|
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: 1544.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 1 MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALD 80
Cdd:PRK08043 1 MLFSFFRNLFRVLYRVRVTGDTQALKGERVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQQWYMRWLKPYIDFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 81 PTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKI 160
Cdd:PRK08043 81 PTKPMAIKHLVRLVEQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 161 SIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKK 240
Cdd:PRK08043 161 TLHILPPTQLPMPDAPRARDRRKLAGEMLHQIMMEARMAVRPRETLYEALLSAQYRYGAGKPCIEDVNFTPDSYRKLLKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 241 TLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH 320
Cdd:PRK08043 241 TLFVGRILEKYSVEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 321 LPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTI 400
Cdd:PRK08043 321 LPEQLTQVRWVYLEDLKDDVTTADKLWIFAHLLMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 401 ADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFAR 480
Cdd:PRK08043 401 ADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFAR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 481 VRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRG 560
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQGGRLQLKG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 561 PNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEG 640
Cdd:PRK08043 561 PNIMNGYLRVEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDK 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138635 641 QHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV 718
Cdd:PRK08043 641 QHATAIKSDASKGEALVLFTTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQHD 718
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
4-714 |
0e+00 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 902.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 4 RLLRALFRGLFRVTIDGvtdqFKH-----EKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWymrWLKPY---VD 75
Cdd:PRK06814 429 DIFSILFRAFYRVEVKG----LENlqkagKKAVIAANHVSFLDGPLLAAYLPEEPTFAIDTDIAKAW---WVKPFlklAK 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 76 FVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTR 155
Cdd:PRK06814 502 ALPVDPTNPMATRTLIKEVQKGEKLVIFPEGRITVTGSLMKIYDGPGMIADKAGAMVVPVRIDGLQFTHFSRLKNQVRRK 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 156 WFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPR-ETLFEALLSAQTRYGRFKPCIEDVSFKEDSY 234
Cdd:PRK06814 582 WFPKVTVTILPPVKLAVDPELKGRERRSAAGAALYDIMSDMMFETSDYdRTLFEALIEAAKIHGFKKLAVEDPVNGPLTY 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 235 QTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLE 314
Cdd:PRK06814 662 RKLLTGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAFIE 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 315 KGKLTHLPEQV-NEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLAN 393
Cdd:PRK06814 742 KARLGPLIEALeFGIRIIYLEDVRAQIGLADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLAN 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 394 VEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFA 473
Cdd:PRK06814 822 RAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILFGTDTFLNGYARYA 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 474 HPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQG 553
Cdd:PRK06814 902 HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGIDEG 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 554 GRLQLRGPNIMRGYLRVENPGVLEQPSaenaqgeldANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLA 633
Cdd:PRK06814 982 GRLFVRGPNVMLGYLRAENPGVLEPPA---------DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELA 1052
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 634 ISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQD 713
Cdd:PRK06814 1053 AELWPDALHAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEE 1132
|
.
gi 488138635 714 P 714
Cdd:PRK06814 1133 A 1133
|
|
| 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: 620.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 225 EDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLK 304
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 305 TIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAML------PQQADGSALILFTSGSEG 378
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPPKWLLrifgvaPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 379 NPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTV 458
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 459 LFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVP-MAAKVNTVGRIL 537
Cdd:cd05909 241 LLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPqSPNKEGTVGRPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 538 PGMEARLINVPG-----IAQGGRLQLRGPNIMRGYLRVENPGVLeqpsaenaqgELDANWYDTGDIVTLDEQGFCAIRGR 612
Cdd:cd05909 321 PGMEVKIVSVETheevpIGEGGLLLVRGPNVMLGYLNEPELTSF----------AFGDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 613 VKRFAKLAGEMVSLESVEQLAISLSPE-GQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVV 691
Cdd:cd05909 391 LSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQV 470
|
490 500
....*....|....*....|
gi 488138635 692 KALPLLGSGKPDFVTLGKMA 711
Cdd:cd05909 471 EEIPLLGTGKPDYVTLKALA 490
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
5-712 |
2.02e-156 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 482.89 E-value: 2.02e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 5 LLRALFRGLFRVTIDGVTD-QFKHEKLIItPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTN 83
Cdd:PRK08633 418 LLLLLMHTRYRLRVEGRENiPAKGGALLL-GNHVSWIDWALLQAASPRPIRFVMERSIYEKWYLKWFFKLFGVIPISSGG 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 84 PMAIKHLVRM-VEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRW--FPKI 160
Cdd:PRK08633 497 SKESLEFIRKaLDDGEVVCIFPEGAITRNGQLNEFKRGFELIVKGTDVPIIPFYIRGLWGSIFSRASGKFLWRWptRIPY 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 161 SIHVLPATTIPMPQAPRSRERRVLAgehLHTIMMAARMATvpRETLFEALLSAQTRYGrFKPCIEDVSFKEDSYQTLLKK 240
Cdd:PRK08633 577 PVTVAFGKPMPAHSTAHEVKQAVFE---LSFDSWKSRKEA--LPPLAEAWIDTAKRNW-SRLAVADSTGGELSYGKALTG 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 241 TLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTH 320
Cdd:PRK08633 651 ALALARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKG 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 321 LPEQVNE-VNWVYLEDLKDTVTLTDKL-----------WILFHLCFPrramlPQQADGSALILFTSGSEGNPKGVVHSHA 388
Cdd:PRK08633 731 FDLELPEnVKVIYLEDLKAKISKVDKLtallaarllpaRLLKRLYGP-----TFKPDDTATIIFSSGSEGEPKGVMLSHH 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 389 SLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGN 468
Cdd:PRK08633 806 NILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRL 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 469 YARF--AHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVP----------MAAKVNTVGRI 536
Cdd:PRK08633 886 YLRNkkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaadfkrqTGSKEGSVGMP 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 537 LPGMEARLIN-------VPGIAqgGRLQLRGPNIMRGYLRveNPgvleQPSAENAQGELDANWYDTGDIVTLDEQGFCAI 609
Cdd:PRK08633 966 LPGVAVRIVDpetfeelPPGED--GLILIGGPQVMKGYLG--DP----EKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTI 1037
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 610 RGRVKRFAKLAGEMVSLESVEQ--LAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRD 687
Cdd:PRK08633 1038 TDRYSRFAKIGGEMVPLGAVEEelAKALGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEELKRAIKESGLPNLWKPSR 1117
|
730 740
....*....|....*....|....*
gi 488138635 688 IRVVKALPLLGSGKPDFVTLGKMAQ 712
Cdd:PRK08633 1118 YFKVEALPLLGSGKLDLKGLKELAL 1142
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
233-717 |
6.35e-98 |
|
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: 309.43 E-value: 6.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTsrq 311
Cdd:COG0318 26 TYAELDARARRLAAALRALGVgPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 flekgklthlpeqvnevnwvyledlkdtvtltdklwilfhlcfprramlpqqadgsALILFTSGSEGNPKGVVHSHASLL 391
Cdd:COG0318 103 --------------------------------------------------------ALILYTSGTTGRPKGVMLTHRNLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 392 ANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSpLHYRVVPELVYDRNCTVLFGTSTFLGNYAR 471
Cdd:COG0318 127 ANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 472 F--AHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINV--PMAAKVNTVGRILPGMEARLINV 547
Cdd:COG0318 206 HpeFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVDE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 548 PGIA----QGGRLQLRGPNIMRGYLRveNPgvleqpsAENAQgELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEM 623
Cdd:COG0318 286 DGRElppgEVGEIVVRGPNVMKGYWN--DP-------EATAE-AFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGEN 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 624 VSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTT---DSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSG 700
Cdd:COG0318 356 VYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrpGAELDAEELRAFLRER-LARYKVPRRVEFVDELPRTASG 434
|
490
....*....|....*..
gi 488138635 701 KPDFVTLGKMAQDPEMS 717
Cdd:COG0318 435 KIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
368-703 |
7.72e-76 |
|
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: 247.58 E-value: 7.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTvGLFTPLMTGSRVFLYPSPLhYRVV 447
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFD-PEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 448 PELVYDRNCTVLFGTSTFLGNYARFA--HPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVP 525
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPesAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 526 --MAAKVNTVGRILPGMEARLINVPGIAQG----GRLQLRGPNIMRGYLRVEnpgvleqpsaENAQGELDANWYDTGDIV 599
Cdd:cd04433 161 ddDARKPGSVGRPVPGVEVRIVDPDGGELPpgeiGELVVRGPSVMKGYWNNP----------EATAAVDEDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 600 TLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLF---TTDSEITRERLIKVARE 676
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVvvlRPGADLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*..
gi 488138635 677 NGVPeLAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd04433 311 RLAP-YKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
233-711 |
5.74e-64 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 222.00 E-value: 5.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSriLQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQF 312
Cdd:PRK06334 47 SYNQVRKAVIALA--TKVSKYPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 313 LEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAML------PQQADGSALILFTSGSEGNPKGVVHS 386
Cdd:PRK06334 125 MQHLAQTHGEDAEYPFSLIYMEEVRKELSFWEKCRIGIYMSIPFEWLMrwfgvsDKDPEDVAVILFTSGTEKLPKGVPLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 387 HASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGL-TVGLFtPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTF 465
Cdd:PRK06334 205 HANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLF-PLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 466 LGNYARFAHPYD--FARVRYVVAGAEKLAESTKQIWQDKF-GIRILEGYGVTECAPVVAINVPMAAKVNT-VGRILPGME 541
Cdd:PRK06334 284 FDYILKTAKKQEscLPSLRFVVIGGDAFKDSLYQEALKTFpHIQLRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 542 ARLIN----VPgIAQG--GRLQLRGPNIMRGYLRvENPGvleqpsaenaQG--ELD-ANWYDTGDIVTLDEQGFCAIRGR 612
Cdd:PRK06334 364 VLIVSeetkVP-VSSGetGLVLTRGTSLFSGYLG-EDFG----------QGfvELGgETWYVTGDLGYVDRHGELFLKGR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 613 VKRFAKLAGEMVSLESVEQLAIS--LSPEGQHAAAAKTDSAKGEA--LVLFTTDSEITRE--RLIKVARENGVPELAVPR 686
Cdd:PRK06334 432 LSRFVKIGAEMVSLEALESILMEgfGQNAADHAGPLVVCGLPGEKvrLCLFTTFPTSISEvnDILKNSKTSSILKISYHH 511
|
490 500
....*....|....*....|....*
gi 488138635 687 DirvVKALPLLGSGKPDFVTLGKMA 711
Cdd:PRK06334 512 Q---VESIPMLGTGKPDYCSLNALA 533
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
221-614 |
2.99e-62 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.10 E-value: 2.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 221 KPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAII 299
Cdd:pfam00501 11 KTALEVGEGRRLTYRELDERANRLAAGLRALGVgKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 300 AASLKTIVTSRQFLEKG--KLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFhlcFPRRAMLPQQADGSALILFTSGSE 377
Cdd:pfam00501 91 DSGAKVLITDDALKLEEllEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAD---VPPPPPPPPDPDDLAYIIYTSGTT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 378 GNPKGVVHSHASLLANVEQIRTIAD----FTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPS--PLHYRVVPELV 451
Cdd:pfam00501 168 GKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGfpALDPAALLELI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 452 YDRNCTVLFGTSTFLgNY---ARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPM-- 526
Cdd:pfam00501 248 ERYKVTVLYGVPTLL-NMlleAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLde 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 527 -AAKVNTVGRILPGMEARLINVPG-----IAQGGRLQLRGPNIMRGYLRveNPGvleqpsaENAQGELDANWYDTGDIVT 600
Cdd:pfam00501 327 dLRSLGSVGRPLPGTEVKIVDDETgepvpPGEPGELCVRGPGVMKGYLN--DPE-------LTAEAFDEDGWYRTGDLGR 397
|
410
....*....|....
gi 488138635 601 LDEQGFCAIRGRVK 614
Cdd:pfam00501 398 RDEDGYLEIVGRKK 411
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
233-701 |
1.03e-61 |
|
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: 213.96 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQ 311
Cdd:cd05936 26 TYRELDALAEAFAAGLQNLGVqPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 FLEKGKLTHLPEQVNEVNwvyLEDLkdtvtltdklwilfhlcfprramlpqqadgsALILFTSGSEGNPKGVVHSHASLL 391
Cdd:cd05936 106 FTDLLAAGAPLGERVALT---PEDV-------------------------------AVLQYTSGTTGVPKGAMLTHRNLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 392 ANVEQIRTIA--DFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVyDRNCTVLFGTSTFLGNY 469
Cdd:cd05936 152 ANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIR-KHRVTIFPGVPTMYIAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 470 ARFAHP--YDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAIN-VPMAAKVNTVGRILPGMEARLIN 546
Cdd:cd05936 231 LNAPEFkkRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNpLDGPRKPGSIGIPLPGTEVKIVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 547 VPG--IAQG--GRLQLRGPNIMRGYLRvenpgvleQPsAENAQGELDAnWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGE 622
Cdd:cd05936 311 DDGeeLPPGevGELWVRGPQVMKGYWN--------RP-EETAEAFVDG-WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 623 MVSLESVEQlAISLSPEGQHAAAAKT-DSAKGEALVLFTT---DSEITRERLIKVARENgvpeLA---VPRDIRVVKALP 695
Cdd:cd05936 381 NVYPREVEE-VLYEHPAVAEAAVVGVpDPYSGEAVKAFVVlkeGASLTEEEIIAFCREQ----LAgykVPRQVEFRDELP 455
|
....*.
gi 488138635 696 LLGSGK 701
Cdd:cd05936 456 KSAVGK 461
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
233-701 |
1.94e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 206.58 E-value: 1.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTsgakgLQSAIIA-----ASLKTI 306
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVkKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR-----LKPEEIAyilndAEDRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 307 VTSRQFLekGKLTHLPEQVNEVN-WVYLEDlkDTVTLTDKLWILFHlcfprrAMLPQQADGS----------ALILFTSG 375
Cdd:PRK06187 108 LVDSEFV--PLLAAILPQLPTVRtVIVEGD--GPAAPLAPEVGEYE------ELLAAASDTFdfpdidendaAAMLYTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 376 SEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGlFTPLMTGSRVfLYPSPLHYRVVPELVYDRN 455
Cdd:PRK06187 178 TTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLP-YLALMAGAKQ-VIPRRFDPENLLDLIETER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 456 CTVLFGTST---FLGNYARfAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVP------M 526
Cdd:PRK06187 256 VTFFFAVPTiwqMLLKAPR-AYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPedqlpgQ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 527 AAKVNTVGRILPGMEARLIN-----VP-GIAQGGRLQLRGPNIMRGYLRvenpgvLEQPSAENaqgeLDANWYDTGDIVT 600
Cdd:PRK06187 335 WTKRRSAGRPLPGVEARIVDddgdeLPpDGGEVGEIIVRGPWLMQGYWN------RPEATAET----IDGGWLHTGDVGY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 601 LDEQGFCAIRGRVKRFAKLAGEMVS---LESveqlAISlspegQH---AAAA---KTDSAKGE---ALVLFTTDSEITRE 668
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIISGGENIYpreLED----ALY-----GHpavAEVAvigVPDEKWGErpvAVVVLKPGATLDAK 475
|
490 500 510
....*....|....*....|....*....|...
gi 488138635 669 RLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK06187 476 ELRAFLRGR-LAKFKLPKRIAFVDELPRTSVGK 507
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
196-701 |
3.82e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 180.49 E-value: 3.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 196 ARMATVPretlfEALLSAQTRYGRfKPCIEDVSfKEDSYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFG 274
Cdd:PRK07656 2 NEWMTLP-----ELLARAARRFGD-KEAYVFGD-QRLTYAELNARVRRAAAALAALGIgKGDRVAIWAPNSPHWVIAALG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 275 ASLRGRIPALLN--YTSGAKGlqsAIIAAS-LKTIVTSRQFLEKG-KLTHLPEQVNEVnwVYLEDLKDT-VTLTDKLWIL 349
Cdd:PRK07656 75 ALKAGAVVVPLNtrYTADEAA---YILARGdAKALFVLGLFLGVDySATTRLPALEHV--VICETEEDDpHTEKMKTFTD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 350 FHLCFPRRAMLPQ-QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTP 428
Cdd:PRK07656 150 FLAAGDPAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 429 LMTGSRVFLYP--SPLHyrvVPELVYDRNCTVLFGTST---FLGNYARfAHPYDFARVRYVVAGAEKLAESTKQIWQDKF 503
Cdd:PRK07656 230 LMRGATILPLPvfDPDE---VFRLIETERITVLPGPPTmynSLLQHPD-RSAEDLSSLRLAVTGAASMPVALLERFESEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 504 GIR-ILEGYGVTECAPVVAINVP-MAAKV--NTVGRILPGMEARLINVPG----IAQGGRLQLRGPNIMRGYlrvenpgv 575
Cdd:PRK07656 306 GVDiVLTGYGLSEASGVTTFNRLdDDRKTvaGTIGTAIAGVENKIVNELGeevpVGEVGELLVRGPNVMKGY-------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 576 LEQPSAENAQgeLDA-NWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE 654
Cdd:PRK07656 378 YDDPEATAAA--IDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGE 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 488138635 655 ---ALVLFTTDSEITRERLIKVAREngvpELA---VPRDIRVVKALPLLGSGK 701
Cdd:PRK07656 456 vgkAYVVLKPGAELTEEELIAYCRE----HLAkykVPRSIEFLDELPKNATGK 504
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
224-701 |
4.59e-48 |
|
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: 176.63 E-value: 4.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 224 IEDVSFKEDSYQTLLKKTLGVSRILQR-FTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAAS 302
Cdd:cd05911 3 IDADTGKELTYAQLRTLSRRLAAGLRKlGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 303 LKTIVTSRQFLEKGKlthlpEQVNEVNWVY----LEDLKDTVTLTDKLWiLFHLCFPRRAMLPQQADGS---ALILFTSG 375
Cdd:cd05911 83 PKVIFTDPDGLEKVK-----EAAKELGPKDkiivLDDKPDGVLSIEDLL-SPTLGEEDEDLPPPLKDGKddtAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 376 SEGNPKGVVHSHASLLANVEQIRTI--ADFTPRDRFMSSLPLFHAFGLTVGLFTPLmTGSRVFLYPSPlHYRVVPELVYD 453
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLSQVQTFlyGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIMPKF-DSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 454 RNCTVLFGTST---FLGNYARFAhPYDFARVRYVVAGAEKLaesTKQIwQDKFGIR-----ILEGYGVTECAPVVAINVP 525
Cdd:cd05911 235 YKITFLYLVPPiaaALAKSPLLD-KYDLSSLRVILSGGAPL---SKEL-QELLAKRfpnatIKQGYGMTETGGILTVNPD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 526 MAAKVNTVGRILPGMEARLINVP-----GIAQGGRLQLRGPNIMRGYLRveNPgvleqpsAENAQGELDANWYDTGDIVT 600
Cdd:cd05911 310 GDDKPGSVGRLLPNVEAKIVDDDgkdslGPNEPGEICVRGPQVMKGYYN--NP-------EATKETFDEDGWLHTGDIGY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 601 LDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAAAK-TDSAKGE---ALVLFTTDSEITRERLIKVARE 676
Cdd:cd05911 381 FDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEH-PGVADAAVIGiPDEVSGElprAYVVRKPGEKLTEKEVKDYVAK 459
|
490 500 510
....*....|....*....|....*....|....
gi 488138635 677 N---------GVpelavprdiRVVKALPLLGSGK 701
Cdd:cd05911 460 KvasykqlrgGV---------VFVDEIPKSASGK 484
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
364-630 |
5.18e-48 |
|
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: 175.86 E-value: 5.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPL- 442
Cdd:cd05907 86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAEt 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 443 ------HYR-----VVP---ELVYDRNCTVLfgTSTFLGNYARFAHpydFARVRYVVAGAEKLAESTKQIWQdKFGIRIL 508
Cdd:cd05907 166 llddlsEVRptvflAVPrvwEKVYAAIKVKA--VPGLKRKLFDLAV---GGRLRFAASGGAPLPAELLHFFR-ALGIPVY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 509 EGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARlinvpgIAQGGRLQLRGPNIMRGYLRveNPgvleQPSAEnaqgEL 588
Cdd:cd05907 240 EGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVR------IADDGEILVRGPNVMLGYYK--NP----EATAE----AL 303
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488138635 589 DAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLA-GEMVSLESVE 630
Cdd:cd05907 304 DADgWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIE 347
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-707 |
1.69e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 166.08 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 252 TVPGEHVGMLLPNATITAAAIFG----ASLRGRIPALLNYTSGAKGLQSAIIAASLKtIVtsrqFLEKGKLTHLpeqvNE 327
Cdd:cd05922 15 GVRGERVVLILPNRFTYIELSFAvayaGGRLGLVFVPLNPTLKESVLRYLVADAGGR-IV----LADAGAADRL----RD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 328 VNWVYLEDlkDTVTLTDKLWILFHLcfprRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRD 407
Cdd:cd05922 86 ALPASPDP--GTVLDADGIRAARAS----APAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 408 RFMSSLPLFHAFGLTVgLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFA-HPYDFARVRYVVA 486
Cdd:cd05922 160 RALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGfDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 487 GAEKLAESTKQIWQDKF-GIRILEGYGVTECAPVVAINVP--MAAKVNTVGRILPGMEARLINVPGIAQG----GRLQLR 559
Cdd:cd05922 239 AGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPerILEKPGSIGLAIPGGEFEILDDDGTPTPpgepGEIVHR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 560 GPNIMRGYLRvenpgvleQPSAENAQGE-LDANWydTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISlSP 638
Cdd:cd05922 319 GPNVMKGYWN--------DPPYRRKEGRgGGVLH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS-IG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 639 EGQHAAAAKTDSAKGEALVLFTT-DSEITRERLIKVARENGvPELAVPRDIRVVKALPLLGSGKPDFVTL 707
Cdd:cd05922 388 LIIEAAAVGLPDPLGEKLALFVTaPDKIDPKDVLRSLAERL-PPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
365-701 |
1.94e-44 |
|
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: 165.48 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 365 DGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPlhy 444
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKF--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 445 rvVPELVYDR----NCTVLFGTSTFLgnYARFAHP----YDFARVRYVVAGAEKLAESTKQIWQDkFGIRILEGYGVTEC 516
Cdd:cd17631 175 --DPETVLDLierhRVTSFFLVPTMI--QALLQHPrfatTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTET 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 517 APVVAINVP--MAAKVNTVGRILPGMEARLI----NVPGIAQGGRLQLRGPNIMRGYLRveNPgvleqpsAENAQGELDA 590
Cdd:cd17631 250 SPGVTFLSPedHRRKLGSAGRPVFFVEVRIVdpdgREVPPGEVGEIVVRGPHVMAGYWN--RP-------EATAAAFRDG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 591 nWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLFTTDSEITR 667
Cdd:cd17631 321 -WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEavvAVVVPRPGAELDE 399
|
330 340 350
....*....|....*....|....*....|....
gi 488138635 668 ERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd17631 400 DELIAHCRER-LARYKIPKSVEFVDALPRNATGK 432
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
370-701 |
3.02e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 162.45 E-value: 3.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 370 ILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVfLYPSP-LHYRVVP 448
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATM-VFPSPsFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 449 ELVYDRNCTVLFGTST-FLgnyARFAHP----YDFARVRY-VVAGAEKLAESTKQIWQdKFGIR-ILEGYGVTECAPVVA 521
Cdd:cd05917 86 EAIEKEKCTALHGVPTmFI---AELEHPdfdkFDLSSLRTgIMAGAPCPPELMKRVIE-VMNMKdVTIAYGMTETSPVST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 522 ---INVPMAAKVNTVGRILPGMEARLIN-----VPGIAQGGRLQLRGPNIMRGYLrvENPgvleQPSAENAQGEldaNWY 593
Cdd:cd05917 162 qtrTDDSIEKRVNTVGRIMPHTEAKIVDpeggiVPPVGVPGELCIRGYSVMKGYW--NDP----EKTAEAIDGD---GWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 594 DTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAAAKTDSAK-GE---ALVLFTTDSEITRER 669
Cdd:cd05917 233 HTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTH-PKVSDVQVVGVPDERyGEevcAWIRLKEGAELTEED 311
|
330 340 350
....*....|....*....|....*....|....*
gi 488138635 670 LIKVARENgvpeLA---VPRDIRVVKALPLLGSGK 701
Cdd:cd05917 312 IKAYCKGK----IAhykVPRYVFFVDEFPLTVSGK 342
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
368-701 |
7.47e-44 |
|
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: 164.00 E-value: 7.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVeqiRTIAD---FTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPsPLHY 444
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANLAANV---RALVDawrWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP-KFDP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 445 RVVPELVYDRNCTVLFGTSTFlgnYARFAHPYDF-------------ARVRYVVAGAEKLAESTKQIWQDKFGIRILEGY 511
Cdd:cd05941 168 KEVAISRLMPSITVFMGVPTI---YTRLLQYYEAhftdpqfaraaaaERLRLMVSGSAALPVPTLEEWEAITGHTLLERY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 512 GVTECapVVAINVPMAA--KVNTVGRILPGMEARLI----NVPGIAQG-GRLQLRGPNIMRGYLRvenpgvleQPSAENA 584
Cdd:cd05941 245 GMTEI--GMALSNPLDGerRPGTVGMPLPGVQARIVdeetGEPLPRGEvGEIQVRGPSVFKEYWN--------KPEATKE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 QGELDaNWYDTGDIVTLDEQGFCAIRGRVK-RFAKLAGEMVSLESVEQLAISL------------SPE-GQHAAAAKTDS 650
Cdd:cd05941 315 EFTDD-GWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHpgvsecavigvpDPDwGERVVAVVVLR 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488138635 651 AKGEALVLfttdseitrERLIKVARENGVPeLAVPRDIRVVKALPLLGSGK 701
Cdd:cd05941 394 AGAAALSL---------EELKEWAKQRLAP-YKRPRRLILVDELPRNAMGK 434
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
364-701 |
1.46e-42 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 159.93 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQI-RTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPl 442
Cdd:cd05919 90 ADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 443 hyrVVPELVYDRNC----TVLFGTSTFLGNYARFAH--PYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTEC 516
Cdd:cd05919 169 ---PTAERVLATLArfrpTVLYGVPTFYANLLDSCAgsPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEV 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 517 APVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQG----GRLQLRGPNIMRGYLRveNPgvlEQPSAENAQGeldanW 592
Cdd:cd05919 246 GHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPpgeeGDLLVRGPSAAVGYWN--NP---EKSRATFNGG-----W 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 593 YDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLF------TTDSEIT 666
Cdd:cd05919 316 YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFvvlkspAAPQESL 395
|
330 340 350
....*....|....*....|....*....|....*
gi 488138635 667 RERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd05919 396 ARDIHRHLLER-LSAHKVPRRIAFVDELPRTATGK 429
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
233-701 |
5.67e-42 |
|
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: 159.84 E-value: 5.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQ 311
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVkREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 FLEK-----GKLTHLPEQV-------NEVNWVYLEDLKDTVTltdklwilfhlcfPRRAMLPQQADGSALILFTSGSEGN 379
Cdd:cd05959 111 LAPVlaaalTKSEHTLVVLivsggagPEAGALLLAELVAAEA-------------EQLKPAATHADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 380 PKGVVHSHASLLANVEQ-IRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSplhyRVVPELVYDR---- 454
Cdd:cd05959 178 PKGVVHLHADIYWTAELyARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPE----RPTPAAVFKRirry 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 455 NCTVLFGTSTFlgnYARF-----AHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAK 529
Cdd:cd05959 254 RPTVFFGVPTL---YAAMlaapnLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 530 VNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLrvENPgvleQPSAENAQGEldanWYDTGDIVTLDEQG 605
Cdd:cd05959 331 YGTTGKPVPGYEVELRDEDGgdVADGepGELYVRGPSSATMYW--NNR----DKTRDTFQGE----WTRTGDKYVRDDDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 606 FCAIRGRVKRFAKLAGEMVSLESVEQLAIslspegQHAA-------AAKTDSA--KGEALVLF---TTDSEITRERLIKV 673
Cdd:cd05959 401 FYTYAGRADDMLKVSGIWVSPFEVESALV------QHPAvleaavvGVEDEDGltKPKAFVVLrpgYEDSEALEEELKEF 474
|
490 500
....*....|....*....|....*...
gi 488138635 674 AReNGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd05959 475 VK-DRLAPYKYPRWIVFVDELPKTATGK 501
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
368-638 |
1.27e-41 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 160.65 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTpLMTGSRVFLYPSP------ 441
Cdd:COG1022 186 ATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAESPdtlaed 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 -LHYR-----VVP---ELVYDR--------------------------NCTVLFGTSTFLGNYARFAhpydFA------- 479
Cdd:COG1022 265 lREVKptfmlAVPrvwEKVYAGiqakaeeagglkrklfrwalavgrryARARLAGKSPSLLLRLKHA----LAdklvfsk 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 480 -------RVRYVVAGAEKLAESTkqiwqDKF----GIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARlinvp 548
Cdd:COG1022 341 lrealggRLRFAVSGGAALGPEL-----ARFfralGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVK----- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 549 gIAQGGRLQLRGPNIMRGYLRveNPgvleqpsAENAQgELDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLA-GEMVSL 626
Cdd:COG1022 411 -IAEDGEILVRGPNVMKGYYK--NP-------EATAE-AFDADgWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAP 479
|
330
....*....|..
