 L--HYRIVPELVYDRNCTVLFGTSTFL-GNYARFANPYDffRVRYVVAGAEKLQDSTRQIWQDKF-GLRILEGYGVTECA 517
Cdd:PRK05691 3945 IahDPQGLLAHVQAQGITVLESVPSLIqGMLAEDRQALD--GLRWMLPTGEAMPPELARQWLQRYpQIGLVNAYGPAECS 4022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 518 PVVSI-NVPMAAKPGTVGRI--------LPGLDARLLAVPgIEDGGRLQLKGPNVMNGYlrVENPgVLEAPT-AENVNGE 587
Cdd:PRK05691 4023 DDVAFfRVDLASTRGSYLPIgsptdnnrLYLLDEALELVP-LGAVGELCVAGTGVGRGY--VGDP-LRTALAfVPHPFGA 4098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 588 VETGWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLEMVETLATAVsAEKMHATVVKSDASKGEALV--LFTTDGEL 665
Cdd:PRK05691 4099 PGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQ-AEVREAAVAVQEGVNGKHLVgyLVPHQTVL 4177
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1937565178 666 KRDALLRYAREH---GIPELAVPRDIRYLKQLPVLGSGKPD 703
Cdd:PRK05691 4178 AQGALLERIKQRlraELPDYMVPLHWLWLDRLPLNANGKLD 4218
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
329-482 |
6.40e-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: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 329 RWVFLEDLKADVTTADKLWI---FAHLLMprqaqvkqqpeddaiILFTSGSEGNPKGVVHSHKSILanVEQIKTIA---D 402
Cdd:cd05943 225 KALTLEDFLATGAAGELEFEplpFDHPLY---------------ILYSSGTTGLPKCIVHGAGGTL--LQHLKEHIlhcD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 403 FTANDRFMsalplfhsFGLTVG------LFTPLLTGAEVFLYP-SPLHYR--IVPELVYDRNCTVlFGTS-TFLGNYAR- 471
Cdd:cd05943 288 LRPGDRLF--------YYTTCGwmmwnwLVSGLAVGATIVLYDgSPFYPDtnALWDLADEEGITV-FGTSaKYLDALEKa 358
|
170
....*....|....
gi 1937565178 472 ---FANPYDFFRVR 482
Cdd:cd05943 359 glkPAETHDLSSLR 372
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
364-522 |
7.28e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.07 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDDAIILF-TSGSEGNPKGVVHSHKSILA---NVEQIKTIADFTANDRFMSALplfhSFGLTVGlFTPLLTGAEVflyp 439
Cdd:COG1541 81 PLEEIVRIHaSSGTTGKPTVVGYTRKDLDRwaeLFARSLRAAGVRPGDRVQNAF----GYGLFTG-GLGLHYGAER---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 440 spLHYRIVP----------ELVYDRNCTVLFGTSTF---LGNYARfANPYDF--FRVRYVVAGAEKLQDSTRQIWQDKFG 504
Cdd:COG1541 152 --LGATVIPagggnterqlRLMQDFGPTVLVGTPSYllyLAEVAE-EEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERWG 228
|
170
....*....|....*...
gi 1937565178 505 LRILEGYGVTECAPVVSI 522
Cdd:COG1541 229 IKAYDIYGLTEVGPGVAY 246
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
364-687 |
8.53e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 48.99 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 364 PEDD--AIILFTSGSEGNPKGVVHSHKsilaNVEQIKTIADFTANDRFMSA-----LPLFHSFGLTVgLFTPLLTGAEVF 436
Cdd:cd17632 220 PDDDplALLIYTSGSTGTPKGAMYTER----LVATFWLKVSSIQDIRPPASitlnfMPMSHIAGRIS-LYGTLARGGTAY 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 437 LYPS--------------PLHYRIVP---ELVYDRNCTVLFGTSTF---LGNYARFANPYDFFRV---RYVVA--GAEKL 491
Cdd:cd17632 295 FAAAsdmstlfddlalvrPTELFLVPrvcDMLFQRYQAELDRRSVAgadAETLAERVKAELRERVlggRLLAAvcGSAPL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 492 QDSTRQIWQDKFGLRILEGYGVTEcAPVVSINvpmaakpgtvGRIL--PGLDARLLAVPgiEDG----------GRLQLK 559
Cdd:cd17632 375 SAEMKAFMESLLDLDLHDGYGSTE-AGAVILD----------GVIVrpPVLDYKLVDVP--ELGyfrtdrphprGELLVK 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 560 GPNVMNGYLRveNPGVleapTAENVNgevETGWYDTGDIV-RFDDQGFVQIQGRAKRFAKIAGEMVS---LEMVETLATA 635
Cdd:cd17632 442 TDTLFPGYYK--RPEV----TAEVFD---EDGFYRTGDVMaELGPDRLVYVDRRNNVLKLSQGEFVTvarLEAVFAASPL 512
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937565178 636 V-------SAEKMH--ATVVKS-DASKGEalvlftTDGELK---RDALLRYAREHGIPELAVPRD 687
Cdd:cd17632 513 VrqifvygNSERAYllAVVVPTqDALAGE------DTARLRaalAESLQRIAREAGLQSYEIPRD 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
