|
Name |
Accession |
Description |
Interval |
E-value |
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
18-312 |
2.76e-94 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 281.25 E-value: 2.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 18 SSERKLSSLFMDLKSLLKGIVLIANVLPVITGFWLAiyftnASFSDQRGLFLLTMIGSTFVMAGALVLNNWYEVDLDREM 97
Cdd:COG0109 7 SSAASLRSTLRDYLALTKPRIILLLLFTALAGMLLA-----AGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 98 ERTKNRPTVTGNFSLKTVLTMGIIFSIIGFVVLY-FTTMEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTPL 176
Cdd:COG0109 82 KRTKNRPLPTGRISPREALIFGLVLGVLGLALLAlFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 177 IGWAALAPSYHYVPIVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLP---LPFFLTS 253
Cdd:COG0109 162 IGWAAVTGSLSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPvslLPYLLGM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1073967947 254 LGTIFVVIATILNVVWILLSVGGFFTNSDaKWARALFLYSVNYLAILFILMIVVTLPIF 312
Cdd:COG0109 242 AGLIYLVVALVLGAWFLYLAVRLYRRPDR-KWARKLFKFSILYLTLLFLALLVDHLLLL 299
|
|
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
18-312 |
1.38e-91 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 274.32 E-value: 1.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 18 SSERKLSSLFMDLKSLLKGIVLIANVLPVITGFWLAIYFTNASfsdqrGLFLLTMIGSTFVMAGALVLNNWYEVDLDREM 97
Cdd:PRK04375 1 VSSSSSRATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPL-----LLLLLTLLGIALVAGAAGALNNYIDRDIDAKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 98 ERTKNRPTVTGNFSLKTVLTMGIIFSIIGFVVLYFTT-MEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTPL 176
Cdd:PRK04375 76 ERTKNRPLVTGRISPREALIFGLVLGVLGFLLLGLFVnPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 177 IGWAALAPSYHYVPIVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLP---LPFFLTS 253
Cdd:PRK04375 156 IGWAAVTGSLSWEALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAvslLPVLLGM 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1073967947 254 LGTIFVVIATILNVVWILLSVGGFFTNSDaKWARALFLYSVNYLAILFILMIVVTLPIF 312
Cdd:PRK04375 236 AGLLYLVVALLLGAWFLYYAWRLYRKDDR-KWARKLFRYSINYLTLLFVALLVDHLLLL 293
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
32-303 |
5.95e-89 |
|
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O synthase, heme A:farnesyltransferase, cytochrome c oxidase subunit X [Cox10]) converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of the heme B porphyrin ring with a hydroxyethyl farnesyl side group. It is localized at the mitochondrial inner membrane. Eukaryotic Cox10 is important for the maturation of the heme A prosthetic group of cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, that catalyzes the electron transfer from reduced cytochrome c to oxygen. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260120 Cd Length: 271 Bit Score: 266.61 E-value: 5.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 32 SLLKGIVLIANVLPVITGFWLAiyftnASFSDQRGLFLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFS 111
Cdd:cd13957 2 ELTKPRITLLVLLTALAGYLLA-----PGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 112 LKTVLTMGIIFSIIGFVVLYFTT-MEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVP 190
Cdd:cd13957 77 PKHALIFGLVLGILGLALLALFVnPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 191 IVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLP---LPFFLTSLGTIFVVIATILNV 267
Cdd:cd13957 157 WLLFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPlslLLYLLGLTGWIYLVVALLLGL 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1073967947 268 VWILLSVGGFFTNSDaKWARALFLYSVNYLAILFIL 303
Cdd:cd13957 237 YFLYLAIKLYRSPDD-KWARKLFFASLIYLPLLFLL 271
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
28-306 |
2.49e-80 |
|
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also called heme O synthase, an enzyme that creates an intermediate in the biosynthesis of heme A. Prior to the description of its enzymatic function, this protein was often called a cytochrome o ubiquinol oxidase assembly factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273645 Cd Length: 280 Bit Score: 245.23 E-value: 2.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 28 MDLKSLLKGIVLIANVLPVITGFWLAIYFTNASFSdqrgLFLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVT 107