gi 488138635 627 ESVEQlAISLSP 638
Cdd:COG1022 480 QPIEN-ALKASP 490
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
233-701 |
2.18e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 159.12 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQ 311
Cdd:COG0365 41 TYAELRREVNRFANALRALGVkKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 FLEKGKLTHLPEQVNEVnwvyLEDLKD--TVTLTDKL--------WILFHlcfprrAMLPQQ----------ADGSALIL 371
Cdd:COG0365 121 GLRGGKVIDLKEKVDEA----LEELPSleHVIVVGRTgadvpmegDLDWD------ELLAAAsaefepeptdADDPLFIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSHASLLANVE-QIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLY---PSPLHYRVV 447
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAAtTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYegrPDFPDPGRL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 448 PELVYDRNCTVLFGTST----FLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTE-CAPVVAI 522
Cdd:COG0365 271 WELIEKYGVTVFFTAPTairaLMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTEtGGIFISN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 523 NVPMAAKVNTVGRILPGMEARLIN-----VPGiAQGGRLQLRG--PNIMRGYLRveNPgvleqpsAENAQG--ELDANWY 593
Cdd:COG0365 351 LPGLPVKPGSMGKPVPGYDVAVVDedgnpVPP-GEEGELVIKGpwPGMFRGYWN--DP-------ERYRETyfGRFPGWY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 594 DTGDIVTLDEQGFCAIRGRV----KRfaklAGEMVS---LESVeqLAislspegQH------AAAAKTDSAKGEALVLF- 659
Cdd:COG0365 421 RTGDGARRDEDGYFWILGRSddviNV----SGHRIGtaeIESA--LV-------SHpavaeaAVVGVPDEIRGQVVKAFv 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 488138635 660 -----TTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:COG0365 488 vlkpgVEPSDELAKELQAHVREE-LGPYAYPREIEFVDELPKTRSGK 533
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
364-698 |
1.95e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 153.62 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQ----IRTIADftPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYP 439
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkawVPGLGD--GPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPlhyrvVPELVYD----RNCTVLFGTSTFLGNYARFA--HPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGV 513
Cdd:PRK05605 296 AP-----DIDLILDamkkHPPTWLPGVPPLYEKIAEAAeeRGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 514 TECAPVVAINvPMAA--KVNTVGRILPGMEARLIN--------VPGiaQGGRLQLRGPNIMRGYLRVEnpgvleqpsAEN 583
Cdd:PRK05605 371 TETSPIIVGN-PMSDdrRPGYVGVPFPDTEVRIVDpedpdetmPDG--EEGELLVRGPQVFKGYWNRP---------EET 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 584 AQGELDaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAKGE----ALVLF 659
Cdd:PRK05605 439 AKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE-VLREHPGVEDAAVVGLPREDGSeevvAAVVL 516
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488138635 660 TTDSEITRERLIKVARENgVPELAVPRDIRVVKALP--LLG 698
Cdd:PRK05605 517 EPGAALDPEGLRAYCREH-LTRYKVPRRFYHVDELPrdQLG 556
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
233-703 |
5.03e-39 |
|
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: 151.31 E-value: 5.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLN----------YTSGAK--------- 292
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIkKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNpaykkaefefYLADLGsklvltpkg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 293 GLQSAIIAASLKTIVTSRQFLEKGKLtHLPEQVNEVNwvYLEDLKDTVTLTDklwilfhlcfprramlPQQADGSALILF 372
Cdd:cd05926 96 ELGPASRAASKLGLAILELALDVGVL-IRAPSAESLS--NLLADKKNAKSEG----------------VPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 373 TSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSplhyrvvpelvy 452
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPR------------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 453 drnctvlFGTSTFLGNYARF--------------------AHPYD-FARVRYVVAGAEKLAESTKQIWQDKFGIRILEGY 511
Cdd:cd05926 225 -------FSASTFWPDVRDYnatwytavptihqillnrpePNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 512 GVTECAPVVAIN--VPMAAKVNTVGRilP-GMEARLINVPG----IAQGGRLQLRGPNIMRGYLrvENPgvleqpsAENA 584
Cdd:cd05926 298 GMTEAAHQMTSNplPPGPRKPGSVGK--PvGVEVRILDEDGeilpPGVVGEICLRGPNVTRGYL--NNP-------EANA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 QGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAA-AKTDSAKGEALVLFTT-- 661
Cdd:cd05926 367 EAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSH-PAVLEAVAfGVPDEKYGEEVAAAVVlr 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 488138635 662 -DSEITRERLIKVARENgvpeLA---VPRDIRVVKALPLLGSGKPD 703
Cdd:cd05926 446 eGASVTEEELRAFCRKH----LAafkVPKKVYFVDELPKTATGKIQ 487
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
373-711 |
1.41e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 146.86 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 373 TSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVfLYPSPLHYR---VVPE 449
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHV-VLAGPAGYRnpgLFDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 450 ---LVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVP- 525
Cdd:cd05944 89 fwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 526 MAAKVNTVGRILPGMEARLINVPGIaqgGRLQLR-GPNIMrGYLRVENPGV----LEQPSAENAQGelDANWYDTGDIVT 600
Cdd:cd05944 169 GPKRPGSVGLRLPYARVRIKVLDGV---GRLLRDcAPDEV-GEICVAGPGVfggyLYTEGNKNAFV--ADGWLNTGDLGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 601 LDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLFTTDSEITRERLIKVAREN 677
Cdd:cd05944 243 LDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGElpvAYVQLKPGAVVEEEELLAWARDH 322
|
330 340 350
....*....|....*....|....*....|....*
gi 488138635 678 gVPE-LAVPRDIRVVKALPLLGSGKPDFVTLGKMA 711
Cdd:cd05944 323 -VPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
365-614 |
6.72e-38 |
|
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: 147.20 E-value: 6.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 365 DGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLY---PSP 441
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLdkiPSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 L-----HYRV-------VPELVYDRNCTVLFGTSTFLGNYARFAHP------YDFA----------RVRYVVAGAEKLAe 493
Cdd:cd05914 169 KiialaFAQVtptlgvpVPLVIEKIFKMDIIPKLTLKKFKFKLAKKinnrkiRKLAfkkvheafggNIKEFVIGGAKIN- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 494 stKQIWQD--KFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRve 571
Cdd:cd05914 248 --PDVEEFlrTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYK-- 323
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488138635 572 NPgvleqpsaENAQGELDAN-WYDTGDIVTLDEQGFCAIRGRVK 614
Cdd:cd05914 324 NP--------EATAEAFDKDgWFHTGDLGKIDAEGYLYIRGRKK 359
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
362-701 |
5.53e-37 |
|
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: 144.06 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 362 QQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYpSP 441
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ-DI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 LHYRVVPELVYDRNCTVLFGTSTFLGNYARFAH--PYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPV 519
Cdd:cd05903 169 WDPDKALALMREHGVTFMMGATPFLTDLLNAVEeaGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 520 VAI--NVPMAAKVNTVGRILPGMEARLINVPGIA----QGGRLQLRGPNIMRGYLRvenpgvleqpSAENAQGELDANWY 593
Cdd:cd05903 249 VTSitPAPEDRRLYTDGRPLPGVEIKVVDDTGATlapgVEGELLSRGPSVFLGYLD----------RPDLTADAAPEGWF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 594 DTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLFTTDSEITRERL 670
Cdd:cd05903 319 RTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGEracAVVVTKSGALLTFDEL 398
|
330 340 350
....*....|....*....|....*....|.
gi 488138635 671 IKVARENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd05903 399 VAYLDRQGVAKQYWPERLVHVDDLPRTPSGK 429
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
254-702 |
1.74e-36 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 145.87 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 254 PGEHVGMLLPNATITAAAIFGASLRGrIPALLNYTsgakgLQSAIIAASL-----KTIVTSRQFLEKG---KLTHLPEQV 325
Cdd:PRK07529 82 PGDVVAFLLPNLPETHFALWGGEAAG-IANPINPL-----LEPEQIAELLraagaKVLVTLGPFPGTDiwqKVAEVLAAL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 326 NEVNWVYLEDLKDTVTLTDKLWILF----------------------HLCFPRramlPQQADGSALILFTSGSEGNPKGV 383
Cdd:PRK07529 156 PELRTVVEVDLARYLPGPKRLAVPLirrkaharildfdaelarqpgdRLFSGR----PIGPDDVAAYFHTGGTTGMPKLA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 384 VHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLyPSPLHYR---VVP---ELVYDRNCT 457
Cdd:PRK07529 232 QHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVL-ATPQGYRgpgVIAnfwKIVERYRIN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 458 VLFGTSTFLGnyARFAHP---YDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAA-KVNTV 533
Cdd:PRK07529 311 FLSGVPTVYA--ALLQVPvdgHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGErRIGSV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 534 GRILPGMEARLinVPGIAQG-----------GRLQLRGPNIMRGYLRVENpgvleqpsaeNAQGELDANWYDTGDIVTLD 602
Cdd:PRK07529 389 GLRLPYQRVRV--VILDDAGrylrdcavdevGVLCIAGPNVFSGYLEAAH----------NKGLWLEDGWLNTGDLGRID 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 603 EQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAA-AKTDSAKGE---ALVLFTTDSEITRERLIKVARENg 678
Cdd:PRK07529 457 ADGYFWLTGRAKDLIIRGGHNIDPAAIEE-ALLRHPAVALAAAvGRPDAHAGElpvAYVQLKPGASATEAELLAFARDH- 534
|
490 500
....*....|....*....|....*
gi 488138635 679 VPE-LAVPRDIRVVKALPLLGSGKP 702
Cdd:PRK07529 535 IAErAAVPKHVRILDALPKTAVGKI 559
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
365-701 |
1.16e-35 |
|
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: 139.92 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 365 DGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYpSPLHY 444
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM-ARWDR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 445 RVVPELVYDRNCTVLFGTSTF---LGNYARFAHpYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVA 521
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMlvdLLATPEFKT-RDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 522 INVPMAAKVNTVGRILPGMEARLINVP-----GIAQGGRLQLRGPNIMRGYLRVENpgvleqpsaENAQG--ELDAN-WY 593
Cdd:cd05935 242 TNPPLRPKLQCLGIP*FGVDARVIDIEtgrelPPNEVGEIVVRGPQIFKGYWNRPE---------ETEESfiEIKGRrFF 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 594 DTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLFTTD--SEITRE 668
Cdd:cd05935 313 RTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEevkAFIVLRPEyrGKVTEE 392
|
330 340 350
....*....|....*....|....*....|...
gi 488138635 669 RLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd05935 393 DIIEWAREQ-MAAYKYPREVEFVDELPRSASGK 424
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
255-701 |
1.91e-35 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 141.73 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 255 GEHVGMLLPNATITAAAIFGASLRGRIPALLN--YT----------SGAKglqsAII-----AASLKTIVTSRQfLEKGK 317
Cdd:PRK08974 74 GDRVALMMPNLLQYPIALFGILRAGMIVVNVNplYTprelehqlndSGAK----AIVivsnfAHTLEKVVFKTP-VKHVI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 318 LTHLPEQVNE-----VNWV--YLE------DLKDTVTLTDKLWILFHLCFPRRAMLPqqaDGSALILFTSGSEGNPKGVV 384
Cdd:PRK08974 149 LTRMGDQLSTakgtlVNFVvkYIKrlvpkyHLPDAISFRSALHKGRRMQYVKPELVP---EDLAFLQYTGGTTGVAKGAM 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 385 HSHASLLANVEQIRTIAD--FTPRDRF-MSSLPLFHAFGLTVG--LFTPLmtGSRVFLYPSPlhyRVVPELVYDRN---C 456
Cdd:PRK08974 226 LTHRNMLANLEQAKAAYGplLHPGKELvVTALPLYHIFALTVNclLFIEL--GGQNLLITNP---RDIPGFVKELKkypF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 457 TVLFGTSTF---LGNYARFaHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVN-T 532
Cdd:PRK08974 301 TAITGVNTLfnaLLNNEEF-QELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSgS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 533 VGRILPGMEARLI----NVPGIAQGGRLQLRGPNIMRGYlrvenpgvLEQPsaENAQGELDANWYDTGDIVTLDEQGFCA 608
Cdd:PRK08974 380 IGLPVPSTEIKLVdddgNEVPPGEPGELWVKGPQVMLGY--------WQRP--EATDEVIKDGWLATGDIAVMDEEGFLR 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 609 IRGRVKRFAKLAGEMVSLESVEQLaISLSPEGQHAAA-AKTDSAKGEALVLFTT--DSEITRERLIKVARENgVPELAVP 685
Cdd:PRK08974 450 IVDRKKDMILVSGFNVYPNEIEDV-VMLHPKVLEVAAvGVPSEVSGEAVKIFVVkkDPSLTEEELITHCRRH-LTGYKVP 527
|
490
....*....|....*.
gi 488138635 686 RDIRVVKALPLLGSGK 701
Cdd:PRK08974 528 KLVEFRDELPKSNVGK 543
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
233-644 |
3.17e-35 |
|
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: 140.06 E-value: 3.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRIL-QRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQ 311
Cdd:cd05904 34 TYAELERRVRRLAAGLaKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 FLEKGKLTHLPEqvnevnwVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQqaDGSALILFTSGSEGNPKGVVHSHASLL 391
Cdd:cd05904 114 LAEKLASLALPV-------VLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKGVMLTHRNLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 392 ANVEQIRTIAD--FTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSplhyrvvpelvydrnctvlFGTSTFLGNY 469
Cdd:cd05904 185 AMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPR-------------------FDLEELLAAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 470 ARF----------------AHP----YDFARVRYVVAGAEKLAESTKQIWQDKF-GIRILEGYGVTECAPVVAINVP--- 525
Cdd:cd05904 246 ERYkvthlpvvppivlalvKSPivdkYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFApek 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 526 MAAKVNTVGRILPGMEARLINV-------PGiaQGGRLQLRGPNIMRGYLRveNPgvleqpsAENAQGELDANWYDTGDI 598
Cdd:cd05904 326 DRAKYGSVGRLVPNVEAKIVDPetgeslpPN--QTGELWIRGPSIMKGYLN--NP-------EATAATIDKEGWLHTGDL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 488138635 599 VTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAA 644
Cdd:cd05904 395 CYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSH-PEILDAA 439
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
233-701 |
4.96e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 140.68 E-value: 4.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNA-----TITAAAIFGASLRGRIPAL----LNYTSGAKGLQSAIIAAS 302
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVqPGDRVGIWAPNCaewllTQFATARIGAILVNINPAYraseLEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 303 LKT---------IVTSRQFLEKGKLTH--LPEQVNEV-----------NWVYLEDLKDTVTLTDklwilfhlCFPRRAML 360
Cdd:PRK12583 127 FKTsdyhamlqeLLPGLAEGQPGALACerLPELRGVVslapapppgflAWHELQARGETVSREA--------LAERQASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 pqQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVfLYPS 440
Cdd:PRK12583 199 --DRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACL-VYPN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 441 ----PLhyrVVPELVYDRNCTVLFGTST-FLgnyARFAHP----YDFARVRY-VVAGAEKLAESTKQIWQDKFGIRILEG 510
Cdd:PRK12583 276 eafdPL---ATLQAVEEERCTALYGVPTmFI---AELDHPqrgnFDLSSLRTgIMAGAPCPIEVMRRVMDEMHMAEVQIA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 511 YGVTECAPVV---AINVPMAAKVNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLrvENPgvleQPSAEN 583
Cdd:PRK12583 350 YGMTETSPVSlqtTAADDLERRVETVGRTQPHLEVKVVDPDGatVPRGeiGELCTRGYSVMKGYW--NNP----EATAES 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 584 aqgeLDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLF 659
Cdd:PRK12583 424 ----IDEDgWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEeivAWVRL 499
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 488138635 660 TTDSEITRERLIKVAREnGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK12583 500 HPGHAASEEELREFCKA-RIAHFKVPRYFRFVDEFPMTVTGK 540
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
363-703 |
8.20e-34 |
|
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: 134.96 E-value: 8.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTVG-LFTPLMTGSRVFLYPSP 441
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSF--SFDVSVWeIFGALLAGATLVVLPEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 LHY--RVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKF-GIRILEGYGVTECAP 518
Cdd:cd05930 169 VRKdpEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 519 VVAINV--PMAAKVNTV--GRILPGMEARLIN-----VP-GIAqgGRLQLRGPNIMRGYLRveNPG-----VLEQPSAEN 583
Cdd:cd05930 249 DATYYRvpPDDEEDGRVpiGRPIPNTRVYVLDenlrpVPpGVP--GELYIGGAGLARGYLN--RPEltaerFVPNPFGPG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 584 AQGeldanwYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTT-- 661
Cdd:cd05930 325 ERM------YRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVpd 398
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488138635 662 -DSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd05930 399 eGGELDEEELRAHLAER-LPDYMVPSAFVVLDALPLTPNGKVD 440
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
365-703 |
1.28e-33 |
|
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: 134.30 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 365 DGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGSRVFlypsplh 443
Cdd:cd05945 97 DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPF--SFDLSVmDLYPALASGATLV------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 444 yrVVPELVYD-----------RNCTVLFGTSTFL------GNYARFAHPydfaRVRYVVAGAEKLAESTKQIWQDKF-GI 505
Cdd:cd05945 168 --PVPRDATAdpkqlfrflaeHGITVWVSTPSFAamcllsPTFTPESLP----SLRHFLFCGEVLPHKTARALQQRFpDA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 506 RILEGYGVTEC-APVVAINV--PMAAKVNTV--GRILPGMEARLIN-----VPGIAQgGRLQLRGPNIMRGYLRVenpgv 575
Cdd:cd05945 242 RIYNTYGPTEAtVAVTYIEVtpEVLDGYDRLpiGYAKPGAKLVILDedgrpVPPGEK-GELVISGPSVSKGYLNN----- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 576 leqPSAENAQGELDAN--WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAA-AKTDSAK 652
Cdd:cd05945 316 ---PEKTAAAFFPDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEA-ALRQVPGVKEAVVvPKYKGEK 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488138635 653 GEALVLF-TTDSEITRERLIKVARENG--VPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd05945 392 VTELIAFvVPKPGAEAGLTKAIKAELAerLPPYMIPRRFVYLDELPLNANGKID 445
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
233-701 |
1.40e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 136.10 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFT--VPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSR 310
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTdlVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 311 QFlekGKLTH--LPEQVNE-VNWVYLEDLKDTV------TLTDKLWIL---FHLcfP-----RRAM----------LPQQ 363
Cdd:PRK12492 131 MF---GKLVQevLPDTGIEyLIEAKMGDLLPAAkgwlvnTVVDKVKKMvpaYHL--PqavpfKQALrqgrglslkpVPVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTI-----ADFTP-----RDRFMSSLPLFHAFGLTVGLFTPLMTGS 433
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRAClsqlgPDGQPlmkegQEVMIAPLPLYHIYAFTANCMCMMVSGN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVFLYPSPlhyRVVPELVYDR---NCTVLFGTSTFLgnYARFAHP----YDFARVRYVVAGAEKLAESTKQIWQDKFGIR 506
Cdd:PRK12492 286 HNVLITNP---RDIPGFIKELgkwRFSALLGLNTLF--VALMDHPgfkdLDFSALKLTNSGGTALVKATAERWEQLTGCT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 507 ILEGYGVTECAPVVAINvPMA--AKVNTVGRILPGMEARLINVPGIAQG----GRLQLRGPNIMRGYlrvenpgvLEQPS 580
Cdd:PRK12492 361 IVEGYGLTETSPVASTN-PYGelARLGTVGIPVPGTALKVIDDDGNELPlgerGELCIKGPQVMKGY--------WQQPE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 581 AeNAQGeLDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLF 659
Cdd:PRK12492 432 A-TAEA-LDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLF 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 488138635 660 TTDSE--ITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK12492 510 VVARDpgLSVEELKAYCKEN-FTGYKVPKHIVLRDSLPMTPVGK 552
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
364-701 |
1.85e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 135.47 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPsplh 443
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP---- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 444 yR----VVPELVYDRNCTVLFGTST----FLGNyARFAHpYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTE 515
Cdd:PRK08314 265 -RwdreAAARLIERYRVTHWTNIPTmvvdFLAS-PGLAE-RDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 CAPVVAINVPMAAKVNTVGRILPGMEARLIN------VPgiaQG--GRLQLRGPNIMRGYLRvenpgvleQPSA-ENAQG 586
Cdd:PRK08314 342 TMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpetleeLP---PGevGEIVVHGPQVFKGYWN--------RPEAtAEAFI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 587 ELDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAIslspegQHAA-------AAKtDSAKGE---A 655
Cdd:PRK08314 411 EIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLY------KHPAiqeacviATP-DPRRGEtvkA 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488138635 656 LVLFTTDSE--ITRERLIKVARENgvpeLA---VPRDIRVVKALPLLGSGK 701
Cdd:PRK08314 484 VVVLRPEARgkTTEEEIIAWAREH----MAaykYPRIVEFVDSLPKSGSGK 530
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
370-701 |
2.99e-33 |
|
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: 130.70 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 370 ILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVflYP-SPLHYRVVP 448
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATV--VPvAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 449 ELVYDRNCTVLFGTSTFLgnYARFAHP----YDFARVRYVVAGAEKLAESTKQIWQDKFGIR-ILEGYGVTECApVVAIN 523
Cdd:cd17638 83 EAIERERITVLPGPPTLF--QSLLDHPgrkkFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG-VATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 524 VPMAAKV---NTVGRILPGMEARlinvpgIAQGGRLQLRGPNIMRGYlrvenpgvLEQPSAENAQgeLDAN-WYDTGDIV 599
Cdd:cd17638 160 RPGDDAEtvaTTCGRACPGFEVR------IADDGEVLVRGYNVMQGY--------LDDPEATAEA--IDADgWLHTGDVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 600 TLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLFTTDSEITRERLIKVARE 676
Cdd:cd17638 224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEvgkAFVVARPGVTLTEEDVIAWCRE 303
|
330 340
....*....|....*....|....*
gi 488138635 677 NgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd17638 304 R-LANYKVPRFVRFLDELPRNASGK 327
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
368-701 |
2.31e-32 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 131.98 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTiAD---FTPRDRFMSSLPLFH--AFGLTvglFTPLMTGSRvFLYPSP- 441
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHRSLVLHAMAALL-TDglgLSESDVVLPVVPMFHvnAWGLP---YAAAMVGAK-LVLPGPy 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 LHYRVVPELVYDRNCTVLFGTSTF---LGNYARfAHPYDFARVRYVVAGAEKLAESTKQIWQDKfGIRILEGYGVTECAP 518
Cdd:cd12119 241 LDPASLAELIEREGVTFAAGVPTVwqgLLDHLE-ANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSP 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 519 VVAINVPMAAKVN-----------TVGRILPGMEARLINVPGIAQG------GRLQLRGPNIMRGYLRVEnpgvleqpsa 581
Cdd:cd12119 319 LGTVARPPSEHSNlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdgkavGELQVRGPWVTKSYYKND---------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 582 ENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSleSVE-QLAISLSPEGQHAAAAKTDSAK-GE---AL 656
Cdd:cd12119 389 EESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWIS--SVElENAIMAHPAVAEAAVIGVPHPKwGErplAV 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488138635 657 VLFTTDSEITRERLIKVAREnGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd12119 467 VVLKEGATVTAEELLEFLAD-KVAKWWLPDDVVFVDEIPKTSTGK 510
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
368-702 |
3.71e-32 |
|
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: 129.72 E-value: 3.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSpLHYRVV 447
Cdd:cd05934 84 ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPR-FSASRF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 448 PELVYDRNCTVLfgtsTFLGNYARF-----AHPYDFA-RVRyVVAGAEKLAEsTKQIWQDKFGIRILEGYGVTECAPVVA 521
Cdd:cd05934 163 WSDVRRYGATVT----NYLGAMLSYllaqpPSPDDRAhRLR-AAYGAPNPPE-LHEEFEERFGVRLLEGYGMTETIVGVI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 522 INVPMAAKVNTVGRILPGMEARLIN-----VPgIAQGGRLQLR---GPNIMRGYLRveNPgvleqpsAENAqgELDAN-W 592
Cdd:cd05934 237 GPRDEPRRPGSIGRPAPGYEVRIVDddgqeLP-AGEPGELVIRglrGWGFFKGYYN--MP-------EATA--EAMRNgW 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 593 YDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAKGE----ALVLFTTDSEITRE 668
Cdd:cd05934 305 FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER-AILRHPAVREAAVVAVPDEVGEdevkAVVVLRPGETLDPE 383
|
330 340 350
....*....|....*....|....*....|....
gi 488138635 669 RLIKVARENgVPELAVPRDIRVVKALPLLGSGKP 702
Cdd:cd05934 384 ELFAFCEGQ-LAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
354-701 |
3.80e-32 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 131.79 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 354 FPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGS 433
Cdd:PRK06087 176 EPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVFLYPsplHYRVVP--ELVYDRNCTVLFGTSTF---LGNYARfAHPYDFARVRYVVAGA----EKLAESTKQiwqdkFG 504
Cdd:PRK06087 256 RSVLLD---IFTPDAclALLEQQRCTCMLGATPFiydLLNLLE-KQPADLSALRFFLCGGttipKKVARECQQ-----RG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 505 IRILEGYGVTECAP--VVAINVPMAAKVNTVGRILPGMEARLIN-----VPGIAQGGRLQlRGPNIMRGYlrvenpgvLE 577
Cdd:PRK06087 327 IKLLSVYGSTESSPhaVVNLDDPLSRFMHTDGYAAAGVEIKVVDearktLPPGCEGEEAS-RGPNVFMGY--------LD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 578 QPSAENAQgeLDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEAL 656
Cdd:PRK06087 398 EPELTARA--LDEEgWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERS 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488138635 657 VLFTTDSEITR----ERLIKVARENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK06087 476 CAYVVLKAPHHsltlEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGK 524
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
233-701 |
2.61e-31 |
|
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: 129.28 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQ--SAIIA-ASLKTIVTS 309
Cdd:cd05931 26 TYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAErlAAILAdAGPRVVLTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 310 RQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDklWILFHLcfprramlpqQADGSALILFTSGSEGNPKGVVHSHAS 389
Cdd:cd05931 106 AAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAAD--WPPPSP----------DPDDIAYLQYTSGSTGTPKGVVVTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 390 LLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYpSPLHYRVVP----ELVYDRNctvlfGTSTF 465
Cdd:cd05931 174 LLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM-SPAAFLRRPlrwlRLISRYR-----ATISA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 466 LGNYArFAH-----------PYDFARVRYVVAGAEKLAESTKQIWQDKF---GIR---ILEGYGVTEC------------ 516
Cdd:cd05931 248 APNFA-YDLcvrrvrdedleGLDLSSWRVALNGAEPVRPATLRRFAEAFapfGFRpeaFRPSYGLAEAtlfvsggppgtg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 517 --------------APVVAINVPMAAKVNTVGRILPGMEARLINvPGIAQG------GRLQLRGPNIMRGYLRveNPGVL 576
Cdd:cd05931 327 pvvlrvdrdalagrAVAVAADDPAARELVSCGRPLPDQEVRIVD-PETGRElpdgevGEIWVRGPSVASGYWG--RPEAT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 577 EQPSAeNAQGELDANWYDTGDIvtldeqGFCA-----IRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQ--HAAAAKTD 649
Cdd:cd05931 404 AETFG-ALAATDEGGWLRTGDL------GFLHdgelyITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgCVAAFSVP 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488138635 650 SAKGEALVLF---TTDSEITRERLIK------VARENGVPelavPRDIRVVK--ALPLLGSGK 701
Cdd:cd05931 477 DDGEERLVVVaevERGADPADLAAIAaairaaVAREHGVA----PADVVLVRpgSIPRTSSGK 535
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
361-646 |
3.89e-31 |
|
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: 126.23 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGSRVFLYP 439
Cdd:TIGR01733 116 PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASL--SFDASVeEIFGALLAGATLVVPP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHYRVVPE---LVYDRNCTVLFGTSTFLGNYARfAHPYDFARVRYVVAGAEKLAESTKQIWQDKFG-IRILEGYGVTE 515
Cdd:TIGR01733 194 EDEERDDAALlaaLIAEHPVTVLNLTPSLLALLAA-ALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 CAPVVAINVPMAAKV-----NTVGRILPGMEARLIN-----VP-GIAqgGRLQLRGPNIMRGYLR---------VENPGv 575
Cdd:TIGR01733 273 TTVWSTATLVDPDDAprespVPIGRPLANTRLYVLDddlrpVPvGVV--GELYIGGPGVARGYLNrpeltaerfVPDPF- 349
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138635 576 leqpsaenaQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAisLSPEGQHAAAA 646
Cdd:TIGR01733 350 ---------AGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL--LRHPGVREAVV 409
|
|
| PlsC |
COG0204 |
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ... |
1-196 |
4.61e-31 |
|
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: 120.88 E-value: 4.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 1 MAYRLLRALFRGL-----FRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVD 75
Cdd:COG0204 11 FRYRLVRLWARLLlrllgVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKIPLLGWLLRALG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 76 FVALDPTNPM----AIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRlqgv 151
Cdd:COG0204 91 AIPVDRSKRRaalrALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGAARLALEAGVPIVPVAIDGTERALPKG---- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488138635 152 lKTRWFPKISIHVLPAttIPmPQAPRSRERRVLAgEHLHTIMMAA 196
Cdd:COG0204 167 -FLPRPGKVTVRIGPP--ID-PSDLEGEDRRELA-ERLRAAIEAL 206
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
368-703 |
4.95e-31 |
|
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: 123.98 E-value: 4.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVgLFTPLMTGSRVFL--YPSPLHYR 445
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLleRNQALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 446 VVPELVydrncTVLFGTSTFLGN-YARFAHPYDFARVRYVVAG-----AEKLAESTKQiwqdkfGIRILEGYGVTECAPV 519
Cdd:cd17630 82 LAPPGV-----THVSLVPTQLQRlLDSGQGPAALKSLRAVLLGgapipPELLERAADR------GIPLYTTYGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 520 VAINVPMAAKVNTVGRILPGMEARlinvpgIAQGGRLQLRGPNIMRGYLRvenpGVLEQPSAENAqgeldanWYDTGDIV 599
Cdd:cd17630 151 VATKRPDGFGRGGVGVLLPGRELR------IVEDGEIWVGGASLAMGYLR----GQLVPEFNEDG-------WFTTKDLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 600 TLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAA-AKTDSAKGEALVLF-TTDSEITRERLIK-VARE 676
Cdd:cd17630 214 ELHADGRLTVLGRADNMIISGGENIQPEEIEA-ALAAHPAVRDAFVvGVPDEELGQRPVAViVGRGPADPAELRAwLKDK 292
|
330 340
....*....|....*....|....*..
gi 488138635 677 NGVPELavPRDIRVVKALPLLGSGKPD 703
Cdd:cd17630 293 LARFKL--PKRIYPVPELPRTGGGKVD 317
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
368-614 |
6.92e-31 |
|
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: 126.70 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPL----- 442
Cdd:cd17640 91 ATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLkddlk 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 443 ----HYRV-VPEL-------VYD------RNCTVLFGTSTFLGNyarfahpydfarVRYVVAGAEKLAESTkqiwqDKF- 503
Cdd:cd17640 171 rvkpHYIVsVPRLweslysgIQKqvskssPIKQFLFLFFLSGGI------------FKFGISGGGALPPHV-----DTFf 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 504 ---GIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINV-------PGiaQGGRLQLRGPNIMRGYLRveNP 573
Cdd:cd17640 234 eaiGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPegnvvlpPG--EKGIVWVRGPQVMKGYYK--NP 309
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488138635 574 GVLEQpsAENAQGeldanWYDTGDIVTLDEQGFCAIRGRVK 614
Cdd:cd17640 310 EATSK--VLDSDG-----WFNTGDLGWLTCGGELVLTGRAK 343
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
368-641 |
1.06e-30 |
|
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: 127.33 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPR----DRFMSSLPLFHAFG-LTVGLFtpLMTGSRVFLYP--- 439
Cdd:cd05927 117 ATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKinptDVYISYLPLAHIFErVVEALF--LYHGAKIGFYSgdi 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 ----------SPLHYRVVPEL---VYDRNCTVLFGTST---FLGNYA------------RFAHPY-DF-----------A 479
Cdd:cd05927 195 rlllddikalKPTVFPGVPRVlnrIYDKIFNKVQAKGPlkrKLFNFAlnyklaelrsgvVRASPFwDKlvfnkikqalgG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 480 RVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVP-------GIAQ 552
Cdd:cd05927 275 NVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPemnydakDPNP 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 553 GGRLQLRGPNIMRGYLRveNPgvleqpsaENAQGELDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLA-GEMVSLESVE 630
Cdd:cd05927 355 RGEVCIRGPNVFSGYYK--DP--------EKTAEALDEDgWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYVAPEKIE 424
|
330
....*....|.
gi 488138635 631 QLAISLSPEGQ 641
Cdd:cd05927 425 NIYARSPFVAQ 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
364-701 |
1.57e-30 |
|
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: 125.14 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPlh 443
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGP-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 444 yRVVPELVYDR----NCTVLFGTSTFlgnYARFA----HPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTE 515
Cdd:cd05972 158 -RFDAERILELleryGVTSFCGPPTA---YRMLIkqdlSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 CAPVVAINVPMAAKVNTVGRILPGMEARLIN------VPG----IAqggrLQLRGPNIMRGYLRVEnpgvleqpsaENAQ 585
Cdd:cd05972 234 TGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDddgrelPPGeegdIA----IKLPPPGLFLGYVGDP----------EKTE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 586 GELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAIslspegQH------AAAAKTDSAKGE---AL 656
Cdd:cd05972 300 ASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALL------EHpavaeaAVVGSPDPVRGEvvkAF 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 488138635 657 VLFT---TDSEITRERLIKVARENGVPElAVPRDIRVVKALPLLGSGK 701
Cdd:cd05972 374 VVLTsgyEPSEELAEELQGHVKKVLAPY-KYPREIEFVEELPKTISGK 420
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
365-701 |
1.84e-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: 124.38 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 365 DGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVgLFTPLMTGSRVFLYPsplHY 444
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYLVD---KF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 445 RV--VPELVYDRNCTVLFGTSTFLGNY-ARFAHPYDfARVRYVVAGAEKLAESTKQIWQDKfGIRILEGYGVTE-CAPVV 520
Cdd:cd05912 153 DAeqVLHLINSGKVTIISVVPTMLQRLlEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTEtCSQIV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 521 AINVPMA-AKVNTVGRILPGMEARLINVPGIAQG-GRLQLRGPNIMRGYLrveNPGVLEQPSAENaqgeldaNWYDTGDI 598
Cdd:cd05912 231 TLSPEDAlNKIGSAGKPLFPVELKIEDDGQPPYEvGEILLKGPNVTKGYL---NRPDATEESFEN-------GWFKTGDI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 599 VTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLF-TTDSEITRERLIKVAREN 677
Cdd:cd05912 301 GYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFvVSERPISEEELIAYCSEK 380
|
330 340
....*....|....*....|....*..
