|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
7-286 |
8.82e-105 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 307.45 E-value: 8.82e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 7 LSHNSSRVTFKELQQIIKMGLVQGNLIPAFASSWLAIVLANHsflssIPQILMMLVGSTLIMGGACALNNYYDQDIDSIM 86
Cdd:PRK04375 1 VSSSSSRATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPP-----LLLLLLTLLGIALVAGAAGALNNYIDRDIDAKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 87 PSKQQRPSVNGKISNRNLLLLSFGMMLVGEALLFAL-NIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSFPGAVPPL 165
Cdd:PRK04375 76 ERTKNRPLVTGRISPREALIFGLVLGVLGFLLLGLFvNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 166 IGWTAIEGNISMVAVALFLVIFCWQPVHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVL---LLPLPLLLND 242
Cdd:PRK04375 156 IGWAAVTGSLSWEALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLlvaVSLLPVLLGM 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518299062 243 LGTTFIILATLLNLGWLYLGLTSFKKDSDqtKWATKMFIYSLNY 286
Cdd:PRK04375 236 AGLLYLVVALLLGAWFLYYAWRLYRKDDR--KWARKLFRYSINY 277
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
17-286 |
5.73e-94 |
|
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: 279.52 E-value: 5.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 17 KELQQIIKMGLVQGNLIPAFASSWLAIvlanHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVN 96
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAP----GGALVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 97 GKISNRNLLLLSFGMMLVGEALLFAL-NIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNI 175
Cdd:TIGR01473 77 GRISPREALAFGLLLGVLGVAILAAFvNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 176 SMVAVALFLVIFCWQPVHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVLLL---PLPLLLNDLGTTFIILAT 252
Cdd:TIGR01473 157 SLGAWLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLpvsLLLAFLGGTGWLYLIVAT 236
|
250 260 270
....*....|....*....|....*....|....
gi 518299062 253 LLNLGWLYLGLTSFKKDSDQTKwATKMFIYSLNY 286
Cdd:TIGR01473 237 LLGALFLYLAFKFYRDPTDRKK-ARKLFKFSLIY 269
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
1-286 |
1.02e-92 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 277.01 E-value: 1.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 1 MNKEQTLSHNSSRVTFKELQQIIKMGLVQGNLIPAFASSWLAIvlanhSFLSSIPQILMMLVGSTLIMGGACALNNYYDQ 80
Cdd:COG0109 1 MSSASASSAASLRSTLRDYLALTKPRIILLLLFTALAGMLLAA-----GGLPDLLLLLLTLLGGALAAGAANALNNYIDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 81 DIDSIMPSKQQRPSVNGKISNRNLLLLSFGMMLVGEALL-FALNIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSFP 159
Cdd:COG0109 76 DIDALMKRTKNRPLPTGRISPREALIFGLVLGVLGLALLaLFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 160 GAVPPLIGWTAIEGNISMVAVALFLVIFCWQPVHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVLLLPLP-- 237
Cdd:COG0109 156 GAMPPLIGWAAVTGSLSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSll 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 518299062 238 -LLLNDLGTTFIILATLLNLGWLYLGLTSFKKDSDqtKWATKMFIYSLNY 286
Cdd:COG0109 236 pYLLGMAGLIYLVVALVLGAWFLYLAVRLYRRPDR--KWARKLFKFSILY 283
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
21-286 |
3.35e-88 |
|
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: 264.30 E-value: 3.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 21 QIIKMGLVQGNLIPAFASSWLAIVLANHSFLssipqILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVNGKIS 100
Cdd:cd13957 2 ELTKPRITLLVLLTALAGYLLAPGGVPDLLL-----LLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 101 NRNLLLLSFGMMLVGEALL-FALNIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVA 179
Cdd:cd13957 77 PKHALIFGLVLGILGLALLaLFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 180 VALFLVIFCWQPVHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVLLL---PLPLLLNDLGTTFIILATLLNL 256
Cdd:cd13957 157 WLLFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVplsLLLYLLGLTGWIYLVVALLLGL 236
|
250 260 270
....*....|....*....|....*....|
gi 518299062 257 GWLYLGLTSFKKDSDqtKWATKMFIYSLNY 286
Cdd:cd13957 237 YFLYLAIKLYRSPDD--KWARKLFFASLIY 264
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
32-284 |
2.05e-50 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 167.02 E-value: 2.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 32 LIPAFASSWLAivlanHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVNGKISNRNLLLLSFGM 111