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGALVNPP----LLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 108 GNFSLKTVLTMGIIFSIIGFVVLY-FTTMEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTPLIGWAALAPSY 186
Cdd:TIGR01473 77 GRISPREALAFGLLLGVLGVAILAaFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 187 HYVPIVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLP---LPFFLTSLGTIFVVIAT 263
Cdd:TIGR01473 157 SLGAWLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPvslLLAFLGGTGWLYLIVAT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1073967947 264 ILNVVWILLSVGGFFTNSDAKWARALFLYSVNYLAILFILMIV 306
Cdd:TIGR01473 237 LLGALFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLI 279
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
43-293 |
4.02e-42 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 145.83 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 43 VLPVITGFWLAIYFTNASFsdqrgLFLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGIIF 122
Cdd:pfam01040 2 LIPALAGLALAAGGVPDLL-----LLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 123 SIIGFVVLYFTTMEAVIYAFIGWFTYVImYTMWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVPIVLALLLFIWQM 202
Cdd:pfam01040 77 LALGLLLLLLLNPLTALLGLAALLLYVL-YTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 203 PHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIII--YVTCLLPLPFFLTSLGTIFVVIATILNVVWILLSVGGFFTN 280
Cdd:pfam01040 156 AIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALllAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLR 235
|
250
....*....|...
gi 1073967947 281 SDAKWARALFLYS 293
Cdd:pfam01040 236 DPKKDAKAFFFLS 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
18-312 |
2.76e-94 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 281.25 E-value: 2.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 18 SSERKLSSLFMDLKSLLKGIVLIANVLPVITGFWLAiyftnASFSDQRGLFLLTMIGSTFVMAGALVLNNWYEVDLDREM 97
Cdd:COG0109 7 SSAASLRSTLRDYLALTKPRIILLLLFTALAGMLLA-----AGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 98 ERTKNRPTVTGNFSLKTVLTMGIIFSIIGFVVLY-FTTMEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTPL 176
Cdd:COG0109 82 KRTKNRPLPTGRISPREALIFGLVLGVLGLALLAlFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 177 IGWAALAPSYHYVPIVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLP---LPFFLTS 253
Cdd:COG0109 162 IGWAAVTGSLSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPvslLPYLLGM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1073967947 254 LGTIFVVIATILNVVWILLSVGGFFTNSDaKWARALFLYSVNYLAILFILMIVVTLPIF 312
Cdd:COG0109 242 AGLIYLVVALVLGAWFLYLAVRLYRRPDR-KWARKLFKFSILYLTLLFLALLVDHLLLL 299
|
|
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
18-312 |
1.38e-91 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 274.32 E-value: 1.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 18 SSERKLSSLFMDLKSLLKGIVLIANVLPVITGFWLAIYFTNASfsdqrGLFLLTMIGSTFVMAGALVLNNWYEVDLDREM 97
Cdd:PRK04375 1 VSSSSSRATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPL-----LLLLLTLLGIALVAGAAGALNNYIDRDIDAKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 98 ERTKNRPTVTGNFSLKTVLTMGIIFSIIGFVVLYFTT-MEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTPL 176
Cdd:PRK04375 76 ERTKNRPLVTGRISPREALIFGLVLGVLGFLLLGLFVnPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 177 IGWAALAPSYHYVPIVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLP---LPFFLTS 253
Cdd:PRK04375 156 IGWAAVTGSLSWEALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAvslLPVLLGM 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1073967947 254 LGTIFVVIATILNVVWILLSVGGFFTNSDaKWARALFLYSVNYLAILFILMIVVTLPIF 312
Cdd:PRK04375 236 AGLLYLVVALLLGAWFLYYAWRLYRKDDR-KWARKLFRYSINYLTLLFVALLVDHLLLL 293
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
32-303 |
5.95e-89 |
|
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O synthase, heme A:farnesyltransferase, cytochrome c oxidase subunit X [Cox10]) converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of the heme B porphyrin ring with a hydroxyethyl farnesyl side group. It is localized at the mitochondrial inner membrane. Eukaryotic Cox10 is important for the maturation of the heme A prosthetic group of cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, that catalyzes the electron transfer from reduced cytochrome c to oxygen. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260120 Cd Length: 271 Bit Score: 266.61 E-value: 5.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 32 SLLKGIVLIANVLPVITGFWLAiyftnASFSDQRGLFLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFS 111