gi 488138635 678 gvpeLA---VPRDIRVVKALPLLGSGK 701
Cdd:cd05912 381 ----LAkykVPKKIYFVDELPRTASGK 403
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
195-685 |
3.10e-30 |
|
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: 125.86 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 195 AARMATVPReTLFEALLSAQTRYGRFKPCIEDVSFKED--SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAA 271
Cdd:cd05906 2 LHRPEGAPR-TLLELLLRAAERGPTKGITYIDADGSEEfqSYQDLLEDARRLAAGLRQLGLrPGDSVILQFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 272 IFGASLRGRIPALL----NYTSGAKGLQSAIIAASL---KTIVTSR----QFLEKGKLTHLPEQVNEVnwvyLEDLKDTv 340
Cdd:cd05906 81 FWACVLAGFVPAPLtvppTYDEPNARLRKLRHIWQLlgsPVVLTDAelvaEFAGLETLSGLPGIRVLS----IEELLDT- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 341 tltdklwilfhlcfPRRAMLPQ-QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAF 419
Cdd:cd05906 156 --------------AADHDLPQsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 420 GLT-VGLFtPLMTGSRVFLYPSPL-------------HYRVvpelvydrnctvlfgTSTFLGNYArFAH----------- 474
Cdd:cd05906 222 GLVeLHLR-AVYLGCQQVHVPTEEiladplrwldlidRYRV---------------TITWAPNFA-FALlndlleeiedg 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 475 PYDFARVRYVVAGAEKL-AESTKQIWQ--DKFGIR---ILEGYGVTE-CAPVVAINVPMAAKVNT------VGRILPGME 541
Cdd:cd05906 285 TWDLSSLRYLVNAGEAVvAKTIRRLLRllEPYGLPpdaIRPAFGMTEtCSGVIYSRSFPTYDHSQalefvsLGRPIPGVS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 542 ARLINVPG----IAQGGRLQLRGPNIMRGYLRveNPgvleqpsAENAQGELDANWYDTGDIVTLDEqGFCAIRGRVKRFA 617
Cdd:cd05906 365 MRIVDDEGqllpEGEVGRLQVRGPVVTKGYYN--NP-------EANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 618 KLAG---EMVSLES-VEQLAIsLSPEGQHAAAAKTDSAKGEALVLF------------TTDSEITRerliKVARENGV-P 680
Cdd:cd05906 435 IVNGvnyYSHEIEAaVEEVPG-VEPSFTAAFAVRDPGAETEELAIFfvpeydlqdalsETLRAIRS----VVSREVGVsP 509
|
....*
gi 488138635 681 ELAVP 685
Cdd:cd05906 510 AYLIP 514
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
368-701 |
5.08e-30 |
|
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: 123.77 E-value: 5.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVV 447
Cdd:cd05969 92 TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESW 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 448 PELVYDRNCTVLFGTST----FLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAIN 523
Cdd:cd05969 172 YGIIERVKVTVWYTAPTairmLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIAN 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 524 VP-MAAKVNTVGRILPGMEARLINVPGIA----QGGRLQLRG--PNIMRGYLRVEnpgvleqpsaENAQGELDANWYDTG 596
Cdd:cd05969 252 YPcMPIKPGSMGKPLPGVKAAVVDENGNElppgTKGILALKPgwPSMFRGIWNDE----------ERYKNSFIDGWYLTG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 597 DIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTT------DSEITRERL 670
Cdd:cd05969 322 DLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfePSDELKEEI 401
|
330 340 350
....*....|....*....|....*....|.
gi 488138635 671 IKVAREnGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd05969 402 INFVRQ-KLGAHVAPREIEFVDNLPKTRSGK 431
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
364-681 |
5.67e-30 |
|
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: 124.63 E-value: 5.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQI--RTIADFTPRDRFMSSLPLFHAF-----------GLTVGLFTP-- 428
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdRVPELLGPDDRYLAYLPLAHIFelaaenvclyrGGTIGYGSPrt 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 429 -------------------LMTG-SRVF----------LYPSPLHYRVVPELVYD-RNCTVLFGTSTFLGNYARFAHPYD 477
Cdd:cd17639 167 ltdkskrgckgdltefkptLMVGvPAIWdtirkgvlakLNPMGGLKRTLFWTAYQsKLKALKEGPGTPLLDELVFKKVRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 478 F--ARVRYVVAGAEKLAESTkQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQG-- 553
Cdd:cd17639 247 AlgGRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYStd 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 554 -----GRLQLRGPNIMRGYLRveNPGVLEQpsAENAQGeldanWYDTGDIVTLDEQGFCAIRGRVKRFAKLA-GEMVSLE 627
Cdd:cd17639 326 kppprGEILIRGPNVFKGYYK--NPEKTKE--AFDGDG-----WFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALE 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488138635 628 SVE-QLAISLSPEG--QHAAAAKTdsaKGEALVLfttdseITRERLIKVARENGVPE 681
Cdd:cd17639 397 KLEsIYRSNPLVNNicVYADPDKS---YPVAIVV------PNEKHLTKLAEKHGVIN 444
|
|
| LPLAT_AGPAT-like |
cd07989 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ... |
6-183 |
9.07e-30 |
|
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: 116.22 E-value: 9.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 6 LRALFRGL-FRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNP 84
Cdd:cd07989 1 LRLLLRLLgVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 85 M----AIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRlqgvLKTRWFPKI 160
Cdd:cd07989 81 RsareALREAIEALKEGESVVIFPEGTRSRDGELLPFKSGAFRLAKEAGVPIVPVAISGTWGSLPKG----KKLPRPGRV 156
|
170 180
....*....|....*....|...
gi 488138635 161 SIHVLPATTIPMPQAPRSRERRV 183
Cdd:cd07989 157 TVRIGEPIPPEGLELAEEDRKEL 179
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
364-701 |
1.47e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 124.01 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRD-RFMSSlPLFHAFGLTVGLFTPLMTGSRVFLYPSPL 442
Cdd:PRK13295 196 PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDvILMAS-PMAHQTGFMYGLMMPVMLGATAVLQDIWD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 443 HYRVVpELVYDRNCTVLFGTSTFLGNYARF--AHPYDFARVR-YVVAGAE---KLAESTKQIwqdkFGIRILEGYGVTEC 516
Cdd:PRK13295 275 PARAA-ELIRTEGVTFTMASTPFLTDLTRAvkESGRPVSSLRtFLCAGAPipgALVERARAA----LGAKIVSAWGMTEN 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 517 APVVAINVPMAAKV--NTVGRILPGMEARLINVPGIA----QGGRLQLRGPNIMRGYLRvenpgvLEQPSAENAQGelda 590
Cdd:PRK13295 350 GAVTLTKLDDPDERasTTDGCPLPGVEVRVVDADGAPlpagQIGRLQVRGCSNFGGYLK------RPQLNGTDADG---- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 591 nWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQL-----AISlspegQHAAAAKTDSAKGE---ALVLFTTD 662
Cdd:PRK13295 420 -WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALlyrhpAIA-----QVAIVAYPDERLGEracAFVVPRPG 493
|
330 340 350
....*....|....*....|....*....|....*....
gi 488138635 663 SEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK13295 494 QSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGK 532
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
254-701 |
2.15e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 123.33 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 254 PGEHVGMLLPNATITAAAIFGASLRGRIPALLN--YT----------SGAKGLQSAIIAASL------KT-----IVTS- 309
Cdd:PRK05677 74 PGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNplYTaremehqfndSGAKALVCLANMAHLaekvlpKTgvkhvIVTEv 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 310 -------RQFLEKGKLTHLPEQVNEVNwvyledLKDTVTLTDKLWIlfHLCFPRRAMLPQQADgSALILFTSGSEGNPKG 382
Cdd:PRK05677 154 admlpplKRLLINAVVKHVKKMVPAYH------LPQAVKFNDALAK--GAGQPVTEANPQADD-VAVLQYTGGTTGVAKG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 383 VVHSHASLLANVEQIRTIADFT---PRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPlhyRVVPELVYD---RNC 456
Cdd:PRK05677 225 AMLTHRNLVANMLQCRALMGSNlneGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNP---RDLPAMVKElgkWKF 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 457 TVLFGTSTF---LGNYARFaHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTV 533
Cdd:PRK05677 302 SGFVGLNTLfvaLCNNEAF-RKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTI 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 534 GRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLrvENPgvleqpsaENAQGELDAN-WYDTGDIVTLDEQGFCA 608
Cdd:PRK05677 381 GIPVPSTLCKVIDDDGneLPLGevGELCVKGPQVMKGYW--QRP--------EATDEILDSDgWLKTGDIALIQEDGYMR 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 609 IRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFT---TDSEITRERLIKVARENgVPELAVP 685
Cdd:PRK05677 451 IVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVvvkPGETLTKEQVMEHMRAN-LTGYKVP 529
|
490
....*....|....*.
gi 488138635 686 RDIRVVKALPLLGSGK 701
Cdd:PRK05677 530 KAVEFRDELPTTNVGK 545
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
358-703 |
7.97e-29 |
|
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: 120.11 E-value: 7.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 358 AMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMsslpLFH--AFGLTV-GLFTPLMTGSR 434
Cdd:cd17643 86 SLLLTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHsyAFDFSVwEIWGALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 435 VFLYP-----SPLHYRvvpELVYDRNCTVLFGT-STFLGNYARFAHPY-DFARVRYVVAGAEKLAESTKQIWQDKFGI-- 505
Cdd:cd17643 162 LVVVPyevarSPEDFA---RLLRDEGVTVLNQTpSAFYQLVEAADRDGrDPLALRYVIFGGEALEAAMLRPWAGRFGLdr 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 506 -RILEGYGVTECA------PVVAINVPMAAKVNtVGRILPG-----MEARLINVPGIAQgGRLQLRGPNIMRGYLRveNP 573
Cdd:cd17643 239 pQLVNMYGITETTvhvtfrPLDAADLPAAAASP-IGRPLPGlrvyvLDADGRPVPPGVV-GELYVSGAGVARGYLG--RP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 574 GVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKG 653
Cdd:cd17643 315 ELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGD 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 488138635 654 EALVLFTTD---SEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17643 395 TRLVAYVVAddgAAADIAELRALLKEL-LPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
355-614 |
8.95e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 120.75 E-value: 8.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 355 PRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSR 434
Cdd:PRK07514 146 DDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGAS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 435 VFLYPsplhyRVVPELVYDR--NCTVLFGTSTFlgnYARF-AHPyDF-----ARVRYVVAGAEKLAESTKQIWQDKFGIR 506
Cdd:PRK07514 226 MIFLP-----KFDPDAVLALmpRATVMMGVPTF---YTRLlQEP-RLtreaaAHMRLFISGSAPLLAETHREFQERTGHA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 507 ILEGYGVTECA-----PVVAINVPmaakvNTVGRILPGMEARlinVPGIAQG--------GRLQLRGPNIMRGYLRVenp 573
Cdd:PRK07514 297 ILERYGMTETNmntsnPYDGERRA-----GTVGFPLPGVSLR---VTDPETGaelppgeiGMIEVKGPNVFKGYWRM--- 365
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488138635 574 gvleqpsAENAQGELDAN-WYDTGDIVTLDEQGFCAIRGRVK 614
Cdd:PRK07514 366 -------PEKTAEEFRADgFFITGDLGKIDERGYVHIVGRGK 400
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
364-703 |
2.29e-28 |
|
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: 118.57 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDR---FMSslPLFHAFGLTVglFTPLMTGSRVFLYPS 440
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRvaqVLS--IAFDACIGEI--FSTLCNGGTLVLADP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 441 PLHYRVVPelvydRNCTVLFGTSTFLGNYArfahPYDFARVRYVVAGAEKLAESTKQIWqdKFGIRILEGYGVTECAPVV 520
Cdd:cd17653 180 SDPFAHVA-----RTVDALMSTPSILSTLS----PQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTISS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 521 AINVPMAAKVNTVGRILPGMEARLIN-----VPgIAQGGRLQLRGPNIMRGYLRvenpgvleQPSAENAQGELDANW--- 592
Cdd:cd17653 249 TMTELLPGQPVTIGKPIPNSTCYILDadlqpVP-EGVVGEICISGVQVARGYLG--------NPALTASKFVPDPFWpgs 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 593 --YDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAaktdSAKGEALVLFTTDSEITRERL 670
Cdd:cd17653 320 rmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAA----IVVNGRLVAFVTPETVDVDGL 395
|
330 340 350
....*....|....*....|....*....|...
gi 488138635 671 IKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17653 396 RSELAKH-LPSYAVPDRIIALDSFPLTANGKVD 427
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
364-695 |
1.30e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 117.01 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLH 443
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTP 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 444 YRVVPELvyDRNCTVLFGTSTFlgnYARFAHPYDFAR----VRYVVAGA--------EKLAESTkqiwqdkfGIRILEGY 511
Cdd:PRK07787 207 EAYAQAL--SEGGTLYFGVPTV---WSRIAADPEAARalrgARLLVSGSaalpvpvfDRLAALT--------GHRPVERY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 512 GVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQG------GRLQLRGPNIMRGYLrvenpgvlEQPSAENAQ 585
Cdd:PRK07787 274 GMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPhdgetvGELQVRGPTLFDGYL--------NRPDATAAA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 586 GELDAnWYDTGDIVTLDEQGFCAIRGRVKR-FAKLAGEMVSLESVEQlAISLSPEGQHAAAAKT-DSAKGEALVLF-TTD 662
Cdd:PRK07787 346 FTADG-WFRTGDVAVVDPDGMHRIVGRESTdLIKSGGYRIGAGEIET-ALLGHPGVREAAVVGVpDDDLGQRIVAYvVGA 423
|
330 340 350
....*....|....*....|....*....|....*..
gi 488138635 663 SEITRERLIK-VAREngvpeLAV---PRDIRVVKALP 695
Cdd:PRK07787 424 DDVAADELIDfVAQQ-----LSVhkrPREVRFVDALP 455
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
361-701 |
1.32e-27 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 118.98 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQI-RTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYP 439
Cdd:PRK06060 141 PMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKF-GIRILEGYGVTECAP 518
Cdd:PRK06060 221 APVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFgGIPILDGIGSTEVGQ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 519 VVAINVPMAAKVNTVGRILPGMEARLINVPGIAQG----GRLQLRGPNIMRGYLRVENPgVLEqpsaenaqgelDANWYD 594
Cdd:PRK06060 301 TFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGpgveGDLWVRGPAIAKGYWNRPDS-PVA-----------NEGWLD 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 595 TGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTT-------DSEITR 667
Cdd:PRK06060 369 TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVatsgatiDGSVMR 448
|
330 340 350
....*....|....*....|....*....|....*..
gi 488138635 668 E---RLIkvareNGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK06060 449 DlhrGLL-----NRLSAFKVPHRFAVVDRLPRTPNGK 480
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
361-701 |
1.54e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 117.27 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLAN-VEQIRTIaDFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLyP 439
Cdd:PRK06839 145 EKNESASFIICYTSGTTGKPKGAVLTQENMFWNaLNNTFAI-DLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIV-P 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHYRVVPELVYDRNCTVLFGTSTF---LGNYARFAHPyDFARVRYVVAGAEKLAESTKQIWQDKfGIRILEGYGVTEC 516
Cdd:PRK06839 223 RKFEPTKALSMIEKHKVTVVMGVPTIhqaLINCSKFETT-NLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTET 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 517 APVVAI--NVPMAAKVNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLrvENPgvleQPSAENAQGelda 590
Cdd:PRK06839 301 SPTVFMlsEEDARRKVGSIGKPVLFCDYELIDENKnkVEVGevGELLIRGPNVMKEYW--NRP----DATEETIQD---- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 591 NWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLFTTDSEITR 667
Cdd:PRK06839 371 GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEipiAFIVKKSSSVLIE 450
|
330 340 350
....*....|....*....|....*....|....
gi 488138635 668 ERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK06839 451 KDVIEHCRLF-LAKYKIPKEIVFLKELPKNATGK 483
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
370-701 |
1.94e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 117.60 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 370 ILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVfLYPS----PLHyr 445
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATM-VYPGegfdPLA-- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 446 vVPELVYDRNCTVLFGTST-FLgnyARFAHP----YDFARVRY-VVAGAEKLAESTKQIwQDKFGIR-ILEGYGVTECAP 518
Cdd:PRK08315 281 -TLAAVEEERCTALYGVPTmFI---AELDHPdfarFDLSSLRTgIMAGSPCPIEVMKRV-IDKMHMSeVTIAYGMTETSP 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 519 VV---AINVPMAAKVNTVGRILPGMEARLIN------VPgIAQGGRLQLRGPNIMRGYLrvENPgvleqpsAENAQGELD 589
Cdd:PRK08315 356 VStqtRTDDPLEKRVTTVGRALPHLEVKIVDpetgetVP-RGEQGELCTRGYSVMKGYW--NDP-------EKTAEAIDA 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 590 ANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAAAKTDSAK-GEALVLFTT---DSEI 665
Cdd:PRK08315 426 DGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTH-PKIQDVQVVGVPDEKyGEEVCAWIIlrpGATL 504
|
330 340 350
....*....|....*....|....*....|....*....
gi 488138635 666 TRERLIKVAREngvpELA---VPRDIRVVKALPLLGSGK 701
Cdd:PRK08315 505 TEEDVRDFCRG----KIAhykIPRYIRFVDEFPMTVTGK 539
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
353-701 |
2.68e-27 |
|
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: 115.65 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 353 CFPRRAMLPQQ---ADGSALILFTSGSEGNPKGVVHSHASLLANVEQI-RTIADFTPRDRFMSSLPLFHAFGLTVGLFTP 428
Cdd:cd05958 82 ARITVALCAHAltaSDDICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 429 LMTGSRVFLYPsplhyRVVPELVYD----RNCTVLFGTSTflGNYARFAHP----YDFARVRYVVAGAEKLAESTKQIWQ 500
Cdd:cd05958 162 FGVGASGVLLE-----EATPDLLLSaiarYKPTVLFTAPT--AYRAMLAHPdaagPDLSSLRKCVSAGEALPAALHRAWK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 501 DKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGylrvenpgvL 576
Cdd:cd05958 235 EATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGnpVPDGtiGRLAVRGPTGCRY---------L 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 577 EQPSAENAqgeLDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAIslspegQHAAAAKT------DS 650
Cdd:cd05958 306 ADKRQRTY---VQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLL------QHPAVAECavvghpDE 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488138635 651 AKGEALVLFTT--DSEITRERLIKVARENGVPELA---VPRDIRVVKALPLLGSGK 701
Cdd:cd05958 377 SRGVVVKAFVVlrPGVIPGPVLARELQDHAKAHIApykYPRAIEFVTELPRTATGK 432
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
365-701 |
1.20e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 114.71 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 365 DGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTP-RDRFMSSLPLFHAFGLTVGLFTPLMTGSRVfLYPSPLH 443
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHDMGMVGFLTVPMYFGAEL-VKVTPMD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 444 YRVVPeLVYDRNCTVLFGTSTFLGNYA---------RFAHP--YDFARVRYVVAGAEKLAESTKQIWQD---KFGIR--- 506
Cdd:PRK07768 231 FLRDP-LLWAELISKYRGTMTAAPNFAyallarrlrRQAKPgaFDLSSLRFALNGAEPIDPADVEDLLDagaRFGLRpea 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 507 ILEGYGVTECAPVVAI--------------------------NVPMAAKVNTVGRILPGMEARLINVPGIAQG----GRL 556
Cdd:PRK07768 310 ILPAYGMAEATLAVSFspcgaglvvdevdadllaalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPprgvGVI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 557 QLRGPNIMRGYLRVENPGvleqpSAENAQGeldanWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISL 636
Cdd:PRK07768 390 ELRGESVTPGYLTMDGFI-----PAQDADG-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARV 459
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488138635 637 S---PEGqhAAAAKTD---SAKGEALVLFTTD--SEITRERLIKVARENGVPELAV-PRDIRVVKA--LPLLGSGK 701
Cdd:PRK07768 460 EgvrPGN--AVAVRLDaghSREGFAVAVESNAfeDPAEVRRIRHQVAHEVVAEVGVrPRNVVVLGPgsIPKTPSGK 533
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
368-707 |
1.51e-26 |
|
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: 113.96 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTV-GLFTPLMTGSRVFLYPSP----- 441
Cdd:cd05920 142 ALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPspdaa 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 ---------LHYRVVPELVydrnctvlfgtSTFLGnyARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYG 512
Cdd:cd05920 222 fplieregvTVTALVPALV-----------SLWLD--AAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 513 VTE---CapVVAINVPMAAKVNTVGR-ILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLRVEnpgvleqpsAENA 584
Cdd:cd05920 289 MAEgllN--YTRLDDPDEVIIHTQGRpMSPDDEIRVVDEEGnpVPPGeeGELLTRGPYTIRGYYRAP---------EHNA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 QGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAA-AKTDSAKGEALVLFT--T 661
Cdd:cd05920 358 RAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRH-PAVHDAAVvAMPDELLGERSCAFVvlR 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488138635 662 DSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTL 707
Cdd:cd05920 437 DPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
357-703 |
3.95e-26 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 112.08 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 357 RAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPL-FHAFglTVGLFTPLMTGSRV 435
Cdd:cd17649 86 GLLLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFnFDGA--HEQLLPPLICGACV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 436 FLYPSPL------HYRVVPELvydrNCTVLFGTSTFLGNYARFA---HPYDFARVRYVVAGAEKLAESTKQIWQdKFGIR 506
Cdd:cd17649 164 VLRPDELwasadeLAEMVREL----GVTVLDLPPAYLQQLAEEAdrtGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 507 ILEGYGVTEcapvvAINVPMAAKVNT----------VGRILPGMEARLIN-----VPgIAQGGRLQLRGPNIMRGYLrvE 571
Cdd:cd17649 239 LFNAYGPTE-----ATVTPLVWKCEAgaaragasmpIGRPLGGRSAYILDadlnpVP-VGVTGELYIGGEGLARGYL--G 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 572 NPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSA 651
Cdd:cd17649 311 RPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEA-ALLEHPGVREAAVVALDGA 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488138635 652 KGEALVLF-----TTDSEITRERLiKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17649 390 GGKQLVAYvvlraAAAQPELRAQL-RTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
230-701 |
2.99e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 110.89 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 230 KEDSYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLN--YT----------SGAK---- 292
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVeKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNplYTereleyqlhdSGAKvilc 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 293 ------GLQSAIIAASLKTIVTSR-------------QFLEKgKLTHLPEQVNEVNWVYLEDL--KDTVTLTDKLwilfh 351
Cdd:PRK06710 128 ldlvfpRVTNVQSATKIEHVIVTRiadflpfpknllyPFVQK-KQSNLVVKVSESETIHLWNSveKEVNTGVEVP----- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 352 lCFPRRAMlpqqadgsALILFTSGSEGNPKGVVHSHASLLAN----VEQIRTIADftPRDRFMSSLPLFHAFGLTVGLFT 427
Cdd:PRK06710 202 -CDPENDL--------ALLQYTGGTTGFPKGVMLTHKNLVSNtlmgVQWLYNCKE--GEEVVLGVLPFFHVYGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 428 PLMTGSRVFLYPSpLHYRVVPELVYDRNCTVLFGTSTFLgnYARFAHP----YDFARVRYVVAGAEKLAESTKQIWQDKF 503
Cdd:PRK06710 271 SIMQGYKMVLIPK-FDMKMVFEAIKKHKVTLFPGAPTIY--IALLNSPllkeYDISSIRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 504 GIRILEGYGVTECAPVVAINVPMAAKV-NTVGRILPGMEARLINV-------PGiaQGGRLQLRGPNIMRGYLRvenpgv 575
Cdd:PRK06710 348 GGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPDTEAMIMSLetgealpPG--EIGEIVVKGPQIMKGYWN------ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 576 leqpSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE- 654
Cdd:PRK06710 420 ----KPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGEt 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 488138635 655 --ALVLFTTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK06710 496 vkAFVVLKEGTECSEEELNQFARKY-LAAYKVPKVYEFRDELPKTTVGK 543
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-701 |
3.92e-25 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 110.35 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 255 GEHVGMLLPNATITAAAIFGASLRGRIPALLN--YT----------SGAKGL----------QSAIIAASLKTIVTSrqf 312
Cdd:PRK08751 76 GDRVALMMPNCLQYPIATFGVLRAGLTVVNVNplYTprelkhqlidSGASVLvvidnfgttvQQVIADTPVKQVITT--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 313 lEKGKLTHLPEQVnEVNWV--YLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQ---ADGSALILFTSGSEGNPKGVVHSH 387
Cdd:PRK08751 153 -GLGDMLGFPKAA-LVNFVvkYVKKLVPEYRINGAIRFREALALGRKHSMPTLqiePDDIAFLQYTGGTTGVAKGAMLTH 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 388 ASLLANVEQ----IRTIADFTP-RDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYR-VVPELVYDRnCTVLFG 461
Cdd:PRK08751 231 RNLVANMQQahqwLAGTGKLEEgCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPgFVKELKKTR-FTAFTG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 462 TSTF---LGNYARFAHpYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINvPMAAKV--NTVGRI 536
Cdd:PRK08751 310 VNTLfngLLNTPGFDQ-IDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACIN-PLTLKEynGSIGLP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 537 LPGMEARLI----NVPGIAQGGRLQLRGPNIMRGYLRvenpgvleqpSAENAQGELDAN-WYDTGDIVTLDEQGFCAIRG 611
Cdd:PRK08751 388 IPSTDACIKddagTVLAIGEIGELCIKGPQVMKGYWK----------RPEETAKVMDADgWLHTGDIARMDEQGFVYIVD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 612 RVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEAL--VLFTTDSEITRERLIKVARENgVPELAVPRDIR 689
Cdd:PRK08751 458 RKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVkvVIVKKDPALTAEDVKAHARAN-LTGYKQPRIIE 536
|
490
....*....|..
gi 488138635 690 VVKALPLLGSGK 701
Cdd:PRK08751 537 FRKELPKTNVGK 548
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
255-668 |
1.54e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 108.14 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 255 GEHVGMLLPNATITAAAIFGASLRGRIPALLN--YTSGAkgLQSAIIAASLKTIVTSRQFLEKgkLTHLPEQvNEVNWVY 332
Cdd:PLN02246 75 GDVVMLLLPNCPEFVLAFLGASRRGAVTTTANpfYTPAE--IAKQAKASGAKLIITQSCYVDK--LKGLAED-DGVTVVT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 333 LEDLKDTvtltdklwilfhlCFPRRAMLpqQADGSAL------------ILFTSGSEGNPKGVVHSHASLLANVEQirtI 400
Cdd:PLN02246 150 IDDPPEG-------------CLHFSELT--QADENELpeveispddvvaLPYSSGTTGLPKGVMLTHKGLVTSVAQ---Q 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 401 AD-------FTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYP----SPL-----HYRV-----VPELVydrnctVL 459
Cdd:PLN02246 212 VDgenpnlyFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPkfeiGALleliqRHKVtiapfVPPIV------LA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 460 FGTSTFLGNyarfahpYDFARVRYVVAGAEKLAESTKQIWQDKFGIRIL-EGYGVTECAPVVAINV-----PMAAKVNTV 533
Cdd:PLN02246 286 IAKSPVVEK-------YDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAGPVLAMCLafakePFPVKSGSC 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 534 GRILPGMEARLINvP------GIAQGGRLQLRGPNIMRGYLRveNPgvleqpsaENAQGELDAN-WYDTGDIVTLDEQGF 606
Cdd:PLN02246 359 GTVVRNAELKIVD-PetgaslPRNQPGEICIRGPQIMKGYLN--DP--------EATANTIDKDgWLHTGDIGYIDDDDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488138635 607 CAIRGRVKRFAKLAGEMVSLESVEQLAISlSPEGQHAAA-AKTDSAKGE---ALVLFTTDSEITRE 668
Cdd:PLN02246 428 LFIVDRLKELIKYKGFQVAPAELEALLIS-HPSIADAAVvPMKDEVAGEvpvAFVVRSNGSEITED 492
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
361-703 |
4.51e-24 |
|
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: 106.13 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQiRTIADFTPRDRFMSSLPL-FHAFglTVGLFTPLMTGSRVFLYP 439
Cdd:cd12117 132 PVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN-TNYVTLGPDDRVLQTSPLaFDAS--TFEIWGALLNGARLVLAP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 S--PLHYRVVPELVYDRNCTVLFGTSTFLGNYARfAHPYDFARVRYVVAGAEKL-AESTKQIWQDKFGIRILEGYGVTE- 515
Cdd:cd12117 209 KgtLLDPDALGALIAEEGVTVLWLTAALFNQLAD-EDPECFAGLRELLTGGEVVsPPHVRRVLAACPGLRLVNGYGPTEn 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 ----CAPVVAINVPMAAKVnTVGRILPGMEARLINVPGIAQG----GRLQLRGPNIMRGYLRveNPGVLEQPSAENAQGE 587
Cdd:cd12117 288 ttftTSHVVTELDEVAGSI-PIGRPIANTRVYVLDEDGRPVPpgvpGELYVGGDGLALGYLN--RPALTAERFVADPFGP 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 588 lDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAKGEA-LVLFTT-DSEI 665
Cdd:cd12117 365 -GERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEA-ALRAHPGVREAVVVVREDAGGDKrLVAYVVaEGAL 442
|
330 340 350
....*....|....*....|....*....|....*...
