|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
1-285 |
1.36e-134 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 382.95 E-value: 1.36e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 1 MFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLI 80
Cdd:PRK04375 9 TLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 81 APSVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSG 160
Cdd:PRK04375 89 SPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 161 ALILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVS 240
Cdd:PRK04375 169 ALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLLG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489955755 241 VWWLGMALRGYKvEDDKVWARKLFVFSIVAITSLSVMMSVDFMVP 285
Cdd:PRK04375 249 AWFLYYAWRLYR-KDDRKWARKLFRYSINYLTLLFVALLVDHLLL 292
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
1-285 |
3.99e-118 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 340.96 E-value: 3.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 1 MFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLI 80
Cdd:COG0109 15 TLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 81 APSVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSG 160
Cdd:COG0109 95 SPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 161 ALILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVS 240
Cdd:COG0109 175 ALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489955755 241 VWWLGMALRGYKVEDDKvWARKLFVFSIVAITSLSVMMSVDFMVP 285
Cdd:COG0109 255 AWFLYLAVRLYRRPDRK-WARKLFKFSILYLTLLFLALLVDHLLL 298
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
6-277 |
1.17e-112 |
|
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: 326.32 E-value: 1.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 6 LQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVS 85
Cdd:cd13957 1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 86 LVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALILL 165
Cdd:cd13957 81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 166 AIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSVWWLG 245
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLY 240
|
250 260 270
....*....|....*....|....*....|..
gi 489955755 246 MALRGYKVEDDKvWARKLFVFSIVAITSLSVM 277
Cdd:cd13957 241 LAIKLYRSPDDK-WARKLFFASLIYLPLLFLL 271
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
3-281 |
5.00e-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: 289.53 E-value: 5.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 3 KQYLQVTKPGIIFGNLISVIGGFLLASKGS-IDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIA 81
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGAlVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 82 PSVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGA 161
Cdd:TIGR01473 81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 162 LILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSV 241
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489955755 242 WWLGMALRGYKVEDDKVWARKLFVFSIVAITSLSVMMSVD 281
Cdd:TIGR01473 241 LFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLID 280
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
18-268 |
5.00e-51 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 168.17 E-value: 5.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 18 LISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVSLVYATLLGIAGF 97
Cdd:pfam01040 2 LIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 98 MLLWFgANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALILLAIFSLWQMPHSY 177
Cdd:pfam01040 82 LLLLL-LNPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 178 AIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSVWWLGMALRGYKVEDDK 257
Cdd:pfam01040 160 ANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLRDPKK 239
|
250
....*....|.
gi 489955755 258 VWARKLFVFSI 268
Cdd:pfam01040 240 DAKAFFFLSSL 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
1-285 |
1.36e-134 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 382.95 E-value: 1.36e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 1 MFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLI 80
Cdd:PRK04375 9 TLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 81 APSVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSG 160
Cdd:PRK04375 89 SPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 161 ALILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVS 240
Cdd:PRK04375 169 ALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYLVVALLLG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489955755 241 VWWLGMALRGYKvEDDKVWARKLFVFSIVAITSLSVMMSVDFMVP 285
Cdd:PRK04375 249 AWFLYYAWRLYR-KDDRKWARKLFRYSINYLTLLFVALLVDHLLL 292
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
1-285 |
3.99e-118 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 340.96 E-value: 3.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 1 MFKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLI 80
Cdd:COG0109 15 TLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 81 APSVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSG 160
Cdd:COG0109 95 SPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 161 ALILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVS 240
Cdd:COG0109 175 ALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489955755 241 VWWLGMALRGYKVEDDKvWARKLFVFSIVAITSLSVMMSVDFMVP 285
Cdd:COG0109 255 AWFLYLAVRLYRRPDRK-WARKLFKFSILYLTLLFLALLVDHLLL 298
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
6-277 |
1.17e-112 |
|
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: 326.32 E-value: 1.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 6 LQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVS 85
Cdd:cd13957 1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 86 LVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALILL 165
Cdd:cd13957 81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 166 AIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSVWWLG 245
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLY 240
|
250 260 270
....*....|....*....|....*....|..