Cdd:pfam01040 2 LIPALAGLALA-----AGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 112 MLVGEALLFALNIPSGVIGLLGIVGYVsFYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVALFLVIFCWQP 191
Cdd:pfam01040 77 LALGLLLLLLLNPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 192 VHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVLLL--PLPLLLNDLGTTFIILATLLNLGWLYLGLTSFKKD 269
Cdd:pfam01040 156 AIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALllLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLR 235
|
250
....*....|....*
gi 518299062 270 SDQTKWATKMFIYSL 284
Cdd:pfam01040 236 DPKKDAKAFFFLSSL 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
7-286 |
8.82e-105 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 307.45 E-value: 8.82e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 7 LSHNSSRVTFKELQQIIKMGLVQGNLIPAFASSWLAIVLANHsflssIPQILMMLVGSTLIMGGACALNNYYDQDIDSIM 86
Cdd:PRK04375 1 VSSSSSRATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPP-----LLLLLLTLLGIALVAGAAGALNNYIDRDIDAKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 87 PSKQQRPSVNGKISNRNLLLLSFGMMLVGEALLFAL-NIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSFPGAVPPL 165
Cdd:PRK04375 76 ERTKNRPLVTGRISPREALIFGLVLGVLGFLLLGLFvNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 166 IGWTAIEGNISMVAVALFLVIFCWQPVHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVL---LLPLPLLLND 242
Cdd:PRK04375 156 IGWAAVTGSLSWEALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLlvaVSLLPVLLGM 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518299062 243 LGTTFIILATLLNLGWLYLGLTSFKKDSDqtKWATKMFIYSLNY 286
Cdd:PRK04375 236 AGLLYLVVALLLGAWFLYYAWRLYRKDDR--KWARKLFRYSINY 277
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
17-286 |
5.73e-94 |
|
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: 279.52 E-value: 5.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 17 KELQQIIKMGLVQGNLIPAFASSWLAIvlanHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVN 96
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAP----GGALVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 97 GKISNRNLLLLSFGMMLVGEALLFAL-NIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNI 175
Cdd:TIGR01473 77 GRISPREALAFGLLLGVLGVAILAAFvNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 176 SMVAVALFLVIFCWQPVHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVLLL---PLPLLLNDLGTTFIILAT 252
Cdd:TIGR01473 157 SLGAWLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLpvsLLLAFLGGTGWLYLIVAT 236
|
250 260 270
....*....|....*....|....*....|....
gi 518299062 253 LLNLGWLYLGLTSFKKDSDQTKwATKMFIYSLNY 286
Cdd:TIGR01473 237 LLGALFLYLAFKFYRDPTDRKK-ARKLFKFSLIY 269
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
1-286 |
1.02e-92 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 277.01 E-value: 1.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 1 MNKEQTLSHNSSRVTFKELQQIIKMGLVQGNLIPAFASSWLAIvlanhSFLSSIPQILMMLVGSTLIMGGACALNNYYDQ 80
Cdd:COG0109 1 MSSASASSAASLRSTLRDYLALTKPRIILLLLFTALAGMLLAA-----GGLPDLLLLLLTLLGGALAAGAANALNNYIDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 81 DIDSIMPSKQQRPSVNGKISNRNLLLLSFGMMLVGEALL-FALNIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSFP 159
Cdd:COG0109 76 DIDALMKRTKNRPLPTGRISPREALIFGLVLGVLGLALLaLFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 160 GAVPPLIGWTAIEGNISMVAVALFLVIFCWQPVHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVLLLPLP-- 237
Cdd:COG0109 156 GAMPPLIGWAAVTGSLSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSll 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 518299062 238 -LLLNDLGTTFIILATLLNLGWLYLGLTSFKKDSDqtKWATKMFIYSLNY 286
Cdd:COG0109 236 pYLLGMAGLIYLVVALVLGAWFLYLAVRLYRRPDR--KWARKLFKFSILY 283
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
21-286 |
3.35e-88 |
|
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: 264.30 E-value: 3.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 21 QIIKMGLVQGNLIPAFASSWLAIVLANHSFLssipqILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVNGKIS 100
Cdd:cd13957 2 ELTKPRITLLVLLTALAGYLLAPGGVPDLLL-----LLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 101 NRNLLLLSFGMMLVGEALL-FALNIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVA 179