gi 488138635 666 TRERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd12117 443 DAAELRAFLRER-LPAYMVPAAFVVLDELPLTANGKVD 479
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
202-703 |
6.63e-24 |
|
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: 106.46 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 202 PRE--TLFEALLSAQTRYGRFKPCIE--DVSFKED-SYQTLLKKTLGVSRILQRFTVPGEH-VGMLLPNATITAAAIFGA 275
Cdd:cd17642 10 PLEdgTAGEQLHKAMKRYASVPGTIAftDAHTGVNySYAEYLEMSVRLAEALKKYGLKQNDrIAVCSENSLQFFLPVIAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 276 SLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKgkLTHLPEQVNEVNWVYLEDLKDTVT--LTDKLWILFHL- 352
Cdd:cd17642 90 LFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQK--VLNVQKKLKIIKTIIILDSKEDYKgyQCLYTFITQNLp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 353 -CFPRRAMLPQQAD---GSALILFTSGSEGNPKGVVHSHASLLANVEQIRT---IADFTPRDRFMSSLPLFHAFGLTVGL 425
Cdd:cd17642 168 pGFNEYDFKPPSFDrdeQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQIIPDTAILTVIPFHHGFGMFTTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 426 fTPLMTGSRVFLYP---------SPLHYRV-----VPELVydrnctVLFGTSTFLGNyarfahpYDFARVRYVVAGAEKL 491
Cdd:cd17642 248 -GYLICGFRVVLMYkfeeelflrSLQDYKVqsallVPTLF------AFFAKSTLVDK-------YDLSNLHEIASGGAPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 492 AESTKQIWQDKFGIR-ILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVP-----GIAQGGRLQLRGPNIMR 565
Cdd:cd17642 314 SKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDtgktlGPNERGELCVKGPMIMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 566 GYlrvenpgvLEQPSAENAQGELDAnWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAA 645
Cdd:cd17642 394 GY--------VNNPEATKALIDKDG-WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVA 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138635 646 AKTDSAKGE---ALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17642 465 GIPDEDAGElpaAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKID 525
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
361-701 |
1.25e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 105.49 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQ----IRTIADFTPRDR---FMSSLPLFHAFGLTVGLFTPLMTGS 433
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQmeawLQPAFEKKPRPDqlnFVCALPLYHIFALTVCGLLGMRTGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVFLYPSPlhyRVVPELV-----YDRNC----TVLFGTstfLGNYARFaHPYDFARVRYVVAGAEKLAESTKQIWQDKFG 504
Cdd:PRK07059 280 RNILIPNP---RDIPGFIkelkkYQVHIfpavNTLYNA---LLNNPDF-DKLDFSKLIVANGGGMAVQRPVAERWLEMTG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 505 IRILEGYGVTECAPVVAINVPMAAKVN-TVGRILPGMEARLINVPG----IAQGGRLQLRGPNIMRGYLrvenpgvleQP 579
Cdd:PRK07059 353 CPITEGYGLSETSPVATCNPVDATEFSgTIGLPLPSTEVSIRDDDGndlpLGEPGEICIRGPQVMAGYW---------NR 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 580 SAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLF 659
Cdd:PRK07059 424 PDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLF 503
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488138635 660 TT--DSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK07059 504 VVkkDPALTEEDVKAFCKER-LTNYKRPKFVEFRTELPKTNVGK 546
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
372-701 |
1.62e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 105.17 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSHAS--LLANVEQIRTIADFTPRDRFMSSLPLFH--AFGLTvglFTPLMTGSRVFLyPSP-LHYRV 446
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHvnAWGLP---YSAPLTGAKLVL-PGPdLDGKS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 447 VPELVYDRNCTVLFGTST-FLG--NYARfAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAI- 522
Cdd:PRK07008 259 LYELIEAERVTFSAGVPTvWLGllNHMR-EAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLc 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 523 -------NVPMAAKVNTV---GRILPGMEARLIN-----VP--GIAQGgRLQLRGPNIMRGYLRVE-NPgvleqpsaena 584
Cdd:PRK07008 338 klkwkhsQLPLDEQRKLLekqGRVIYGVDMKIVGddgreLPwdGKAFG-DLQVRGPWVIDRYFRGDaSP----------- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 qgeLDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISlSPEGQHAAAAKTDSAKGEA----LVLFT 660
Cdd:PRK07008 406 ---LVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA-HPAVAEAACIACAHPKWDErpllVVVKR 481
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488138635 661 TDSEITRERLIKVArENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK07008 482 PGAEVTREELLAFY-EGKVAKWWIPDDVVFVDAIPHTATGK 521
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
363-713 |
2.15e-23 |
|
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: 104.16 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFM--SSlplfHAFGLTVG-LFTPLMTGSRVFLyP 439
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfAS----YTFDVSILeIFTTLAAGGCLCI-P 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SpLHYRV--VPELVYDRNCTVLFGTSTFlgnyARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKfgIRILEGYGVTECA 517
Cdd:cd05918 179 S-EEDRLndLAGFINRLRVTWAFLTPSV----ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAECT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 518 PVVAINVPMA-AKVNTVGRIL--------PGMEARLinVPgIAQGGRLQLRGPNIMRGYLR---------VENPGVLEQP 579
Cdd:cd05918 252 IAATVSPVVPsTDPRNIGRPLgatcwvvdPDNHDRL--VP-IGAVGELLIEGPILARGYLNdpektaaafIEDPAWLKQE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 580 SAEnAQGELdanwYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAA----KTDSAKGEA 655
Cdd:cd05918 329 GSG-RGRRL----YRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEH-HLRQSLPGAKEVVVevvkPKDGSSSPQ 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488138635 656 LVLFTTDSEITRERLIKVARENGVPELA-------------------VPRDIRVVKALPLLGSGKPDFVTLGKMAQD 713
Cdd:cd05918 403 LVAFVVLDGSSSGSGDGDSLFLEPSDEFralvaelrsklrqrlpsymVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
368-701 |
2.52e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 104.24 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLAnvEQIRTIA--DFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPlhyr 445
Cdd:PRK08316 174 AQILYTSGTESLPKGAMLTHRALIA--EYVSCIVagDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAP---- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 446 vVPELVYDR----NCTVLFGTSTF---LGNYARFAhPYDFARVRYVVAGA-----EKLAEstkqiWQDKF-GIRILEGYG 512
Cdd:PRK08316 248 -DPELILRTieaeRITSFFAPPTVwisLLRHPDFD-TRDLSSLRKGYYGAsimpvEVLKE-----LRERLpGLRFYNCYG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 513 VTECAPVVAINVP--MAAKVNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLRveNPgvleQPSAENAQG 586
Cdd:PRK08316 321 QTEIAPLATVLGPeeHLRRPGSAGRPVLNVETRVVDDDGndVAPGevGEIVHRSPQLMLGYWD--DP----EKTAEAFRG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 587 eldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAK-GE---ALVLFTTD 662
Cdd:PRK08316 395 ----GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE-ALYTHPAVAEVAVIGLPDPKwIEavtAVVVPKAG 469
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 488138635 663 SEITRERLIKVAREngvpELA---VPRDIRVVKALPLLGSGK 701
Cdd:PRK08316 470 ATVTEDELIAHCRA----RLAgfkVPKRVIFVDELPRNPSGK 507
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
366-701 |
6.75e-23 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 100.80 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 366 GSALILFTSGSEGNPKGVVHSHASLLANVEQIRT-IADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHY 444
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 445 RVVPEL-VYDRNCTVLFGTS-TFLGNYARFAHPYdFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAI 522
Cdd:cd17635 82 SLFKILtTNAVTTTCLVPTLlSKLVSELKSANAT-VPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 523 NVPMAAK-VNTVGRILPGMEARLINVPGIA----QGGRLQLRGPNIMRGYLrvENPgvleQPSAENAQGEldanWYDTGD 597
Cdd:cd17635 161 PTDDDSIeINAVGRPYPGVDVYLAATDGIAgpsaSFGTIWIKSPANMLGYW--NNP----ERTAEVLIDG----WVNTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 598 IVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVAREN 677
Cdd:cd17635 231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALKHT 310
|
330 340
....*....|....*....|....*..
gi 488138635 678 GVPEL---AVPRDIRVVKALPLLGSGK 701
Cdd:cd17635 311 IRRELepyARPSTIVIVTDIPRTQSGK 337
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
357-701 |
6.82e-23 |
|
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: 102.13 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 357 RAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAF--GLTVGLFTPLMTGSR 434
Cdd:cd05971 80 SALVTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPADWAWigGLLDVLLPSLYFGVP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 435 VFLY-PSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARV--RYVVAGAEKLAESTKQIWQDKFGIRILEGY 511
Cdd:cd05971 160 VLAHrMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVklRAIATGGESLGEELLGWAREQFGVEVNEFY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 512 GVTECAPVVAIN-VPMAAKVNTVGRILPGMEARLINVPG----IAQGGRLQLRGPN--IMRGYLRveNPGVLEQPSAena 584
Cdd:cd05971 240 GQTECNLVIGNCsALFPIKPGSMGKPIPGHRVAIVDDNGtplpPGEVGEIAVELPDpvAFLGYWN--NPSATEKKMA--- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 qgeldANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAA-AKTDSAKGEA----LVL- 658
Cdd:cd05971 315 -----GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE-CLLKHPAVLMAAVvGIPDPIRGEIvkafVVLn 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488138635 659 --FTTDSEITRE--RLIKVArengVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd05971 389 pgETPSDALAREiqELVKTR----LAAHEYPREIEFVNELPRTATGK 431
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
360-632 |
7.83e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 103.90 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 360 LPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQI-----RTIADFTPRDRFMSSLPLFHAFGLTVglftplmtgSR 434
Cdd:PTZ00216 259 IPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALedrlnDLIGPPEEDETYCSYLPLAHIMEFGV---------TN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 435 VFLYpsplhyrvvpelvydRNCTVLFGTS-TFLGNYAR-----------------------------------------F 472
Cdd:PTZ00216 330 IFLA---------------RGALIGFGSPrTLTDTFARphgdltefrpvfligvprifdtikkaveaklppvgslkrrvF 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 473 AHPYD-------------------FA--------RVRYVVAGAEKLAESTKQIWQDKFGiRILEGYGVTECAPVVAINVP 525
Cdd:PTZ00216 395 DHAYQsrlralkegkdtpywnekvFSapravlggRVRAMLSGGGPLSAATQEFVNVVFG-MVIQGWGLTETVCCGGIQRT 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 526 MAAKVNTVGRILPGMEARLINVPGIAQG------GRLQLRGPNIMRGYLRvenpgvleQPsaENAQGELDAN-WYDTGDI 598
Cdd:PTZ00216 474 GDLEPNAVGQLLKGVEMKLLDTEEYKHTdtpeprGEILLRGPFLFKGYYK--------QE--ELTREVLDEDgWFHTGDV 543
|
330 340 350
....*....|....*....|....*....|....*
gi 488138635 599 VTLDEQGFCAIRGRVKRFAK-LAGEMVSLESVEQL 632
Cdd:PTZ00216 544 GSIAANGTLRIIGRVKALAKnCLGEYIALEALEAL 578
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
364-701 |
2.00e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 101.42 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYP---- 439
Cdd:PRK09088 134 PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNgfep 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 ------------SPLHYRVVPELVydrnctvlfgtstflgnyARF-AHP-YDFARVRYVVA----GAEKLAESTKQiWQD 501
Cdd:PRK09088 214 krtlgrlgdpalGITHYFCVPQMA------------------QAFrAQPgFDAAALRHLTAlftgGAPHAAEDILG-WLD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 502 KfGIRILEGYGVTECAPVVAINVP---MAAKVNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLRveNPg 574
Cdd:PRK09088 275 D-GIPMVDGFGMSEAGTVFGMSVDcdvIRAKAGAAGIPTPTVQTRVVDDQGndCPAGvpGELLLRGPNLSPGYWR--RP- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 575 vleQPSAENAQGEldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE 654
Cdd:PRK09088 351 ---QATARAFTGD---GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGE 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488138635 655 ALVLFTTDSEITRERLIKVAR--ENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK09088 425 VGYLAIVPADGAPLDLERIRShlSTRLAKYKVPKHLRLVDALPRTASGK 473
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
355-620 |
5.35e-22 |
|
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: 100.24 E-value: 5.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 355 PRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSR 434
Cdd:cd05932 127 PLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 435 VFLYPS------------PLHYRVVPEL-------VYDR----NCTVLFGTStFLGNYAR--FAHPYDFARVRYVVAGAE 489
Cdd:cd05932 207 VAFAESldtfvedvqrarPTLFFSVPRLwtkfqqgVQDKipqqKLNLLLKIP-VVNSLVKrkVLKGLGLDQCRLAGCGSA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 490 KLAESTKQiWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARlinvpgIAQGGRLQLRGPNIMRGYLR 569
Cdd:cd05932 286 PVPPALLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVR------ISEDGEILVRSPALMMGYYK 358
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488138635 570 venpgvleQPSAENAQGELDAnWYDTGDIVTLDEQGFCAIRGRVKRFAKLA 620
Cdd:cd05932 359 --------DPEATAEAFTADG-FLRTGDKGELDADGNLTITGRVKDIFKTS 400
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
253-701 |
5.59e-22 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 100.73 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 253 VPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEV---- 328
Cdd:cd17634 107 KKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDAlnpn 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 329 -----NWVYLEDLKDTVTLTDKLWILFHLCF----PRRAMLPQQADGSALILFTSGSEGNPKGVVHSHAS-LLANVEQIR 398
Cdd:cd17634 187 vtsveHVIVLKRTGSDIDWQEGRDLWWRDLIakasPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 399 TIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLY------PSPLHYRvvpELVYDRNCTVLFGTSTFLGNYARf 472
Cdd:cd17634 267 YVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYegvpnwPTPARMW---QVVDKHGVNILYTAPTAIRALMA- 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 473 AHP-----YDFARVRYVVAGAEKLAESTKQIWQDKFGIR---ILEGYGVTE----CAPVVAINVPMAAKVNTvgRILPGM 540
Cdd:cd17634 343 AGDdaiegTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTEtggfMITPLPGAIELKAGSAT--RPVFGV 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 541 EARLIN-----VPGIAQGG-RLQLRGPNIMRGYLRvenpgvlEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVK 614
Cdd:cd17634 421 QPAVVDneghpQPGGTEGNlVITDPWPGQTRTLFG-------DHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSD 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 615 RFAKLAGEMVSLESVEQLAISlSPEGQHAAAAKT-DSAKGEALVLFT------TDSEITRERLI-KVARENGVPelAVPR 686
Cdd:cd17634 494 DVINVAGHRLGTAEIESVLVA-HPKVAEAAVVGIpHAIKGQAPYAYVvlnhgvEPSPELYAELRnWVRKEIGPL--ATPD 570
|
490
....*....|....*
gi 488138635 687 DIRVVKALPLLGSGK 701
Cdd:cd17634 571 VVHWVDSLPKTRSGK 585
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
361-701 |
6.45e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 100.22 E-value: 6.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSAlILFTSGSEGNPKGVVHSHASLL---ANVEQIRTIadfTPRDRFMSSLPLFHAFGLTVgLFTPLMTGSRVFL 437
Cdd:PRK06155 177 VQPGDTAA-ILYTSGTTGPSKGVCCPHAQFYwwgRNSAEDLEI---GADDVLYTTLPLFHTNALNA-FFQALLAGATYVL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 438 YPSPLHYRVVPELVyDRNCTVLFgtstFLGNY-----ARFAHPYDFA-RVRyvVAGAEKLAESTKQIWQDKFGIRILEGY 511
Cdd:PRK06155 252 EPRFSASGFWPAVR-RHGATVTY----LLGAMvsillSQPARESDRAhRVR--VALGPGVPAALHAAFRERFGVDLLDGY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 512 GVTECAPVVAINVPmAAKVNTVGRILPGMEARLINVPGIA----QGGRLQLRGPN---IMRGYLRVENPGVleqpsaeNA 584
Cdd:PRK06155 325 GSTETNFVIAVTHG-SQRPGSMGRLAPGFEARVVDEHDQElpdgEPGELLLRADEpfaFATGYFGMPEKTV-------EA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 QGELdanWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAKGE----ALVLFT 660
Cdd:PRK06155 397 WRNL---WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQ-VLLSHPAVAAAAVFPVPSELGEdevmAAVVLR 472
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488138635 661 TDSEITRERLIKVArENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK06155 473 DGTALEPVALVRHC-EPRLAYFAVPRYVEFVAALPKTENGK 512
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
254-712 |
7.93e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 100.12 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 254 PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKlTHLPE-QVNEVNWVY 332
Cdd:PRK06178 82 AGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVE-QVRAEtSLRHVIVTS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 333 LEDL---KDTVTLTDKL---------WILF----HLCfPRRAMLPQQA-DGSALILFTSGSEGNPKGVVHSHASLlanve 395
Cdd:PRK06178 161 LADVlpaEPTLPLPDSLraprlaaagAIDLlpalRAC-TAPVPLPPPAlDALAALNYTGGTTGMPKGCEHTQRDM----- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 396 qIRTIADFTP-------RDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYP--SPL-------HYRVVpelvydrNCTVL 459
Cdd:PRK06178 235 -VYTAAAAYAvavvggeDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLArwDAVafmaaveRYRVT-------RTVML 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 460 FGTSTFLGNYARFaHPYDFARVRYV--VAGAEKLAESTKQIWQDKFGIRILEG-YGVTECAPVVAINVPM--------AA 528
Cdd:PRK06178 307 VDNAVELMDHPRF-AEYDLSSLRQVrvVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAGFqdddfdllSQ 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 529 KVnTVGRILPGMEARLIN------VPgIAQGGRLQLRGPNIMRGYLRvenpgvleQPSAeNAQGELDAnWYDTGDIVTLD 602
Cdd:PRK06178 386 PV-FVGLPVPGTEFKICDfetgelLP-LGAEGEIVVRTPSLLKGYWN--------KPEA-TAEALRDG-WLHTGDIGKID 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 603 EQGFCAIRGRVKRFAKLAGEMVSLESVEQLAislspeGQHAA------AAKTDSAKGEALVLFTT---DSEITRERLIKV 673
Cdd:PRK06178 454 EQGFLHYLGRRKEMLKVNGMSVFPSEVEALL------GQHPAvlgsavVGRPDPDKGQVPVAFVQlkpGADLTAAALQAW 527
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 488138635 674 AREN----GVPElavprdIRVVKALPLLGSGKPDFVTLGKMAQ 712
Cdd:PRK06178 528 CRENmavyKVPE------IRIVDALPMTATGKVRKQDLQALAE 564
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
368-703 |
2.00e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.81 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLypsPLHYRVV 447
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLL---PARGRFS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 448 PELVYD--RNCTVLFGTST------FLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPV 519
Cdd:PRK05852 256 AHTFWDdiKAVGATWYTAVptihqiLLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 520 VA-INVPMA-------AKVNTVGRIlPGMEARLINVPGI----AQGGRLQLRGPNIMRGYLrvENPgvleqpsaENAQGE 587
Cdd:PRK05852 336 VTtTQIEGIgqtenpvVSTGLVGRS-TGAQIRIVGSDGLplpaGAVGEVWLRGTTVVRGYL--GDP--------TITAAN 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 588 LDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLFTTDSE 664
Cdd:PRK05852 405 FTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEavaAVIVPRESAP 484
|
330 340 350
....*....|....*....|....*....|....*....
gi 488138635 665 ITRERLIKVAREnGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK05852 485 PTAEELVQFCRE-RLAAFEIPASFQEASGLPHTAKGSLD 522
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
357-703 |
4.16e-21 |
|
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: 96.77 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 357 RAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRD-RFMSSLPLFHAFglTVGLFTPLMTGSrV 435
Cdd:cd17654 110 RHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDiLFLTSPLTFDPS--VVEIFLSLSSGA-T 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 436 FLYpSPLHYRVVPELVYD-----RNCTVLFGTSTFLgnyARFAHPYDFARV-------RYVVAGAEKLAEST-KQIWQDK 502
Cdd:cd17654 187 LLI-VPTSVKVLPSKLADilfkrHRITVLQATPTLF---RRFGSQSIKSTVlsatsslRVLALGGEPFPSLViLSSWRGK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 503 F-GIRILEGYGVTE-CAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNimRGYLRvenPGVLEQPs 580
Cdd:cd17654 263 GnRTRIFNIYGITEvSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLN--RVCIL---DDEVTVP- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 581 aenaqgelDANWYDTGDIVTLdEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEgqhAAAAKTDSAKgEALVLFT 660
Cdd:cd17654 337 --------KGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV---ESCAVTLSDQ-QRLIAFI 403
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488138635 661 TdSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17654 404 V-GESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVD 445
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
372-703 |
6.34e-21 |
|
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: 94.39 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTpLMTGsRVFLYPSPLHYRVVPELV 451
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISA-LYLG-GTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 452 YDRNCTVLFGTSTFLGNYARFAHPYdfARVRYVVAGAEKLAESTKQIWQDKF-GIRILEGYGVTECAPVVAINVPMAAKV 530
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPE--SKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNFNQESRPP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 531 NTVGRILPGMEARLINVPGIAQgGRLQLRGPNIMRGYLRVE--NPGvleqpsaenaqgeldaNWYDTGDIVTLDEQGFCA 608
Cdd:cd17633 163 NSVGRPFPNVEIEIRNADGGEI-GKIFVKSEMVFSGYVRGGfsNPD----------------GWMSVGDIGYVDEEGYLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 609 IRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENgVPELAVPRDI 688
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQLKRFLKQK-LSRYEIPKKI 304
|
330
....*....|....*
gi 488138635 689 RVVKALPLLGSGKPD 703
Cdd:cd17633 305 IFVDSLPYTSSGKIA 319
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
355-703 |
7.87e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 355 PRRAMLPQQAdgsALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGS 433
Cdd:PRK12316 4687 PAVRLHPDNL---AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF--SFDGSHeGLYHPLINGA 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVFLYPSPLH--YRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLA-ESTKQIWQDKFGIRILEG 510
Cdd:PRK12316 4762 SVVIRDDSLWdpERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAqASYDLAWRALKPVYLFNG 4841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 511 YGVTECAPVVAI-----NVPMAAKVNTVGRILPGMEARLINVPG----IAQGGRLQLRGPNIMRGYLrvENPGVLEQPSA 581
Cdd:PRK12316 4842 YGPTETTVTVLLwkardGDACGAAYMPIGTPLGNRSGYVLDGQLnplpVGVAGELYLGGEGVARGYL--ERPALTAERFV 4919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 582 ENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEqlaislSPEGQHAAAAKT-----DSAKGEAL 656
Cdd:PRK12316 4920 PDPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIE------ARLREHPAVREAvviaqEGAVGKQL 4993
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 488138635 657 V--LFTTDSEIT---------RERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK12316 4994 VgyVVPQDPALAdadeaqaelRDELKAALRER-LPEYMVPAHLVFLARMPLTPNGKLD 5050
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
255-701 |
1.00e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 96.18 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 255 GEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKgkltHLPEQVNEVNWVYLE 334
Cdd:PRK03640 52 GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAK----LIPGISVKFAELMNG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 335 DLKDTVTLTDklwilFHLcfprramlpqqaDGSALILFTSGSEGNPKGVV---HSH-ASLLANVEQIrtiaDFTPRDRFM 410
Cdd:PRK03640 128 PKEEAEIQEE-----FDL------------DEVATIMYTSGTTGKPKGVIqtyGNHwWSAVGSALNL----GLTEDDCWL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 411 SSLPLFHAFGLTVgLFTPLMTGSRVFLYPsplHYRV--VPELVYDRNCTVLFGTSTFL---------GNYarfahPYDFa 479
Cdd:PRK03640 187 AAVPIFHISGLSI-LMRSVIYGMRVVLVE---KFDAekINKLLQTGGVTIISVVSTMLqrllerlgeGTY-----PSSF- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 480 rvRYVVAGAEKLAESTKQIWQDKfGIRILEGYGVTE-CAPVVAINvP--MAAKVNTVGRILPGMEARL---INVPGIAQG 553
Cdd:PRK03640 257 --RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTEtASQIVTLS-PedALTKLGSAGKPLFPCELKIekdGVVVPPFEE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 554 GRLQLRGPNIMRGYLRvenpgvleQPSAENAQgeLDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLA 633
Cdd:PRK03640 333 GEIVVKGPNVTKGYLN--------REDATRET--FQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488138635 634 ISLSPEGQHAAAAKTDSAKGEALVLF-TTDSEITRERLIKVARENgvpeLA---VPRDIRVVKALPLLGSGK 701
Cdd:PRK03640 403 LSHPGVAEAGVVGVPDDKWGQVPVAFvVKSGEVTEEELRHFCEEK----LAkykVPKRFYFVEELPRNASGK 470
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
368-703 |
1.36e-20 |
|
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: 95.98 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTV-GLFTPLMTGSRVFL--YPSPLH- 443
Cdd:COG1021 187 AFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTVVLapDPSPDTa 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 444 ------YRV-----VPELVydrnctvlfgtSTFLgNYARfAHPYDFARVRYVVAGAEKLAEST-KQIwQDKFGIRILEGY 511
Cdd:COG1021 267 fplierERVtvtalVPPLA-----------LLWL-DAAE-RSRYDLSSLRVLQVGGAKLSPELaRRV-RPALGCTLQQVF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 512 GVTE---CapVVAINVPMAAKVNTVGR-ILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLRVEnpgvleqpsAEN 583
Cdd:COG1021 333 GMAEglvN--YTRLDDPEEVILTTQGRpISPDDEVRIVDEDGnpVPPGevGELLTRGPYTIRGYYRAP---------EHN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 584 AQGELDANWYDTGDIVTLDEQGFCAIRGRVK----RfaklAGEMVSLESVEQLAISLsPEGQHAAA-AKTDSAKGEALVL 658
Cdd:COG1021 402 ARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdqinR----GGEKIAAEEVENLLLAH-PAVHDAAVvAMPDEYLGERSCA 476
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488138635 659 F--TTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:COG1021 477 FvvPRGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKID 523
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
360-703 |
1.71e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 97.54 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 360 LPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVgLFTPLMTGSRVFLYP 439
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATLHLLP 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHYRvvPE----LVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDK-FGIRILEGYGVT 514
Cdd:PRK12467 730 PDCARD--AEafaaLMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALgPGARLINHYGPT 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 515 ECAPVVAI----NVPMAAKVNTVGRILPG-----MEARLINVPGIAQgGRLQLRGPNIMRGYLRveNPGVLEQ---PSAE 582
Cdd:PRK12467 808 ETTVGVSTyelsDEERDFGNVPIGQPLANlglyiLDHYLNPVPVGVV-GELYIGGAGLARGYHR--RPALTAErfvPDPF 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 583 NAQGEldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAAAKTDSAKGEALVLF--- 659
Cdd:PRK12467 885 GADGG---RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQ-PGVREAVVLAQPGDAGLQLVAYlvp 960
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488138635 660 -----TTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK12467 961 aavadGAEHQATRDELKAQLRQV-LPDYMVPAHLLLLDSLPLTPNGKLD 1008
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
370-703 |
2.54e-20 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 92.72 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 370 ILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLypSPLHYRVVPE 449
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVM--EKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 450 LVYDRNCTVLFGTSTFLGNY--ARFAHPYDFARVRYvVAGAEklAESTKQIWQDKFGIRILEGYGVTECAPVVAINvPMA 527
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLldAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTETSGLVTLS-PYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 528 AKVNTVGRILPGMEARLIN-----VPgIAQGGRLQLRGPNIMRGYLRVEnpgvleqpsAENAQgELDANWYDTGDIVTLD 602
Cdd:cd17637 159 ERPGSAGRPGPLVRVRIVDdndrpVP-AGETGEIVVRGPLVFQGYWNLP---------ELTAY-TFRNGWHHTGDLGRFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 603 EQGFCAIRGRV--KRFAKLAGEMVSLESVEQlAISlspegQHAAAAKT------DSAKGE---ALVLFTTDSEITRERLI 671
Cdd:cd17637 228 EDGYLWYAGRKpeKELIKPGGENVYPAEVEK-VIL-----EHPAIAEVcvigvpDPKWGEgikAVCVLKPGATLTADELI 301
|
330 340 350
....*....|....*....|....*....|....*..
gi 488138635 672 -----KVARengvpeLAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17637 302 efvgsRIAR------YKKPRYVVFVEALPKTADGSID 332
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
355-701 |
6.13e-20 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 94.06 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 355 PRRAMLPQQADGSALIL-FTSGSEGNPKGVVHSHASLLANVEQI--RTIADfTPRDRFMSSLPLFHAFGLTVgLFTPLMT 431
Cdd:PRK05851 141 NRSASLTPPDSGGPAVLqGTAGSTGTPRTAILSPGAVLSNLRGLnaRVGLD-AATDVGCSWLPLYHDMGLAF-LLTAALA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 432 GSRVFLYP------SPLH-----------YRVVPELVYDrnctvlfgtstFLGNYARFAHPYDFARVRYVVAGAEKL-AE 493
Cdd:PRK05851 219 GAPLWLAPttafsaSPFRwlswlsdsratLTAAPNFAYN-----------LIGKYARRVSDVDLGALRVALNGGEPVdCD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 494 STKQIWQD--KFGIR---ILEGYGVTECAPVVAINVP----MAAKVNT-----------VGRILPGMEARL--------I 545
Cdd:PRK05851 288 GFERFATAmaPFGFDagaAAPSYGLAESTCAVTVPVPgiglRVDEVTTddgsgarrhavLGNPIPGMEVRIspgdgaagV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 546 NVPGIaqgGRLQLRGPNIMRGYLRvenpgvlEQPsaenaqgeLDA-NWYDTGDIVTLDEQGFcAIRGRVKRFAKLAGEMV 624
Cdd:PRK05851 368 AGREI---GEIEIRGASMMSGYLG-------QAP--------IDPdDWFPTGDLGYLVDGGL-VVCGRAKELITVAGRNI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 625 SLESVEQLAISLS--PEGQHAAAAKTDSAKGEALVLFT----TDSEITRERLIK-VARENGVpelaVPRDIRVVK--ALP 695
Cdd:PRK05851 429 FPTEIERVAAQVRgvREGAVVAVGTGEGSARPGLVIAAefrgPDEAGARSEVVQrVASECGV----VPSDVVFVApgSLP 504
|
....*.
gi 488138635 696 LLGSGK 701
Cdd:PRK05851 505 RTSSGK 510
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
372-701 |
7.83e-20 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 93.66 E-value: 7.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSHAS-----LLANVEQIRTIADftpRDRFMSSLPLFHA--FGLTvglFTPLMTGSRVFLYPSPLHY 444
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSnvlhaLMANNGDALGTSA---ADTMLPVVPLFHAnsWGIA---FSAPSMGTKLVMPGAKLDG 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 445 RVVPELVYDRNCTVLFGTST---FLGNYARfAHPYDFARVRYVVAGAEKLAESTKQIWQDkFGIRILEGYGVTECAPVVA 521
Cdd:PRK06018 258 ASVYELLDTEKVTFTAGVPTvwlMLLQYME-KEGLKLPHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEMSPLGT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 522 I--------NVPMAAKVN---TVGRILPGMEARLINVPGIAQG------GRLQLRGPNIMRGYLRVENPgVLEqpsaena 584
Cdd:PRK06018 336 LaalkppfsKLPGDARLDvlqKQGYPPFGVEMKITDDAGKELPwdgktfGRLKVRGPAVAAAYYRVDGE-ILD------- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 qgelDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISlSPEGQHAAAAKTDSAK-GEA---LVLFT 660
Cdd:PRK06018 408 ----DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVG-HPKVAEAAVIGVYHPKwDERpllIVQLK 482
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488138635 661 TDSEITRERLIKVArENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK06018 483 PGETATREEILKYM-DGKIAKWWMPDDVAFVDAIPHTATGK 522
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
255-701 |
1.81e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 92.60 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 255 GEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKgkLTHLPEQVNEVNWVYLE 334
Cdd:PLN02574 92 GDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEK--LSPLGVPVIGVPENYDF 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 335 DLKDTVTLTDKLWILFHLCFPRRAMLPQqaDGSALILFTSGSEGNPKGVVHSHASLLANVE-----QIRTIADFTPRDRF 409
Cdd:PLN02574 170 DSKRIEFPKFYELIKEDFDFVPKPVIKQ--DDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfEASQYEYPGSDNVY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 410 MSSLPLFHAFGLTVGLFTPLMTGSRVFLYP--------------SPLHYRVVPELVydrnctvlfgtsTFLGNYARFAHP 475
Cdd:PLN02574 248 LAALPMFHIYGLSLFVVGLLSLGSTIVVMRrfdasdmvkvidrfKVTHFPVVPPIL------------MALTKKAKGVCG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 476 YDFARVRYVVAGAEKLAESTKQIWQDKFG-IRILEGYGVTECAPV--VAINVPMAAKVNTVGRILPGMEARLINV----- 547
Cdd:PLN02574 316 EVLKSLKQVSCGAAPLSGKFIQDFVQTLPhVDFIQGYGMTESTAVgtRGFNTEKLSKYSSVGLLAPNMQAKVVDWstgcl 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 548 --PGiaQGGRLQLRGPNIMRGYLrveNPGVLEQPSAENaqgeldANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVS 625
Cdd:PLN02574 396 lpPG--NCGELWIQGPGVMKGYL---NNPKATQSTIDK------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIA 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 626 LESVEQLAISlSPEGQHAAAAKT-DSAKGE---ALVLFTTDSEITRERLIKVARENGVPELAVpRDIRVVKALPLLGSGK 701
Cdd:PLN02574 465 PADLEAVLIS-HPEIIDAAVTAVpDKECGEipvAFVVRRQGSTLSQEAVINYVAKQVAPYKKV-RKVVFVQSIPKSPAGK 542
|
|
| PlsC |
smart00563 |
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ... |
30-139 |
3.61e-19 |
|
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: 83.56 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 30 LIITPNHVSFLDGALLALFLP---IKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNP----MAIKHLVRMVEQGRPVVI 102
Cdd:smart00563 1 ALVVANHQSFLDPLVLSALLPrklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGrkarAALREAVELLKEGEWLLI 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 488138635 103 FPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDG 139
Cdd:smart00563 81 FPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIRG 117
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
368-703 |
4.10e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.10 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGSRVFLYPSPLHYRV 446
Cdd:PRK12316 658 AYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVVAAPGDHRDP 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 447 --VPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKL-AESTKQIWQDKFGIRILEGYGVTECAPVVA-- 521
Cdd:PRK12316 736 akLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALpADAQEQVFAKLPQAGLYNLYGPTEAAIDVThw 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 522 INVPMAAKVNTVGRILPGMEARLIN-----VP-GIAqgGRLQLRGPNIMRGYLRveNPGVLEQ---PSaENAQGEldaNW 592
Cdd:PRK12316 816 TCVEEGGDSVPIGRPIANLACYILDanlepVPvGVL--GELYLAGRGLARGYHG--RPGLTAErfvPS-PFVAGE---RM 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 593 YDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLiK 672
Cdd:PRK12316 888 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAVDGKQLVGYVVLESEGGDWREAL-K 965
|
330 340 350
....*....|....*....|....*....|.
