|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
1-286 |
4.41e-136 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 386.42 E-value: 4.41e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 1 MMFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGL 80
Cdd:PRK04375 8 ATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 81 ISPGVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDS 160
Cdd:PRK04375 88 ISPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 161 GAAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAV 240
Cdd:PRK04375 168 EALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1228173701 241 SVWWLGMALRGYKvEDDKVWARKLFGFSIIAITALSIMMSVDFMVP 286
Cdd:PRK04375 248 GAWFLYYAWRLYR-KDDRKWARKLFRYSINYLTLLFVALLVDHLLL 292
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
2-286 |
1.56e-120 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 347.12 E-value: 1.56e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 2 MFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLI 81
Cdd:COG0109 15 TLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 82 SPGVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSG 161
Cdd:COG0109 95 SPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 162 AAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAVS 241
Cdd:COG0109 175 ALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1228173701 242 VWWLGMALRGYKVEDDKvWARKLFGFSIIAITALSIMMSVDFMVP 286
Cdd:COG0109 255 AWFLYLAVRLYRRPDRK-WARKLFKFSILYLTLLFLALLVDHLLL 298
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
7-278 |
2.95e-115 |
|
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: 332.87 E-value: 2.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 7 LQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVS 86
Cdd:cd13957 1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 87 LVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAILL 166
Cdd:cd13957 81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 167 AIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAVSVWWLG 246
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLY 240
|
250 260 270
....*....|....*....|....*....|..
gi 1228173701 247 MALRGYKVEDDKvWARKLFGFSIIAITALSIM 278
Cdd:cd13957 241 LAIKLYRSPDDK-WARKLFFASLIYLPLLFLL 271
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
4-282 |
1.29e-100 |
|
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: 296.08 E-value: 1.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 4 KQYLQVTKPGIIFGNLISVIGGFLLASKGS-IDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLIS 82
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGAlVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 83 PGVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGA 162
Cdd:TIGR01473 81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 163 AILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAVSV 242
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1228173701 243 WWLGMALRGYKVEDDKVWARKLFGFSIIAITALSIMMSVD 282
Cdd:TIGR01473 241 LFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLID 280
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
19-270 |
9.19e-53 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 172.80 E-value: 9.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 19 LISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGF 98
Cdd:pfam01040 2 LIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 99 MLLWFgANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAILLAIFSLWQMPHSY 178
Cdd:pfam01040 82 LLLLL-LNPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 179 AIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYkYLVVAAAVSVWWLGMALRGYKVEDDK 258
Cdd:pfam01040 160 ANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGL-YLLLALLLAALALLYAARLLRLRDPK 238
|
250
....*....|..
gi 1228173701 259 VWARKLFGFSII 270
Cdd:pfam01040 239 KDAKAFFFLSSL 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
1-286 |
4.41e-136 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 386.42 E-value: 4.41e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 1 MMFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGL 80
Cdd:PRK04375 8 ATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 81 ISPGVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDS 160
Cdd:PRK04375 88 ISPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 161 GAAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAV 240
Cdd:PRK04375 168 EALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1228173701 241 SVWWLGMALRGYKvEDDKVWARKLFGFSIIAITALSIMMSVDFMVP 286
Cdd:PRK04375 248 GAWFLYYAWRLYR-KDDRKWARKLFRYSINYLTLLFVALLVDHLLL 292
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
2-286 |
1.56e-120 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 347.12 E-value: 1.56e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 2 MFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLI 81
Cdd:COG0109 15 TLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 82 SPGVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSG 161
Cdd:COG0109 95 SPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 162 AAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAVS 241
Cdd:COG0109 175 ALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1228173701 242 VWWLGMALRGYKVEDDKvWARKLFGFSIIAITALSIMMSVDFMVP 286
Cdd:COG0109 255 AWFLYLAVRLYRRPDRK-WARKLFKFSILYLTLLFLALLVDHLLL 298
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
7-278 |
2.95e-115 |
|
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: 332.87 E-value: 2.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 7 LQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVS 86
Cdd:cd13957 1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 87 LVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAILL 166
Cdd:cd13957 81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 167 AIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAVSVWWLG 246
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLY 240
|
250 260 270
....*....|....*....|....*....|..