Cdd:cd13957 77 PKHALIFGLVLGILGLALLaLFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 180 VALFLVIFCWQPVHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVLLL---PLPLLLNDLGTTFIILATLLNL 256
Cdd:cd13957 157 WLLFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVplsLLLYLLGLTGWIYLVVALLLGL 236
|
250 260 270
....*....|....*....|....*....|
gi 518299062 257 GWLYLGLTSFKKDSDqtKWATKMFIYSLNY 286
Cdd:cd13957 237 YFLYLAIKLYRSPDD--KWARKLFFASLIY 264
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
32-284 |
2.05e-50 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 167.02 E-value: 2.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 32 LIPAFASSWLAivlanHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVNGKISNRNLLLLSFGM 111
Cdd:pfam01040 2 LIPALAGLALA-----AGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 112 MLVGEALLFALNIPSGVIGLLGIVGYVsFYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVALFLVIFCWQP 191
Cdd:pfam01040 77 LALGLLLLLLLNPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 192 VHFYALAIKRKDEYSLANIPMLPSVKGFNRTRVSMFIWLVLLL--PLPLLLNDLGTTFIILATLLNLGWLYLGLTSFKKD 269
Cdd:pfam01040 156 AIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALllLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLR 235
|
250
....*....|....*
gi 518299062 270 SDQTKWATKMFIYSL 284
Cdd:pfam01040 236 DPKKDAKAFFFLSSL 250
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
31-189 |
1.97e-23 |
|
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: 96.84 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 31 NLIPAFASSWLAIVLANHsFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVNGKISNRNLLLLSFG 110
Cdd:COG0382 14 GILLLLWPTLWALFLAAG-GLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISLREALLLAIV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518299062 111 MMLVGEALLFALNIPSGVIGLLGIVGyVSFYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVALFLVIFCW 189
Cdd:COG0382 93 LLLLALALALLLNPLTFLLALAALAL-AWAYSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPLSAWLLALAAFLW 170
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
32-189 |
2.98e-19 |
|
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: 85.21 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 32 LIPAFASSWLAivlANHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVNGKISNRNLLLLSFGM 111
Cdd:cd13959 13 LPPALWGLLLA---AGGLPLPLLKLLLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVKEALLFLAVQ 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518299062 112 MLVGEALLFALNIPSGVIGLLGIVGyVSFYSiWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVALFLVIFCW 189
Cdd:cd13959 90 LLLGLALLLQLNPLTILLSPIALLL-VLIYP-LMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPALLLYLAVIFW 165
|
|
| PLN02776 |
PLN02776 |
prenyltransferase |
53-286 |
1.21e-18 |
|
prenyltransferase
Pssm-ID: 215415 Cd Length: 341 Bit Score: 84.80 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 53 SIPQILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVNGKISNRNLLLLSFGMMLVGEALL-FALNIPSGVIGL 131
Cdd:PLN02776 27 DLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVAWAVVVGAAGVALLaYKTNMLTAGLGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 132 LGIVGYVSFYSIWSKRHtVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVALFLVIFCWQPVHFYALAIKRKDEYSLANIP 211
Cdd:PLN02776 107 GNILLYAFVYTPLKQIH-PANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAALYFWQMPHFMALAYMCRDDYAAGGYR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 212 MLPSVKGFNR------TRVSMFIwlvllLPLPLLLNDLGTT---FIILATLLNLGWLYlGLTSFKKDSDQTKwATKMFIY 282
Cdd:PLN02776 186 MLSLADATGRrtalvaLRNCLYL-----APLGFLAYDWGVTsspFALEAALLTAYLAA-SAASFYREPTNAN-ARKMFHG 258
|
....
gi 518299062 283 SLNY 286
Cdd:PLN02776 259 SLLY 262
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
30-189 |
7.65e-18 |
|
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: 81.24 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 30 GNLIPAFASSWLAIVLANHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSImpSKQQRPSVNGKISNRNLLLLSF 109
Cdd:cd13956 7 YTLLYVLAPALAGAALAGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAI--NKPDRPLPSGRLSPRQALAFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 110 GMMLVGEALLFALNIPSGVIGLLGIVGyVSFYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIE-GNISMVAVALFLVIFC 188
Cdd:cd13956 85 ALLLVGLALALALGPLALLLLLAGLLL-GLAYSLGLKRLKLGGWGVLGYATGLALLPGLGAVAaGGLVPLALLLALVFLL 163
|
.