233-439 |
8.68e-06 |
|
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: 48.88 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTL-FVGRILEK-YSKQGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLSSAITAAQINTIFTSr 310
Cdd:cd05905 16 TWGKLLSRAEkIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 311 qFLDkgklwhLPEQLTQVRWVFLEDLKADVTTADKLWIF-------AHLLMPRQAQVKQQPEDDAIILFTSGSEGNPKGV 383
Cdd:cd05905 95 -EAC------LKGLPKKLLKSKTAAEIAKKKGWPKILDFvkipkskRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937565178 384 VHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
Cdd:cd05905 168 AVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIP 223
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
526-701 |
1.11e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 48.60 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 526 MAAKPGTVGRILPGLDARLLAvpgiEDGGRLqlkgPNVMNGYLRVEN--PGVLEaptaeNVNGE----VET------GWY 593
Cdd:PRK00174 419 TPLKPGSATRPLPGIQPAVVD----EEGNPL----EGGEGGNLVIKDpwPGMMR-----TIYGDherfVKTyfstfkGMY 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 594 DTGDIVRFDDQGFVQIQGRAKRFAKIAGE----------MVSLEMVetlatavsAEkmhATVV-KSDASKGEALVLFTT- 661
Cdd:PRK00174 486 FTGDGARRDEDGYYWITGRVDDVLNVSGHrlgtaeiesaLVAHPKV--------AE---AAVVgRPDDIKGQGIYAFVTl 554
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937565178 662 -DGELKRDALLRYAREH---GIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:PRK00174 555 kGGEEPSDELRKELRNWvrkEIGPIAKPDVIQFAPGLPKTRSGK 598
|
|
| PLN02901 |
PLN02901 |
1-acyl-sn-glycerol-3-phosphate acyltransferase |
14-140 |
1.15e-05 |
|
1-acyl-sn-glycerol-3-phosphate acyltransferase
Pssm-ID: 215488 [Multi-domain] Cd Length: 214 Bit Score: 47.03 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 14 FRIRVTG-------DTQALYgervliTPNHVSFLDgvLLALFLPVRPV-FAVYSSISEKWYMRWLKPLIDFVPL---DPT 82
Cdd:PLN02901 35 YKIEVEGlenlpspDEPAVY------VSNHQSFLD--IYTLFHLGRPFkFISKTSIFLIPIIGWAMYMTGHIPLkrmDRR 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937565178 83 KPM-MIKHLVRLIGQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSQATVVPLRIDGA 140
Cdd:PLN02901 107 SQLeCLKRCMELLKKGASVFFFPEGTRSKDGKLAAFKKGAFSVAAKTGVPVVPITLVGT 165
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
355-713 |
3.30e-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: 47.29 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 355 PRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILAnVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
Cdd:cd05938 134 PASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGAT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 435 VFLYPSplhyrivpelvydrnctvlFGTSTFLGNyARFANPYDFFRV----RYVVAGAEKLQDSTRQ------------I 498
Cdd:cd05938 213 CVLKPK-------------------FSASQFWDD-CRKHNVTVIQYIgellRYLCNQPQSPNDRDHKvrlaignglradV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 499 W---QDKFG-LRILEGYGVTEcAPVVSINvpMAAKPGTVGR-------ILP---------------GLDARLLAVPGIED 552
Cdd:cd05938 273 WrefLRRFGpIRIREFYGSTE-GNIGFFN--YTGKIGAVGRvsylyklLFPfelikfdvekeepvrDAQGFCIPVAKGEP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 553 G---GRLQLKGPnvMNGYLRveNPGVLEAPTAENV--NGEVetgWYDTGDIVRFDDQGFVQIQGRAKRFAKIAGEMVSLE 627
Cdd:cd05938 350 GllvAKITQQSP--FLGYAG--DKEQTEKKLLRDVfkKGDV---YFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATT 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 628 MVETLATAV----SAEKMHATVVKSDASKGEALVLFTTDGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSgkpd 703
Cdd:cd05938 423 EVADVLGLLdflqEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREY-LPAYARPRFLRIQDSLEITGT---- 497
|
410
....*....|.