gi 1228173701 247 MALRGYKVEDDKvWARKLFGFSIIAITALSIM 278
Cdd:cd13957 241 LAIKLYRSPDDK-WARKLFFASLIYLPLLFLL 271
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
4-282 |
1.29e-100 |
|
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: 296.08 E-value: 1.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 4 KQYLQVTKPGIIFGNLISVIGGFLLASKGS-IDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLIS 82
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGAlVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 83 PGVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGA 162
Cdd:TIGR01473 81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 163 AILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAVSV 242
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1228173701 243 WWLGMALRGYKVEDDKVWARKLFGFSIIAITALSIMMSVD 282
Cdd:TIGR01473 241 LFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLID 280
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
19-270 |
9.19e-53 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 172.80 E-value: 9.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 19 LISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGF 98
Cdd:pfam01040 2 LIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 99 MLLWFgANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAILLAIFSLWQMPHSY 178
Cdd:pfam01040 82 LLLLL-LNPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 179 AIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYkYLVVAAAVSVWWLGMALRGYKVEDDK 258
Cdd:pfam01040 160 ANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGL-YLLLALLLAALALLYAARLLRLRDPK 238
|
250
....*....|..
gi 1228173701 259 VWARKLFGFSII 270
Cdd:pfam01040 239 KDAKAFFFLSSL 250
|
|
| PLN02776 |
PLN02776 |
prenyltransferase |
25-290 |
6.68e-38 |
|
prenyltransferase
Pssm-ID: 215415 Cd Length: 341 Bit Score: 136.80 E-value: 6.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 25 GFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGFMLLWFG 104
Cdd:PLN02776 17 GFVLGSGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVAWAVVVGAAGVALLAYK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 105 ANPLACWLGVMGFVVYVGVYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAILLAIFSLWQMPHSYAIAIFR 184
Cdd:PLN02776 97 TNMLTAGLGAGNILLYAFVYT-PLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAALYFWQMPHFMALAYMC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 185 FKDYQAANIPVLPVV-----KGISVAKNHiTLYIIA--------------FAVATLMLTLggyagykYLVVAAAVsvwwl 245
Cdd:PLN02776 176 RDDYAAGGYRMLSLAdatgrRTALVALRN-CLYLAPlgflaydwgvtsspFALEAALLTA-------YLAASAAS----- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1228173701 246 gmalrgYKVEDDKVWARKLFGFSIIAITALSIMMSVDfMVPNSQN 290
Cdd:PLN02776 243 ------FYREPTNANARKMFHGSLLYLPAFMALLLLH-RVPNDNQ 280
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
4-265 |
8.82e-25 |
|
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: 100.30 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 4 KQYLQVTKPGIIFGNLISVIG---GFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGL 80
Cdd:COG0382 1 RAYLRLLRLDRPIGILLLLWPtlwALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 81 ISPGVSLVYATLLGIAGFMLLWFgANPLACWLGVMGFVVyVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDS 160
Cdd:COG0382 81 ISLREALLLAIVLLLLALALALL-LNPLTFLLALAALAL-AWAYSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 161 GAAILLAIFSLWQMphSYAI--AIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAA 238
Cdd:COG0382 159 SAWLLALAAFLWTL--AYDTiyDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLAGLGLLYLLGLL 236
|
250 260
....*....|....*....|....*...
gi 1228173701 239 AVSV-WWLGMALRGYKVEDDKVWARKLF 265
Cdd:COG0382 237 AALLlLYLSQLWLLRPRKKDPARALKLF 264
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
25-174 |
1.09e-21 |
|
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: 91.76 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 25 GFLLASKGSIDYPLFIYTLVGVSLVVAS--GCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGFMLLW 102
Cdd:cd13959 19 GLLLAAGGLPLPLLKLLLLFLLGAFLMRsaGCTINDIADRDIDAKVPRTKNRPLASGAISVKEALLFLAVQLLLGLALLL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1228173701 103 FgANPLACWLGVMGFVVyVGVYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAILLAIFSLWQM 174