gi 488138635 673 VARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK12316 966 AHLAASLPEYMVPAQWLALERLPLTPNGKLD 996
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
364-607 |
5.71e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 90.21 E-value: 5.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFT--PLMTGSRvflyPSP 441
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSviPDMDPTR----PAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 LHYRVVPELVYDRNCTVLFGTSTFLGNYARF--AHPYDFARVRYVV-AGAE---KLAESTKQIWQDkfGIRILEGYGVTE 515
Cdd:cd05910 160 ADPQKLVGAIRQYGVSIVFGSPALLERVARYcaQHGITLPSLRRVLsAGAPvpiALAARLRKMLSD--EAEILTPYGATE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 CAPVVAI----------NVPMAAKVNTVGRILPGMEARLINV---PGIAQGGRLQL----------RGPNIMRGYLRVEN 572
Cdd:cd05910 238 ALPVSSIgsrellatttAATSGGAGTCVGRPIPGVRVRIIEIddePIAEWDDTLELprgeigeitvTGPTVTPTYVNRPV 317
|
250 260 270
....*....|....*....|....*....|....*...
gi 488138635 573 PGVLEQpSAENAQGeldaNWYDTGDIVTLDEQG---FC 607
Cdd:cd05910 318 ATALAK-IDDNSEG----FWHRMGDLGYLDDEGrlwFC 350
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
363-703 |
5.97e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.53 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGSRVFLYPSP 441
Cdd:PRK12467 3235 MGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF--SFDGAQeRFLWTLICGGCLVVRDND 3312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 L-----HYRvvpeLVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRIL-EGYGVTE 515
Cdd:PRK12467 3313 LwdpeeLWQ----AIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLtNGYGPTE 3388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 CAPVVAI------NVPMAAKVnTVGRILPGMEARLIN-----VPgIAQGGRLQLRGPNIMRGYLRveNPGVLEQPSAENA 584
Cdd:PRK12467 3389 AVVTVTLwkcggdAVCEAPYA-PIGRPVAGRSIYVLDgqlnpVP-VGVAGELYIGGVGLARGYHQ--RPSLTAERFVADP 3464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 QGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAKGEALVLFTTDSE 664
Cdd:PRK12467 3465 FSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEA-RLLQHPSVREAVVLARDGAGGKQLVAYVVPAD 3543
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488138635 665 ITRERLIKVARE--NGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK12467 3544 PQGDWRETLRDHlaASLPDYMVPAQLLVLAAMPLGPNGKVD 3584
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
358-614 |
6.18e-19 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 90.73 E-value: 6.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 358 AMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFT--PLMTGSRv 435
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPALGMTSviPDMDPTR- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 436 flyPSplhyRVVPELVY----DRNCTVLFGTSTFLGNYARF--AHPYDFARVRYV-VAGAE---KLAESTKQIWQDkfGI 505
Cdd:PRK09274 246 ---PA----TVDPAKLFaaieRYGVTNLFGSPALLERLGRYgeANGIKLPSLRRViSAGAPvpiAVIERFRAMLPP--DA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 506 RILEGYGVTECAPVVAI----------NVPMAAKVNTVGRILPGMEARLINV-----PGIAQGGRLQ--------LRGPN 562
Cdd:PRK09274 317 EILTPYGATEALPISSIesreilfatrAATDNGAGICVGRPVDGVEVRIIAIsdapiPEWDDALRLAtgeigeivVAGPM 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 488138635 563 IMRGYlrVENPGVLEQPSAENAQGELdanWYDTGDIVTLDEQG---FCairGRVK 614
Cdd:PRK09274 397 VTRSY--YNRPEATRLAKIPDGQGDV---WHRMGDLGYLDAQGrlwFC---GRKA 443
|
|
| Acyltransferase |
pfam01553 |
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ... |
15-137 |
7.80e-19 |
|
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: 83.10 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 15 RVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIK---PVFAVYTSITDTWYMRWLKPYVDFVALDPTNPM----AI 87
Cdd:pfam01553 1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLLSLALYKRgrpLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKdaagTL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488138635 88 KHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRL 137
Cdd:pfam01553 81 EYLVELLREGKLVVIFPEGTRSREGELLPFKKGAFRLAIEAGVPIVPVAI 130
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
206-695 |
8.19e-19 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 90.63 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 206 LFEALLSAQTRYGRFKPCI----EDVSFKEDSYQTLLKKTLGVSRILQRFTVP-GEHVGMLLPNATITAAAIFGASLRGR 280
Cdd:cd05968 62 IVEQLLDKWLADTRTRPALrwegEDGTSRTLTYGELLYEVKRLANGLRALGVGkGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 281 I--PALLNYTSGAkgLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNE-------VNWVYLE---DLKDTVTLTDKLWI 348
Cdd:cd05968 142 IvvPIFSGFGKEA--AATRLQDAEAKALITADGFTRRGREVNLKEEADKacaqcptVEKVVVVrhlGNDFTPAKGRDLSY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 349 LFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASL-LANVEQIRTIADFTPRDRFMsslpLFHAFGLTVG--- 424
Cdd:cd05968 220 DEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLT----WFTDLGWMMGpwl 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 425 LFTPLMTGSRVFLY------PSPLHyrvVPELVYDRNCTVLfGTSTFLgnyARFAHPYDFARVRYVVAGAEKLAESTKQI 498
Cdd:cd05968 296 IFGGLILGATMVLYdgapdhPKADR---LWRMVEDHEITHL-GLSPTL---IRALKPRGDAPVNAHDLSSLRVLGSTGEP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 499 WQDK-----FGIR------ILEGYGVTECAPVVAINVPM----AAKVNTVgriLPGMEARLIN---VPGIAQGGRLQLRG 560
Cdd:cd05968 369 WNPEpwnwlFETVgkgrnpIINYSGGTEISGGILGNVLIkpikPSSFNGP---VPGMKADVLDesgKPARPEVGELVLLA 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 561 P--NIMRGYLRVENPGVleqpsaENAQGELDANWYDtGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSP 638
Cdd:cd05968 446 PwpGMTRGFWRDEDRYL------ETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPA 518
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488138635 639 EGQHAAAAKTDSAKGEALVLFT------TDSEITRERLIK-VARENGVPelAVPRDIRVVKALP 695
Cdd:cd05968 519 VLESAAIGVPHPVKGEAIVCFVvlkpgvTPTEALAEELMErVADELGKP--LSPERILFVKDLP 580
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
357-630 |
1.59e-18 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 90.16 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 357 RAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHA-----------FGLTVGL 425
Cdd:PLN02736 213 QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIyervnqivmlhYGVAVGF 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 426 FT----PLM---TGSRVFLYPSplhyrvVPEL---VYDRnCTVLFGTSTFLGNyARFAHPYD------------------ 477
Cdd:PLN02736 293 YQgdnlKLMddlAALRPTIFCS------VPRLynrIYDG-ITNAVKESGGLKE-RLFNAAYNakkqalengknpspmwdr 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 478 --F--------ARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINV 547
Cdd:PLN02736 365 lvFnkikaklgGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDV 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 548 PGIAQG--------GRLQLRGPNIMRGYLRVEnpgvleqpsaENAQGELDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAK 618
Cdd:PLN02736 445 PEMNYTsedqpyprGEICVRGPIIFKGYYKDE----------VQTREVIDEDgWLHTGDIGLWLPGGRLKIIDRKKNIFK 514
|
330
....*....|...
gi 488138635 619 LA-GEMVSLESVE 630
Cdd:PLN02736 515 LAqGEYIAPEKIE 527
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
355-703 |
2.70e-18 |
|
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: 88.49 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 355 PRRAMLPQQAdgsALILFTSGSEGNPKGVVHSHASLlanVEQIRTIAD---FTPRDRFMSSLPLfhAFGLTVG-LFTPLM 430
Cdd:cd17646 131 PLVPPRPDNL---AYVIYTSGSTGRPKGVMVTHAGI---VNRLLWMQDeypLGPGDRVLQKTPL--SFDVSVWeLFWPLV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 431 TGSRVFLyPSPLHYRVVP---ELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRI 507
Cdd:cd17646 203 AGARLVV-ARPGGHRDPAylaALIREHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAEL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 508 LEGYGVTECA--------------PVVAINVPMAakvNTVGRILpgmEARLINVP-GIAqgGRLQLRGPNIMRGYLR--- 569
Cdd:cd17646 282 HNLYGPTEAAidvthwpvrgpaetPSVPIGRPVP---NTRLYVL---DDALRPVPvGVP--GELYLGGVQLARGYLGrpa 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 570 ------VENPGvleqpsaenAQGeldANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHA 643
Cdd:cd17646 354 ltaerfVPDPF---------GPG---SRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTHA 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488138635 644 AA-AKTDSAKGEALVLFTT--------DSEITRERLikvaRENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17646 421 VVvARAAPAGAARLVGYVVpaagaagpDTAALRAHL----AER-LPEYMVPAAFVVLDALPLTANGKLD 484
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
254-694 |
4.40e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.39 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 254 PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKgkLTHLPEQVNEVNWVYL 333
Cdd:PRK08279 86 KGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEA--FEEARADLARPPRLWV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 334 EDLkDTVTLTDKLWILFHLCFPRRAMLPQQADGS-----ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDR 408
Cdd:PRK08279 164 AGG-DTLDDPEGYEDLAAAAAGAPTTNPASRSGVtakdtAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 409 FMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPElVYDRNCTvLFGtstFLGNYARF-----AHPYDFA-RVR 482
Cdd:PRK08279 243 LYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDD-VRRYRAT-AFQ---YIGELCRYllnqpPKPTDRDhRLR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 483 YVV-AGaekLAESTKQIWQDKFGI-RILEGYGVTEcAPVVAINVpmAAKVNTVGRIlPGMEARLINVPGIAQGGRLQLRG 560
Cdd:PRK08279 318 LMIgNG---LRPDIWDEFQQRFGIpRILEFYAASE-GNVGFINV--FNFDGTVGRV-PLWLAHPYAIVKYDVDTGEPVRD 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 561 PNimrGYLRVENPGvlE-----------QP------SAEN---------AQGelDAnWYDTGDIVTLDEQGFCAIRGRV- 613
Cdd:PRK08279 391 AD---GRCIKVKPG--EvglligritdrGPfdgytdPEASekkilrdvfKKG--DA-WFNTGDLMRDDGFGHAQFVDRLg 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 614 -----KrfaklaGEMVSLESVEQlAISLSPEGQHAAA-----AKTDSAKGEALVLFTTDSEITRERLIKVARENgVPELA 683
Cdd:PRK08279 463 dtfrwK------GENVATTEVEN-ALSGFPGVEEAVVygvevPGTDGRAGMAAIVLADGAEFDLAALAAHLYER-LPAYA 534
|
490
....*....|.
gi 488138635 684 VPRDIRVVKAL 694
Cdd:PRK08279 535 VPLFVRLVPEL 545
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
258-624 |
1.10e-17 |
|
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: 87.03 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 258 VGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQsaIIAASLKT---IVTSRQFLEK-----GKLTHL-------- 321
Cdd:cd05933 36 VGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQ--YVAETSEAnilVVENQKQLQKilqiqDKLPHLkaiiqyke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 322 ---PEQVNEVNWVYLEDLKDTVTLTDKLWIlfhlcfprraMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIR 398
Cdd:cd05933 114 plkEKEPNLYSWDEFMELGRSIPDEQLDAI----------ISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAAS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 399 TIADFTPRDR----FMSSLPLFHAFGLTVGLFTPLMTGSRVFL------------------------------------- 437
Cdd:cd05933 184 QHMDLRPATVgqesVVSYLPLSHIAAQILDIWLPIKVGGQVYFaqpdalkgtlvktlrevrptafmgvprvwekiqekmk 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 438 --------------------------------YPSPLHYRVVPELVYDRnctvlfgTSTFLGnyarfahpydFARVRYVV 485
Cdd:cd05933 264 avgaksgtlkrkiaswakgvgletnlklmggeSPSPLFYRLAKKLVFKK-------VRKALG----------LDRCQKFF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 486 AGAEKLAESTKQIWQDkFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINvPGIAQGGRLQLRGPNIMR 565
Cdd:cd05933 327 TGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHN-PDADGIGEICFWGRHVFM 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138635 566 GYLRVEnpgvleqpsaENAQGELDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLA-GEMV 624
Cdd:cd05933 405 GYLNME----------DKTEEAIDEDgWLHSGDLGKLDEDGFLYITGRIKELIITAgGENV 455
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
360-659 |
1.71e-17 |
|
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: 86.00 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 360 LPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYP 439
Cdd:cd05908 101 LCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHYRvVPEL----VYDRNCTVL----FGTSTFLGNY-ARFAHPYDFARVRYVVAGAEKLA-----ESTKQIwqDKFGI 505
Cdd:cd05908 181 TRLFIR-RPILwlkkASEHKATIVsspnFGYKYFLKTLkPEKANDWDLSSIRMILNGAEPIDyelchEFLDHM--SKYGL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 506 R---ILEGYGVTECA--------------------------PVVAINV--PMAAKVNTVGRILPGMEARLINVP--GIAQ 552
Cdd:cd05908 258 KrnaILPVYGLAEASvgaslpkaqspfktitlgrrhvthgePEPEVDKkdSECLTFVEVGKPIDETDIRICDEDnkILPD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 553 G--GRLQLRGPNIMRGYLrvENPgvleqpsAENAQGELDANWYDTGDivtldeQGF-----CAIRGRVKRFAKLAGEMVS 625
Cdd:cd05908 338 GyiGHIQIRGKNVTPGYY--NNP-------EATAKVFTDDGWLKTGD------LGFirngrLVITGREKDIIFVNGQNVY 402
|
330 340 350
....*....|....*....|....*....|....*..
gi 488138635 626 LESVEQLAISLSPE--GQHAAAAKTDS-AKGEALVLF 659
Cdd:cd05908 403 PHDIERIAEELEGVelGRVVACGVNNSnTRNEEIFCF 439
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
233-701 |
2.03e-17 |
|
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: 85.26 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSrq 311
Cdd:cd05973 2 TFGELRALSARFANALQELGVgPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 flekgklthlpeqvnevnwvyledlkdtVTLTDKLwilfhlcfprramlpqqADGSALILFTSGSEGNPKGVVHSHASLL 391
Cdd:cd05973 80 ----------------------------AANRHKL-----------------DSDPFVMMFTSGTTGLPKGVPVPLRALA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 392 ANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLhyrvVPELVYDrnCTVLFGTSTFLGNYAR 471
Cdd:cd05973 115 AFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGF----SVESTWR--VIERLGVTNLAGSPTA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 472 F----AHPYDFA-----RVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMA--AKVNTVGRILPGM 540
Cdd:cd05973 189 YrllmAAGAEVParpkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 541 EARLI----NVPGIAQGGRLQL---RGPNI-MRGYLRVENPGVleqpsaenaqgelDANWYDTGDIVTLDEQGFCAIRGR 612
Cdd:cd05973 269 RVAVLdddgDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI-------------DGGYYLTGDTVEFDPDGSFSFIGR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 613 VKRFAKLAGEMVSLESVEQLAIslspegQHAAAAktdsakgEALVLFTTDSEitRERLIK---VAREN--GVPEL----- 682
Cdd:cd05973 336 ADDVITMSGYRIGPFDVESALI------EHPAVA-------EAAVIGVPDPE--RTEVVKafvVLRGGheGTPALadelq 400
|
490 500
....*....|....*....|....*....
gi 488138635 683 ----------AVPRDIRVVKALPLLGSGK 701
Cdd:cd05973 401 lhvkkrlsahAYPRTIHFVDELPKTPSGK 429
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
279-701 |
2.16e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.01 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 279 GRIPALLNYTSGAKGLQSAII---AASLKTIVTSRQFLEKGKLTHLPEqvneVNW-VYLEDLKDTVTL-------TDKLW 347
Cdd:PLN02860 81 GGIVAPLNYRWSFEEAKSAMLlvrPVMLVTDETCSSWYEELQNDRLPS----LMWqVFLESPSSSVFIflnsfltTEMLK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 348 ilfhlcfpRRAMLPQQAD------GSALILFTSGSEGNPKGVVHSHASL----LANVeqirTIADFTPRDRFMSSLPLFH 417
Cdd:PLN02860 157 --------QRALGTTELDyawapdDAVLICFTSGTTGRPKGVTISHSALivqsLAKI----AIVGYGEDDVYLHTAPLCH 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 418 AFGLTVGLfTPLMTGSRVFLYPSpLHYRVVPELVYDRNCTVLFGTSTFLGN---YARFAHPYD-FARVRYVVAGA----E 489
Cdd:PLN02860 225 IGGLSSAL-AMLMVGACHVLLPK-FDAKAALQAIKQHNVTSMITVPAMMADlisLTRKSMTWKvFPSVRKILNGGgslsS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 490 KLAESTKQIWQDKfgiRILEGYGVTE-CAPV--VAINVPMAAKVNT--------------------VGRILPGMEARlIN 546
Cdd:PLN02860 303 RLLPDAKKLFPNA---KLFSAYGMTEaCSSLtfMTLHDPTLESPKQtlqtvnqtksssvhqpqgvcVGKPAPHVELK-IG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 547 VPGIAQGGRLQLRGPNIMRGYLRvENPgvlEQPSAENAQGeldanWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSL 626
Cdd:PLN02860 379 LDESSRVGRILTRGPHVMLGYWG-QNS---ETASVLSNDG-----WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYP 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 627 ESVEQLaisLSpegQHAAAAKT------DSAKGEALVLFT--------TDSE---------ITRERLIKVARENGVPELA 683
Cdd:PLN02860 450 EEVEAV---LS---QHPGVASVvvvgvpDSRLTEMVVACVrlrdgwiwSDNEkenakknltLSSETLRHHCREKNLSRFK 523
|
490
....*....|....*....
gi 488138635 684 VPRDI-RVVKALPLLGSGK 701
Cdd:PLN02860 524 IPKLFvQWRKPFPLTTTGK 542
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
354-709 |
2.27e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 354 FPRRAMLPQQA-DGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDR---FMSslplFHAFGLTVGLFTPL 429
Cdd:PRK12316 2134 YPDTAPAVQLAgENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCelqFMS----FSFDGAHEQWFHPL 2209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 430 MTGSRVFLYPSPLHyrvVPELVYD----RNCTVLFGTSTFLGNYARFAHpYDFAR--VRYVVAGAEKL-AESTKQIWQDK 502
Cdd:PRK12316 2210 LNGARVLIRDDELW---DPEQLYDemerHGVTILDFPPVYLQQLAEHAE-RDGRPpaVRVYCFGGEAVpAASLRLAWEAL 2285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 503 FGIRILEGYGVTECAPVVAI-----NVPMAAKVNTVGRILPGMEARLINV------PGIAqgGRLQLRGPNIMRGYLrvE 571
Cdd:PRK12316 2286 RPVYLFNGYGPTEAVVTPLLwkcrpQDPCGAAYVPIGRALGNRRAYILDAdlnllaPGMA--GELYLGGEGLARGYL--N 2361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 572 NPGVLEQ---PSAENAQGELdanWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAAAKT 648
Cdd:PRK12316 2362 RPGLTAErfvPDPFSASGER---LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAH-PAVREAVVVAQ 2437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488138635 649 DSAKGEALVLFTT--DSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGK 709
Cdd:PRK12316 2438 DGASGKQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
201-701 |
2.66e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 85.80 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 201 VPRE-TLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLR 278
Cdd:PLN02330 24 VPDKlTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLrKGQVVVVVLPNVAEYGIVALGIMAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 279 GRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQV-------NEVNWVYLEDLKDTV--TLTDKLWIL 349
Cdd:PLN02330 104 GGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVlgeekieGAVNWKELLEAADRAgdTSDNEEILQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 350 FHLCfprraMLPqqadgsalilFTSGSEGNPKGVVHSHASLLANV---------EQIRTIADftprdrfMSSLPLFHAFG 420
Cdd:PLN02330 184 TDLC-----ALP----------FSSGTTGISKGVMLTHRNLVANLcsslfsvgpEMIGQVVT-------LGLIPFFHIYG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 421 LTVGLFTPLMTGSRVflypsplhyrvvpeLVYDRnctvlFGTSTFLgnYARFAHPYDFA--------------------- 479
Cdd:PLN02330 242 ITGICCATLRNKGKV--------------VVMSR-----FELRTFL--NALITQEVSFApivppiilnlvknpiveefdl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 480 ---RVRYVVAGAEKLAESTKQIWQDKF-GIRILEGYGVTE--CAPVVAINVPMA---AKVNTVGRILPGMEARLINvPGI 550
Cdd:PLN02330 301 sklKLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEhsCITLTHGDPEKGhgiAKKNSVGFILPNLEVKFID-PDT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 551 AQG------GRLQLRGPNIMRGYLRvenpgvleqpSAENAQGELDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEM 623
Cdd:PLN02330 380 GRSlpkntpGELCVRSQCVMQGYYN----------NKEETDRTIDEDgWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 624 VSLESVEQLAISlSPEGQHAAAAK-TDSAKGE---ALVLFTTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGS 699
Cdd:PLN02330 450 VAPAELEAILLT-HPSVEDAAVVPlPDEEAGEipaACVVINPKAKESEEDILNFVAAN-VAHYKKVRVVQFVDSIPKSLS 527
|
..
gi 488138635 700 GK 701
Cdd:PLN02330 528 GK 529
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
347-702 |
2.77e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.83 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 347 WILFHLCFPRRAMLPQ-QADGSALILFTSGSEGNPKGVVHSHASLLANVEQI-RTIADFTPRDRFMSSLPLFHAFGLtVG 424
Cdd:PRK09192 157 HAWFKALPEADVALPRpTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIsHDGLKVRPGDRCVSWLPFYHDMGL-VG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 425 LF-TPLMTGSRVFLYPS------PLHYRvvpELVYDRNCTVLFgTSTF-------LGNYARFAHpYDFARVRyvVAG--- 487
Cdd:PRK09192 236 FLlTPVATQLSVDYLPTrdfarrPLQWL---DLISRNRGTISY-SPPFgyelcarRVNSKDLAE-LDLSCWR--VAGiga 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 488 -----------AEK----------------LAEST---------KQIWQDKFGIRILEGYGVTEcaPVVAINVPMAAKVN 531
Cdd:PRK09192 309 dmirpdvlhqfAEAfapagfddkafmpsygLAEATlavsfsplgSGIVVEEVDRDRLEYQGKAV--APGAETRRVRTFVN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 532 TvGRILPGMEARLINVPGIA----QGGRLQLRGPNIMRGYLRvenpgvleqpsAENAQGELDA-NWYDTGDIVTLDEqGF 606
Cdd:PRK09192 387 C-GKALPGHEIEIRNEAGMPlperVVGHICVRGPSLMSGYFR-----------DEESQDVLAAdGWLDTGDLGYLLD-GY 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 607 CAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQH--AAAAKTDSAKGEALVLF----TTDSEiTRERLI-----KVAR 675
Cdd:PRK09192 454 LYITGRAKDLIIINGRNIWPQDIEWIAEQE-PELRSgdAAAFSIAQENGEKIVLLvqcrISDEE-RRGQLIhalaaLVRS 531
|
410 420 430
....*....|....*....|....*....|
gi 488138635 676 ENGVP---ELAVPRdirvvkALPLLGSGKP 702
Cdd:PRK09192 532 EFGVEaavELVPPH------SLPRTSSGKL 555
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
360-599 |
3.31e-17 |
|
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: 86.45 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 360 LPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRF--MSSLplfhAFGLTVG-LFTPLMTGSRVF 436
Cdd:COG1020 612 VPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVlqFASL----SFDASVWeIFGALLSGATLV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 437 LYP-----SPLHYRvvpELVYDRNCTVLFGTSTFLGNYARfAHPYDFARVRYVVAGAEKLAESTKQIWQDKF-GIRILEG 510
Cdd:COG1020 688 LAPpearrDPAALA---ELLARHRVTVLNLTPSLLRALLD-AAPEALPSLRLVLVGGEALPPELVRRWRARLpGARLVNL 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 511 YGVTECAPVVAI----NVPMAAKVNTVGRILPGMEARLIN-----VP-GIAqgGRLQLRGPNIMRGYLRveNPGVleqpS 580
Cdd:COG1020 764 YGPTETTVDSTYyevtPPDADGGSVPIGRPIANTRVYVLDahlqpVPvGVP--GELYIGGAGLARGYLN--RPEL----T 835
|
250 260
....*....|....*....|...
gi 488138635 581 AE----NAQGELDANWYDTGDIV 599
Cdd:COG1020 836 AErfvaDPFGFPGARLYRTGDLA 858
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
364-703 |
4.55e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.38 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGSRVFLyPSPL 442
Cdd:PRK05691 1272 GDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI--SFDVSVwECFWPLITGCRLVL-AGPG 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 443 HYR---VVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKL-AESTKQIWQDKFGIRILEGYGVTEcap 518
Cdd:PRK05691 1349 EHRdpqRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALpAELRNRVLQRLPQVQLHNRYGPTE--- 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 519 vVAINVPM------AAKVNTVGRILPGMEARLINV------PGIAqgGRLQLRGPNIMRGYLRveNPGVLEQPSAENAQG 586
Cdd:PRK05691 1426 -TAINVTHwqcqaeDGERSPIGRPLGNVLCRVLDAelnllpPGVA--GELCIGGAGLARGYLG--RPALTAERFVPDPLG 1500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 587 ELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEqlAISLSPEG-QHAAAAKTDSAKGEALVLFTT---D 662
Cdd:PRK05691 1501 EDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ--ARLLAQPGvAQAAVLVREGAAGAQLVGYYTgeaG 1578
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488138635 663 SEITRERLiKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK05691 1579 QEAEAERL-KAALAAELPEYMVPAQLIRLDQMPLGPSGKLD 1618
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
364-703 |
5.06e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.16 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPlFHAFGLTVGLFTPLMTGSRVFLYPSPLH 443
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLAGPEDW 3273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 444 Y--RVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQdkFGIRILEGYGVTECAPVVA 521
Cdd:PRK12316 3274 RdpALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVT 3351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 522 INVPMAAKVNT--VGRILPGMEARLINVPG----IAQGGRLQLRGPNIMRGYLrvENPGVLEQPSAENAQGElDANWYDT 595
Cdd:PRK12316 3352 HWQCVEEGKDAvpIGRPIANRACYILDGSLepvpVGALGELYLGGEGLARGYH--NRPGLTAERFVPDPFVP-GERLYRT 3428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 596 GDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEqlAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVAR 675
Cdd:PRK12316 3429 GDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE--ARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHL 3506
|
330 340
....*....|....*....|....*...