gi 489955755 246 MALRGYKVEDDKvWARKLFVFSIVAITSLSVM 277
Cdd:cd13957 241 LAIKLYRSPDDK-WARKLFFASLIYLPLLFLL 271
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
3-281 |
5.00e-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: 289.53 E-value: 5.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 3 KQYLQVTKPGIIFGNLISVIGGFLLASKGS-IDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIA 81
Cdd:TIGR01473 1 KDYLQLTKPRIISLLLITAFAGMWLAPGGAlVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 82 PSVSLVYATLLGIAGFMLLWFGANPLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGA 161
Cdd:TIGR01473 81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 162 LILLAIFSLWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSV 241
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFLGGTGWLYLIVATLLGA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489955755 242 WWLGMALRGYKVEDDKVWARKLFVFSIVAITSLSVMMSVD 281
Cdd:TIGR01473 241 LFLYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLID 280
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
18-268 |
5.00e-51 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 168.17 E-value: 5.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 18 LISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVSLVYATLLGIAGF 97
Cdd:pfam01040 2 LIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 98 MLLWFgANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALILLAIFSLWQMPHSY 177
Cdd:pfam01040 82 LLLLL-LNPLTALLGLAALLLYV-LYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 178 AIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSVWWLGMALRGYKVEDDK 257
Cdd:pfam01040 160 ANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLRDPKK 239
|
250
....*....|.
gi 489955755 258 VWARKLFVFSI 268
Cdd:pfam01040 240 DAKAFFFLSSL 250
|
|
| PLN02776 |
PLN02776 |
prenyltransferase |
24-198 |
2.04e-35 |
|
prenyltransferase
Pssm-ID: 215415 Cd Length: 341 Bit Score: 130.25 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 24 GFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVSLVYATLLGIAGFMLLWFG 103
Cdd:PLN02776 17 GFVLGSGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVAWAVVVGAAGVALLAYK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 104 ANPLACWLGVMGFVVYVGVYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALILLAIFSLWQMPHSYAIAIFR 183
Cdd:PLN02776 97 TNMLTAGLGAGNILLYAFVYT-PLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAALYFWQMPHFMALAYMC 175
|
170
....*....|....*
gi 489955755 184 FKDYQAANIPVLPVV 198
Cdd:PLN02776 176 RDDYAAGGYRMLSLA 190
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
3-270 |
4.98e-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: 95.68 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 3 KQYLQVTKPGIIFGNLISVIG---GFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGL 79
Cdd:COG0382 1 RAYLRLLRLDRPIGILLLLWPtlwALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 80 IAPSVSLVYATLLGIAGFMLLWFgANPLACWLGVMGFVVyVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDS 159
Cdd:COG0382 81 ISLREALLLAIVLLLLALALALL-LNPLTFLLALAALAL-AWAYSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 160 GALILLAIFSLWQMphSYAI--AIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAA 237
Cdd:COG0382 159 SAWLLALAAFLWTL--AYDTiyDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLAGLGLLYLLGLL 236
|
250 260 270
....*....|....*....|....*....|....
gi 489955755 238 AVSV-WWLGMALRGYKVEDDKVWARKLFVFSIVA 270
Cdd:COG0382 237 AALLlLYLSQLWLLRPRKKDPARALKLFKLNMLL 270
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
24-173 |
5.27e-20 |
|
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: 87.14 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 24 GFLLASKGSIDYTLFIYTLVGVSLVVAS--GCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVSLVYATLLGIAGFMLLW 101
Cdd:cd13959 19 GLLLAAGGLPLPLLKLLLLFLLGAFLMRsaGCTINDIADRDIDAKVPRTKNRPLASGAISVKEALLFLAVQLLLGLALLL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955755 102 FgANPLACWLGVMGFVVyVGVYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALILLAIFSLWQM 173
Cdd:cd13959 99 Q-LNPLTILLSPIALLL-VLIYP-LMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPALLLYLAVIFWTA 167
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
5-263 |
2.73e-11 |
|
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: 62.52 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 5 YLQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVS--LVVASGCVFNNYIDMDIDKKmerTK-NRVLVKGLIA 81
Cdd:cd13961 2 YLELIRPPNLLMAALAQYLGALFALGPLLSLNDLELLLLFLSvfLIAAAGYIINDYFDVEIDRI---NKpDRPIPSGRIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 82 PSVSLVYATLLGIAGFMLlwfganplACWLGVMGFVVYVGV------YSLYMKRHSVYGTLIGSLSGAAPPVIGycAVTN 155
Cdd:cd13961 79 RREALILSILLNALGLIL--------AFLLSPLALLIALLNslllwlYSHKLKRTPLIGNLLVALLTGLPFLFG--GLAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 156 EFDSGALILLAIFSlwqmphsYAIAIFR--FKDYQ------AANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGY 227
Cdd:cd13961 149 GNLLLIILLLALFA-------FLITLGReiVKDIEdvegdrAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPYLLGG 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 489955755 228 AGYKYLVVAAAVSVWWLGMALRGYKVEDDKVWARKL 263
Cdd:cd13961 222 LGILYLILIIIADLLFLYSAIRLAKSPKDYSKLSKL 257
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
6-270 |
3.05e-10 |
|
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: 59.67 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 6 LQVTKPGIIFGNLISVIGGFLLASKGSIDY-TLFIYTLVGVSLVVASGCVFNNYIDMDIDKkmERTKNRVLVKGLIAPSV 84
Cdd:cd13956 1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLpALLLLALLAVFLGAGAGYALNDYTDRELDA--INKPDRPLPSGRLSPRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 85 SLVYATLLGIAGFmLLWFGANPLACWLGVMGFVVYVgVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALIL 164
Cdd:cd13956 79 ALAFAAALLLVGL-ALALALGPLALLLLLAGLLLGL-AYSLGLKRLKLGGWGVLGYATGLALLPGLGAVAAGGLVPLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 165 LAIFSLWQMphSYAIAIFRFKDY---QAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSV 241
Cdd:cd13956 157 LALVFLLLG--LGINLYNDLPDVegdRAAGIRTLPVRLGPRRARRLAAGLLLAALILVVLLAVAGLLGPLALLALLAVAL 234
|
250 260
....*....|....*....|....*....
gi 489955755 242 WWLGMALRGYKVEDDKVWARKLFVFSIVA 270
Cdd:cd13956 235 LALRARFARADRLPALPRGFLLLAVYRLL 263
|
|
| ubiA |
PRK12884 |
prenyltransferase; Reviewed |
3-255 |
2.35e-07 |
|
prenyltransferase; Reviewed
Pssm-ID: 183812 Cd Length: 279 Bit Score: 51.11 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 3 KQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVsLVVASGCVFNNYIDMDIDKKmeRTKNRVLVKGLIAP 82
Cdd:PRK12884 5 KAYLELLRPEHGLMAGIAVVLGAIIALGGLPLDEALLGFLTAF-FASGSANALNDYFDYEVDRI--NRPDRPIPSGRISR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 83 SVSLVYATLLGIAGFMLLWFgANPLACwLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDsgAL 162
Cdd:PRK12884 82 REALLLAILLFILGLIAAYL-ISPLAF-LVVILVSVLGILYNWKLKEYGLIGNLYVAFLTGMTFIFGGIAVGELNE--AV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 163 ILLAIFS-LWQMPHSYAIAIFRFKDYQAANIPVLPVVKGISVAKNHITLYIIAFAVATLMLSLGGYAGYKYLVVAAAVSV 241
Cdd:PRK12884 158 ILLAAMAfLMTLGREIMKDIEDVEGDRLRGARTLAILYGEKIAGRIAAALFILAVLLSPLPYLFGIFNILYLAPVLVADL 237
|
250
....*....|....*..
gi 489955755 242 WWL---GMALRGYKVED 255
Cdd:PRK12884 238 IFLysaYSLLRSQDRET 254
|
|
| ubiA |
PRK12874 |
4-hydroxybenzoate polyprenyltransferase; |
55-156 |
2.79e-07 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 237242 Cd Length: 291 Bit Score: 50.78 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 55 FNNYIDMDIDKKMERTKNRVLVKGLIAPSvSLVYATLLGIAGFMLLWFGANPLACWLGVMgFVVYVGVYSlYMKRHSVYG 134
Cdd:PRK12874 66 FNRLVDRDIDKDNPRTANRPSVDGRISVK-SMVLFIVLNALIFIGVSYFINPLAFKLSFP-FLIVLGGYS-YFKRFSSLA 142
|
90 100
....*....|....*....|..
