|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
15-307 |
8.46e-137 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 388.73 E-value: 8.46e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 15 RAMSTLLAYLALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLA 94
Cdd:PRK04375 5 SSRATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 95 REAVPTRNALALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGT 174
Cdd:PRK04375 85 TGRISPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 175 IAWPALAMFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLALA--TSWLYGAVA 252
Cdd:PRK04375 165 LSWEALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLgmAGLLYLVVA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 308338667 253 LVAGGWFLTMAHQLYagvRAGEPVRPLRLFLQSNNYLAVVFCALAVDSVIALPTL 307
Cdd:PRK04375 245 LLLGAWFLYYAWRLY---RKDDRKWARKLFRYSINYLTLLFVALLVDHLLLLSLL 296
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
7-304 |
6.89e-124 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 356.36 E-value: 6.89e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 7 VAPRRVTGRAMSTLLAYLALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMK 86
Cdd:COG0109 3 SASASSAASLRSTLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 87 RTARRPLAREAVPTRNALALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMI 166
Cdd:COG0109 83 RTKNRPLPTGRISPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 167 GWSAITGTIAWPALAMFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLAL--AT 244
Cdd:COG0109 163 GWAAVTGSLSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYLlgMA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 245 SWLYGAVALVAGGWFLTMAHQLYagvRAGEPVRPLRLFLQSNNYLAVVFCALAVDSVIAL 304
Cdd:COG0109 243 GLIYLVVALVLGAWFLYLAVRLY---RRPDRKWARKLFKFSILYLTLLFLALLVDHLLLL 299
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
22-299 |
1.64e-102 |
|
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: 301.47 E-value: 1.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 22 AYLALTKPRVIELLLVTAIPAMLLADRGA-IHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPT 100
Cdd:TIGR01473 2 DYLQLTKPRIISLLLITAFAGMWLAPGGAlVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 101 RNALALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPAL 180
Cdd:TIGR01473 82 REALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 181 AMFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLAL--ATSWLYGAVALVAGGW 258
Cdd:TIGR01473 162 LLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFlgGTGWLYLIVATLLGAL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 308338667 259 FLTMAHQLYagVRAGEPVRPLRLFLQSNNYLAVVFCALAVD 299
Cdd:TIGR01473 242 FLYLAFKFY--RDPTDRKKARKLFKFSLIYLALLFVALLID 280
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
24-295 |
1.48e-97 |
|
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: 288.57 E-value: 1.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 24 LALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNA 103
Cdd:cd13957 1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 104 LALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMF 183
Cdd:cd13957 81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 184 AIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLAL--ATSWLYGAVALVAGGWFLT 261
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLlgLTGWIYLVVALLLGLYFLY 240
|
250 260 270
....*....|....*....|....*....|....
gi 308338667 262 MAHQLYagvRAGEPVRPLRLFLQSNNYLAVVFCA 295
Cdd:cd13957 241 LAIKLY---RSPDDKWARKLFFASLIYLPLLFLL 271
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
35-267 |
1.17e-44 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 152.38 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 35 LLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALALGLTLTVIS 114
Cdd:pfam01040 1 LLIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 115 FFWLWcATNLLAGVLALVTVAFYvFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMFAIIFFWTPPHT 194
Cdd:pfam01040 81 LLLLL-LLNPLTALLGLAALLLY-VLYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308338667 195 WALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLALA-TSWLYGAVALVAGGWFLTMAHQLY 267
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLlLGGLYLLLALLLAALALLYAARLL 232
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04375 |
PRK04375 |
protoheme IX farnesyltransferase; Provisional |
15-307 |
8.46e-137 |
|
protoheme IX farnesyltransferase; Provisional
Pssm-ID: 235293 Cd Length: 296 Bit Score: 388.73 E-value: 8.46e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 15 RAMSTLLAYLALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLA 94
Cdd:PRK04375 5 SSRATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 95 REAVPTRNALALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGT 174
Cdd:PRK04375 85 TGRISPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 175 IAWPALAMFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLALA--TSWLYGAVA 252
Cdd:PRK04375 165 LSWEALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLgmAGLLYLVVA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 308338667 253 LVAGGWFLTMAHQLYagvRAGEPVRPLRLFLQSNNYLAVVFCALAVDSVIALPTL 307
Cdd:PRK04375 245 LLLGAWFLYYAWRLY---RKDDRKWARKLFRYSINYLTLLFVALLVDHLLLLSLL 296
|
|
| CyoE |
COG0109 |
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ... |
7-304 |
6.89e-124 |