gi 488138635 676 ENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK12316 3507 KASLPEYMVPAHLLFLERMPLTPNGKLD 3534
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
347-701 |
5.21e-17 |
|
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: 84.85 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 347 WILFH-LC------FPRR-AMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHA 418
Cdd:cd05970 159 WIDFRkLIknaspdFERPtANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 419 FGLTVGLFTPLMTGSRVFLYPsplHYRVVPELVYDRncTVLFGTSTFLG--NYARF-----AHPYDFARVRYVVAGAEKL 491
Cdd:cd05970 239 KAVWGKIYGQWIAGAAVFVYD---YDKFDPKALLEK--LSKYGVTTFCAppTIYRFliredLSRYDLSSLRYCTTAGEAL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 492 AESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPG----IAQGGRLQLRGPN----- 562
Cdd:cd05970 314 NPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGrsceAGEEGEIVIRTSKgkpvg 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 563 IMRGYLRvenpgvleqpSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQH 642
Cdd:cd05970 394 LFGGYYK----------DAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEC 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488138635 643 AAAAKTDSAKGE---ALVLFTTD---SEITRERLIKVARENGVPELAvPRDIRVVKALPLLGSGK 701
Cdd:cd05970 464 AVTGVPDPIRGQvvkATIVLAKGyepSEELKKELQDHVKKVTAPYKY-PRIVEFVDELPKTISGK 527
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
291-712 |
5.43e-17 |
|
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: 85.06 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 291 AKGLQSAIIAASLKTIVTSRQFLEKGK----LTHLPEQVNEVNW------VYLEDLKDTVTLTDKLWILFHLCFP---RR 357
Cdd:cd05967 143 AKELASRIDDAKPKLIVTASCGIEPGKvvpyKPLLDKALELSGHkphhvlVLNRPQVPADLTKPGRDLDWSELLAkaePV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 358 AMLPQQADGSALILFTSGSEGNPKGVVHSHAS-LLANVEQIRTIADFTPRDRFMSSLPLfhafGLTVG----LFTPLMTG 432
Cdd:cd05967 223 DCVPVAATDPLYILYTSGTTGKPKGVVRDNGGhAVALNWSMRNIYGIKPGDVWWAASDV----GWVVGhsyiVYGPLLHG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 433 SRVFLY-------PSPLHY-RVVPElvYDRNCtvLFGTSTFL---------GNYARfahPYDFARVRYVVAGAEKLAEST 495
Cdd:cd05967 299 ATTVLYegkpvgtPDPGAFwRVIEK--YQVNA--LFTAPTAIrairkedpdGKYIK---KYDLSSLRTLFLAGERLDPPT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 496 KQIWQDKFGIRILEGYGVTECA-PVVAINV---PMAAKVNTVGRILPGMEARLINvpgiAQGGRLqlrGPNIMrGYLRVE 571
Cdd:cd05967 372 LEWAENTLGVPVIDHWWQTETGwPITANPVglePLPIKAGSPGKPVPGYQVQVLD----EDGEPV---GPNEL-GNIVIK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 572 ---NPGVL-----EQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHA 643
Cdd:cd05967 444 lplPPGCLltlwkNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE-SVLSHPAVAEC 522
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488138635 644 AA-AKTDSAKGE---ALVLFTTDSEIT----RERLIKVARENGVPeLAVPRDIRVVKALPLLGSGKPDFVTLGKMAQ 712
Cdd:cd05967 523 AVvGVRDELKGQvplGLVVLKEGVKITaeelEKELVALVREQIGP-VAAFRLVIFVKRLPKTRSGKILRRTLRKIAD 598
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
338-703 |
6.14e-17 |
|
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: 84.32 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 338 DTVTLTDKLWILFHLCFPRRAmlPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfh 417
Cdd:cd17651 111 VAVTLLDQPGAAAGADAEPDP--ALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGL-- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 418 AFGLTVG-LFTPLMTGSRVFLYPSplHYRVVPE----LVYDRNCTVLFGTSTFLGNYARFA--HPYDFARVRYVVAGAEK 490
Cdd:cd17651 187 GFDVSVQeIFSTLCAGATLVLPPE--EVRTDPPalaaWLDEQRISRVFLPTVALRALAEHGrpLGVRLAALRYLLTGGEQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 491 L--AESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAK----VNTVGRILPGMEARLIN-----VPgIAQGGRLQLR 559
Cdd:cd17651 265 LvlTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAawpaPPPIGRPIDNTRVYVLDaalrpVP-PGVPGELYIG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 560 GPNIMRGYLRveNPGVLEQPSAENAQGElDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEqLAISLSPE 639
Cdd:cd17651 344 GAGLARGYLN--RPELTAERFVPDPFVP-GARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIE-AALARHPG 419
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138635 640 GQHAAAAKTDSAKGE----ALVLFTTDSEITRERLiKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17651 420 VREAVVLAREDRPGEkrlvAYVVGDPEAPVDAAEL-RAALATHLPEYMVPSAFVLLDALPLTPNGKLD 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
368-703 |
8.97e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 8.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDrfmsSLPLFHAFGLTV---GLFTPLMTGSRVFLYPSPLHY 444
Cdd:PRK12467 1721 AYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD----VVLQFTSFAFDVsvwELFWPLINGARLVIAPPGAHR 1796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 445 RvvPELVYDRNC----TVLFGTSTFLGNYARFAHPYDFAR-VRYVVAGAEKLAESTKQIWQDKFGIR-ILEGYGVTECA- 517
Cdd:PRK12467 1797 D--PEQLIQLIErqqvTTLHFVPSMLQQLLQMDEQVEHPLsLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAv 1874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 518 ---------------PVVAINVPMAakvNTVGRILpgmEARLINVPgIAQGGRLQLRGPNIMRGYLRveNPGVLEQPSAE 582
Cdd:PRK12467 1875 dvthwtcrrkdlegrDSVPIGQPIA---NLSTYIL---DASLNPVP-IGVAGELYLGGVGLARGYLN--RPALTAERFVA 1945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 583 NAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlaiSLSPEGQ--HAAAAKTDSAKGEALV--L 658
Cdd:PRK12467 1946 DPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEA---RLREQGGvrEAVVIAQDGANGKQLVayV 2022
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488138635 659 FTTDSEIT---------RERLiKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK12467 2023 VPTDPGLVdddeaqvalRAIL-KNHLKASLPEYMVPAHLVFLARMPLTPNGKLD 2075
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
355-703 |
9.71e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 83.49 E-value: 9.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 355 PRRAMLPqqaDGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGS 433
Cdd:cd12116 119 PRTPVSP---DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTY--AFDISLlELLLPLLAGA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVFLYPSPLHY--RVVPELVYDRNCTVLFGTST----FLGnyarfAHPYDFARVRYVVAG-------AEKLAESTKQIWQ 500
Cdd:cd12116 194 RVVIAPRETQRdpEALARLIEAHSITVMQATPAtwrmLLD-----AGWQGRAGLTALCGGealppdlAARLLSRVGSLWN 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 501 dkfgirileGYGVTE------CAPVVAinvpmAAKVNTVGRILPG-----MEARLINVP-GIAqgGRLQLRGPNIMRGYL 568
Cdd:cd12116 269 ---------LYGPTEttiwstAARVTA-----AAGPIPIGRPLANtqvyvLDAALRPVPpGVP--GELYIGGDGVAQGYL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 569 RveNPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKT 648
Cdd:cd12116 333 G--RPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRE 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488138635 649 DSAKGE--ALVLFTTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd12116 411 DGGDRRlvAYVVLKAGAAPDAAALRAHLRAT-LPAYMVPSAFVRLDALPLTANGKLD 466
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
233-714 |
1.06e-16 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 83.17 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRq 311
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLkPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVDA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 flekgklthlpeqvnevnwvyledlkdtvtltdklwilfhlcfprramlpqqadgsALILFTSGSEGNPKG--VVHSHAS 389
Cdd:cd05940 84 --------------------------------------------------------ALYIYTSGTTGLPKAaiISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 390 LLANVEQIRTIAdfTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVyDRNCTVLfgtsTFLGNY 469
Cdd:cd05940 108 RGGAFFAGSGGA--LPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIR-KYQATIF----QYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 470 ARF-----AHPYDFA-RVRYVVAGAEKlaestKQIW---QDKFGI-RILEGYGVTECApVVAINVPmaAKVNTVGRILP- 538
Cdd:cd05940 181 CRYllnqpPKPTERKhKVRMIFGNGLR-----PDIWeefKERFGVpRIAEFYAATEGN-SGFINFF--GKPGAIGRNPSl 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 539 ---GMEARLINVPgiAQGGRLqLRGPNimrGYLRVENPG-----VLEQPSAENAQGELDAN----------------WYD 594
Cdd:cd05940 253 lrkVAPLALVKYD--LESGEP-IRDAE---GRCIKVPRGepgllISRINPLEPFDGYTDPAatekkilrdvfkkgdaWFN 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 595 TGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEqlAISLSPEGQHAAAA------KTDSAKGEALVLFTTDSEITRE 668
Cdd:cd05940 327 TGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVA--AVLGAFPGVEEANVygvqvpGTDGRAGMAAIVLQPNEEFDLS 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 488138635 669 RLIKVARENgVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDP 714
Cdd:cd05940 405 ALAAHLEKN-LPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
225-701 |
1.17e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 83.79 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 225 EDVSFKEDSYQT-----LLKKtLGVSRilqrftvpGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAII 299
Cdd:PRK04319 72 EKYTYKELKELSnkfanVLKE-LGVEK--------GDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 300 AASLKTIVTSRQFLEKGKLTHLPEqvneVNWVYLEDlkDTVTLTDKLWILFHLCF---PRRAMLPQQADGSALILFTSGS 376
Cdd:PRK04319 143 DSEAKVLITTPALLERKPADDLPS----LKHVLLVG--EDVEEGPGTLDFNALMEqasDEFDIEWTDREDGAILHYTSGS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 377 EGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSplhyRVVPELVY---- 452
Cdd:PRK04319 217 TGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG----RFSPERWYrile 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 453 DRNCTVLFGTST----FLGNYARFAHPYDFARVRYVVAGAEKL-AESTKqiW-QDKFGIRILEGYGVTECAPVVAINVP- 525
Cdd:PRK04319 293 DYKVTVWYTAPTairmLMGAGDDLVKKYDLSSLRHILSVGEPLnPEVVR--WgMKVFGLPIHDNWWMTETGGIMIANYPa 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 526 MAAKVNTVGRILPGMEARLI----NVPGIAQGGRLQLRG--PNIMRGYLRveNPgvleqpsaENAQGELDANWYDTGDIV 599
Cdd:PRK04319 371 MDIKPGSMGKPLPGIEAAIVddqgNELPPNRMGNLAIKKgwPSMMRGIWN--NP--------EKYESYFAGDWYVSGDSA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 600 TLDEQGFCAIRGRVKRFAKLAGEMVSLESVEqlaislSPEGQHAAAA------KTDSAKGEALVLF------TTDSEITR 667
Cdd:PRK04319 441 YMDEDGYFWFQGRVDDVIKTSGERVGPFEVE------SKLMEHPAVAeagvigKPDPVRGEIIKAFvalrpgYEPSEELK 514
|
490 500 510
....*....|....*....|....*....|....
gi 488138635 668 ERLIKVAREnGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK04319 515 EEIRGFVKK-GLGAHAAPREIEFKDKLPKTRSGK 547
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
370-701 |
1.30e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 83.40 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 370 ILFTSGSEGNPKGVVHSHASL-LANVEQIRTIAdFTPRDRFMSSLPLFH--AFGL------------------------- 421
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLhWKSIDHVIALG-LTASERLLVVGPLYHvgAFDLpgiavlwvggtlrihrefdpeavla 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 422 -------TVGLFTPLMTgSRVFLYPSPlhyrvvpelvyDRnctvlfgtstflgnyarfahpYDFARVRYVVAGAEKLAES 494
Cdd:PRK06145 233 aierhrlTCAWMAPVML-SRVLTVPDR-----------DR---------------------FDLDSLAWCIGGGEKTPES 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 495 TKQIWQDKF-GIRILEGYGVTEcapVVAINVPMAA-----KVNTVGRILPGMEARLINVPG----IAQGGRLQLRGPNIM 564
Cdd:PRK06145 280 RIRDFTRVFtRARYIDAYGLTE---TCSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGrwlpPNMKGEICMRGPKVT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 565 RGYLRvenpgvleqpSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAA 644
Cdd:PRK06145 357 KGYWK----------DPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAV 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 645 AAKTDSAKGE---ALVLFTTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK06145 427 IGVHDDRWGEritAVVVLNPGATLTLEALDRHCRQR-LASFKVPRQLKVRDELPRNPSGK 485
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
244-703 |
1.37e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 83.50 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 244 VSRILQRFT----VPGEHVGMLLPNATITAAAIFGASLRG-RIPALlnYTSGAKGLQSAIIA-ASLKT-IVTSRQFLEKG 316
Cdd:PRK06188 47 ISRYIQAFEalglGTGDAVALLSLNRPEVLMAIGAAQLAGlRRTAL--HPLGSLDDHAYVLEdAGISTlIVDPAPFVERA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 317 KltHLPEQVNEVNwvYLEDLKDTVTLTDkLWILFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQ 396
Cdd:PRK06188 125 L--ALLARVPSLK--HVLTLGPVPDGVD-LLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 397 IRTIADFTPRDRFMSSLPLFHAFGLtvgLFTP-LMTGSRVFLYPSPLHYRVVpELVYDRNCTVLFGTSTFLgnYARFAHP 475
Cdd:PRK06188 200 QLAEWEWPADPRFLMCTPLSHAGGA---FFLPtLLRGGTVIVLAKFDPAEVL-RAIEEQRITATFLVPTMI--YALLDHP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 476 ----YDFARVRYVVAGAE-----KLAESTkqiwqDKFGIRILEGYGVTECapvvainvPMAAKV--------------NT 532
Cdd:PRK06188 274 dlrtRDLSSLETVYYGASpmspvRLAEAI-----ERFGPIFAQYYGQTEA--------PMVITYlrkrdhdpddpkrlTS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 533 VGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLRvenpgvleQPsAENAQGeLDANWYDTGDIVTLDEQGFCA 608
Cdd:PRK06188 341 CGRPTPGLRVALLDEDGreVAQGevGEICVRGPLVMDGYWN--------RP-EETAEA-FRDGWLHTGDVAREDEDGFYY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 609 IRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAK-GEAL---VLFTTDSEITRERLIKVARE-NGVPelA 683
Cdd:PRK06188 411 IVDRKKDMIVTGGFNVFPREVED-VLAEHPAVAQVAVIGVPDEKwGEAVtavVVLRPGAAVDAAELQAHVKErKGSV--H 487
|
490 500
....*....|....*....|
gi 488138635 684 VPRDIRVVKALPLLGSGKPD 703
Cdd:PRK06188 488 APKQVDFVDSLPLTALGKPD 507
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
254-701 |
1.62e-16 |
|
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: 83.12 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 254 PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLThlpEQVNEVNWVYL 333
Cdd:cd12118 53 RGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFEYEDLLA---EGDPDFEWIPP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 334 EDLKDTVTLTdklwilfhlcfprramlpqqadgsalilFTSGSEGNPKGVVHSH--ASLLANVEQIRTIADftPRDRFMS 411
Cdd:cd12118 130 ADEWDPIALN----------------------------YTSGTTGRPKGVVYHHrgAYLNALANILEWEMK--QHPVYLW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 412 SLPLFHAFGLTVGLFTPLMTGSRVFLYpsplhyRVVPELVYD----RNCTVLFGTSTFLGNYARFAH----PYDfARVRY 483
Cdd:cd12118 180 TLPMFHCNGWCFPWTVAAVGGTNVCLR------KVDAKAIYDliekHKVTHFCGAPTVLNMLANAPPsdarPLP-HRVHV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 484 VVAGAEKLAESTKQIWQdkFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEAR------------------LI 545
Cdd:cd12118 253 MTAGAPPPAAVLAKMEE--LGFDVTHVYGLTETYGPATVCAWKPEWDELPTEERARLKARqgvryvgleevdvldpetMK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 546 NVPGIAQG-GRLQLRGPNIMRGYLRveNPgvleQPSAENAQGeldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMV 624
Cdd:cd12118 331 PVPRDGKTiGEIVFRGNIVMKGYLK--NP----EATAEAFRG----GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 625 SleSVEQLAISLSPEGQHAAA--AKTDSAKGEALVLFTT---DSEITRERLIKVARENgVPELAVPRDIrVVKALPLLGS 699
Cdd:cd12118 401 S--SVEVEGVLYKHPAVLEAAvvARPDEKWGEVPCAFVElkeGAKVTEEEIIAFCREH-LAGFMVPKTV-VFGELPKTST 476
|
..
gi 488138635 700 GK 701
Cdd:cd12118 477 GK 478
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
365-701 |
2.35e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 82.90 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 365 DGSALILFTSGSEGNPKGVVHSHASLLAN-VEQIRTIADFTPRDRFMSSLPLFHAFGLTvGLFTPLMTGSRVFLYP---- 439
Cdd:PRK07786 174 DSPALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIYPlgaf 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 --SPLHYRVVPELVydrnctvlfgTSTFLGNY-------ARFAHPYDFArVRYVVAGAEKLAESTKQIWQDKF-GIRILE 509
Cdd:PRK07786 253 dpGQLLDVLEAEKV----------TGIFLVPAqwqavcaEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFpEAQILA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 510 GYGVTECAPVVAINVPMAA--KVNTVGRILPGMEARLI--NVPGIAQG--GRLQLRGPNIMRGYLRveNPgvleQPSAEN 583
Cdd:PRK07786 322 AFGQTEMSPVTCMLLGEDAirKLGSVGKVIPTVAARVVdeNMNDVPVGevGEIVYRAPTLMSGYWN--NP----EATAEA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 584 AQGeldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEA----LVLF 659
Cdd:PRK07786 396 FAG----GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVpvavAAVR 471
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 488138635 660 TTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK07786 472 NDDAALTLEDLAEFLTDR-LARYKHPKALEIVDALPRNPAGK 512
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
233-701 |
2.71e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 82.35 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQ 311
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVaPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 FLEKgklthlpeqvnevnwvyLEDLKDTVTLTDKLWILFHLCFPRramlPQQADGSALILFTSGSEGNPKGVVHShASLL 391
Cdd:PRK13383 142 FAER-----------------IAGADDAVAVIDPATAGAEESGGR----PAVAAPGRIVLLTSGTTGKPKGVPRA-PQLR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 392 ANVEQIRTIADFT---PRDRFMSSLPLFHAFGLTVGLFTPLMTGS----RVF-----LYPSPLH----YRVVPelvydrn 455
Cdd:PRK13383 200 SAVGVWVTILDRTrlrTGSRISVAMPMFHGLGLGMLMLTIALGGTvlthRHFdaeaaLAQASLHradaFTAVP------- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 456 ctVLFGTSTFLGNYARFAHPydFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECApVVAINVPMAAK--VNTV 533
Cdd:PRK13383 273 --VVLARILELPPRVRARNP--LPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVG-IGALATPADLRdaPETV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 534 GRILPGMEARLINVPGIAQGGRLQLRgpnIMRGylrvenpgvleqpsaenaqGELDANWY-------------DTGDIVT 600
Cdd:PRK13383 348 GKPVAGCPVRILDRNNRPVGPRVTGR---IFVG-------------------GELAGTRYtdgggkavvdgmtSTGDMGY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 601 LDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTT-------DSEITRERLikv 673
Cdd:PRK13383 406 LDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVlhpgsgvDAAQLRDYL--- 482
|
490 500
....*....|....*....|....*...
gi 488138635 674 arENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK13383 483 --KDRVSRFEQPRDINIVSSIPRNPTGK 508
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
233-703 |
1.40e-15 |
|
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: 80.01 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRq 311
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVrPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 flekgkltHLPEQVNEVNWVYLEDLKDTVTLTDklwilfhlcFPRRAMLPQQAdgsALILFTSGSEGNPKGVVHSHASLL 391
Cdd:cd12114 93 --------PDAQLDVAVFDVLILDLDALAAPAP---------PPPVDVAPDDL---AYVIFTSGSTGTPKGVMISHRAAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 392 ANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGSRVFLyPSPLHYRVV---PELVYDRNCTV------LFG 461
Cdd:cd12114 153 NTILDINRRFAVGPDDRVLALSSL--SFDLSVyDIFGALSAGATLVL-PDEARRRDPahwAELIERHGVTLwnsvpaLLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 462 tstFLGNYARfAHPYDFARVRYVVAG----AEKLAESTKQIWQDkfgIRILEGYGVTECA------PVVAinVPMAAKVN 531
Cdd:cd12114 230 ---MLLDVLE-AAQALLPSLRLVLLSgdwiPLDLPARLRALAPD---ARLISLGGATEASiwsiyhPIDE--VPPDWRSI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 532 TVGRILPGMEARLIN-----VP-GIAqgGRLQLRGPNIMRGYLRveNPGVLEQPSAENAQGELdanWYDTGDIVTLDEQG 605
Cdd:cd12114 301 PYGRPLANQRYRVLDprgrdCPdWVP--GELWIGGRGVALGYLG--DPELTAARFVTHPDGER---LYRTGDLGRYRPDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 606 FCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAAAKTDSAKGEALVLF--------TTDSEITRERLIKVaren 677
Cdd:cd12114 374 TLEFLGRRDGQVKVRGYRIELGEIEAALQAH-PGVARAVVVVLGDPGGKRLAAFvvpdndgtPIAPDALRAFLAQT---- 448
|
490 500
....*....|....*....|....*.
gi 488138635 678 gVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd12114 449 -LPAYMIPSRVIALEALPLTANGKVD 473
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
204-695 |
1.47e-15 |
|
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: 79.86 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 204 ETLFEALLSAQTRyGRFKPCIEDVSFKED-SYQTLLKKTLGV-SRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRI 281
Cdd:cd05923 1 QTVFEMLRRAASR-APDACAIADPARGLRlTYSELRARIEAVaARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 282 PALLNYTSGAKGLQSAIIAASLKTIVtsrqflekgkLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLP 361
Cdd:cd05923 80 PALINPRLKAAELAELIERGEMTAAV----------IAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 362 QQAdgsALILFTSGSEGNPKGVVHSHASLLANVEQIRTIAD--FTPRDRFMSSLPLFHAFGLtVGLFTPLMTGSRVFLYP 439
Cdd:cd05923 150 EQP---AFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGF-FAVLVAALALDGTYVVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHYRVVPELVYDRNCTVLFGTSTF---LGNYARFAhPYDFARVRYVV-AGAEKLAESTKQIWQDKFGiRILEGYGVTE 515
Cdd:cd05923 226 EEFDPADALKLIEQERVTSLFATPTHldaLAAAAEFA-GLKLSSLRHVTfAGATMPDAVLERVNQHLPG-EKVNIYGTTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 capvvAINVPMAAKVNTVGRILPGM--EARLINVpgiaqGGRLQLRGPNIMRGYLRVENP------GVLEQPSAENAQge 587
Cdd:cd05923 304 -----AMNSLYMRDARTGTEMRPGFfsEVRIVRI-----GGSPDEALANGEEGELIVAAAadaaftGYLNQPEATAKK-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 588 LDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLaISLSPEGQHAAA-AKTDSAKGEALVLFTTDSE-- 664
Cdd:cd05923 372 LQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERV-LSRHPGVTEVVViGVADERWGQSVTACVVPREgt 450
|
490 500 510
....*....|....*....|....*....|.
gi 488138635 665 ITRERLIKVARENGVPELAVPRDIRVVKALP 695
Cdd:cd05923 451 LSADELDQFCRASELADFKRPRRYFFLDELP 481
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
368-703 |
1.52e-15 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 79.75 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASllanVEQIRT--IADFTPRDRFMSSLPLFHAFgltvgLFTP--------LMTGSRVFL 437
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGS----VVNLRTslSERYFGRDNGDEAVLFFSNY-----VFDFfveqmtlaLLNGQKLVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 438 YPSPLhyRVVPELVYD----RNCTVLFGTSTFLgnyarfaHPYDFAR---VRYVVAGAEKLAESTKQIWQDKFGIRILEG 510
Cdd:cd17648 168 PPDEM--RFDPDRFYAyinrEKVTYLSGTPSVL-------QQYDLARlphLKRVDAAGEEFTAPVFEKLRSRFAGLIINA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 511 YGVTECApVVAINVPM---AAKVNTVGRILPGMEARLIN-----VPgIAQGGRLQLRGPNIMRGYLR---------VENP 573
Cdd:cd17648 239 YGPTETT-VTNHKRFFpgdQRFDKSLGRPVRNTKCYVLNdamkrVP-VGAVGELYLGGDGVARGYLNrpeltaerfLPNP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 574 GVLEQPSAENAQGELdanwYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKG 653
Cdd:cd17648 317 FQTEQERARGRNARL----YKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQA 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488138635 654 EA-----LV-LFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17648 393 QSriqkyLVgYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLD 448
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
361-703 |
2.43e-15 |
|
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: 79.29 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTVG-LFTPLMTGSRVFLYP 439
Cdd:cd17655 133 VSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASI--SFDASVTeIFASLLSGNTLYIVR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHYRVVPELVY--DRNCTVLFGTSTFLgNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFG--IRILEGYGVTE 515
Cdd:cd17655 211 KETVLDGQALTQYirQNRITIIDLTPAHL-KLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGtnPTITNAYGPTE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 C---------------APVVAINVPMAAK----VNTVGRILPgmearlINVPgiaqgGRLQLRGPNIMRGYLR------- 569
Cdd:cd17655 290 TtvdasiyqyepetdqQVSVPIGKPLGNTriyiLDQYGRPQP------VGVA-----GELYIGGEGVARGYLNrpeltae 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 570 --VENPGVleqpsaenaQGEldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAK 647
Cdd:cd17655 359 kfVDDPFV---------PGE---RMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIAR 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138635 648 TDSAKGEAL-VLFTTDSEIT----RERLikvAREngVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17655 427 KDEQGQNYLcAYIVSEKELPvaqlREFL---ARE--LPDYMIPSYFIKLDEIPLTPNGKVD 482
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
361-703 |
3.76e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 78.88 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHA----SLLANVEqirtIADFTPRDRFMSSLPLFHAFGLT----VGLFtplMTG 432
Cdd:PRK10946 178 PSPADEVAFFQLSGGSTGTPKLIPRTHNdyyySVRRSVE----ICGFTPQTRYLCALPAAHNYPMSspgaLGVF---LAG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 433 SRVFLY--PSPL-------HYRV-----VPELVydrnctvlfgtSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQI 498
Cdd:PRK10946 251 GTVVLApdPSATlcfplieKHQVnvtalVPPAV-----------SLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARR 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 499 WQDKFGIRILEGYGVTE-CAPVVAINVPMAAKVNTVGR-ILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLRveN 572
Cdd:PRK10946 320 IPAELGCQLQQVFGMAEgLVNYTRLDDSDERIFTTQGRpMSPDDEVWVADADGnpLPQGevGRLMTRGPYTFRGYYK--S 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 573 PgvleqpsAENAQGeLDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLaISLSPEGQHAA-AAKTDS 650
Cdd:PRK10946 398 P-------QHNASA-FDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENL-LLRHPAVIHAAlVSMEDE 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 488138635 651 AKGEALVLFTtdseITRERLIKVA-----RENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK10946 469 LMGEKSCAFL----VVKEPLKAVQlrrflREQGIAEFKLPDRVECVDSLPLTAVGKVD 522
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
362-718 |
6.42e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 78.29 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 362 QQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADF--TPRDRFMSSLPLFH--AFGLTVGLF---TPL-MTGS 433
Cdd:PRK05620 178 LDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLavTHGESFLCCVPIYHvlSWGVPLAAFmsgTPLvFPGP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVflypSPLHYRVVPELVYDRnctVLFGTST----FLGNYARfaHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILE 509
Cdd:PRK05620 258 DL----SAPTLAKIIATAMPR---VAHGVPTlwiqLMVHYLK--NPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVH 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 510 GYGVTECAPVVAINVPMA-----AKVN---TVGRILPGMEARLINVPGIAQG-----GRLQLRGPNIMRGYLRVENP--- 573
Cdd:PRK05620 329 VWGMTETSPVGTVARPPSgvsgeARWAyrvSQGRFPASLEYRIVNDGQVMEStdrneGEIQVRGNWVTASYYHSPTEegg 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 574 ---GVLEQPSAENAQGELDAN-WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTD 649
Cdd:PRK05620 409 gaaSTFRGEDVEDANDRFTADgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPD 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488138635 650 SAKGE---ALVLFTTDSEITRE---RLIKVARENgVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV 718
Cdd:PRK05620 489 DKWGErplAVTVLAPGIEPTREtaeRLRDQLRDR-LPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLADGDFEI 562
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
363-657 |
1.14e-14 |
|
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: 77.47 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIR-TIADFTPRDRFM-SSLPLFHAFGLTVGLFTPLMTGSRVFL--- 437
Cdd:cd05921 163 GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEqTYPFFGEEPPVLvDWLPWNHTFGGNHNFNLVLYNGGTLYIddg 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 438 YPSPLHYRVVPELVYDRNCTVLF----GTSTFLGNY-------ARFahpydFARVRYVVAGAEKLAESTKQIWQD----- 501
Cdd:cd05921 243 KPMPGGFEETLRNLREISPTVYFnvpaGWEMLVAALekdealrRRF-----FKRLKLMFYAGAGLSQDVWDRLQAlavat 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 502 -KFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLinVPgiaQGGRLQLR--GPNIMRGYLRvenpgvleQ 578
Cdd:cd05921 318 vGERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL--VP---SGGKYEVRvkGPNVTPGYWR--------Q 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 579 PSAeNAQGELDANWYDTGDIVTL----DEQGFCAIRGRVKRFAKLA-GEMVSLESVEQLAIS-LSPEGQHAAAAKTDSAK 652
Cdd:cd05921 385 PEL-TAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLAsGTWVSVGPLRARAVAaCAPLVHDAVVAGEDRAE 463
|
....*
gi 488138635 653 GEALV 657
Cdd:cd05921 464 VGALV 468
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
317-638 |
1.61e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 77.46 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 317 KLTHLPEQVNEV-NWVYLEDLKDTVTLTDKL---WILFHLC--------FPRRAMLPQQADgSALILFTSGSEGNPKGVV 384
Cdd:PLN02387 191 KLIDISSQLETVkRVIYMDDEGVDSDSSLSGssnWTVSSFSeveklgkeNPVDPDLPSPND-IAVIMYTSGSTGLPKGVM 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 385 HSHASLLANVEQIRTI-ADFTPRDRFMSSLPLFHAF-----------GLTVGLFTPLM---TGSRV---------FLYPS 440
Cdd:PLN02387 270 MTHGNIVATVAGVMTVvPKLGKNDVYLAYLPLAHILelaaesvmaavGAAIGYGSPLTltdTSNKIkkgtkgdasALKPT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 441 PLhyRVVP-------------------------ELVYDRNCTVLFGtsTFLGNYARFAHPYDF-----------ARVRYV 484
Cdd:PLN02387 350 LM--TAVPaildrvrdgvrkkvdakgglakklfDIAYKRRLAAIEG--SWFGAWGLEKLLWDAlvfkkiravlgGRIRFM 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 485 VAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPgiaQGGRLQ------- 557
Cdd:PLN02387 426 LSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWE---EGGYLIsdkpmpr 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 558 ----LRGPNIMRGYLRVEnpgvlEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKL-AGEMVSLESVEQl 632
Cdd:PLN02387 503 geivIGGPSVTLGYFKNQ-----EKTDEVYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLqHGEYVSLGKVEA- 576
|
....*.
gi 488138635 633 AISLSP 638
Cdd:PLN02387 577 ALSVSP 582
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
363-703 |
1.73e-14 |
|
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: 76.14 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSslplFHAFGLTVG---LFTPLMTGSRVFLYP 439
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQ----FASPSFDASvweLLMALLAGATLVLAP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SplhYRVVP-----ELVYDRNCTVLFGTSTFLGNYARFAHPydfARVRYVVAGAEKLAESTKQiWQDkfGIRILEGYGVT 514
Cdd:cd17652 167 A---EELLPgeplaDLLREHRITHVTLPPAALAALPPDDLP---DLRTLVVAGEACPAELVDR-WAP--GRRMINAYGPT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 515 ECAPVVAINVPM-AAKVNTVGRILPG-----MEARLINVP-GIAqgGRLQLRGPNIMRGYLRveNPGVLEQPSAENAQGE 587
Cdd:cd17652 238 ETTVCATMAGPLpGGGVPPIGRPVPGtrvyvLDARLRPVPpGVP--GELYIAGAGLARGYLN--RPGLTAERFVADPFGA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 588 LDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTT---DSE 664
Cdd:cd17652 314 PGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVpapGAA 393
|
330 340 350
....*....|....*....|....*....|....*....
gi 488138635 665 ITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17652 394 PTAAELRAHLAER-LPGYMVPAAFVVLDALPLTPNGKLD 431
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
363-703 |
2.56e-14 |
|
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: 75.97 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANV---EQIRTIADFTPRDRFMSSLplfhAFGLTVGLFT-PLMTGSRvfLY 438
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAhawRREYELDSFPVRLLQMASF----SFDVFAGDFArSLLNGGT--LV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 439 PSPLHYRVVPELVYD----RNCTVLFGTSTFLGNYARFA--HPYDFARVRYVVAGAEKLAESTKQIWQDKFG--IRILEG 510
Cdd:cd17650 165 ICPDEVKLDPAALYDlilkSRITLMESTPALIRPVMAYVyrNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGqgMRIINS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 511 YGVTEC-----------APVVAI-NVPmaakvntVGRILPGM-----EARLINVP-GIAqgGRLQLRGPNIMRGYLrvEN 572
Cdd:cd17650 245 YGVTEAtidstyyeegrDPLGDSaNVP-------IGRPLPNTamyvlDERLQPQPvGVA--GELYIGGAGVARGYL--NR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 573 PGVLEQPSAEN--AQGEldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDS 650
Cdd:cd17650 314 PELTAERFVENpfAPGE---RMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIES-QLARHPAIDEAVVAVRED 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488138635 651 AKGEA-LVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17650 390 KGGEArLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
368-633 |
3.48e-14 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 76.07 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 368 ALILFTSGSEGNPKGVVHSHASLLANVEQIR-TIADFTPRD-RFMSSLPLFHAFGltvglftplmtGSRVF---LYPSPL 442
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAqTFPFLAEEPpVLVDWLPWNHTFG-----------GNHNLgivLYNGGT 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 443 HY----RVVPELVYD--RNC-----TVLFGTSTF---LGNY--------ARFahpydFARVRYVVAGAEKLAEStkqIWQ 500
Cdd:PRK08180 281 LYiddgKPTPGGFDEtlRNLreispTVYFNVPKGwemLVPAlerdaalrRRF-----FSRLKLLFYAGAALSQD---VWD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 501 --DKFG-------IRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLinVPgiaQGGRLQLR--GPNIMRGYLR 569
Cdd:PRK08180 353 rlDRVAeatcgerIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKL--VP---VGGKLEVRvkGPNVTPGYWR 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488138635 570 veNPgvleqpsAENAQGELDANWYDTGDIVTL-D----EQGFcAIRGRVKRFAKLA-GEMVS-----LESVEQLA 633
Cdd:PRK08180 428 --AP-------ELTAEAFDEEGYYRSGDAVRFvDpadpERGL-MFDGRIAEDFKLSsGTWVSvgplrARAVSAGA 492
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
358-703 |
4.19e-14 |
|
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: 75.28 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 358 AMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFM--SSLPlFHAFGLTvgLFTPLMTGSRV 435
Cdd:cd17645 97 KILLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLvyASFS-FDASAWE--IFPHLTAGAAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 436 FLYPSPLHYRVVPelvYDRNCTVLFGTSTFL--GNYARFAHpYDFARVRYVVAGAEKLAESTKQIWQdkfgirILEGYGV 513
Cdd:cd17645 174 HVVPSERRLDLDA---LNDYFNQEGITISFLptGAAEQFMQ-LDNQSLRVLLTGGDKLKKIERKGYK------LVNNYGP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 514 TECAPVVAI--------NVPMAAKVNTVgRILPGMEARLINVPGIAqgGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQ 585
Cdd:cd17645 244 TENTVVATSfeidkpyaNIPIGKPIDNT-RVYILDEALQLQPIGVA--GELCIAGEGLARGYLNRPELTAEKFIVHPFVP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 586 GEldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEI 665
Cdd:cd17645 321 GE---RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEE 397
|
330 340 350
....*....|....*....|....*....|....*...
gi 488138635 666 TRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17645 398 IPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
372-715 |
5.08e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 75.20 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSHASLLANVEQirTIADF--TPRDRFMSSLPLFHAFGLtVGLFTPLMTGSRVFLYPsplhyRVVPE 449
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHSFDC--NVHDFhmKREDSVLIAGTLVHSLFL-YGAISTLYVGQTVHLMR-----KFIPN 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 450 LVYDR----NCTVLFGTSTFLGNYARFAHPYDfARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAInVP 525
Cdd:PRK07638 222 QVLDKleteNISVMYTVPTMLESLYKENRVIE-NKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTAL-VD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 526 --MAAKVNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLrveNPGVLeqPSAENAQGeldanWYDTGDIV 599
Cdd:PRK07638 300 eeSERRPNSVGRPFHNVQVRICNEAGeeVQKGeiGTVYVKSPQFFMGYI---IGGVL--ARELNADG-----WMTVRDVG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 600 TLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLsPEGQHAAA-AKTDSAKGEALVLFTTDSEITRErlIKVARENG 678
Cdd:PRK07638 370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEH-PAVDEIVViGVPDSYWGEKPVAIIKGSATKQQ--LKSFCLQR 446
|
330 340 350
....*....|....*....|....*....|....*..