gi 518299062 189 W 189
Cdd:cd13956 164 L 164
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
31-188 |
1.75e-13 |
|
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: 69.07 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 31 NLIPAFASSWLAIVLANHSFLSSIPQILMMLVGST-LIMGGACALNNYYDQDIDSImpSKQQRPSVNGKISNRNLLLLSF 109
Cdd:cd13961 10 NLLMAALAQYLGALFALGPLLSLNDLELLLLFLSVfLIAAAGYIINDYFDVEIDRI--NKPDRPIPSGRISRREALILSI 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518299062 110 GMMLVGEALLFALNIPSGVIGLLGIVGYVsFYSIWSKRHTVWNTVIGSFPGAVPPLIGWtAIEGNISMVAVALFLVIFC 188
Cdd:cd13961 88 LLNALGLILAFLLSPLALLIALLNSLLLW-LYSHKLKRTPLIGNLLVALLTGLPFLFGG-LAAGNLLLIILLLALFAFL 164
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
31-148 |
5.01e-09 |
|
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: 56.05 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 31 NLIPAFASSWLAIVLAnHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSImpSKQQRPSVNGKISNRNLLLLSFG 110
Cdd:cd13964 9 NLFTVPADVLAGAALA-GGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDAR--ERPERPIPSGRVSRGAALALGAG 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 518299062 111 MMLVGEALLFALNIPSGVIGLLgIVGYVSFYSIWSKRH 148
Cdd:cd13964 86 LLAAGVALAALVGRLSGLVALL-LAAAILLYDAWLKHT 122
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
31-187 |
7.95e-08 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 52.65 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 31 NLIPAFASSWLAIVLANHSFLSSIPQILMMLVGStLIMGGACALNNYYDQDIDSImpSKQQRPSVNGKISNRNLLLLSFG 110
Cdd:PRK09573 14 NCIGASIGAIIGYLIASNFKIDLKGIILAALVVF-LVCAGGNVINDIYDIEIDKI--NKPERPIPSGRISLKEAKIFSIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 111 MMLVGEALLFALNIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVIGSfpgavppLIGWTAIEGNIS----MVAVALFLVI 186
Cdd:PRK09573 91 LFIVGLILSIFINIYAFLIALLNSILLYLYAKDLKKTGLIGNLIVAY-------LTGLSFIFGGLAvfnvLRIIILFLCA 163
|
.
gi 518299062 187 F 187
Cdd:PRK09573 164 F 164
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
41-187 |
8.42e-08 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 52.27 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 41 LAIVLAnHSFLSSIPQILMMLVGsTLIMGGACALNNYYDQDIDSImpSKQQRPSVNGKISNRNLLLLSFGMMLVGEALLF 120
Cdd:PRK12884 25 LGAIIA-LGGLPLDEALLGFLTA-FFASGSANALNDYFDYEVDRI--NRPDRPIPSGRISRREALLLAILLFILGLIAAY 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518299062 121 ALN-IPSGVIGLLGIVGYVsfYSIWSKRHTVWNTVIGSFPGAVPPLIGWTAIeGNISMVAVALFLVIF 187
Cdd:PRK12884 101 LISpLAFLVVILVSVLGIL--YNWKLKEYGLIGNLYVAFLTGMTFIFGGIAV-GELNEAVILLAAMAF 165
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
32-203 |
1.09e-07 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 52.36 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 32 LIPAFASSWLaivlaNHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSIMPSKQQRPSVNGKISNRNLLLLSFGM 111
Cdd:PRK12873 26 LIPAGWSLWL-----TPSAPPSLLLLLLIILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLARGKISLKTAYSLLIVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 112 MLVgeALLFALNIPS---------GVIGLLGIVGYVSfysiwSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVal 182
Cdd:PRK12873 101 LLL--SLFVVLSLPQpsrnlclslAFLALPPILIYPS-----AKRWFAYPQAILALCWGFAVLIPWAAAEGSLNGGWP-- 171
|
170 180
....*....|....*....|....*....