Cdd:cd13959 99 Q-LNPLTILLSPIALLL-VLIYP-LMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPALLLYLAVIFWTA 167
|
|
| ubiA_proteo |
TIGR01474 |
4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of ... |
36-243 |
4.53e-15 |
|
4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of integral membrane proteins that condenses para-hydroxybenzoate with any of several polyprenyldiphosphates. Heterologous expression studies suggest that for, many but not all members, the activity seen (e.g. octaprenyltransferase in E. coli) reflects available host isoprenyl pools rather than enzyme specificity. A fairly deep split by both clustering (UPGMA) and phylogenetics (NJ tree) separates this group (mostly Proteobacterial and mitochondrial), with several characterized members, from another group (mostly archaeal and Gram-positive bacterial) lacking characterized members. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 130539 Cd Length: 281 Bit Score: 73.51 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 36 YPLFIYTlVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGFMLLwFGANPLACWLGVM 115
Cdd:TIGR01474 40 YLLGLFT-VGAILMRGAGCVINDIWDRDFDPQVERTKSRPLASGAVSVRQAILFLLVQLLVALGVL-LQLNPLTILLGVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 116 GFVVyVGVYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAILLAIFSLWQMPHSYAIAIFRFKDYQAANIP- 194
Cdd:TIGR01474 118 SLAL-VATYP-FMKRITYWPQLVLGLAFGWGALMGWAAVTGDLSTAAWVLYLANILWTLGYDTIYAMQDKEDDIKIGVKs 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1228173701 195 --------VLPVVKGISvaknhiTLYIIAFAVATLMLTLGgyAGYkYLVVAAAVSVW 243
Cdd:TIGR01474 196 talrfgdnTKPWLGGLY------ALMILLLALAGLIAGLG--PVY-YLGLAAAALLL 243
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
6-278 |
1.58e-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: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 6 YLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVS--LVVASGCVFNNYIDRDIDRKmerTK-NRVLVKGLIS 82
Cdd:cd13961 2 YLELIRPPNLLMAALAQYLGALFALGPLLSLNDLELLLLFLSvfLIAAAGYIINDYFDVEIDRI---NKpDRPIPSGRIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 83 PGVSLVYATLLGIAGFMLlwfganplACWLGVMGFVVYVGV------YSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTG 156
Cdd:cd13961 79 RREALILSILLNALGLIL--------AFLLSPLALLIALLNslllwlYSHKLKRTPLIGNLLVALLTGLPFLFGGLAAGN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 157 DFdsGAAILLAIFSlwqmphsYAIAIFR--FKDYQ------AANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGY 228
Cdd:cd13961 151 LL--LIILLLALFA-------FLITLGReiVKDIEdvegdrAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPYLLGG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1228173701 229 AGYKYLVVAAAVSVWWLGMALRGYKVEDDKVWARKLFGFsIIAITALSIM 278
Cdd:cd13961 222 LGILYLILIIIADLLFLYSAIRLAKSPKDYSKLSKLLKL-AMLLGLLAFL 270
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
7-278 |
4.55e-13 |
|
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: 67.76 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 7 LQVTKPGIIFGNLISVIGGFLLASKGSIDYP-LFIYTLVGVSLVVASGCVFNNYIDRDIDRkmERTKNRVLVKGLISPGV 85
Cdd:cd13956 1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLPaLLLLALLAVFLGAGAGYALNDYTDRELDA--INKPDRPLPSGRLSPRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 86 SLVYATLLGIAGFmLLWFGANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAIL 165
Cdd:cd13956 79 ALAFAAALLLVGL-ALALALGPLALLLLLAGLLLGL-AYSLGLKRLKLGGWGVLGYATGLALLPGLGAVAAGGLVPLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 166 LAIFSLWQMPHSYAIAIFRFKDY-QAANIPVLPVVKGISVAK-NHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAVSVW 243
Cdd:cd13956 157 LALVFLLLGLGINLYNDLPDVEGdRAAGIRTLPVRLGPRRARrLAAGLLLAALILVVLLAVAGLLGPLALLALLAVALLA 236
|
250 260 270
....*....|....*....|....*....|....*
gi 1228173701 244 WLGMALRGYKVEDDKVWARKLFGFSIIAITALSIM 278
Cdd:cd13956 237 LRARFARADRLPALPRGFLLLAVYRLLLFAALLLA 271
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
56-157 |
1.88e-09 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 237242 Cd Length: 291 Bit Score: 57.32 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 56 FNNYIDRDIDRKMERTKNRVLVKGLISPGvSLVYATLLGIAGFMLLWFGANPLACWLGVMgFVVYVGVYSlYMKRHSVYG 135
Cdd:PRK12874 66 FNRLVDRDIDKDNPRTANRPSVDGRISVK-SMVLFIVLNALIFIGVSYFINPLAFKLSFP-FLIVLGGYS-YFKRFSSLA 142
|
90 100
....*....|....*....|..