Cdd:cd13957 2 ELTKPRITLLVLLTALAGYLLA-----PGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 112 LKTVLTMGIIFSIIGFVVLYFTT-MEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVP 190
Cdd:cd13957 77 PKHALIFGLVLGILGLALLALFVnPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 191 IVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLP---LPFFLTSLGTIFVVIATILNV 267
Cdd:cd13957 157 WLLFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPlslLLYLLGLTGWIYLVVALLLGL 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1073967947 268 VWILLSVGGFFTNSDaKWARALFLYSVNYLAILFIL 303
Cdd:cd13957 237 YFLYLAIKLYRSPDD-KWARKLFFASLIYLPLLFLL 271
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
28-306 |
2.49e-80 |
|
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also called heme O synthase, an enzyme that creates an intermediate in the biosynthesis of heme A. Prior to the description of its enzymatic function, this protein was often called a cytochrome o ubiquinol oxidase assembly factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273645 Cd Length: 280 Bit Score: 245.23 E-value: 2.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 28 MDLKSLLKGIVLIANVLPVITGFWLAIYFTNASFSdqrgLFLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVT 107
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGALVNPP----LLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 108 GNFSLKTVLTMGIIFSIIGFVVLY-FTTMEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTPLIGWAALAPSY 186
Cdd:TIGR01473 77 GRISPREALAFGLLLGVLGVAILAaFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 187 HYVPIVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLP---LPFFLTSLGTIFVVIAT 263
Cdd:TIGR01473 157 SLGAWLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPvslLLAFLGGTGWLYLIVAT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1073967947 264 ILNVVWILLSVGGFFTNSDAKWARALFLYSVNYLAILFILMIV 306
Cdd:TIGR01473 237 LLGALFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLI 279
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
43-293 |
4.02e-42 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 145.83 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 43 VLPVITGFWLAIYFTNASFsdqrgLFLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGIIF 122
Cdd:pfam01040 2 LIPALAGLALAAGGVPDLL-----LLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 123 SIIGFVVLYFTTMEAVIYAFIGWFTYVImYTMWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVPIVLALLLFIWQM 202
Cdd:pfam01040 77 LALGLLLLLLLNPLTALLGLAALLLYVL-YTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 203 PHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIII--YVTCLLPLPFFLTSLGTIFVVIATILNVVWILLSVGGFFTN 280
Cdd:pfam01040 156 AIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALllAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLR 235
|
250
....*....|...
gi 1073967947 281 SDAKWARALFLYS 293
Cdd:pfam01040 236 DPKKDAKAFFFLS 248
|
|
| PLN02776 |
PLN02776 |
prenyltransferase |
68-310 |
3.18e-30 |
|
prenyltransferase
Pssm-ID: 215415 Cd Length: 341 Bit Score: 116.77 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 68 FLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGIIFSIIGFVVLYF-TTMEA--------V 138
Cdd:PLN02776 31 LGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVAWAVVVGAAGVALLAYkTNMLTaglgagniL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 139 IYAFIgwftyvimYTmWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVPIVLALLLFIWQMPHTFAIAMRRHDEYKA 218
Cdd:PLN02776 111 LYAFV--------YT-PLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAALYFWQMPHFMALAYMCRDDYAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 219 AGVAMLPVvrgFDFTKRQI--IIYVTC--LLPLPFFLTSLGTI---FVVIATILNvVWILLSVGGFFTNSDAKWARALFL 291
Cdd:PLN02776 182 GGYRMLSL---ADATGRRTalVALRNClyLAPLGFLAYDWGVTsspFALEAALLT-AYLAASAASFYREPTNANARKMFH 257
|
250
....*....|....*....
