|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
1-286 |
8.84e-135 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 383.34 E-value: 8.84e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 1 MMFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGL 80
Cdd:PRK04375 8 ATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 81 ISPAVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDS 160
Cdd:PRK04375 88 ISPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 161 GAAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAV 240
Cdd:PRK04375 168 EALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 83288463 241 SVWWLGMALRGYKvADDRIWARKLFGFSIIAITALSVMMSVDFMVP 286
Cdd:PRK04375 248 GAWFLYYAWRLYR-KDDRKWARKLFRYSINYLTLLFVALLVDHLLL 292
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
2-286 |
2.56e-118 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 341.73 E-value: 2.56e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 2 MFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLI 81
Cdd:COG0109 15 TLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 82 SPAVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSG 161
Cdd:COG0109 95 SPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 162 AAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVS 241
Cdd:COG0109 175 ALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 83288463 242 VWWLGMALRGYKVADDRiWARKLFGFSIIAITALSVMMSVDFMVP 286
Cdd:COG0109 255 AWFLYLAVRLYRRPDRK-WARKLFKFSILYLTLLFLALLVDHLLL 298
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
7-278 |
5.30e-113 |
|
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: 327.09 E-value: 5.30e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 7 LQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVS 86
Cdd:cd13957 1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 87 LVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILL 166
Cdd:cd13957 81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 167 AIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSVWWLG 246
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLY 240
|
250 260 270
....*....|....*....|....*....|..
gi 83288463 247 MALRGYKVADDRiWARKLFGFSIIAITALSVM 278
Cdd:cd13957 241 LAIKLYRSPDDK-WARKLFFASLIYLPLLFLL 271
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
4-282 |
1.67e-98 |
|
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: 290.69 E-value: 1.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 4 KQYLQVTKPGIIFGNLISVIGGFLLASKGS-IDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLIS 82
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGAlVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 83 PAVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGA 162
Cdd:TIGR01473 81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 163 AILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSV 242
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 83288463 243 WWLGMALRGYKVADDRIWARKLFGFSIIAITALSVMMSVD 282
Cdd:TIGR01473 241 LFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLID 280
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
19-270 |
1.58e-50 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 167.02 E-value: 1.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 19 LISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGF 98
Cdd:pfam01040 2 LIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 99 MLLWFgANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILLAIFSLWQMPHSY 178
Cdd:pfam01040 82 LLLLL-LNPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 179 AIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYkYLVVAAAVSVWWLGMALRGYKVADDR 258
Cdd:pfam01040 160 ANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGL-YLLLALLLAALALLYAARLLRLRDPK 238
|
250
....*....|..
gi 83288463 259 IWARKLFGFSII 270
Cdd:pfam01040 239 KDAKAFFFLSSL 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
1-286 |
8.84e-135 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 383.34 E-value: 8.84e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 1 MMFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGL 80
Cdd:PRK04375 8 ATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 81 ISPAVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDS 160
Cdd:PRK04375 88 ISPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 161 GAAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAV 240
Cdd:PRK04375 168 EALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 83288463 241 SVWWLGMALRGYKvADDRIWARKLFGFSIIAITALSVMMSVDFMVP 286
Cdd:PRK04375 248 GAWFLYYAWRLYR-KDDRKWARKLFRYSINYLTLLFVALLVDHLLL 292
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
2-286 |
2.56e-118 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 341.73 E-value: 2.56e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 2 MFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLI 81
Cdd:COG0109 15 TLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 82 SPAVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSG 161
Cdd:COG0109 95 SPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 162 AAILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVS 241
Cdd:COG0109 175 ALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 83288463 242 VWWLGMALRGYKVADDRiWARKLFGFSIIAITALSVMMSVDFMVP 286
Cdd:COG0109 255 AWFLYLAVRLYRRPDRK-WARKLFKFSILYLTLLFLALLVDHLLL 298
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
7-278 |
5.30e-113 |
|
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: 327.09 E-value: 5.30e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 7 LQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVS 86
Cdd:cd13957 1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 87 LVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILL 166
Cdd:cd13957 81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 167 AIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSVWWLG 246
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLY 240
|
250 260 270
....*....|....*....|....*....|..