gi 518299062 183 flVIFCWQPVHF--------YALAIKRKD 203
Cdd:PRK12873 172 --LLFCWLATLLwtfgfdtvYAMADRRDD 198
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
71-189 |
6.35e-06 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 237242 Cd Length: 291 Bit Score: 46.92 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 71 ACALNNYYDQDIDSIMPSKQQRPSVNGKISNRNLLL--LSFGMMLVGEA-----LLFALNIPsgvigLLGIVGYVSFYsi 143
Cdd:PRK12874 63 AMAFNRLVDRDIDKDNPRTANRPSVDGRISVKSMVLfiVLNALIFIGVSyfinpLAFKLSFP-----FLIVLGGYSYF-- 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 518299062 144 wsKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVALFLVIFCW 189
Cdd:PRK12874 136 --KRFSSLAHLVLGLSLGLAPIAGVVAVLGEIPLWSVFLALGVMFW 179
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
57-189 |
1.97e-05 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 45.45 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 57 ILMMLVGS-TLIMGgacaLNNYYDQDIDSIMPSKQQRPSVNGKISNRNLLL---LSFGMMLVGEALLFALNIPSGVIGLL 132
Cdd:PRK12886 47 ILMAMVGArTAAMG----FNRLIDAEIDARNPRTAGRAIPAGLISKGSAILfivLSSLLMLFAAWFLNPLCLYLSPPALF 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 518299062 133 GIVGYVsfysiWSKRHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVALFLVIFCW 189
Cdd:PRK12886 123 FLLLYS-----YCKRFTALAHVVLGFCLALAPLGAWIAIRGTIELPAILLGLAVLFW 174
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
35-187 |
4.33e-05 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 44.19 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 35 AFASSWLAI--VLANHSFLSSIPQILMMLVGSTLIMGGACALNNYYDQDIDSImpSKQQRPSVNGKISNRNLLLLSFGMM 112
Cdd:PRK12882 16 AVVAGVAAFigAFIAGGILSSPSLTGLAFAAVFLATGAGNAINDYFDREIDRI--NRPDRPIPSGAVSPRGALAFSILLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 113 LVGEALLFALNIPSGVIGLLGIVGYVSFYSIWSKRHTVWNTVI----GS---FPGAVpplIGWTAIEGNISMVAVAlFLV 185
Cdd:PRK12882 94 AAGVALAFLLPPLCLAIALFNSLLLVLYAETLKGTPGLGNASVayltGStflFGGAA---VGTEGLLALLVLFALA-ALA 169
|
..
gi 518299062 186 IF 187
Cdd:PRK12882 170 TL 171
|
|
| ubiA |
PRK12888 |
4-hydroxybenzoate octaprenyltransferase; |
70-189 |
7.27e-05 |
|
4-hydroxybenzoate octaprenyltransferase;
Pssm-ID: 183814 Cd Length: 284 Bit Score: 43.56 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 70 GACALNNYYDQDIDSIMPSKQQRPSVNGKISNRN---LLLLSFGMMLVGEALLFALNIPSGVIGLLGIVGYVsfysiWSK 146
Cdd:PRK12888 54 FAMAANRIIDREIDARNPRTAGRELVTGAVSVRTawtGALVALAVFLGAAALLNPLCLALAPLAVAPLVVYP-----YAK 128
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 518299062 147 RHTVWNTVIGSFPGAVPPLIGWTAIEGNISMVAVALFLVIFCW 189
Cdd:PRK12888 129 RFTNFPHAILGLAQAVGPVGAWIAVTGTWSWPAVLLGLAVGLW 171
|
|
| PRK07566 |
PRK07566 |
chlorophyll synthase ChlG; |
57-135 |
3.58e-04 |
|
chlorophyll synthase ChlG;
Pssm-ID: 236052 Cd Length: 314 Bit Score: 41.45 E-value: 3.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518299062 57 ILMMLVGSTLIMGGACALNNYYDQDIDSImpSKQQRPSVNGKISNRNLLLLSFGMMLVGEALLFALNIPSGVIGLLGIV 135
Cdd:PRK07566 67 LAGMLLAGPLLCGTSQTLNDYFDREVDAI--NEPYRPIPSGAISLRWVLYLIAVLTVLGLAVAYLLGPWVFLAALLGLF 143
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
32-147 |
4.26e-04 |
|
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: 41.34 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518299062 32 LIPAFASSWLAIVLANHSFLSSIPQI-LMMLVGSTLIMGGACALNNYYD--QDIDSIMPSKQQRPSVNGKISNRNLLLLS 108
Cdd:cd13962 9 LPASLAPVLLGTALAYYLGGFFNWLLfLLALLAALLLQIGVNLANDYFDykKGTDTEPRSGPSRVLVSGLLSPRQVLRAA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 518299062 109 FGMMLV----GEALLFALNIPSGVIGLLGIV-GYvsFYSIWSKR 147
Cdd:cd13962 89 LVLLLLaallGLYLVALGGWLLLLLGLLGILaGY--FYTGGPFP 130
|
|
| |