gi 1073967947 292 YSVNYLAILFILMIVVTLP 310
Cdd:PLN02776 258 GSLLYLPAFMALLLLHRVP 276
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
41-306 |
1.47e-18 |
|
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate polyprenyltransferase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440151 Cd Length: 280 Bit Score: 83.74 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 41 ANVLPVITGFWLAIYFTNASFSDqRGLFLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGI 120
Cdd:COG0382 13 IGILLLLWPTLWALFLAAGGLPD-LLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISLREALLLAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 121 IFSIIGFVVLYFTTMEAVIYAFIGWFTyVIMYTMWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVPIVLALLLFIW 200
Cdd:COG0382 92 VLLLLALALALLLNPLTFLLALAALAL-AWAYSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPLSAWLLALAAFLW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 201 QMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQI---IIYVTCLLPLPFFLTSLGTIFVVIATILNVVWILLSVGGF 277
Cdd:COG0382 171 TLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAgvlYALAVLLLLLLGLLAGLGLLYLLGLLAALLLLYLSQLWLL 250
|
250 260 270
....*....|....*....|....*....|
gi 1073967947 278 -FTNSDAKWARALFLYSVNYLAILFILMIV 306
Cdd:COG0382 251 rPRKKDPARALKLFKLNMLLGLLLFLGIAL 280
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
42-307 |
3.94e-15 |
|
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260119 [Multi-domain] Cd Length: 271 Bit Score: 73.92 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 42 NVLPVITGFWLAIYFTNASFSDQRGLFLLTMIGSTFVMAGALVLNNWYEVDLDREmeRTKNRPTVTGNFSLKTVLTMGII 121
Cdd:cd13956 8 TLLYVLAPALAGAALAGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAI--NKPDRPLPSGRLSPRQALAFAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 122 FSIIGFVVLYFTTMEAVIYAFIGWFTYVImYTMWMKRKYTLNTVMGSISGAVTPLIGWAALA-PSYHYVPIVLALLLFIW 200
Cdd:cd13956 86 LLLVGLALALALGPLALLLLLAGLLLGLA-YSLGLKRLKLGGWGVLGYATGLALLPGLGAVAaGGLVPLALLLALVFLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 201 QMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLLPLPFFLTSLGTIFVVIATILNVVWILLSVGGFFTN 280
Cdd:cd13956 165 GLGINLYNDLPDVEGDRAAGIRTLPVRLGPRRARRLAAGLLLAALILVVLLAVAGLLGPLALLALLAVALLALRARFARA 244
|
250 260
....*....|....*....|....*..
gi 1073967947 281 SDAKWARALFLYSVNYLAILFILMIVV 307
Cdd:cd13956 245 DRLPALPRGFLLLAVYRLLLFAALLLA 271
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
44-306 |
1.33e-12 |
|
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known as Coq2, catalyzes the prenylation of p-hydroxybenzoate with an all-trans polyprenyl group, an important step in ubiquinone (CoQ) biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260122 [Multi-domain] Cd Length: 272 Bit Score: 66.72 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 44 LPVITGFWLAIYFTNASFSDQRGLFLLtmiGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGIIFS 123
Cdd:cd13959 14 PPALWGLLLAAGGLPLPLLKLLLLFLL---GAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVKEALLFLAVQL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 124 IIGFVVLYFTTMEAVIYAFIGWFTYVImYTmWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVPIVLALLLFIWQMp 203
Cdd:cd13959 91 LLGLALLLQLNPLTILLSPIALLLVLI-YP-LMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPALLLYLAVIFWTA- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 204 hTF----AIAMRRHDeyKAAGVAMLPVVRGfDFTKRQIIIY---VTCLLPLPFFLTSLGTIF-VVIATILNVVWILLSVg 275
Cdd:cd13959 168 -GYdtiyAHQDREDD--RKIGVKSTAVLFG-DRTKLILALLlhlFVALLLLAGGLAGLGWPYyLGLGAAAHLLWQEHRL- 242
|
250 260 270
....*....|....*....|....*....|.