gi 489955755 135 TLIGSLSGAAPPVIGYCAVTNE 156
Cdd:PRK12874 143 HLVLGLSLGLAPIAGVVAVLGE 164
|
|
| PT_UbiA_UBIAD1 |
cd13962 |
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ... |
6-274 |
3.56e-06 |
|
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: 47.51 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 6 LQVTKPGIIFGNLISVIGGFLLASK--GSIDYTLFIYTLVGVSLVVASGCVFNNYID--MDIDKKMERTKNRVLVKGLIA 81
Cdd:cd13962 1 LLAARPRTLPASLAPVLLGTALAYYlgGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRSGPSRVLVSGLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 82 PSVSLVYATLLGIAGFML---LWFGANPLACWLGVMGFVVYVGvYSLYMKRHSVYG---TLIGSLSGAAPPVIGYCAVTN 155
Cdd:cd13962 81 PRQVLRAALVLLLLAALLglyLVALGGWLLLLLGLLGILAGYF-YTGGPFPLSYRGlgeLFVFLFFGLLAVLGTYYVQTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 156 EFDSGALILLAIFSLWqmphSYAIAI---FRfkDYQ---AANIPVLPVVKGISVAKN-HITLYIIAFAVATLMLSLGGYA 228
Cdd:cd13962 160 SLSWEVLLAALPLGLL----IAAILLannIR--DIEadrAAGKRTLAVRLGRKRARRlYAALLLLAYLLLLLLVLLGLLP 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489955755 229 GYKYLVVAAAVSVWWLGMALRGYKVEDDKVWARKLFVFSIVAITSL 274
Cdd:cd13962 234 LWSLLALLSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLL 279
|
|
| PRK09573 |
PRK09573 |
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed |
2-171 |
4.80e-06 |
|
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
Pssm-ID: 181963 Cd Length: 279 Bit Score: 46.88 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 2 FKQYLQVTKPGIIFGNLISVIGGFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKmeRTKNRVLVKGLIA 81
Cdd:PRK09573 3 IKAYFELIRPKNCIGASIGAIIGYLIASNFKIDLKGIILAALVVFLVCAGGNVINDIYDIEIDKI--NKPERPIPSGRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 82 PSVSLVYATLLGIAGFMLLWFGAnpLACWLGVMGFVVYVGVYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGA 161
Cdd:PRK09573 81 LKEAKIFSITLFIVGLILSIFIN--IYAFLIALLNSILLYLYAKDLKKTGLIGNLIVAYLTGLSFIFGGLAVFNVLRIII 158
|
170
....*....|
gi 489955755 162 LILLAIFSLW 171
Cdd:PRK09573 159 LFLCAFFSTW 168
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
24-171 |
2.11e-05 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 45.07 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 24 GFLLASKG--SIDYTLFIYTLVGVSLVVASGcvFNNYIDMDIDKKMERTKNRVLVKGLIAPSVSLVYaTLLGIAGFMLLW 101
Cdd:PRK12886 30 GAVLAALGlpGASQLDWILMAMVGARTAAMG--FNRLIDAEIDARNPRTAGRAIPAGLISKGSAILF-IVLSSLLMLFAA 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 102 FGANPLACWLGVMGFVVYVGvYSlYMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALILLAIFSLW 171
Cdd:PRK12886 107 WFLNPLCLYLSPPALFFLLL-YS-YCKRFTALAHVVLGFCLALAPLGAWIAIRGTIELPAILLGLAVLFW 174
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
17-131 |
3.69e-05 |
|
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: 44.49 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 17 NLISVIG----GFLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKmERtKNRVLVKGLIAPSVSLVYATLL 92
Cdd:cd13964 9 NLFTVPAdvlaGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDAR-ER-PERPIPSGRVSRGAALALGAGL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489955755 93 GIAGFMLLWF-GANPLACWLGVMGFVVyvgVYSLYMKRHS 131
Cdd:cd13964 87 LAAGVALAALvGRLSGLVALLLAAAIL---LYDAWLKHTP 123
|
|
| PLN02809 |
PLN02809 |
4-hydroxybenzoate nonaprenyltransferase |
26-165 |
6.09e-05 |
|
4-hydroxybenzoate nonaprenyltransferase