gi 83288463 247 MALRGYKVADDRiWARKLFGFSIIAITALSVM 278
Cdd:cd13957 241 LAIKLYRSPDDK-WARKLFFASLIYLPLLFLL 271
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
4-282 |
1.67e-98 |
|
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: 290.69 E-value: 1.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 4 KQYLQVTKPGIIFGNLISVIGGFLLASKGS-IDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLIS 82
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGAlVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 83 PAVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGA 162
Cdd:TIGR01473 81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 163 AILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSV 242
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 83288463 243 WWLGMALRGYKVADDRIWARKLFGFSIIAITALSVMMSVD 282
Cdd:TIGR01473 241 LFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLID 280
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
19-270 |
1.58e-50 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 167.02 E-value: 1.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 19 LISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGF 98
Cdd:pfam01040 2 LIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 99 MLLWFgANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILLAIFSLWQMPHSY 178
Cdd:pfam01040 82 LLLLL-LNPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 179 AIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYkYLVVAAAVSVWWLGMALRGYKVADDR 258
Cdd:pfam01040 160 ANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGL-YLLLALLLAALALLYAARLLRLRDPK 238
|
250
....*....|..
gi 83288463 259 IWARKLFGFSII 270
Cdd:pfam01040 239 KDAKAFFFLSSL 250
|
|
| PLN02776 |
PLN02776 |
prenyltransferase |
25-199 |
9.35e-38 |
|
prenyltransferase
Pssm-ID: 215415 Cd Length: 341 Bit Score: 136.41 E-value: 9.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 25 GFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLWFG 104
Cdd:PLN02776 17 GFVLGSGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVAWAVVVGAAGVALLAYK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 105 ANPLACWLGVMGFVVYVGVYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILLAIFSLWQMPHSYAIAIFR 184
Cdd:PLN02776 97 TNMLTAGLGAGNILLYAFVYT-PLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAALYFWQMPHFMALAYMC 175
|
170
....*....|....*
gi 83288463 185 FKDYQAANIPVLPVV 199
Cdd:PLN02776 176 RDDYAAGGYRMLSLA 190
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
4-265 |
3.18e-24 |
|
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: 98.76 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 4 KQYLQVTKPGIIFGNLISVIG---GFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGL 80
Cdd:COG0382 1 RAYLRLLRLDRPIGILLLLWPtlwALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 81 ISPAVSLVYATLLGIAGFMLLWFgANPLACWLGVMGFVVyVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDS 160
Cdd:COG0382 81 ISLREALLLAIVLLLLALALALL-LNPLTFLLALAALAL-AWAYSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 161 GAAILLAIFSLWQMphSYAI--AIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAA 238
Cdd:COG0382 159 SAWLLALAAFLWTL--AYDTiyDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLAGLGLLYLLGLL 236
|
250 260
....*....|....*....|....*...