gi 1073967947 276 gfFTNSDAKWARALFLYSVNYLAILFILMIV 306
Cdd:cd13959 243 --DLPDPLRSCLAFFLSNGWVGLLLFAGLLL 271
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
46-303 |
3.53e-09 |
|
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate synthase (DGGGPS) transfers a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260124 Cd Length: 270 Bit Score: 56.74 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 46 VITGFWLAIYFTNASFSDQRGLFLLTMIGSTFVMAGALVLNNWYEVDLDREmeRTKNRPTVTGNFSLKTVLTMGIIFSII 125
Cdd:cd13961 15 ALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDRI--NKPDRPIPSGRISRREALILSILLNAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 126 GFVVLYFTTMEAVIYAFIGWFTyVIMYTMWMKRKYTLNTVMGSISGAVTPLIGWAAlAPSYHYVPIVLALLLFIWQMPHT 205
Cdd:cd13961 93 GLILAFLLSPLALLIALLNSLL-LWLYSHKLKRTPLIGNLLVALLTGLPFLFGGLA-AGNLLLIILLLALFAFLITLGRE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 206 FAIAMRRHDEYKAAGVAMLPVVRGFDFTKR---QIIIYVTCLLPLPFFLTSLGTIFVVIATILNVVWILLSVGGFFTNSD 282
Cdd:cd13961 171 IVKDIEDVEGDRAEGARTLPIVYGIKKAKKiaaLLLLLAILLSPLPYLLGGLGILYLILIIIADLLFLYSAIRLAKSPKD 250
|
250 260
....*....|....*....|.
gi 1073967947 283 AKWARALFLYSVnYLAILFIL 303
Cdd:cd13961 251 YSKLSKLLKLAM-LLGLLAFL 270
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
69-312 |
1.18e-08 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 54.96 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 69 LLTMIGSTFVMAGALVLNNWYEVDLDReMERTkNRPTVTGNFSLKTVLTMGIIFSIIGFVVLYFTTMEAVIYAFIGWFtY 148
Cdd:PRK12884 40 LLGFLTAFFASGSANALNDYFDYEVDR-INRP-DRPIPSGRISRREALLLAILLFILGLIAAYLISPLAFLVVILVSV-L 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 149 VIMYTMWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVpIVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVR 228
Cdd:PRK12884 117 GILYNWKLKEYGLIGNLYVAFLTGMTFIFGGIAVGELNEAV-ILLAAMAFLMTLGREIMKDIEDVEGDRLRGARTLAILY 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 229 GFDFTKR--QIIIYVTCLL-PLPFFLTSLGtIFVVIATILNVVWILLSVGGFFTNSDAKWARAlflYSVNYLAILFILMI 305
Cdd:PRK12884 196 GEKIAGRiaAALFILAVLLsPLPYLFGIFN-ILYLAPVLVADLIFLYSAYSLLRSQDRETIRK---VRKITLTAMLLALV 271
|
....*..
gi 1073967947 306 VVTLPIF 312
Cdd:PRK12884 272 AFALGAI 278
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
39-307 |
1.56e-07 |
|
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.
Pssm-ID: 260125 Cd Length: 283 Bit Score: 51.75 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 39 LIANVLPVITGFWLAIYFTNASFSdqrGLFLLTMIGSTFVMAGALVLNNW--YEVDLDREMERTKNRPTVTGNFSLKTVL 116
Cdd:cd13962 9 LPASLAPVLLGTALAYYLGGFFNW---LLFLLALLAALLLQIGVNLANDYfdYKKGTDTEPRSGPSRVLVSGLLSPRQVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 117 TMGIIFSIIGFVV-LYFTTMEAVIYAFIGWFTYV--IMYTMWMKRKYtlNTVMGSIS-----GAVTPLIGWAALAPSYHY 188
Cdd:cd13962 86 RAALVLLLLAALLgLYLVALGGWLLLLLGLLGILagYFYTGGPFPLS--YRGLGELFvflffGLLAVLGTYYVQTGSLSW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 189 VPIVLALLLFIWqmphTFAIAM----RRHDEYKAAGVAMLPVVRGFDFTKR--QIIIYVTCLLPLPFFLTSLGTIFVVIA 262
Cdd:cd13962 164 EVLLAALPLGLL----IAAILLanniRDIEADRAAGKRTLAVRLGRKRARRlyAALLLLAYLLLLLLVLLGLLPLWSLLA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1073967947 263 TILnvVWILLSVGGFFTNSDAKWARALFLYSVNYLAILFILMIVV 307
Cdd:cd13962 240 LLS--LPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLLLAL 282
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
40-275 |
8.12e-06 |
|
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.