gi 488138635 679 VPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPE 715
Cdd:PRK07638 447 LSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
257-701 |
7.22e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 74.68 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 257 HVGMLLPN-----ATITAAAIFGASLRGripalLNYTSGAKGLQSAIIAASLKTIVTSRQflekgkltHLPeqvnevnwv 331
Cdd:PRK13388 54 HVGVLLGNtpemlFWLAAAALGGYVLVG-----LNTTRRGAALAADIRRADCQLLVTDAE--------HRP--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 332 YLEDLK---DTVTLTDK-LWIlfHLCFPRRAMLPQQADGSA---LILFTSGSEGNPKGVVHSHASLL----ANVEQIrti 400
Cdd:PRK13388 112 LLDGLDlpgVRVLDVDTpAYA--ELVAAAGALTPHREVDAMdpfMLIFTSGTTGAPKAVRCSHGRLAfagrALTERF--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 401 aDFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSplhyrvvpelvydrnctvlFGTSTFLGNYARFAHPYdFAR 480
Cdd:PRK13388 187 -GLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAK-------------------FSASGFLDDVRRYGATY-FNY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 481 V----RYVVAGAEK---------------LAESTKQIWQDKFGIRILEGYGVTECApvVAINVPMAAKVNTVGRILPGME 541
Cdd:PRK13388 246 VgkplAYILATPERpddadnplrvafgneASPRDIAEFSRRFGCQVEDGYGSSEGA--VIVVREPGTPPGSIGRGAPGVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 542 ------------------ARLINvPGIAQGGRLQLRGPNIMRGYLRveNPGvleqpsaenAQGELDAN-WYDTGDIVTLD 602
Cdd:PRK13388 324 iynpetltecavarfdahGALLN-ADEAIGELVNTAGAGFFEGYYN--NPE---------ATAERMRHgMYWSGDLAYRD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 603 EQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE----ALVLFTTDSEITRERLIKVARENG 678
Cdd:PRK13388 392 ADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDqvmaALVLRDGATFDPDAFAAFLAAQPD 471
|
490 500
....*....|....*....|...
gi 488138635 679 VPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK13388 472 LGTKAWPRYVRIAADLPSTATNK 494
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
254-701 |
8.73e-14 |
|
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: 74.42 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 254 PGEHVGMLLPN---------ATITAAAIFgaslrgrIPALLNYTsgAKGLQSAIIAASLKTIVTSRqflekgklthlpEQ 324
Cdd:cd05928 66 RGDRVAVILPRvpewwlvnvACIRTGLVF-------IPGTIQLT--AKDILYRLQASKAKCIVTSD------------EL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 325 VNEVNWVYLE--DLKDTVTLTDKL---WILF----------HLCFPRRAMLPQQadgsalILFTSGSEGNPKGVVHSHAS 389
Cdd:cd05928 125 APEVDSVASEcpSLKTKLLVSEKSrdgWLNFkellneasteHHCVETGSQEPMA------IYFTSGTTGSPKMAEHSHSS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 390 L-LANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPlhyRVVPELVYDR----NCTVLFGTST 464
Cdd:cd05928 199 LgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLP---RFDPLVILKTlssyPITTFCGAPT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 465 -----FLGNYARfahpYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPG 539
Cdd:cd05928 276 vyrmlVQQDLSS----YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 540 MEARLINVPG--IAQG--GRLQLR-GPN----IMRGYlrVENPgvleQPSAENAQGeldaNWYDTGDIVTLDEQGFCAIR 610
Cdd:cd05928 352 YDVQIIDDNGnvLPPGteGDIGIRvKPIrpfgLFSGY--VDNP----EKTAATIRG----DFYLTGDRGIMDEDGYFWFM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 611 GRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE---ALVLFTTD-SEITRERLIKVARE---NGVPELA 683
Cdd:cd05928 422 GRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEvvkAFVVLAPQfLSHDPEQLTKELQQhvkSVTAPYK 501
|
490
....*....|....*...
gi 488138635 684 VPRDIRVVKALPLLGSGK 701
Cdd:cd05928 502 YPRKVEFVQELPKTVTGK 519
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
361-630 |
1.03e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 74.49 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPR-----DRFMSSLPLFHAFGLTVGLFTpLMTGSRV 435
Cdd:PLN02861 216 PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRvateeDSYFSYLPLAHVYDQVIETYC-ISKGASI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 436 FLYPSPLHYRV-------------VPElVYDRNCTVLFGTSTFLGNYAR----FAHPYDF-------------------- 478
Cdd:PLN02861 295 GFWQGDIRYLMedvqalkptifcgVPR-VYDRIYTGIMQKISSGGMLRKklfdFAYNYKLgnlrkglkqeeasprldrlv 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 479 ---------ARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTE----CAPVVAINVPMaakVNTVGRILPGMEARLI 545
Cdd:PLN02861 374 fdkikeglgGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEscggCFTSIANVFSM---VGTVGVPMTTIEARLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 546 NVPGIAQG-------GRLQLRGPNIMRGYLRveNPGVLEQPsaenaqgeLDANWYDTGDIVTLDEQGFCAIRGRVKRFAK 618
Cdd:PLN02861 451 SVPEMGYDalsdvprGEICLRGNTLFSGYHK--RQDLTEEV--------LIDGWFHTGDIGEWQPNGAMKIIDRKKNIFK 520
|
330
....*....|...
gi 488138635 619 LA-GEMVSLESVE 630
Cdd:PLN02861 521 LSqGEYVAVENLE 533
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
359-703 |
1.04e-13 |
|
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: 74.01 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 359 MLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMsslpLFHAFGLTVG---LFTPLMTGSRV 435
Cdd:cd17644 100 VLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVL----QFASIAFDVAaeeIYVTLLSGATL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 436 FLYP----SPLHYRVvpELVYDRNCTVLFGTSTFLGNYARFAHPYDFA---RVRYVVAGAEKLAESTKQIWQDKFG--IR 506
Cdd:cd17644 176 VLRPeemrSSLEDFV--QYIQQWQLTVLSLPPAYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 507 ILEGYGVTEC---APVVAINVPMAAKVN--TVGRILPG-----MEARLINVPgIAQGGRLQLRGPNIMRGYL-RVE--NP 573
Cdd:cd17644 254 LINVYGPTEAtiaATVCRLTQLTERNITsvPIGRPIANtqvyiLDENLQPVP-VGVPGELHIGGVGLARGYLnRPEltAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 574 GVLEQPSAENAQGELdanwYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKG 653
Cdd:cd17644 333 KFISHPFNSSESERL----YKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGN 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 488138635 654 EALVLFTTdSEITRERLIKVARE---NGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17644 409 KRLVAYIV-PHYEESPSTVELRQflkAKLPDYMIPSAFVVLEELPLTPNGKID 460
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
363-597 |
1.49e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 73.37 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVgLFTPLMTGSRVFLYPS-P 441
Cdd:PRK09029 133 QPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGI-VWRWLYAGATLVVRDKqP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 L--------HYRVVPE-----LVYDRNCTVLfgTSTFLGnyarfahpydfarvryvvaGAEKLAESTKQIWQdkFGIRIL 508
Cdd:PRK09029 212 LeqalagctHASLVPTqlwrlLDNRSEPLSL--KAVLLG-------------------GAAIPVELTEQAEQ--QGIRCW 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 509 EGYGVTECAPVVainvpmAAK----VNTVGRILPGMEARLINvpgiaqgGRLQLRGPNIMRGYLRvenpgvleqpsaena 584
Cdd:PRK09029 269 CGYGLTEMASTV------CAKradgLAGVGSPLPGREVKLVD-------GEIWLRGASLALGYWR--------------- 320
|
250
....*....|....*...
gi 488138635 585 QGEL-----DANWYDTGD 597
Cdd:PRK09029 321 QGQLvplvnDEGWFATRD 338
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
363-703 |
2.23e-13 |
|
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: 72.74 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRtiADFTPRDR--FMSSLPLfhAFGLTV-GLFTPLMTGSRVFLYP 439
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAA--AAFSAEELagVLASTSI--CFDLSVfELFGPLATGGKVVLAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHyrvVPELVYDRNCTVLFGTSTFLGNYARF-AHPydfARVRYVVAGAEKL-AESTKQIWQDKFGIRILEGYGVTECA 517
Cdd:cd12115 179 NVLA---LPDLPAAAEVTLINTVPSAAAELLRHdALP---ASVRVVNLAGEPLpRDLVQRLYARLQVERVVNLYGPSEDT 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 518 --PVVAINVPMAAKVNTVGRILPGMEARLIN-----VP-GIAqgGRLQLRGPNIMRGYLRveNPGVleqpSAE----NAQ 585
Cdd:cd12115 253 tySTVAPVPPGASGEVSIGRPLANTQAYVLDralqpVPlGVP--GELYIGGAGVARGYLG--RPGL----TAErflpDPF 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 586 GElDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEqlAISLSPEGQHAAA--AKTDSAKGEALVLFTT-- 661
Cdd:cd12115 325 GP-GARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIE--AALRSIPGVREAVvvAIGDAAGERRLVAYIVae 401
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488138635 662 -DSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd12115 402 pGAAGLVEDLRRHLGTR-LPAYMVPSRFVRLDALPLTPNGKID 443
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
171-701 |
5.18e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 72.27 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 171 PMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRF-------------KPCIEDvSFKEDSYQTL 237
Cdd:PRK07788 2 KLMKSVSGYLTRGSAEAHYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFaglvahaarrapdRAALID-ERGTLTYAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 238 LKKTLGVSRILQRFTV-PGEHVGMLLPNA-----TITAAAIFGASLrgripALLNYTSGAKGLQSAIIAASLKTIVTSRQ 311
Cdd:PRK07788 81 DEQSNALARGLLALGVrAGDGVAVLARNHrgfvlALYAAGKVGARI-----ILLNTGFSGPQLAEVAAREGVKALVYDDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 FL--------EKGKLTHLPEQVNEV-----NWVYLEDLKDTVTltdklwilfhlcfprRAMLPQQADGSALILFTSGSEG 378
Cdd:PRK07788 156 FTdllsalppDLGRLRAWGGNPDDDepsgsTDETLDDLIAGSS---------------TAPLPKPPKPGGIVILTSGTTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 379 NPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFG---LTVGlftpLMTGSRVFlypspLHYRVVPE----LV 451
Cdd:PRK07788 221 TPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGwahLTLA----MALGSTVV-----LRRRFDPEatleDI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 452 YDRNCTVLFGTSTFLGNYarFAHP------YDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECApVVAINVP 525
Cdd:PRK07788 292 AKHKATALVVVPVMLSRI--LDLGpevlakYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVA-FATIATP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 526 --MAAKVNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLRVENPgvleqpsaENAQGELdanwyDTGDIV 599
Cdd:PRK07788 369 edLAEAPGTVGRPPKGVTVKILDENGneVPRGvvGRIFVGNGFPFEGYTDGRDK--------QIIDGLL-----SSGDVG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 600 TLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLaISLSPEGQHAAAAKTDS----AKGEALVLFTTDSEITRERLIKVAR 675
Cdd:PRK07788 436 YFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDL-LAGHPDVVEAAVIGVDDeefgQRLRAFVVKAPGAALDEDAIKDYVR 514
|
570 580
....*....|....*....|....*....
gi 488138635 676 ENgvpeLA---VPRDIRVVKALPLLGSGK 701
Cdd:PRK07788 515 DN----LArykVPRDVVFLDELPRNPTGK 539
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
255-714 |
1.26e-12 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 70.53 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 255 GEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTS-RQFLEKGKLTHLPEQvnevnwvyl 333
Cdd:cd05939 28 GDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNlLDPLLTQSSTEPPSQ--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 334 edlkDTVTLTDKLwilfhlCFprramlpqqadgsaliLFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSL 413
Cdd:cd05939 99 ----DDVNFRDKL------FY----------------IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 414 PLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVyDRNCTVlfgtSTFLGNYARF--AHPYDFA----RVRYVVAG 487
Cdd:cd05939 153 PLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCV-KYNCTI----VQYIGEICRYllAQPPSEEeqkhNVRLAVGN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 488 AEKlaestKQIWQ---DKFGI-RILEGYGVTECapvvaiNVPMAAKVNTVG------RILPGM-EARLINV--------- 547
Cdd:cd05939 228 GLR-----PQIWEqfvRRFGIpQIGEFYGATEG------NSSLVNIDNHVGacgfnsRILPSVyPIRLIKVdedtgelir 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 548 ----------PGiaQGGRL--QLRGPNIMRGYLRVENPGVLEQPSAENAQGELDAnWYDTGDIVTLDEQGFCAIRGRVKR 615
Cdd:cd05939 297 dsdglcipcqPG--EPGLLvgKIIQNDPLRRFDGYVNEGATNKKIARDVFKKGDS-AFLSGDVLVMDELGYLYFKDRTGD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 616 FAKLAGEMVSLESVEQLaisLSP-----------------EGQHAAAAKTDSAKgealvlfTTDSEITRERLIKVareng 678
Cdd:cd05939 374 TFRWKGENVSTTEVEGI---LSNvlgledvvvygvevpgvEGRAGMAAIVDPER-------KVDLDRFSAVLAKS----- 438
|
490 500 510
....*....|....*....|....*....|....*.
gi 488138635 679 VPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDP 714
Cdd:cd05939 439 LPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
361-701 |
1.62e-12 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 70.48 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLL----ANVEQIRTIADftprDRFMSSLPLFHA-FGLTVGLFTpLMTGSRV 435
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITHYNLRfagyYSAWQCALRDD----DVYLTVMPAFHIdCQCTAAMAA-FSAGATF 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 436 FL---YPS------------------PLHYR---VVPELVYDRN-C--TVLFgtstFLgnyarfahpydfarvryvvaga 488
Cdd:PRK08008 244 VLlekYSArafwgqvckyratiteciPMMIRtlmVQPPSANDRQhClrEVMF----YL---------------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 489 eKLAESTKQIWQDKFGIRILEGYGVTECApVVAINVPMAAKVN--TVGRilPGM--EARLINVPG--IAQG--GRLQLR- 559
Cdd:PRK08008 298 -NLSDQEKDAFEERFGVRLLTSYGMTETI-VGIIGDRPGDKRRwpSIGR--PGFcyEAEIRDDHNrpLPAGeiGEICIKg 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 560 --GPNIMRGYlrvenpgvLEQPSAENAQGELDAnWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLaISLS 637
Cdd:PRK08008 374 vpGKTIFKEY--------YLDPKATAKVLEADG-WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI-IATH 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138635 638 PEGQHAAAAKT-DSAKGEAL---VLFTTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK08008 444 PKIQDIVVVGIkDSIRDEAIkafVVLNEGETLSEEEFFAFCEQN-MAKFKVPSYLEIRKDLPRNCSGK 510
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
257-695 |
1.64e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 70.48 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 257 HVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKgkLTHLPEQVNEVNwvyledl 336
Cdd:PRK07867 56 HVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAEL--LDGLDPGVRVIN------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 337 KDTVTLTDKLWILFHLCFPRRAMlpqQADGSALILFTSGSEGNPKGVVHSHASLLAnveQIRTIAD---FTPRDRFMSSL 413
Cdd:PRK07867 127 VDSPAWADELAAHRDAEPPFRVA---DPDDLFMLIFTSGTSGDPKAVRCTHRKVAS---AGVMLAQrfgLGPDDVCYVSM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 414 PLFHAFGLTVGLFTPLMTGSRVFLYP-----------------------SPLHYRV-VPELVYDRNCT--VLFGTSTFLG 467
Cdd:PRK07867 201 PLFHSNAVMAGWAVALAAGASIALRRkfsasgflpdvrrygatyanyvgKPLSYVLaTPERPDDADNPlrIVYGNEGAPG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 468 NYARFAhpydfarvryvvagaeklaestkqiwqDKFGIRILEGYGVTECApvVAINVPMAAKVNTVGRILPGMEarLINV 547
Cdd:PRK07867 281 DIARFA---------------------------RRFGCVVVDGFGSTEGG--VAITRTPDTPPGALGPLPPGVA--IVDP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 548 -------PG-IAQGGRLQ----------LRGPNIMRGYLRveNPgvleQPSAENAQGeldaNWYDTGDIVTLDEQGFCAI 609
Cdd:PRK07867 330 dtgtecpPAeDADGRLLNadeaigelvnTAGPGGFEGYYN--DP----EADAERMRG----GVYWSGDLAYRDADGYAYF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 610 RGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGE----ALVL---FTTDSEITRERLikVARENGVPEl 682
Cdd:PRK07867 400 AGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDqvmaALVLapgAKFDPDAFAEFL--AAQPDLGPK- 476
|
490
....*....|...
gi 488138635 683 AVPRDIRVVKALP 695
Cdd:PRK07867 477 QWPSYVRVCAELP 489
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
372-701 |
4.84e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 69.28 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSH--ASLLANVEQIRTIADFTPRdrFMSSLPLFHAFGLTVGLFTPLMTGSRVFLypsplHYRVVPE 449
Cdd:PLN03102 193 YTSGTTADPKGVVISHrgAYLSTLSAIIGWEMGTCPV--YLWTLPMFHCNGWTFTWGTAARGGTSVCM-----RHVTAPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 450 LVYD---RNCTVLFGTST---FLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIwqDKFGIRILEGYGVTEC-APVVAI 522
Cdd:PLN03102 266 IYKNiemHNVTHMCCVPTvfnILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV--QRLGFQVMHAYGLTEAtGPVLFC 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 523 -----------NVPMAAKVNTVGRILPGMEARLIN------VPGIAQG-GRLQLRGPNIMRGYLRveNPGVLEQPsaena 584
Cdd:PLN03102 344 ewqdewnrlpeNQQMELKARQGVSILGLADVDVKNketqesVPRDGKTmGEIVIKGSSIMKGYLK--NPKATSEA----- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 qgeLDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQL----------AISLSPegqHAAAAKTDSA--- 651
Cdd:PLN03102 417 ---FKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVlykypkvletAVVAMP---HPTWGETPCAfvv 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 488138635 652 --KGEALVLFTTDSEITRER-LIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PLN03102 491 leKGETTKEDRVDKLVTRERdLIEYCREN-LPHFMCPRKVVFLQELPKNGNGK 542
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
279-701 |
1.02e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 67.86 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 279 GRIPA---LLNYTSGAKGLQSAIIAASLKTIVTSRQFLE--KGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKlwilfhlc 353
Cdd:PRK13382 114 NRIGAdilLLNTSFAGPALAEVVTREGVDTVIYDEEFSAtvDRALADCPQATRIVAWTDEDHDLTVEVLIAA-------- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 354 fPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHAsllANVEQIRTIADFTP---RDRFMSSLPLFHAFGLTVGLFTPLM 430
Cdd:PRK13382 186 -HAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGP---GGIGTLKAILDRTPwraEEPTVIVAPMFHAWGFSQLVLAASL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 431 TGSRVflypspLHYRVVPE----LVyDRN-----CTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQD 501
Cdd:PRK13382 262 ACTIV------TRRRFDPEatldLI-DRHratglAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 502 KFGIRILEGYGVTEcAPVVAINVP--MAAKVNTVGRILPGMEARLIN-----VPGiAQGGRLQLRGPNIMRGYlrveNPG 574
Cdd:PRK13382 335 QFGDVIYNNYNATE-AGMIATATPadLRAAPDTAGRPAEGTEIRILDqdfreVPT-GEVGTIFVRNDTQFDGY----TSG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 575 vleqpsaenAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAK-G 653
Cdd:PRK13382 409 ---------STKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEK-TLATHPDVAEAAVIGVDDEQyG 478
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 488138635 654 EAL---VLFTTDSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK13382 479 QRLaafVVLKPGASATPETLKQHVRDN-LANYKVPRDIVVLDELPRGATGK 528
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
200-712 |
1.56e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 67.46 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 200 TVPRETLFEALLSAQTRYgrfKPciEDVSFKED----SYQTLLKKTLGVSRILQRFTV-PGEHVGMLLPN-----ATITA 269
Cdd:PRK06164 5 AAPRADTLASLLDAHARA---RP--DAVALIDEdrplSRAELRALVDRLAAWLAAQGVrRGDRVAVWLPNciewvVLFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 270 AAIFGASL-----------------RGRiPALLNYTSGAKGLQ-SAIIAASLKTIVTSRQ--FLEKGKLTHLPEQVNEVn 329
Cdd:PRK06164 80 CARLGATViavntryrshevahilgRGR-ARWLVVWPGFKGIDfAAILAAVPPDALPPLRaiAVVDDAADATPAPAPGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 330 WVYLEDLKDTVTLTdklwilfhlcfprrAMLPQQADGSAL-ILFT-SGSEGNPKGVVHSHASLLANVEQIRTIADFTPRD 407
Cdd:PRK06164 158 RVQLFALPDPAPPA--------------AAGERAADPDAGaLLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 408 RFMSSLPLFHAFGLTvGLFTPLMTGSRVFLYPSPLHYRVVpELVYDRNCTVLFGTSTFLGNYARFA-HPYDFARVRYV-- 484
Cdd:PRK06164 224 VLLAALPFCGVFGFS-TLLGALAGGAPLVCEPVFDAARTA-RALRRHRVTHTFGNDEMLRRILDTAgERADFPSARLFgf 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 485 ---VAGAEKLAESTKQiwqdkFGIRILEGYGVTECAPVVAI---NVPMAAKVNTVGRIL-PGMEARLINVPGIA-----Q 552
Cdd:PRK06164 302 asfAPALGELAALARA-----RGVPLTGLYGSSEVQALVALqpaTDPVSVRIEGGGRPAsPEARVRARDPQDGAllpdgE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 553 GGRLQLRGPNIMRGYLrvENPgvleqpsaENAQGELDAN-WYDTGDI-VTLDEQGFcAIRGRVKRFAKLAGEMVSLESVE 630
Cdd:PRK06164 377 SGEIEIRAPSLMRGYL--DNP--------DATARALTDDgYFRTGDLgYTRGDGQF-VYQTRMGDSLRLGGFLVNPAEIE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 631 QLAISLspEGQHAAAAKTDSAKGEALV---LFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSG---KPDF 704
Cdd:PRK06164 446 HALEAL--PGVAAAQVVGATRDGKTVPvafVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQK 523
|
....*...
gi 488138635 705 VTLGKMAQ 712
Cdd:PRK06164 524 HRLREMAQ 531
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
291-701 |
4.16e-11 |
|
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: 66.05 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 291 AKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEV--------NWVYLEDLKDTVTLTDKLWILFH----LCFPRRA 358
Cdd:cd05966 145 AESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDEAlekcpsveKVLVVKRTGGEVPMTEGRDLWWHdlmaKQSPECE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 359 MLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQ-IRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFL 437
Cdd:cd05966 225 PEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATtFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVM 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 438 Y---PSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARF--AHP--YDFARVR-----------------YVVAGAEKLAe 493
Cdd:cd05966 305 FegtPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFgdEWVkkHDLSSLRvlgsvgepinpeawmwyYEVIGKERCP- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 494 stkqI----WQDKFGirileGYGVTeCAPVVAinvPMaaKVNTVGRILPGMEARLIN-----VPGiAQGGRLQLRG--PN 562
Cdd:cd05966 384 ----IvdtwWQTETG-----GIMIT-PLPGAT---PL--KPGSATRPFFGIEPAILDeegneVEG-EVEGYLVIKRpwPG 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 563 IMRG-----------YLRVEnPGvleqpsaenaqgeldanWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQ 631
Cdd:cd05966 448 MARTiygdheryedtYFSKF-PG-----------------YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVES 509
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138635 632 lAISLSPEGQHAAA-AKTDSAKGEALVLFTT------DSEITRERLIK-VARENGvpELAVPRDIRVVKALPLLGSGK 701
Cdd:cd05966 510 -ALVAHPAVAEAAVvGRPHDIKGEAIYAFVTlkdgeePSDELRKELRKhVRKEIG--PIATPDKIQFVPGLPKTRSGK 584
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
361-442 |
4.67e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 66.12 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIrtIADF-------TPRDRFMSS-LPLFHAFGLTVGLFTPLMTG 432
Cdd:PRK05850 156 PRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQL--MSDYfgdtggvPPPDTTVVSwLPFYHDMGLVLGVCAPILGG 233
|
90
....*....|
gi 488138635 433 SRVFLYpSPL 442
Cdd:PRK05850 234 CPAVLT-SPV 242
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
369-700 |
4.71e-11 |
|
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: 64.63 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 369 LILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLypsplhYRVVP 448
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFV------RRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 449 E----LVYDRNCTVLFGTSTFLGNYARF--AHPYDFARVRYVVAGAEKLAESTkqIWQDKFGiRILEGYGVTECAPVVAI 522
Cdd:cd17636 78 EevleLIEAERCTHAFLLPPTIDQIVELnaDGLYDLSSLRSSPAAPEWNDMAT--VDTSPWG-RKPGGYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 523 NVPMAAKVNTVGRILPGMEARLINVPG--IAQG--GRLQLRGPNIMRGYLRVEnpgvleqpsAENAQGELDAnWYDTGDI 598
Cdd:cd17636 155 AALGGGAIGGAGRPSPLVQVRILDEDGreVPDGevGEIVARGPTVMAGYWNRP---------EVNARRTRGG-WHHTNDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 599 VTLDEQGFCAIRGRVKRFAKLAGEMV----------SLESVEQLAISLSPEGQHAAAAKtdsakgeALVLFTTDSEITRE 668
Cdd:cd17636 225 GRREPDGSLSFVGPKTRMIKSGAENIypaeverclrQHPAVADAAVIGVPDPRWAQSVK-------AIVVLKPGASVTEA 297
|
330 340 350
....*....|....*....|....*....|..
gi 488138635 669 RLIKVARENgVPELAVPRDIRVVKALPLLGSG 700
Cdd:cd17636 298 ELIEHCRAR-IASYKKPKSVEFADALPRTAGG 328
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
364-675 |
1.15e-10 |
|
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: 64.13 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMS-SLPLF--HAFGltvGLFTPLMTGSRVFLYPS 440
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNiSSPGWakHAWS---CFFAPWNAGATVFLFNY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 441 P-LHYRVVPELVYDRNCTVLFGTSTFL-----GNYARFAHPydfarVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVT 514
Cdd:cd05974 161 ArFDAKRVLAALVRYGVTTLCAPPTVWrmliqQDLASFDVK-----LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 515 ECAPVVAINVPMAAKVNTVGRILPGMEARLIN-VPGIAQGGRLQL-----RGPNIMRGYlrVENPGVLeqpsaenaQGEL 588
Cdd:cd05974 236 ETTALVGNSPGQPVKAGSMGRPLPGYRVALLDpDGAPATEGEVALdlgdtRPVGLMKGY--AGDPDKT--------AHAM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 589 DANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVS---LES-------VEQLAISLSPEGQHAAAAKT--------DS 650
Cdd:cd05974 306 RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISpfeLESvliehpaVAEAAVVPSPDPVRLSVPKAfivlragyEP 385
|
330 340
....*....|....*....|....*
gi 488138635 651 AKGEALVLFttdsEITRERLIKVAR 675
Cdd:cd05974 386 SPETALEIF----RFSRERLAPYKR 406
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
361-632 |
1.57e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 64.45 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIAD-----FTPRDRFMSSLPLFHAF-----------GLTVG 424
Cdd:PLN02430 216 PPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHILdrmieeyffrkGASVG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 425 LF----------------TPLMTGSRVF--LYP---------SPLHYRVVPELvYDRNCTVLFgtstfLGNYARFAHPY- 476
Cdd:PLN02430 296 YYhgdlnalrddlmelkpTLLAGVPRVFerIHEgiqkalqelNPRRRLIFNAL-YKYKLAWMN-----RGYSHKKASPMa 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 477 DF-----------ARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVP--MAAkVNTVGRILPGMEAR 543
Cdd:PLN02430 370 DFlafrkvkaklgGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPdeMCM-LGTVGAPAVYNELR 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 544 LINVP-------GIAQGGRLQLRGPNIMRGYLRveNPGVLEQPSAENaqgeldanWYDTGDIVTLDEQGFCAIRGRVKRF 616
Cdd:PLN02430 449 LEEVPemgydplGEPPRGEICVRGKCLFSGYYK--NPELTEEVMKDG--------WFHTGDIGEILPNGVLKIIDRKKNL 518
|
330
....*....|....*..
gi 488138635 617 AKLA-GEMVSLESVEQL 632
Cdd:PLN02430 519 IKLSqGEYVALEYLENV 535
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
355-703 |
1.61e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 64.68 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 355 PRRAMLPQQAdgsALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLfhAFGLTV-GLFTPLMTGS 433
Cdd:PRK10252 591 PLQLSQPHHT---AYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPC--SFDVSVwEFFWPFIAGA 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVFLYPSPLH------------YRV-----VPELVydrnctvlfgtSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTK 496
Cdd:PRK10252 666 KLVMAEPEAHrdplamqqffaeYGVttthfVPSML-----------AAFVASLTPEGARQSCASLRQVFCSGEALPADLC 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 497 QIWQDKFGIRILEGYGVTECA--------------PVVAINVPMAAKV-NTVGRILpgmEARLINVP-GIAqgGRLQLRG 560
Cdd:PRK10252 735 REWQQLTGAPLHNLYGPTEAAvdvswypafgeelaAVRGSSVPIGYPVwNTGLRIL---DARMRPVPpGVA--GDLYLTG 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 561 PNIMRGYLrvENPGV-----LEQPSAENAQ----GELdANWYDTGDIVTL---DEQgfCAIRGRVKRFAKLAGEMVSLES 628
Cdd:PRK10252 810 IQLAQGYL--GRPDLtasrfIADPFAPGERmyrtGDV-ARWLDDGAVEYLgrsDDQ--LKIRGQRIELGEIDRAMQALPD 884
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 629 VEQlAISLSPEGQHAAAAKTD---------SAKGEALvlfttDSEITRERLikvarENGVPELAVPRDIRVVKALPLLGS 699
Cdd:PRK10252 885 VEQ-AVTHACVINQAAATGGDarqlvgylvSQSGLPL-----DTSALQAQL-----RERLPPHMVPVVLLQLDQLPLSAN 953
|
....