gi 1228173701 136 TLIGSLSGAAPPVIGYCAVTGD 157
Cdd:PRK12874 143 HLVLGLSLGLAPIAGVVAVLGE 164
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
4-256 |
5.09e-09 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 56.12 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 4 KQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVsLVVASGCVFNNYIDRDIDRKmERTkNRVLVKGLISP 83
Cdd:PRK12884 5 KAYLELLRPEHGLMAGIAVVLGAIIALGGLPLDEALLGFLTAF-FASGSANALNDYFDYEVDRI-NRP-DRPIPSGRISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 84 GVSLVYATLLGIAGFMLLWFgANPLACwLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDsgAA 163
Cdd:PRK12884 82 REALLLAILLFILGLIAAYL-ISPLAF-LVVILVSVLGILYNWKLKEYGLIGNLYVAFLTGMTFIFGGIAVGELNE--AV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 164 ILLAIFS-LWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLTLGGYAGYKYLVVAAAVSV 242
Cdd:PRK12884 158 ILLAAMAfLMTLGREIMKDIEDVEGDRLRGARTLAILYGEKIAGRIAAALFILAVLLSPLPYLFGIFNILYLAPVLVADL 237
|
250
....*....|....*..
gi 1228173701 243 WWL---GMALRGYKVED 256
Cdd:PRK12884 238 IFLysaYSLLRSQDRET 254
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
18-183 |
1.05e-07 |
|
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: 52.20 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 18 NLISVIG----GFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKmERtKNRVLVKGLISPGVSLVYATLL 93
Cdd:cd13964 9 NLFTVPAdvlaGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDAR-ER-PERPIPSGRVSRGAALALGAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 94 GIAGFMLLWF-GANPLACWLGVMGFVVyvgVYSLYMKRHSvygtligslsgAAPPVIGYCAVtGDFDSGAAILLAIFSLW 172
Cdd:cd13964 87 LAAGVALAALvGRLSGLVALLLAAAIL---LYDAWLKHTP-----------LGPLLMGLCRG-LNLLLGASAAAAGGLGP 151
|
170
....*....|.
gi 1228173701 173 QMPHSYAIAIF 183
Cdd:cd13964 152 ALLAALALGVY 162
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
7-275 |
1.60e-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: 51.36 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 7 LQVTKPGIIFGNLISVIGGFLLASK--GSIDYPLFIYTLVGVSLVVASGCVFNNYID--RDIDRKMERTKNRVLVKGLIS 82
Cdd:cd13962 1 LLAARPRTLPASLAPVLLGTALAYYlgGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRSGPSRVLVSGLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 83 PGVSLVYATLLGIAGFML---LWFGANPLACWLGVMGFVVYVGvYSLYMKRHSVYG---TLIGSLSGAAPPVIGYCAVTG 156
Cdd:cd13962 81 PRQVLRAALVLLLLAALLglyLVALGGWLLLLLGLLGILAGYF-YTGGPFPLSYRGlgeLFVFLFFGLLAVLGTYYVQTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 157 DFDSGAAILLAIFSLWqmphSYAIAI---FRfkDYQ---AANIPVLPVVKGISVAKN-HITLYIIAFAVATLMLTLGGYA 229
Cdd:cd13962 160 SLSWEVLLAALPLGLL----IAAILLannIR--DIEadrAAGKRTLAVRLGRKRARRlYAALLLLAYLLLLLLVLLGLLP 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1228173701 230 GYKYLVVAAAVSVWWLGMALRGYKVEDDKVWARKLFGFSIIAITAL 275
Cdd:cd13962 234 LWSLLALLSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLL 279
|
|
| PLN02809 |
PLN02809 |
4-hydroxybenzoate nonaprenyltransferase |
27-159 |
4.86e-07 |
|
4-hydroxybenzoate nonaprenyltransferase
Pssm-ID: 178405 Cd Length: 289 Bit Score: 50.07 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 27 LLASKGSI-DYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISP--GVSLVYATLLGIAGFMLlwf 103
Cdd:PLN02809 34 LAAPPGSLpDLKMLALFGCGALLLRGAGCTINDLLDRDIDKKVERTKLRPIASGALTPfqGVGFLGAQLLLGLGILL--- 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1228173701 104 GANPLACWLGVMGFVVyVGVYSLyMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFD 159
Cdd:PLN02809 111 QLNNYSRILGASSLLL-VFTYPL-MKRFTFWPQAFLGLTFNWGALLGWAAVKGSLD 164
|
|
| ubiA |
PRK12888 |