Pssm-ID: 260127 Cd Length: 282 Bit Score: 46.42 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 40 IANVLPVIT----GFWLAIYFTNASFSdqrglFLLTMIGSTFVMAGALVLNNWYEVDLDREmERtKNRPTVTGNFSLKTV 115
Cdd:cd13964 7 LPNLFTVPAdvlaGAALAGGGLGPVLR-----LALLLLASVLLYAAGMVLNDVFDAELDAR-ER-PERPIPSGRVSRGAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 116 LTMGIIFSIIGFVVLYFTTMEAVIYAfIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVTpLIGWAALAPSYHYVPIVLAL 195
Cdd:cd13964 80 LALGAGLLAAGVALAALVGRLSGLVA-LLLAAAILLYDAWLKHTPLGPLLMGLCRGLNL-LLGASAAAAGGLGPALLAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 196 LLFIwqmpHTFAIAMRRHDEYKAAGVAMLPVVRGFdftkrqiiiyVTCLLPLPFFLTSLGTIFVVIATILnVVWILLSVG 275
Cdd:cd13964 158 ALGV----YIAGVTYIARGEVHGGPRRLLPLALLA----------VLLVIGLALALAAPRGGRVLLALLF-LALFAAWVG 222
|
|
| ubiA |
PRK13106 |
prenyltransferase; Reviewed |
77-176 |
1.54e-05 |
|
prenyltransferase; Reviewed
Pssm-ID: 237283 Cd Length: 300 Bit Score: 45.87 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 77 FVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGIIFSIIGFVVLYFTTMEAVIYAFIGWFtyVIMYTMWM 156
Cdd:PRK13106 60 FLRTAGMTNDNLADLEIDAKNPRTKNRPLVTGAIKISEAKALITAGLILFFASAYLVNRWALLLSPIVAL--IAMSYPYM 137
|
90 100
....*....|....*....|....*..
gi 1073967947 157 KRK-----YTLNTVMGSI--SGAVTPL 176
Cdd:PRK13106 138 KRYtafanYHLASIQGLAvfSGAVAVL 164
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
28-303 |
2.87e-05 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 44.95 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 28 MDLKSLLKgIVLIANVL----PVITGFWLAIYFTNASFsdqrgLFLLTMIGSTFVMAGALVLNNWYEVDLDREmeRTKNR 103
Cdd:PRK09573 1 MSIKAYFE-LIRPKNCIgasiGAIIGYLIASNFKIDLK-----GIILAALVVFLVCAGGNVINDIYDIEIDKI--NKPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 104 PTVTGNFSLKTVLTMGIIFSIIGFVVLYFTTMEAVIYAFIGWFTYVIMYTMWMKRKYTLNTVMGSISGAVtplIGWAALA 183
Cdd:PRK09573 73 PIPSGRISLKEAKIFSITLFIVGLILSIFINIYAFLIALLNSILLYLYAKDLKKTGLIGNLIVAYLTGLS---FIFGGLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 184 PSYHYVPIVLALLLFIWQMPHTFAIAMRRHDEYKAAGVAMLPVVRGFDFTKRQIIIYVTCLL---PLPFFLTSLGTIFVV 260
Cdd:PRK09573 150 VFNVLRIIILFLCAFFSTWSREIVKDIEDIEGDLKENVITLPIKYGIKKSWYIAKILLILAIvlsPLPYFLGIFGIYYLI 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1073967947 261 IATILNVVWILLSVGGFFTNS--DAKWARALFLYSVNYLAILFIL 303
Cdd:PRK09573 230 VVIICDILFIIAMLILLKNPSieGASKASKYLKIIMILGLIAFLI 274
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
48-264 |
4.86e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 41.21 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 48 TGFWLAiyFTNASFSDQRGLFLLTMIGSTfvmAGALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGIIFSIIGF 127