gi 488138635 700 GKPD 703
Cdd:PRK10252 954 GKLD 957
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
232-714 |
1.95e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 63.61 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 232 DSYQTLLKKTLGVsrilqrftVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLqsaiiAASLKtIVTSRQ 311
Cdd:cd05937 16 LRYAHWLHDDLGV--------QAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPL-----IHCLK-LSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 312 flekgklthlpeqvnevnwvyledlkdtVTLTDklwilfhlcfprramlpqqaDGSALILFTSGSEGNPKGVVHSHASLL 391
Cdd:cd05937 82 ----------------------------VIVDP--------------------DDPAILIYTSGTTGLPKAAAISWRRTL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 392 ANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPElVYDRNCTVLfgtsTFLGNYAR 471
Cdd:cd05937 114 VTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKD-VRDSGATII----QYVGELCR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 472 F-----AHPYDFA-RVRyvVAGAEKLAESTKQIWQDKFGIRIL-EGYGVTEcAPVVAINVPMAA-KVNTVGRILPGMEAR 543
Cdd:cd05937 189 YllstpPSPYDRDhKVR--VAWGNGLRPDIWERFRERFNVPEIgEFYAATE-GVFALTNHNVGDfGAGAIGHHGLIRRWK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 544 LINVPGIAQ----------------GGRLQLRGPNIMRGYLRVEN----PGVLEQPSAENA--------QGELdanWYDT 595
Cdd:cd05937 266 FENQVVLVKmdpetddpirdpktgfCVRAPVGEPGEMLGRVPFKNreafQGYLHNEDATESklvrdvfrKGDI---YFRT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 596 GDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAislspeGQHAAAAKT----------DSAKGEALVLFTTDS-- 663
Cdd:cd05937 343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVL------GAHPDIAEAnvygvkvpghDGRAGCAAITLEESSav 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 488138635 664 --EITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDP 714
Cdd:cd05937 417 ptEFTKSLLASLARKN-LPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
372-701 |
2.75e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 63.43 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSH--ASLLANVEQIrtIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLypsplhYRVVPE 449
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHrgAYLNALSNIL--AWGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGTNVCL------RKVDPK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 450 LVYD----RNCTVLFGTS---TFLGN-----YARFAHPydfarVRYVVAGA---EKLAESTKQIwqdkfGIRILEGYGVT 514
Cdd:PRK08162 261 LIFDlireHGVTHYCGAPivlSALINapaewRAGIDHP-----VHAMVAGAappAAVIAKMEEI-----GFDLTHVYGLT 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 515 ECAPVVAIN--------VPMAAKVNTVGR------ILPGME----ARLINVPgiAQG---GRLQLRGPNIMRGYLRveNP 573
Cdd:PRK08162 331 ETYGPATVCawqpewdaLPLDERAQLKARqgvrypLQEGVTvldpDTMQPVP--ADGetiGEIMFRGNIVMKGYLK--NP 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 574 gvleQPSAENAQGeldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQL-----AISLSpegqhAAAAKT 648
Cdd:PRK08162 407 ----KATEEAFAG----GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVlyrhpAVLVA-----AVVAKP 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488138635 649 DSAKGE---ALVLFTTDSEITRERLIKVARENgvpeLA---VPRDIrVVKALPLLGSGK 701
Cdd:PRK08162 474 DPKWGEvpcAFVELKDGASATEEEIIAHCREH----LAgfkVPKAV-VFGELPKTSTGK 527
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
248-701 |
2.79e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 63.59 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 248 LQRFTVPGEHVGMLLPNATITAAAIFGASLRGRI--PALLNYTSGAKGLQSAIIA-ASLKTIVTS-------RQFLEKGK 317
Cdd:PRK07769 72 LQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIavPLFDPAEPGHVGRLHAVLDdCTPSAILTTtdsaegvRKFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 318 LTHLPEQV------NEVN--WVYLEDLKDTVtltdklwilfhlcfprramlpqqadgsALILFTSGSEGNPKGVVHSHAS 389
Cdd:PRK07769 152 AKERPRVIavdavpDEVGatWVPPEANEDTI---------------------------AYLQYTSGSTRIPAGVQITHLN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 390 LLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPL---HYRVVPELVYDRNCTVlfGTSTFL 466
Cdd:PRK07769 205 LPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFvrrPGRWIRELARKPGGTG--GTFSAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 467 GNYArFAH------------PYDFARVRYVVAGAEKLAESTKQIWQDKF---GIR---ILEGYGVTECAPVVAiNVPM-- 526
Cdd:PRK07769 283 PNFA-FEHaaarglpkdgepPLDLSNVKGLLNGSEPVSPASMRKFNEAFapyGLPptaIKPSYGMAEATLFVS-TTPMde 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 527 AAKVNTVGRILPGmEARLINVPGIAQG--------------------------------GRLQLRGPNIMRGYL-RVENP 573
Cdd:PRK07769 361 EPTVIYVDRDELN-AGRFVEVPADAPNavaqvsagkvgvsewavivdpetaselpdgqiGEIWLHGNNIGTGYWgKPEET 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 574 -----GVLEQPSAEN-AQG-ELDANWYDTGDI-VTLDeqGFCAIRGRVKRFAKLAG--------EMVSLESVEQL----- 632
Cdd:PRK07769 440 aatfqNILKSRLSEShAEGaPDDALWVRTGDYgVYFD--GELYITGRVKDLVIIDGrnhypqdlEYTAQEATKALrtgyv 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 633 -AISLsPEGQHAAAAKTDSAKGealvlFTTDSEITRERLIKVA-----------------------RENGVPelavPRDI 688
Cdd:PRK07769 518 aAFSV-PANQLPQVVFDDSHAG-----LKFDPEDTSEQLVIVAerapgahkldpqpiaddiraaiaVRHGVT----VRDV 587
|
570
....*....|....*
gi 488138635 689 RVVKA--LPLLGSGK 701
Cdd:PRK07769 588 LLVPAgsIPRTSSGK 602
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
372-612 |
4.67e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 62.75 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSH---ASLLANveqirTIADFTP----RDRFMSSLPLFHAFGltVGLFTPLMTGSRVFLYPSPlhy 444
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHgqmAFVITN-----HLADLMPgtteQDASLVVAPLSHGAG--IHQLCQVARGAATVLLPSE--- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 445 RVVPE----LVYDRNCTVLFGTSTFLGNYARfaHP----YDFARVRYVV-AGAEKLAESTKQIWQdKFGIRILEGYG--- 512
Cdd:PRK07470 240 RFDPAevwaLVERHRVTNLFTVPTILKMLVE--HPavdrYDHSSLRYVIyAGAPMYRADQKRALA-KLGKVLVQYFGlge 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 513 VTECAPVV------AINVPMAaKVNTVGRILPGMEARLINVPG----IAQGGRLQLRGPNIMRGYLRveNPgvleqpsAE 582
Cdd:PRK07470 317 VTGNITVLppalhdAEDGPDA-RIGTCGFERTGMEVQIQDDEGrelpPGETGEICVIGPAVFAGYYN--NP-------EA 386
|
250 260 270
....*....|....*....|....*....|
gi 488138635 583 NAQGELDAnWYDTGDIVTLDEQGFCAIRGR 612
Cdd:PRK07470 387 NAKAFRDG-WFRTGDLGHLDARGFLYITGR 415
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
356-703 |
5.90e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 61.60 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 356 RRAMLPQQA--DGSALILFTSGSEGNPKGVVHSHASLLANveqirtiADFTPR-----DRFMSSLPLFHAFGLTVgLFTP 428
Cdd:PRK07824 24 RDALRVGEPidDDVALVVATSGTTGTPKGAMLTAAALTAS-------ADATHDrlggpGQWLLALPAHHIAGLQV-LVRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 429 LMTGSR-VFLYPS-----PLHYRVVPELVYDRNCTVLFGTSTF--LGNYARFAHPYDFARVryVVAGA---EKLAESTKQ 497
Cdd:PRK07824 96 VIAGSEpVELDVSagfdpTALPRAVAELGGGRRYTSLVPMQLAkaLDDPAATAALAELDAV--LVGGGpapAPVLDAAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 498 IwqdkfGIRILEGYGVTECAPVVAINvpmaakvntvGRILPGMEARLInvpgiaqGGRLQLRGPNIMRGYLRVENPGVLE 577
Cdd:PRK07824 174 A-----GINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVE-------DGRIALGGPTLAKGYRNPVDPDPFA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 578 QPSaenaqgeldanWYDTGDIVTLDEqGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPE--------------GQHA 643
Cdd:PRK07824 232 EPG-----------WFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEA-ALATHPAvadcavfglpddrlGQRV 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 644 AAAKTDSAKGealvlfttdSEITRERLIKVAREngVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK07824 299 VAAVVGDGGP---------APTLEALRAHVART--LDRTAAPRELHVVDELPRRGIGKVD 347
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
363-703 |
8.99e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 61.83 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIrtIADF-TPRDRFMSSLPLFhAFGLTV-GLFTPLMTGSRVFLYPS 440
Cdd:PRK04813 141 KGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWM--LEDFaLPEGPQFLNQAPY-SFDLSVmDLYPTLASGGTLVALPK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 441 ------PLHYRVVPELVYDrnctVLFGTSTF------LGNYARFAHPydfARVRYVVAGaEKLAESTKQIWQDKF-GIRI 507
Cdd:PRK04813 218 dmtanfKQLFETLPQLPIN----VWVSTPSFadmcllDPSFNEEHLP---NLTHFLFCG-EELPHKTAKKLLERFpSATI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 508 LEGYGVTEcAPV----VAINVPMAAKVNT--VGRILPGMEARLINVPG----IAQGGRLQLRGPNIMRGYLrvENPGVLE 577
Cdd:PRK04813 290 YNTYGPTE-ATVavtsIEITDEMLDQYKRlpIGYAKPDSPLLIIDEEGtklpDGEQGEIVISGPSVSKGYL--NNPEKTA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 578 QpsaenAQGELDANW-YDTGDIVTLDEqGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAA-KTDSAKGEA 655
Cdd:PRK04813 367 E-----AFFTFDGQPaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQ-NLRQSSYVESAVVVpYNKDHKVQY 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488138635 656 LV--------LFTTDSEITRErlIKVARENGVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:PRK04813 440 LIayvvpkeeDFEREFELTKA--IKKELKERLMEYMIPRKFIYRDSLPLTPNGKID 493
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
365-568 |
9.13e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 61.99 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 365 DGSALILFTSGSEGNPKGVVHSHASLLAN---VEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSp 441
Cdd:PRK12582 220 DTVAKYLFTSGSTGMPKAVINTQRMMCANiamQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGTLYIDDG- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 442 lhyRVVPELVYD--RNCTVLfgTSTFLGN----YARFAHPYD---------FARVRYVVAGAEKLAESTKQIWQD----K 502
Cdd:PRK12582 299 ---KPLPGMFEEtiRNLREI--SPTVYGNvpagYAMLAEAMEkddalrrsfFKNLRLMAYGGATLSDDLYERMQAlavrT 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 503 FGIRIL--EGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVpgiaqGGRLQLR--GPNIMRGYL 568
Cdd:PRK12582 374 TGHRIPfyTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPV-----GDKYEVRvkGPNVTPGYH 438
|
|
| LPLAT |
cd06551 |
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ... |
4-140 |
1.35e-09 |
|
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: 58.19 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 4 RLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITD-----TWYMRWLKpyvdFVA 78
Cdd:cd06551 2 RYLLLNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLLLERGLRRDVYGLMDEellerYPFFTRLG----AFS 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138635 79 LDPTNPM-AIKHLVRMV----EQGRPVVIFPEGRIT-VTGSLMKIYDGAAFVAAKSGAAVVPIRLDGP 140
Cdd:cd06551 78 VDRDSPRsAAKSLKYVArllsKPGSVVWIFPEGTRTrRDKRPLQFKPGVAHLAEKAGVPIVPVALRYT 145
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
369-704 |
2.09e-09 |
|
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: 60.09 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 369 LILFTSGSEGNPKGVVHSH---------ASLLANVEQIrTIADFTPRD------RFMSSLPLFHAFGLTVGLFTPLMtGS 433
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifrmlmgGADFGTGEFT-PSEDAHKAAaaaagtVMFPAPPLMHGTGSWTAFGGLLG-GQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVFLYPSPLHYRVVPELVYDRNCTVLfgtsTFLGN-YAR-------FAHPYDFARVRYVVAGAEKLAESTKQIWQD-KFG 504
Cdd:cd05924 85 TVVLPDDRFDPEEVWRTIEKHKVTSM----TIVGDaMARplidalrDAGPYDLSSLFAISSGGALLSPEVKQGLLElVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 505 IRILEGYGVTEC-APVVAINVPMAAKVNTvgRILPGMEARLIN------VPGIAQGGRLQLRGpNIMRGYLRVenpgvlE 577
Cdd:cd05924 161 ITLVDAFGSSETgFTGSGHSAGSGPETGP--FTRANPDTVVLDddgrvvPPGSGGVGWIARRG-HIPLGYYGD------E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 578 QPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAAAAKTDSAK-GE-- 654
Cdd:cd05924 232 AKTAETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEE-ALKSHPAVYDVLVVGRPDERwGQev 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488138635 655 -ALVLFTTDSEITRERLIKVARengvPELA---VPRDIRVVKALPLLGSGKPDF 704
Cdd:cd05924 311 vAVVQLREGAGVDLEELREHCR----TRIArykLPKQVVFVDEIERSPAGKADY 360
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
360-716 |
2.79e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.95 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 360 LPQQadgSALILFTSGSEGNPKGVVHSHASLLANVEQIrtIADFTPRD-----RFMSSlpLFHAfgLTVGLFTPLMTGSR 434
Cdd:PRK05691 2331 LPQH---QAYLIYTSGSTGKPKGVVVSHGEIAMHCQAV--IERFGMRAddcelHFYSI--NFDA--ASERLLVPLLCGAR 2401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 435 VFLYPS-PLHYRVVPELVYDRNCTVLFGTSTFLGNYARF-AHPYDFARVRYVVAGAEKLA-ESTKQIWQDKFGIRILEGY 511
Cdd:PRK05691 2402 VVLRAQgQWGAEEICQLIREQQVSILGFTPSYGSQLAQWlAGQGEQLPVRMCITGGEALTgEHLQRIRQAFAPQLFFNAY 2481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 512 GVTEC--------APVV----AINVPMAAKVNT-VGRILpgmEARLINVPgiaQG--GRLQLRGPNIMRGYLRveNPGV- 575
Cdd:PRK05691 2482 GPTETvvmplaclAPEQleegAASVPIGRVVGArVAYIL---DADLALVP---QGatGELYVGGAGLAQGYHD--RPGLt 2553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 576 ----LEQPSAENAqGELdanwYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISlSPEGQHAAAAKTDSA 651
Cdd:PRK05691 2554 aerfVADPFAADG-GRL----YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE-HPAVREAVVLALDTP 2627
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488138635 652 KGEALVLF-------TTDSEIT--RERLIKVARENgVPELAVPRDIRVVKALPLLGSGKPDFVTLGkmAQDPEM 716
Cdd:PRK05691 2628 SGKQLAGYlvsavagQDDEAQAalREALKAHLKQQ-LPDYMVPAHLILLDSLPLTANGKLDRRALP--APDPEL 2698
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
361-701 |
3.06e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 60.10 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 361 PQQADGSALIlFTSGSEGNPKGVVHSHAS--LLANVEQIR-TIADFTPRDRFMSSLPLFH----AFGLTVGLFtplmtGS 433
Cdd:PRK12406 149 PPVPQPQSMI-YTSGTTGHPKGVRRAAPTpeQAAAAEQMRaLIYGLKPGIRALLTGPLYHsapnAYGLRAGRL-----GG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 434 RVFLYPsplhyRVVPE----LVYDRNCTVLFGTSTF------LGNYARFAhpYDFARVRYVVAGAEKLAESTKQIWQDKF 503
Cdd:PRK12406 223 VLVLQP-----RFDPEellqLIERHRITHMHMVPTMfirllkLPEEVRAK--YDVSSLRHVIHAAAPCPADVKRAMIEWW 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 504 GIRILEGYGVTECAPVVAINVPMA-AKVNTVGRILPGMEARLINVPG--IAQGGRLQLrgpnimrgYLRVE-NPGVLEQP 579
Cdd:PRK12406 296 GPVIYEYYGSTESGAVTFATSEDAlSHPGTVGKAAPGAELRFVDEDGrpLPQGEIGEI--------YSRIAgNPDFTYHN 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 580 SAEnAQGELD-ANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGemVSLESVEQLAISLSPEGQH--AAAAKTDSAKGEAL 656
Cdd:PRK12406 368 KPE-KRAEIDrGGFITSGDVGYLDADGYLFLCDRKRDMVISGG--VNIYPAEIEAVLHAVPGVHdcAVFGIPDAEFGEAL 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 488138635 657 VLF-------TTDSEITRERLikvarENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:PRK12406 445 MAVvepqpgaTLDEADIRAQL-----KARLAGYKVPKHIEIMAELPREDSGK 491
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
364-701 |
8.79e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 58.48 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIA----DFTPRDRFMSSLPLFHAFGLTvGLFTPLMTGSRVFlyP 439
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGlnwvTWVVGETTYSPLPATHIGGLW-WILTCLMHGGLCV--T 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 440 SPLHYRVVPELVYDRNCTVLFGTSTFLgnyARFAHPYDFARV-----RYVVAGAEK-LAESTKQIwqDKFGIRILEGYGV 513
Cdd:PRK05857 245 GGENTTSLLEILTTNAVATTCLVPTLL---SKLVSELKSANAtvpslRLVGYGGSRaIAADVRFI--EATGVRTAQVYGL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 514 TE------CAPVVAINVpmaAKVN--TVGRILPGMEARLI-------NVPGIAQG---GRLQLRGPNIMRGYLrvENPgv 575
Cdd:PRK05857 320 SEtgctalCLPTDDGSI---VKIEagAVGRPYPGVDVYLAatdgigpTAPGAGPSasfGTLWIKSPANMLGYW--NNP-- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 576 leqpsaENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEA 655
Cdd:PRK05857 393 ------ERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAL 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 488138635 656 L---VLFTTDSEITRERLIK---VARENGVPE-LAVPRDIRVVKALPLLGSGK 701
Cdd:PRK05857 467 VglaVVASAELDESAARALKhtiAARFRRESEpMARPSTIVIVTDIPRTQSGK 519
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
258-701 |
2.13e-08 |
|
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: 57.44 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 258 VGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGK-----LTHLPEQVNEVN-WV 331
Cdd:cd05915 52 VATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEairgeLKTVQHFVVMDEkAP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 332 YLEDLKDTVTLTDKlwilfhlcfPRRAMlpQQADGSALIlFTSGSEGNPKGVVHSHASLLANVEQIRTIADFT--PRDRF 409
Cdd:cd05915 132 EGYLAYEEALGEEA---------DPVRV--PERAACGMA-YTTGTTGLPKGVVYSHRALVLHSLAASLVDGTAlsEKDVV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 410 MSSLPLFHAFGLTVgLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYA--RFAHPYDFARVRYVVAG 487
Cdd:cd05915 200 LPVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALAdyLESTGHRLKTLRRLVVG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 488 AEKLAESTKQIwqDKFG-IRILEGYGVTECAPV----------------VAINVPMAAKVNTVGRILPGMEARLINVPGI 550
Cdd:cd05915 279 GSAAPRSLIAR--FERMgVEVRQGYGLTETSPVvvqnfvkshleslseeEKLTLKAKTGLPIPLVRLRVADEEGRPVPKD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 551 AQGGR-LQLRGPNIMRGYLRVEnpgvlEQPSAENAQGeldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESV 629
Cdd:cd05915 357 GKALGeVQLKGPWITGGYYGNE-----EATRSALTPD----GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDL 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488138635 630 EQLAISLSPEGQHAAAAKTDSAKGEALVLFT--TDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGK 701
Cdd:cd05915 428 ENALMGHPKVKEAAVVAIPHPKWQERPLAVVvpRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGK 501
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
363-614 |
2.17e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.87 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 363 QADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRT--IADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYpS 440
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-S 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 441 PLHY--RVV----------------PELVYdRNCTVLFGTSTFLGnyarfahpYDFARVRYVVAGAEKLAESTKQIWQDK 502
Cdd:PRK05691 243 PAYFleRPLrwleaiseyggtisggPDFAY-RLCSERVSESALER--------LDLSRWRVAYSGSEPIRQDSLERFAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 503 F---GIR---ILEGYGVTEC-------------------APVVAINVPMAAKVNTV---GRILPG-----MEARLINVPG 549
Cdd:PRK05691 314 FaacGFDpdsFFASYGLAEAtlfvsggrrgqgipaleldAEALARNRAEPGTGSVLmscGRSQPGhavliVDPQSLEVLG 393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488138635 550 IAQGGRLQLRGPNIMRGYLRveNPgvleQPSAEnAQGELDAN-WYDTGDIVTLDEqGFCAIRGRVK 614
Cdd:PRK05691 394 DNRVGEIWASGPSIAHGYWR--NP----EASAK-TFVEHDGRtWLRTGDLGFLRD-GELFVTGRLK 451
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
373-522 |
7.45e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 55.16 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 373 TSGSEGNPKGVVHSHASLLA---NVEQIRTIADFTPRDRFmsslplFHAFGLtvGLFT---PLMTGSRVflypspLHYRV 446
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRwaeLFARSLRAAGVRPGDRV------QNAFGY--GLFTgglGLHYGAER------LGATV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 447 VP----------ELVYDRNCTVLFGTSTF---LGNYARfAHPYDFAR--VRYVVAGAEKLAESTKQIWQDKFGIRILEGY 511
Cdd:COG1541 157 IPagggnterqlRLMQDFGPTVLVGTPSYllyLAEVAE-EEGIDPRDlsLKKGIFGGEPWSEEMRKEIEERWGIKAYDIY 235
|
170
....*....|.
gi 488138635 512 GVTECAPVVAI 522
Cdd:COG1541 236 GLTEVGPGVAY 246
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
478-630 |
1.99e-07 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 54.35 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 478 FARVRYVVAGAEKLAESTKQIWQdKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVpgiaqgGRLQ 557
Cdd:cd17641 323 FSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV------GEIL 395
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488138635 558 LRGPNIMRGYlrvenpgvLEQPSAeNAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLA-GEMVSLESVE 630
Cdd:cd17641 396 VRSPGVFVGY--------YKNPEA-TAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIE 460
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
629-701 |
2.85e-07 |
|
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: 48.31 E-value: 2.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488138635 629 VEQlAISLSPEGQHAAA-AKTDSAKGEALVLFTT---DSEITRERLIKVARENgVPELAVPRDIRVVKALPLLGSGK 701
Cdd:pfam13193 2 VES-ALVSHPAVAEAAVvGVPDELKGEAPVAFVVlkpGVELLEEELVAHVREE-LGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02901 |
PLN02901 |
1-acyl-sn-glycerol-3-phosphate acyltransferase |
35-139 |
4.49e-07 |
|
1-acyl-sn-glycerol-3-phosphate acyltransferase
Pssm-ID: 215488 [Multi-domain] Cd Length: 214 Bit Score: 51.27 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 35 NHVSFLD-GALLALFLPIKpvFAVYTSI----TDTWYMrWLKPYVDFVALDPTNPM-AIKHLVRMVEQGRPVVIFPEGRI 108
Cdd:PLN02901 57 NHQSFLDiYTLFHLGRPFK--FISKTSIflipIIGWAM-YMTGHIPLKRMDRRSQLeCLKRCMELLKKGASVFFFPEGTR 133
|
90 100 110
....*....|....*....|....*....|.
gi 488138635 109 TVTGSLMKIYDGAAFVAAKSGAAVVPIRLDG 139
Cdd:PLN02901 134 SKDGKLAAFKKGAFSVAAKTGVPVVPITLVG 164
|
|
| LPLAT_LPCAT1-like |
cd07991 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ... |
7-174 |
6.34e-07 |
|
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: 50.68 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 7 RALFR--GLFRVTIDGVTDQFKHEKLIITpNHVSFLDGALLALFLPikPVFAVYTSITDTWYMRWLKPYVDFVALDPTNP 84
Cdd:cd07991 2 RVLLFafGFYVIKVHGKPDPPEAPRIIVA-NHTSFIDPLILFSDLF--PSIVAKKELGKLPFIGTILRALGCIFVDRSEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 85 MAIKHLVRMVEQ------GRPVVIFPEGriTVTG--SLMKIYDGaAFVAaksGAAVVP--IRLDGPEFTHF--GRLQGVL 152
Cdd:cd07991 79 KDRKKVVEEIKEratdpnWPPILIFPEG--TTTNgkALIMFKKG-AFEP---GVPVQPvaIRYPNKFVDAFwnSSGYSSL 152
|
170 180
....*....|....*....|....*...
gi 488138635 153 K------TRWFPKISIHVLPATTIPMPQ 174
Cdd:cd07991 153 MylfrllTQPANVLEVEFLPVYTPSEEG 180
|
|
| LPLAT_ACT14924-like |
cd07986 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ... |
30-139 |
1.78e-06 |
|
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: 49.17 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 30 LIITPNH-VSFLDG-ALLALFLPIKPVFAVYTSiTDTWYMRWLKPYvdFVALDPTNPMA--------IKHLVRMVEQGRP 99
Cdd:cd07986 24 VVIVANHpFGILDGlILADLLGSVRPDVRILAN-QLLSKIPELRDL--FIPVDPLEGRAalaknresLREALRHLKNGGA 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488138635 100 VVIFPEGRI-TVTGSLMKIYD-----GAAFVAAKSGAAVVPIRLDG 139
Cdd:cd07986 101 LIIFPAGRVsTASPPFGRVSDrpwnpFVARLARKAKAPVVPVYFSG 146
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
233-439 |
3.48e-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: 50.42 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 233 SYQTLLKKTLGVSRILQRFTV--PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGA---KGLQSAI-IAASLKTI 306
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGlkPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISqqlGFLLGTCkVRVALTVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 307 VTSRQFleKGKLTHLPEQVNEVNWVYLEDLKDTVTLTdklwilFHLCFPRR---AMLPQQADGSALILFTSGSEGNPKGV 383
Cdd:cd05905 96 ACLKGL--PKKLLKSKTAAEIAKKKGWPKILDFVKIP------KSKRSKLKkwgPHPPTRDGDTAYIEYSFSSDGSLSGV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488138635 384 VHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYP 439
Cdd:cd05905 168 AVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIP 223
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
372-701 |
1.03e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 48.69 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 372 FTSGSEGNPKGVVHSH--ASLLANVEQIrtIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYpsplhyRVVPE 449
Cdd:PLN02479 202 YTSGTTASPKGVVLHHrgAYLMALSNAL--IWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNICLR------QVTAK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 450 LVYdrNCTVLFGTSTFLG---------NYARFAHPYDFARVRYV-VAGAEK----LAESTKQiwqdkfGIRILEGYGVTE 515
Cdd:PLN02479 274 AIY--SAIANYGVTHFCAapvvlntivNAPKSETILPLPRVVHVmTAGAAPppsvLFAMSEK------GFRVTHTYGLSE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 516 -------CA---------PVVAINVPMAAKVNTVGriLPGMEA--RLINVPGIAQG---GRLQLRGPNIMRGYLRveNPg 574
Cdd:PLN02479 346 tygpstvCAwkpewdslpPEEQARLNARQGVRYIG--LEGLDVvdTKTMKPVPADGktmGEIVMRGNMVMKGYLK--NP- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 575 vleQPSAENAQGeldaNWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQlAISLSPEGQHAA-AAKTDSAKG 653
Cdd:PLN02479 421 ---KANEEAFAN----GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVEN-VVYTHPAVLEASvVARPDERWG 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488138635 654 EALVLFTT--------DSEITRERLIKVARENgVPELAVPRDIrVVKALPLLGSGK 701
Cdd:PLN02479 493 ESPCAFVTlkpgvdksDEAALAEDIMKFCRER-LPAYWVPKSV-VFGPLPKTATGK 546
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
364-703 |
3.56e-05 |
|
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: 47.08 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 364 ADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRtiaDFTPRDRFMSSLPlFHAFGLTVG---LFTPLMTGSRVFLYPS 440
Cdd:cd17656 127 SDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER---EKTNINFSDKVLQ-FATCSFDVCyqeIFSTLLSGGTLYIIRE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 441 PLHyRVVPEL---VYDRNCTVLFGTSTFL---GNYARFAHPYdFARVRYVVAGAEKLAEStkQIWQDKF---GIRILEGY 511
Cdd:cd17656 203 ETK-RDVEQLfdlVKRHNIEVVFLPVAFLkfiFSEREFINRF-PTCVKHIITAGEQLVIT--NEFKEMLhehNVHLHNHY 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 512 GVTECAPVVAINV---PMAAKVNTVGRILPGMEARLINVPGIAQG----GRLQLRGPNIMRGYLRVEnpgvlEQPSAENA 584
Cdd:cd17656 279 GPSETHVVTTYTInpeAEIPELPPIGKPISNTWIYILDQEQQLQPqgivGELYISGASVARGYLNRQ-----ELTAEKFF 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 585 QGELDAN--WYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEAL-VLFTT 661
Cdd:cd17656 354 PDPFDPNerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLcAYFVM 433
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488138635 662 DSEITRERLI-KVAREngVPELAVPRDIRVVKALPLLGSGKPD 703
Cdd:cd17656 434 EQELNISQLReYLAKQ--LPEYMIPSFFVPLDQLPLTPNGKVD 474
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
370-482 |
8.74e-05 |
|
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: 45.72 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 370 ILFTSGSEGNPKGVVHSH-ASLLANVEQIRTIADFTPRDRFMsslplfhaFGLTVG------LFTPLMTGSRVFLYP-SP 441
Cdd:cd05943 254 ILYSSGTTGLPKCIVHGAgGTLLQHLKEHILHCDLRPGDRLF--------YYTTCGwmmwnwLVSGLAVGATIVLYDgSP 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488138635 442 LHYR--VVPELVYDRNCTVlFGTS-TFLGNYAR----FAHPYDFARVR 482
Cdd:cd05943 326 FYPDtnALWDLADEEGITV-FGTSaKYLDALEKaglkPAETHDLSSLR 372
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
254-439 |
2.76e-04 |
|
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: 44.20 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 254 PGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEkGKLTHLPE-QVNEVNWVY 332
Cdd:cd05938 30 PGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPELQE-AVEEVLPAlRADGVSVWY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 333 LED---LKDTVTLTDKLWILFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLA--NVEQIRTIadfTPRD 407
Cdd:cd05938 109 LSHtsnTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQcsGFLSLCGV---TADD 185
|
170 180 190
....*....|....*....|....*....|..
gi 488138635 408 RFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYP 439
Cdd:cd05938 186 VIYITLPLYHSSGFLLGIGGCIELGATCVLKP 217
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
370-482 |
1.63e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.70 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 370 ILFTSGSEGNPKGVVHSHASLLanVEQIRTIA---DFTPRDRFM--------------SSLplfhAFGLTVGLFtplmTG 432
Cdd:PRK03584 268 ILYSSGTTGLPKCIVHGHGGIL--LEHLKELGlhcDLGPGDRFFwyttcgwmmwnwlvSGL----LVGATLVLY----DG 337
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488138635 433 SRVflYPSPlhyRVVPELVYDRNCTVlFGTS-TFLGNYARF-AHP---YDFARVR 482
Cdd:PRK03584 338 SPF--YPDP---NVLWDLAAEEGVTV-FGTSaKYLDACEKAgLVPgetHDLSALR 386
|
|
| COG3176 |
COG3176 |
Putative hemolysin [General function prediction only]; |
6-154 |
3.05e-03 |
|
Putative hemolysin [General function prediction only];
Pssm-ID: 442409 Cd Length: 270 Bit Score: 40.02 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 6 LRALFRGL-FRVTID-GVTDQF-KHEKLIITPNH-VSFLDG-ALLALFLPIKPVFAVYTS-----ITDTWYmrwlKPYvd 75
Cdd:COG3176 46 LRYVFEELgARLEVPeGDLDRIdADGHLLVVANHpLGILDGlALLKLVGTVRPDYRILANdlalrIPGGFY----SEL-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 76 FVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRItvtGSLMKIYD-----GAAFVAAKSGAAVVPIRLDGPEFTHF---GR 147
Cdd:COG3176 120 EFPVDPFNLETLKAARRHLLEGGRSCVFPAGRV---SGARRVIDllwsgLAAKLARKAGAPVVPVYFDGRNSGLFylfGS 196
|
....*..
gi 488138635 148 LQGVLKT 154
Cdd:COG3176 197 IHPTLRT 203
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
370-386 |
5.89e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 39.74 E-value: 5.89e-03
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
30-143 |
6.98e-03 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-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 lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.
Pssm-ID: 153246 [Multi-domain] Cd Length: 192 Bit Score: 38.35 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 30 LIITPnHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPY-----VDFVALDptnpMAIKHLVRMVEQGRPVVIFP 104
Cdd:cd07984 23 ILLTA-HFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLITRGrerfgARLIPRG----GGLRELIRALKKGEIVGILP 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488138635 105 ------EGRITVT--GSLMKIYDGAAFVAAKSGAAVVPI---RLDGPEFT 143
Cdd:cd07984 98 dqdpgrKGGVFVPffGRPAATPTGPARLALKTGAPVVPAfayRLPGGGYR 147
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
591-701 |
8.89e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 39.35 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138635 591 NWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGE----------MVSLESVeqlaislspegqhAAAA---KTDSAKGEALV 657
Cdd:PRK00174 483 GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHrlgtaeiesaLVAHPKV-------------AEAAvvgRPDDIKGQGIY 549
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488138635 658 LFTT--DSEITRERLIK-----VARENGvPeLAVPRDIRVVKALPLLGSGK 701
Cdd:PRK00174 550 AFVTlkGGEEPSDELRKelrnwVRKEIG-P-IAKPDVIQFAPGLPKTRSGK 598
|
|
| |