4-hydroxybenzoate octaprenyltransferase; |
57-249 |
1.23e-06 |
|
4-hydroxybenzoate octaprenyltransferase;
Pssm-ID: 183814 Cd Length: 284 Bit Score: 48.95 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 57 NNYIDRDIDRKMERTKNRVLVKGLIS-----PGVSLVYATLLGIAGFMllwfgaNPLACWLGVMGFVVYVgVYSlYMKRH 131
Cdd:PRK12888 59 NRIIDREIDARNPRTAGRELVTGAVSvrtawTGALVALAVFLGAAALL------NPLCLALAPLAVAPLV-VYP-YAKRF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 132 SVYGTLIGSLSGAAPPVIGYCAVTGDFDSGAAILLAIFSLWqmphsyaIA----IFRFKDYQA---ANIPVLPVVKGISV 204
Cdd:PRK12888 131 TNFPHAILGLAQAVGPVGAWIAVTGTWSWPAVLLGLAVGLW-------IGgfdlIYACQDAEVdrrIGVRSVPARFGVRA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1228173701 205 AknhitlyiIAFAVATLMLTLGGYAGYKYLVVAAAvsVWWLGMAL 249
Cdd:PRK12888 204 A--------LWASRVAHVVTFALFVWFGLAVGFGA--LWWIGLAI 238
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
56-168 |
1.72e-06 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 48.53 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 56 FNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYaTLLGIAGFMLLWFGANPLACWLGVMGFVVYVGvYSlYMKRHSVYG 135
Cdd:PRK12886 61 FNRLIDAEIDARNPRTAGRAIPAGLISKGSAILF-IVLSSLLMLFAAWFLNPLCLYLSPPALFFLLL-YS-YCKRFTALA 137
|
90 100 110
....*....|....*....|....*....|...
gi 1228173701 136 TLIGSLSGAAPPVIGYCAVTGDFDSgAAILLAI 168
Cdd:PRK12886 138 HVVLGFCLALAPLGAWIAIRGTIEL-PAILLGL 169
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
43-101 |
2.74e-05 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 44.65 E-value: 2.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 43 LVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVS-LVYATLLGIAGFMLL 101
Cdd:PRK12873 50 ILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLARGKISLKTAySLLIVLLLLSLFVVL 109
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
1-172 |
4.59e-05 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 44.18 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 1 MMFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKmeRTKNRVLVKGL 80
Cdd:PRK09573 1 MSIKAYFELIRPKNCIGASIGAIIGYLIASNFKIDLKGIILAALVVFLVCAGGNVINDIYDIEIDKI--NKPERPIPSGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 81 ISPGVSLVYATLLGIAGFMLLWFGAnpLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGDFDS 160
Cdd:PRK09573 79 ISLKEAKIFSITLFIVGLILSIFIN--IYAFLIALLNSILLYLYAKDLKKTGLIGNLIVAYLTGLSFIFGGLAVFNVLRI 156
|
170
....*....|..
gi 1228173701 161 GAAILLAIFSLW 172
Cdd:PRK09573 157 IILFLCAFFSTW 168
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
6-143 |
1.19e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 42.65 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 6 YLQVTKPG-IIFGNLISVIGGFLlaSKGSIDYPLFIYTLVG-VSLVVASGCVFNNYIDRDIDRKMErtKNRVLVKGLISP 83
Cdd:PRK12882 7 YLELTRPVnAVVAGVAAFIGAFI--AGGILSSPSLTGLAFAaVFLATGAGNAINDYFDREIDRINR--PDRPIPSGAVSP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228173701 84 GVSLVYATLLGIAGfMLLWFGANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTL-IGSLSG 143
Cdd:PRK12882 83 RGALAFSILLFAAG-VALAFLLPPLCLAIALFNSLLLV-LYAETLKGTPGLGNAsVAYLTG 141
|
|
| PT_UbiA_2 |
cd13963 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
27-130 |
2.00e-04 |
|
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: 260126 Cd Length: 278 Bit Score: 42.08 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 27 LLASKGSIDYPLFIYTLVGV---SLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGFMLLWF 103
Cdd:cd13963 20 LLFAGQLFDPDLLLAALLAFvafCLAASAVYILNDLLDLEADRLHPTKRNRPIASGRLSIPAALALAVVLLLAGLALALL 99
|
90 100
....*....|....*....|....*..