Cdd:PRK12886 29 IGAVLA--ALGLPGASQLDWILMAMVGAR---TAAMGFNRLIDAEIDARNPRTAGRAIPAGLISKGSAILFIVLSSLLML 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 128 VVLYFTTMEAVIYAFIGWFtYVIMYTmWMKRKYTLNTVMGSISGAVTPLIGWAALAPSYHYVPIVLALLLFIWQMPHTFA 207
Cdd:PRK12886 104 FAAWFLNPLCLYLSPPALF-FLLLYS-YCKRFTALAHVVLGFCLALAPLGAWIAIRGTIELPAILLGLAVLFWVAGFDIL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 208 IAMRRHDEYKAAGVAMLPV---VRGFDFTKRQIIIYVTCLLPLPFFLTSLGTIFVVIATI 264
Cdd:PRK12886 182 YALQDLEFDRKEGLHSIPAklgVNGSLWIARVFHLLMIGFLFALGISAGLGPWFLAGLAV 241
|
|
| MenA |
COG1575 |
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ... |
39-309 |
2.16e-03 |
|
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441183 Cd Length: 290 Bit Score: 38.97 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 39 LIANVLPVITGFWLAIYFTNaSFSdqRGLFLLTMIGSTFVMAGALVLNNW--YEVDLDREMERTKNRPTVTGNFSLKTVL 116
Cdd:COG1575 11 LPAAVAPVLLGTALAYYETG-SFN--WLLFLLALLAALLLQIGVNLANDYfdYKKGTDTEERVGPSRVIVSGLLSPKQVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 117 TMGIIFSIIGFVV-LYFTTMEAVIYAFIGWFTYV--IMYTMWmKRKYTlNTVMGSIS-----GAVTPLIGWAALAPSYHY 188
Cdd:COG1575 88 RAALLLLALALLLgLYLVLLSGWPLLLLGLLGILaaIFYTGG-PFPLG-YRGLGELFvflffGLVAVLGTYYVQTGTLSW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 189 VPIVLALLLFIWqmphTFAIAM----RRHDEYKAAGVAMLPVVRGFDFTKR--QIIIYVTCLLPLPFFLTSLGTIFVVIA 262
Cdd:COG1575 166 AALLASLPVGLL----SAAVLLannlRDIETDRAAGKRTLAVRLGRKRARRlyAALLLLAYLLILLLVLLGLLPPWALLA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1073967947 263 tILNVVWILLSVGGFFTNSDAKwARALFLYSVNYLAILFILMIVVTL 309
Cdd:COG1575 242 -LLSLPLALKLVRRVLRGAKPE-ALIPALKNTALLNLLFGLLLALGL 286
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
67-129 |
6.40e-03 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 37.72 E-value: 6.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1073967947 67 LFLLTMIGSTFVMAGALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGIIFSIIGFVV 129
Cdd:PRK12873 45 LLLLIILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLARGKISLKTAYSLLIVLLLLSLFV 107
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
82-200 |
7.95e-03 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 237242 Cd Length: 291 Bit Score: 37.29 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073967947 82 ALVLNNWYEVDLDREMERTKNRPTVTGNFSLKTVLTMGIIFSIIGFVVLYFTTMEAVIYAFIgwFTYVIMYTMWMKRKYT 161
Cdd:PRK12874 63 AMAFNRLVDRDIDKDNPRTANRPSVDGRISVKSMVLFIVLNALIFIGVSYFINPLAFKLSFP--FLIVLGGYSYFKRFSS 140
|
90 100 110
....*....|....*....|....*....|....*....
gi 1073967947 162 LNTVMGSISGAVTPLIGWAALAPSYHYVPIVLALLLFIW 200
Cdd:PRK12874 141 LAHLVLGLSLGLAPIAGVVAVLGEIPLWSVFLALGVMFW 179
|
|
| |