Pssm-ID: 178405 Cd Length: 289 Bit Score: 43.91 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 26 LLASKGSI-DYTLFIYTLVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVSLVY---------ATLLGIA 95
Cdd:PLN02809 34 LAAPPGSLpDLKMLALFGCGALLLRGAGCTINDLLDRDIDKKVERTKLRPIASGALTPFQGVGFlgaqlllglGILLQLN 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 96 GFMLLWfGANPLAcwlgvmgfvvYVGVYSLyMKRHSVYGTLIGSLSGAAPPVIGYCAVTNEFDSGALILL 165
Cdd:PLN02809 114 NYSRIL-GASSLL----------LVFTYPL-MKRFTFWPQAFLGLTFNWGALLGWAAVKGSLDPAVVLPL 171
|
|
| ubiA |
PRK12888 |
4-hydroxybenzoate octaprenyltransferase; |
56-248 |
4.50e-04 |
|
4-hydroxybenzoate octaprenyltransferase;
Pssm-ID: 183814 Cd Length: 284 Bit Score: 41.24 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 56 NNYIDMDIDKKMERTKNRVLVKGliapSVSLVYATLLGIAGFMLLWFGA---NPLACWLGVMGFVVYVgVYSlYMKRHSV 132
Cdd:PRK12888 59 NRIIDREIDARNPRTAGRELVTG----AVSVRTAWTGALVALAVFLGAAallNPLCLALAPLAVAPLV-VYP-YAKRFTN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 133 YGTLIGSLSGAAPPVIGYCAVTNEFDSGALILLAIFSLWqmphsyaIA----IFRFKDYQA---ANIPVLPVVKGISVAk 205
Cdd:PRK12888 133 FPHAILGLAQAVGPVGAWIAVTGTWSWPAVLLGLAVGLW-------IGgfdlIYACQDAEVdrrIGVRSVPARFGVRAA- 204
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489955755 206 nhitlyiIAFAVATLMLSLGGYAGYKYLVVAAAvsVWWLGMAL 248
Cdd:PRK12888 205 -------LWASRVAHVVTFALFVWFGLAVGFGA--LWWIGLAI 238
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
42-100 |
1.09e-03 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 40.03 E-value: 1.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 42 LVGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVS-LVYATLLGIAGFMLL 100
Cdd:PRK12873 50 ILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLARGKISLKTAySLLIVLLLLSLFVVL 109
|
|
| ubiA |
PRK12876 |
prenyltransferase; Reviewed |
50-129 |
1.18e-03 |
|
prenyltransferase; Reviewed
Pssm-ID: 237244 Cd Length: 300 Bit Score: 39.73 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 50 ASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVSLVYATLLGIAGFMLLWFgANPLACWLGVMGFVVYVgVYSlYMKR 129
Cdd:PRK12876 61 TVGIIVNQIIDCAIDKKNPRTSSRVLPAKLLSINFSMLLLTLCSFLFLSLCWL-LNPLCFSLAVLSTLLMI-IYP-YTKR 137
|
|
| PRK08238 |
PRK08238 |
UbiA family prenyltransferase; |
43-130 |
1.60e-03 |
|
UbiA family prenyltransferase;
Pssm-ID: 236195 [Multi-domain] Cd Length: 479 Bit Score: 39.86 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 43 VGVSLVVASGCVFNNYIDMDIDKKMERTKNRVLVKGLIAPSVSLVYATLLGIAGFMLLWFGanPLACWLGVMGFVVYVGV 122
Cdd:PRK08238 233 LAFSLCASAVYILNDLLDLEADRAHPRKRRRPFASGALPIPFGLAAAPLLLLAGLALALAL--GPAFLLVLLAYLALTLA 310
|
....*...
gi 489955755 123 YSLYMKRH 130
Cdd:PRK08238 311 YSLRLKRK 318
|
|
| ubiA |
PRK12883 |
prenyltransferase UbiA-like protein; Reviewed |
2-153 |
2.87e-03 |
|
prenyltransferase UbiA-like protein; Reviewed
Pssm-ID: 171796 Cd Length: 277 Bit Score: 38.56 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955755 2 FKQYLQVTKP-GIIFGNLISVIGGfLLASKGSIDYTLFIYTLVGVSLVVASGCVFNNYIDMDIDkKMERtKNRVLVKGLI 80
Cdd:PRK12883 3 LKAFIEITRPhNCILAGIVGILGS-LVALGGIPPIKTLILIFLVVYLGCSGGNTINDYFDYEID-KINR-PNRPLPRGAM 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955755 81 APSVSLVYATLLGIAGFMLLWFganpLACWLGVMGFVVYVG--VYSLYMKRHSVYGTLIGSLSGAAPPVIGYCAV 153
Cdd:PRK12883 80 SRKAALYYSLLLFAVGLALAYL----INIEAFLFALGAYVLmfLYAWKLKPLPFIGNVVVALLTGATPIYGAIAV 150
|
|
| |