gi 1228173701 104 gaNPLACWLGVMGFVVYVGVYSLYMKR 130
Cdd:cd13963 100 --LSPAFLLVLLAYLVLNLAYSLKLKR 124
|
|
| ubiA |
PRK12876 |
prenyltransferase; Reviewed |
51-130 |
3.05e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 237244 Cd Length: 300 Bit Score: 41.66 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 51 ASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGFMLLWFgANPLACWLGVMGFVVYVgVYSlYMKR 130
Cdd:PRK12876 61 TVGIIVNQIIDCAIDKKNPRTSSRVLPAKLLSINFSMLLLTLCSFLFLSLCWL-LNPLCFSLAVLSTLLMI-IYP-YTKR 137
|
|
| PRK08238 |
PRK08238 |
UbiA family prenyltransferase; |
44-131 |
3.46e-04 |
|
UbiA family prenyltransferase;
Pssm-ID: 236195 [Multi-domain] Cd Length: 479 Bit Score: 41.78 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 44 VGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGFMLLWFGanPLACWLGVMGFVVYVGV 123
Cdd:PRK08238 233 LAFSLCASAVYILNDLLDLEADRAHPRKRRRPFASGALPIPFGLAAAPLLLLAGLALALAL--GPAFLLVLLAYLALTLA 310
|
....*...
gi 1228173701 124 YSLYMKRH 131
Cdd:PRK08238 311 YSLRLKRK 318
|
|
| PRK12324 |
PRK12324 |
decaprenyl-phosphate phosphoribosyltransferase; |
47-129 |
7.60e-04 |
|
decaprenyl-phosphate phosphoribosyltransferase;
Pssm-ID: 237058 Cd Length: 295 Bit Score: 40.23 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 47 SLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPGVSLVYATLLGIAGFMLLWFGANPLACWLgvmgfVVYVGV--- 123
Cdd:PRK12324 56 CLASSAVYLVNDIRDVEADRLHPTKRNRPIASGVVSVSLAYILAVVLLVASLALAYLLSPKLALVL-----LVYLVLnla 130
|
....*.
gi 1228173701 124 YSLYMK 129
Cdd:PRK12324 131 YSFKLK 136
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
1-154 |
8.52e-04 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 40.10 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 1 MMFKQYLQVTKP-GIIFGNLISVIGGfLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDrKMERtKNRVLVKG 79
Cdd:PRK12883 1 MELKAFIEITRPhNCILAGIVGILGS-LVALGGIPPIKTLILIFLVVYLGCSGGNTINDYFDYEID-KINR-PNRPLPRG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1228173701 80 LISPGVSLVYATLLGIAGFMLLWFganpLACWLGVMGFVVYVG--VYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAV 154
Cdd:PRK12883 78 AMSRKAALYYSLLLFAVGLALAYL----INIEAFLFALGAYVLmfLYAWKLKPLPFIGNVVVALLTGATPIYGAIAV 150
|
|
| ubiA |
PRK13106 |
prenyltransferase; Reviewed |
25-145 |
2.36e-03 |
|
prenyltransferase; Reviewed
Pssm-ID: 237283 Cd Length: 300 Bit Score: 38.94 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 25 GFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLIspgvSLVYATLLGIAGFMLLWFG 104
Cdd:PRK13106 37 GAFVAIKGIPPISTLILIFLALFFLRTAGMTNDNLADLEIDAKNPRTKNRPLVTGAI----KISEAKALITAGLILFFAS 112
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1228173701 105 ANPLACWLGVMGFVVYVGVYSL-YMKR-HSVYGTLIGSLSGAA 145
Cdd:PRK13106 113 AYLVNRWALLLSPIVALIAMSYpYMKRyTAFANYHLASIQGLA 155
|
|
| ubiA |
PRK05951 |
prenyltransferase; Reviewed |
32-122 |
7.51e-03 |
|
prenyltransferase; Reviewed
Pssm-ID: 180323 Cd Length: 296 Bit Score: 37.45 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228173701 32 GSIDYPLFIYTLVGVSLVVASGCVFNNYID--RDID-RKMERTKNRVLVKGLISPGVSLVYATLLGIAGFMLLWF----- 103
Cdd:PRK05951 35 RSFDPLLGALMLLGYFLLHASLNVFNDYKDyvLDCDhHETTGYRQHPIQAGIMTLGHLRVLGIALGAIALQLGWSlvldr 114
|
90 100
....*....|....*....|.
gi 1228173701 104 --GANPLAcWLGVMGFVVYVG 122
Cdd:PRK05951 115 giGAVTLA-LLGVFLWTCYMG 134
|
|
| |