gi 83288463 239 AVSV-WWLGMALRGYKVADDRIWARKLF 265
Cdd:COG0382 237 AALLlLYLSQLWLLRPRKKDPARALKLF 264
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
25-174 |
4.46e-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: 90.22 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 25 GFLLASKGSIDYPLFIYTLVGVSLVVAS--GCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLW 102
Cdd:cd13959 19 GLLLAAGGLPLPLLKLLLLFLLGAFLMRsaGCTINDIADRDIDAKVPRTKNRPLASGAISVKEALLFLAVQLLLGLALLL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83288463 103 FgANPLACWLGVMGFVVyVGVYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILLAIFSLWQM 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 |
5.34e-14 |
|
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: 70.42 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 36 YPLFIYTlVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLwFGANPLACWLGVM 115
Cdd:TIGR01474 40 YLLGLFT-VGAILMRGAGCVINDIWDRDFDPQVERTKSRPLASGAVSVRQAILFLLVQLLVALGVL-LQLNPLTILLGVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 116 GFVVyVGVYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILLAIFSLWQMPHSYAIAIFRFKDYQAANIP- 194
Cdd:TIGR01474 118 SLAL-VATYP-FMKRITYWPQLVLGLAFGWGALMGWAAVTGDLSTAAWVLYLANILWTLGYDTIYAMQDKEDDIKIGVKs 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 83288463 195 --------VLPVVKGISvaknhiTLYIIAFAVATLMLSLGgyAGYkYLVVAAAVSVW 243
Cdd:TIGR01474 196 talrfgdnTKPWLGGLY------ALMILLLALAGLIAGLG--PVY-YLGLAAAALLL 243
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
6-271 |
1.12e-12 |
|
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: 66.76 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 6 YLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVS--LVVASGCVFNNYIDRDIDRKmerTK-NRVLVKGLIS 82
Cdd:cd13961 2 YLELIRPPNLLMAALAQYLGALFALGPLLSLNDLELLLLFLSvfLIAAAGYIINDYFDVEIDRI---NKpDRPIPSGRIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 83 PAVSLVYATLLGIAGFMLLWFGanPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGycAVTGEFDSGA 162
Cdd:cd13961 79 RREALILSILLNALGLILAFLL--SPLALLIALLNSLLLWLYSHKLKRTPLIGNLLVALLTGLPFLFG--GLAAGNLLLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 163 AILLAIFSlwqmphsYAIAIFR--FKDYQ------AANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYL 234
Cdd:cd13961 155 ILLLALFA-------FLITLGReiVKDIEdvegdrAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPYLLGGLGILYL 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 83288463 235 VVAAAVSVWWLGMALRGYKVADDRIWARKLFGFSIIA 271
Cdd:cd13961 228 ILIIIADLLFLYSAIRLAKSPKDYSKLSKLLKLAMLL 264
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
7-278 |
6.01e-12 |
|
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: 64.68 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 7 LQVTKPGIIFGNLISVIGGFLLASKGSIDYP-LFIYTLVGVSLVVASGCVFNNYIDRDIDRkmERTKNRVLVKGLISPAV 85
Cdd:cd13956 1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLPaLLLLALLAVFLGAGAGYALNDYTDRELDA--INKPDRPLPSGRLSPRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 86 SLVYATLLGIAGFmLLWFGANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDSGAAIL 165
Cdd:cd13956 79 ALAFAAALLLVGL-ALALALGPLALLLLLAGLLLGL-AYSLGLKRLKLGGWGVLGYATGLALLPGLGAVAAGGLVPLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 166 LAIFSLWQMPHSYAIAIFRFKDY-QAANIPVLPVVKGISVAK-NHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSVW 243
Cdd:cd13956 157 LALVFLLLGLGINLYNDLPDVEGdRAAGIRTLPVRLGPRRARrLAAGLLLAALILVVLLAVAGLLGPLALLALLAVALLA 236
|
250 260 270
....*....|....*....|....*....|....*
gi 83288463 244 WLGMALRGYKVADDRIWARKLFGFSIIAITALSVM 278
Cdd:cd13956 237 LRARFARADRLPALPRGFLLLAVYRLLLFAALLLA 271
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
56-157 |
2.17e-09 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 237242 Cd Length: 291 Bit Score: 57.32 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 56 FNNYIDRDIDRKMERTKNRVLVKGLISpAVSLVYATLLGIAGFMLLWFGANPLACWLGVMgFVVYVGVYSlYMKRHSVYG 135
Cdd:PRK12874 66 FNRLVDRDIDKDNPRTANRPSVDGRIS-VKSMVLFIVLNALIFIGVSYFINPLAFKLSFP-FLIVLGGYS-YFKRFSSLA 142
|
90 100
....*....|....*....|..