gi 1937565178 704 FVTLKG-MVEE 713
Cdd:cd05938 498 FKQQKVrLVEE 508
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
370-463 |
3.45e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 47.10 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 370 ILFTSGSEGNPKGVVHSHKSILanVEQIKTIA---DFTANDRFMsalplfhsFGLTVG------LFTPLLTGAEVFLYP- 439
Cdd:PRK03584 268 ILYSSGTTGLPKCIVHGHGGIL--LEHLKELGlhcDLGPGDRFF--------WYTTCGwmmwnwLVSGLLVGATLVLYDg 337
|
90 100 110
....*....|....*....|....*....|
gi 1937565178 440 SPLHyrivP------ELVYDRNCTVlFGTS 463
Cdd:PRK03584 338 SPFY----PdpnvlwDLAAEEGVTV-FGTS 362
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
233-432 |
1.45e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 45.12 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 233 TYRKLLTKTLFVGRILEKYSKQGEKIGLMLPN-----AGISAAVIFGAVSrgrIPAMMNYTAG-VKGLSSAITAAQINTI 306
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQVAGPGDRVAILAPQgidyvAGFFAAIKAGTIA---VPLFAPELPGhAERLDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 307 FTS-------RQFLDKgklwhLPeQLTQVRWVFLEDLKADVttadklwifAHLLMPRQAQVkqqpEDDAIILFTSGSEGN 379
Cdd:PRK12476 147 LTTtaaaeavEGFLRN-----LP-RLRRPRVIAIDAIPDSA---------GESFVPVELDT----DDVSHLQYTSGSTRP 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937565178 380 PKGVVHSHKSILANVEQ-IKTIADFTANDRFMSALPLFHSFGLTVGLFtPLLTG 432
Cdd:PRK12476 208 PVGVEITHRAVGTNLVQmILSIDLLDRNTHGVSWLPLYHDMGLSMIGF-PAVYG 260
|
|
| LPLAT_LPCAT1-like |
cd07991 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ... |
6-106 |
2.07e-04 |
|
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: 43.36 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 6 FRTLFRVL--FRIRVTGdTQALYGERVLITPNHVSFLDGVLLALFLPvrpvfavYSSISEKWyMRWLkPLI-------DF 76
Cdd:cd07991 1 ARVLLFAFgfYVIKVHG-KPDPPEAPRIIVANHTSFIDPLILFSDLF-------PSIVAKKE-LGKL-PFIgtilralGC 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 1937565178 77 VPLDPTKPMMIKHLVRLI------GQGRPVVIFPEG 106
Cdd:cd07991 71 IFVDRSEPKDRKKVVEEIkeratdPNWPPILIFPEG 106
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
643-701 |
2.42e-04 |
|
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: 40.22 E-value: 2.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937565178 643 ATVV-KSDASKGEALVLFTT---DGELKRDALLRYAREHgIPELAVPRDIRYLKQLPVLGSGK 701
Cdd:pfam13193 15 AAVVgVPDELKGEAPVAFVVlkpGVELLEEELVAHVREE-LGPYAVPKEVVFVDELPKTRSGK 76
|
|
| COG3176 |
COG3176 |
Putative hemolysin [General function prediction only]; |
5-145 |
2.70e-04 |
|
Putative hemolysin [General function prediction only];
Pssm-ID: 442409 Cd Length: 270 Bit Score: 43.49 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 5 FFRTLFRvLFRIRVTGDTQALygER------VLITPNH-VSFLDGV-LLALFLPVRPVFAVYSS-----ISEKWYmrwlK 71
Cdd:COG3176 45 FLRYVFE-ELGARLEVPEGDL--DRidadghLLVVANHpLGILDGLaLLKLVGTVRPDYRILANdlalrIPGGFY----S 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937565178 72 PLidFVPLDPTKPMMIKHLVRLIGQGRPVVIFPEGRISvtgSLMKIYD-----GAGFVAAKSQATVVPLRIDGAELTFF 145
Cdd:COG3176 118 EL--EFPVDPFNLETLKAARRHLLEGGRSCVFPAGRVS---GARRVIDllwsgLAAKLARKAGAPVVPVYFDGRNSGLF 191
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
352-437 |
1.21e-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: 42.12 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 352 LLMPRQAQVKQQPEDDAIILFTSGSEGNPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSfGLTVGLFTPLLT 431
Cdd:cd17647 96 LIVIRAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHD-PIQRDMFTPLFL 174
|
....*.
gi 1937565178 432 GAEVFL 437
Cdd:cd17647 175 GAQLLV 180
|
|
| LPLAT_AAK14816-like |
cd07992 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ... |
5-106 |
2.24e-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: 39.94 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937565178 5 FFRTLFRVLFR-IRVTGDTQALYGERVLITPNHV-SFLDGVLLALFLPVRPVFAVYSSISEKWYMRWLKPLIDFVPLDPT 82
Cdd:cd07992 4 LSRVILRIYFRrITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPVYRP 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 1937565178 83 K------------PMMIKHLVRLIGQGRPVVIFPEG 106
Cdd:cd07992 84 KdlarggigkisnAAVFDAVGEALKAGGAIGIFPEG 119
|
|
| |