gi 83288463 136 TLIGSLSGAAPPVIGYCAVTGE 157
Cdd:PRK12874 143 HLVLGLSLGLAPIAGVVAVLGE 164
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
4-258 |
1.51e-08 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 54.58 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 4 KQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVsLVVASGCVFNNYIDRDIDRKmeRTKNRVLVKGLISP 83
Cdd:PRK12884 5 KAYLELLRPEHGLMAGIAVVLGAIIALGGLPLDEALLGFLTAF-FASGSANALNDYFDYEVDRI--NRPDRPIPSGRISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 84 AVSLVYATLLGIAGFMLLWFgANPLACwLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDsgAA 163
Cdd:PRK12884 82 REALLLAILLFILGLIAAYL-ISPLAF-LVVILVSVLGILYNWKLKEYGLIGNLYVAFLTGMTFIFGGIAVGELNE--AV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 164 ILLAIFS-LWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSV 242
Cdd:PRK12884 158 ILLAAMAfLMTLGREIMKDIEDVEGDRLRGARTLAILYGEKIAGRIAAALFILAVLLSPLPYLFGIFNILYLAPVLVADL 237
|
250
....*....|....*.
gi 83288463 243 WWLGMALRGYKVADDR 258
Cdd:PRK12884 238 IFLYSAYSLLRSQDRE 253
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
7-275 |
4.66e-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: 50.20 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 7 LQVTKPGIIFGNLISVIGGFLLASK--GSIDYPLFIYTLVGVSLVVASGCVFNNYID--RDIDRKMERTKNRVLVKGLIS 82
Cdd:cd13962 1 LLAARPRTLPASLAPVLLGTALAYYlgGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRSGPSRVLVSGLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 83 PAVSLVYATLLGIAGFML---LWFGANPLACWLGVMGFVVYVGvYSLYMKRHSVYG---TLIGSLSGAAPPVIGYCAVTG 156
Cdd:cd13962 81 PRQVLRAALVLLLLAALLglyLVALGGWLLLLLGLLGILAGYF-YTGGPFPLSYRGlgeLFVFLFFGLLAVLGTYYVQTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 157 EFDSGAAILLAIFSLWqmphSYAIAI---FRfkDYQ---AANIPVLPVVKGISVAKN-HITLYIIAFAVATLMLSLGGYA 229
Cdd:cd13962 160 SLSWEVLLAALPLGLL----IAAILLannIR--DIEadrAAGKRTLAVRLGRKRARRlYAALLLLAYLLLLLLVLLGLLP 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 83288463 230 GYKYLVVAAAVSVWWLGMALRGYKVADDRIWARKLFGFSIIAITAL 275
Cdd:cd13962 234 LWSLLALLSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLL 279
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
18-132 |
1.46e-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: 48.73 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 18 NLISVIG----GFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKmERtKNRVLVKGLISPAVSLVYATLL 93
Cdd:cd13964 9 NLFTVPAdvlaGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDAR-ER-PERPIPSGRVSRGAALALGAGL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 83288463 94 GIAGFMLLWF-GANPLACWLGVMGFVVyvgVYSLYMKRHS 132
Cdd:cd13964 87 LAAGVALAALvGRLSGLVALLLAAAIL---LYDAWLKHTP 123
|
|
| PLN02809 |
PLN02809 |
4-hydroxybenzoate nonaprenyltransferase |
27-159 |
1.75e-06 |
|
4-hydroxybenzoate nonaprenyltransferase
Pssm-ID: 178405 Cd Length: 289 Bit Score: 48.53 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 27 LLASKGSI-DYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVY---------ATLLGIA 96
Cdd:PLN02809 34 LAAPPGSLpDLKMLALFGCGALLLRGAGCTINDLLDRDIDKKVERTKLRPIASGALTPFQGVGFlgaqlllglGILLQLN 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83288463 97 GFMLLWfGANPLAcwlgvmgfvvYVGVYSLyMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFD 159
Cdd:PLN02809 114 NYSRIL-GASSLL----------LVFTYPL-MKRFTFWPQAFLGLTFNWGALLGWAAVKGSLD 164
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
56-168 |
6.44e-06 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 46.61 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 56 FNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYaTLLGIAGFMLLWFGANPLACWLGVMGFVVYVGvYSlYMKRHSVYG 135
Cdd:PRK12886 61 FNRLIDAEIDARNPRTAGRAIPAGLISKGSAILF-IVLSSLLMLFAAWFLNPLCLYLSPPALFFLLL-YS-YCKRFTALA 137
|
90 100 110
....*....|....*....|....*....|...
gi 83288463 136 TLIGSLSGAAPPVIGYCAVTGEFDSgAAILLAI 168
Cdd:PRK12886 138 HVVLGFCLALAPLGAWIAIRGTIEL-PAILLGL 169
|
|
| ubiA |
PRK12888 |
4-hydroxybenzoate octaprenyltransferase; |
57-249 |
1.90e-05 |
|
4-hydroxybenzoate octaprenyltransferase;
Pssm-ID: 183814 Cd Length: 284 Bit Score: 45.10 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 57 NNYIDRDIDRKMERTKNRVLVKGlispAVSLVYATLLGIAGFMLLWFGA---NPLACWLGVMGFVVYVgVYSlYMKRHSV 133
Cdd:PRK12888 59 NRIIDREIDARNPRTAGRELVTG----AVSVRTAWTGALVALAVFLGAAallNPLCLALAPLAVAPLV-VYP-YAKRFTN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 134 YGTLIGSLSGAAPPVIGYCAVTGEFDSGAAILLAIFSLWqmphsyaIA----IFRFKDYQA---ANIPVLPVVKGISVAk 206
Cdd:PRK12888 133 FPHAILGLAQAVGPVGAWIAVTGTWSWPAVLLGLAVGLW-------IGgfdlIYACQDAEVdrrIGVRSVPARFGVRAA- 204
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 83288463 207 nhitlyiIAFAVATLMLSLGGYAGYKYLVVAAAvsVWWLGMAL 249
Cdd:PRK12888 205 -------LWASRVAHVVTFALFVWFGLAVGFGA--LWWIGLAI 238
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
43-101 |
2.72e-05 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 45.04 E-value: 2.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83288463 43 LVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLIS--PAVSLVyATLLGIAGFMLL 101
Cdd:PRK12873 50 ILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLARGKISlkTAYSLL-IVLLLLSLFVVL 109
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
1-172 |
4.84e-05 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 44.18 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 1 MMFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKmeRTKNRVLVKGL 80
Cdd:PRK09573 1 MSIKAYFELIRPKNCIGASIGAIIGYLIASNFKIDLKGIILAALVVFLVCAGGNVINDIYDIEIDKI--NKPERPIPSGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 81 ISPAVSLVYATLLGIAGFMLLWFGAnpLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTGEFDS 160
Cdd:PRK09573 79 ISLKEAKIFSITLFIVGLILSIFIN--IYAFLIALLNSILLYLYAKDLKKTGLIGNLIVAYLTGLSFIFGGLAVFNVLRI 156
|
170
....*....|..
gi 83288463 161 GAAILLAIFSLW 172
Cdd:PRK09573 157 IILFLCAFFSTW 168
|
|
| ubiA |
PRK12882 |
prenyltransferase; Reviewed |
6-143 |
2.41e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 183811 Cd Length: 276 Bit Score: 41.88 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 6 YLQVTKPG-IIFGNLISVIGGFLlaSKGSIDYPLFIYTLVG-VSLVVASGCVFNNYIDRDIDRKMErtKNRVLVKGLISP 83
Cdd:PRK12882 7 YLELTRPVnAVVAGVAAFIGAFI--AGGILSSPSLTGLAFAaVFLATGAGNAINDYFDREIDRINR--PDRPIPSGAVSP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83288463 84 AVSLVYATLLGIAGfMLLWFGANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTL-IGSLSG 143
Cdd:PRK12882 83 RGALAFSILLFAAG-VALAFLLPPLCLAIALFNSLLLV-LYAETLKGTPGLGNAsVAYLTG 141
|
|
| PRK08238 |
PRK08238 |
UbiA family prenyltransferase; |
44-131 |
2.42e-04 |
|
UbiA family prenyltransferase;
Pssm-ID: 236195 [Multi-domain] Cd Length: 479 Bit Score: 42.17 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 44 VGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLWFGanPLACWLGVMGFVVYVGV 123
Cdd:PRK08238 233 LAFSLCASAVYILNDLLDLEADRAHPRKRRRPFASGALPIPFGLAAAPLLLLAGLALALAL--GPAFLLVLLAYLALTLA 310
|
....*...
gi 83288463 124 YSLYMKRH 131
Cdd:PRK08238 311 YSLRLKRK 318
|
|
| PT_UbiA_2 |
cd13963 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
27-130 |
3.06e-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: 41.69 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 27 LLASKGSIDYPLFIYTLVGV---SLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLWF 103
Cdd:cd13963 20 LLFAGQLFDPDLLLAALLAFvafCLAASAVYILNDLLDLEADRLHPTKRNRPIASGRLSIPAALALAVVLLLAGLALALL 99
|
90 100
....*....|....*....|....*..
gi 83288463 104 gaNPLACWLGVMGFVVYVGVYSLYMKR 130
Cdd:cd13963 100 --LSPAFLLVLLAYLVLNLAYSLKLKR 124
|
|
| ubiA |
PRK12876 |
prenyltransferase; Reviewed |
51-130 |
4.04e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 237244 Cd Length: 300 Bit Score: 41.27 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 51 ASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLWFgANPLACWLGVMGFVVYVgVYSlYMKR 130
Cdd:PRK12876 61 TVGIIVNQIIDCAIDKKNPRTSSRVLPAKLLSINFSMLLLTLCSFLFLSLCWL-LNPLCFSLAVLSTLLMI-IYP-YTKR 137
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
1-154 |
1.03e-03 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 40.10 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 1 MMFKQYLQVTKP-GIIFGNLISVIGGfLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDrKMERtKNRVLVKG 79
Cdd:PRK12883 1 MELKAFIEITRPhNCILAGIVGILGS-LVALGGIPPIKTLILIFLVVYLGCSGGNTINDYFDYEID-KINR-PNRPLPRG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83288463 80 LISPAVSLVYATLLGIAGFMLLWFganpLACWLGVMGFVVYVG--VYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAV 154
Cdd:PRK12883 78 AMSRKAALYYSLLLFAVGLALAYL----INIEAFLFALGAYVLmfLYAWKLKPLPFIGNVVVALLTGATPIYGAIAV 150
|
|
| ubiA |
PRK13106 |
prenyltransferase; Reviewed |
25-145 |
1.24e-03 |
|
prenyltransferase; Reviewed
Pssm-ID: 237283 Cd Length: 300 Bit Score: 39.71 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 25 GFLLASKGSIDYPLFIYTLVGVSLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGlispAVSLVYATLLGIAGFMLLWFG 104
Cdd:PRK13106 37 GAFVAIKGIPPISTLILIFLALFFLRTAGMTNDNLADLEIDAKNPRTKNRPLVTG----AIKISEAKALITAGLILFFAS 112
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 83288463 105 ANPLACWLGVMGFVVYVGVYSL-YMKR-HSVYGTLIGSLSGAA 145
Cdd:PRK13106 113 AYLVNRWALLLSPIVALIAMSYpYMKRyTAFANYHLASIQGLA 155
|
|
| PRK12324 |
PRK12324 |
decaprenyl-phosphate phosphoribosyltransferase; |
47-129 |
2.10e-03 |
|
decaprenyl-phosphate phosphoribosyltransferase;
Pssm-ID: 237058 Cd Length: 295 Bit Score: 39.08 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83288463 47 SLVVASGCVFNNYIDRDIDRKMERTKNRVLVKGLISPAVSLVYATLLGIAGFMLLWFGANPLACWLgvmgfVVYVGV--- 123
Cdd:PRK12324 56 CLASSAVYLVNDIRDVEADRLHPTKRNRPIASGVVSVSLAYILAVVLLVASLALAYLLSPKLALVL-----LVYLVLnla 130
|
....*.
gi 83288463 124 YSLYMK 129
Cdd:PRK12324 131 YSFKLK 136
|
|
| |