|
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 439879 Cd Length: 299 Bit Score: 356.36 E-value: 6.89e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 7 VAPRRVTGRAMSTLLAYLALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMK 86
Cdd:COG0109 3 SASASSAASLRSTLRDYLALTKPRIILLLLFTALAGMLLAAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 87 RTARRPLAREAVPTRNALALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMI 166
Cdd:COG0109 83 RTKNRPLPTGRISPREALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 167 GWSAITGTIAWPALAMFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLAL--AT 244
Cdd:COG0109 163 GWAAVTGSLSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYLlgMA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 245 SWLYGAVALVAGGWFLTMAHQLYagvRAGEPVRPLRLFLQSNNYLAVVFCALAVDSVIAL 304
Cdd:COG0109 243 GLIYLVVALVLGAWFLYLAVRLY---RRPDRKWARKLFKFSILYLTLLFLALLVDHLLLL 299
|
|
| cyoE_ctaB |
TIGR01473 |
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ... |
22-299 |
1.64e-102 |
|
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: 301.47 E-value: 1.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 22 AYLALTKPRVIELLLVTAIPAMLLADRGA-IHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPT 100
Cdd:TIGR01473 2 DYLQLTKPRIISLLLITAFAGMWLAPGGAlVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 101 RNALALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPAL 180
Cdd:TIGR01473 82 REALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 181 AMFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLAL--ATSWLYGAVALVAGGW 258
Cdd:TIGR01473 162 LLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFlgGTGWLYLIVATLLGAL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 308338667 259 FLTMAHQLYagVRAGEPVRPLRLFLQSNNYLAVVFCALAVD 299
Cdd:TIGR01473 242 FLYLAFKFY--RDPTDRKKARKLFKFSLIYLALLFVALLID 280
|
|
| PT_UbiA_Cox10 |
cd13957 |
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ... |
24-295 |
1.48e-97 |
|
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: 288.57 E-value: 1.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 24 LALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNA 103
Cdd:cd13957 1 LELTKPRITLLVLLTALAGYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 104 LALGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMF 183
Cdd:cd13957 81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 184 AIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLAL--ATSWLYGAVALVAGGWFLT 261
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLlgLTGWIYLVVALLLGLYFLY 240
|
250 260 270
....*....|....*....|....*....|....
gi 308338667 262 MAHQLYagvRAGEPVRPLRLFLQSNNYLAVVFCA 295
Cdd:cd13957 241 LAIKLY---RSPDDKWARKLFFASLIYLPLLFLL 271
|
|
| UbiA |
pfam01040 |
UbiA prenyltransferase family; |
35-267 |
1.17e-44 |
|
UbiA prenyltransferase family;
Pssm-ID: 460038 [Multi-domain] Cd Length: 250 Bit Score: 152.38 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 35 LLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALALGLTLTVIS 114
Cdd:pfam01040 1 LLIPALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 115 FFWLWcATNLLAGVLALVTVAFYvFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMFAIIFFWTPPHT 194
Cdd:pfam01040 81 LLLLL-LLNPLTALLGLAALLLY-VLYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308338667 195 WALAMRYKQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLALA-TSWLYGAVALVAGGWFLTMAHQLY 267
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLlLGGLYLLLALLLAALALLYAARLL 232
|
|
| PLN02776 |
PLN02776 |
prenyltransferase |
26-301 |
6.57e-29 |
|
prenyltransferase
Pssm-ID: 215415 Cd Length: 341 Bit Score: 113.30 E-value: 6.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 26 LTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALA 105
Cdd:PLN02776 1 LSKARLSALVVATSGAGFVLGSGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 106 LGLTLTVISFFWLWCATNLLAGVLALVTVAFYVFVYTlWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMFAI 185
Cdd:PLN02776 81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYT-PLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 186 IFFWTPPHTWALAMRYKQDYQVAGVPMLPAV-ATERQVTKQILIYTWLTVAATLVLALA--TSWLYGAVALVAGGWFLTM 262
Cdd:PLN02776 160 LYFWQMPHFMALAYMCRDDYAAGGYRMLSLAdATGRRTALVALRNCLYLAPLGFLAYDWgvTSSPFALEAALLTAYLAAS 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 308338667 263 AHQLYagvRAGEPVRPLRLFLQSNNYLAVVFCALAVDSV 301
Cdd:PLN02776 240 AASFY---REPTNANARKMFHGSLLYLPAFMALLLLHRV 275
|
|
| UbiA |
COG0382 |
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ... |
26-298 |
1.69e-20 |
|
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: 89.13 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 26 LTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALA 105
Cdd:COG0382 9 LDRPIGILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISLREALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 106 LGLTLTVISFFwLWCATNLLAGVLALVTVAFyVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMFAI 185
Cdd:COG0382 89 LAIVLLLLALA-LALLLNPLTFLLALAALAL-AWAYSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPLSAWLLALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 186 IFFWtpphTWALAMRY----KQDYQVAGVPMLPAVATERQVTKQILIYTWLTVAATLVLALAT--SWLYgAVALVAGGWF 259
Cdd:COG0382 167 AFLW----TLAYDTIYdledREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLAglGLLY-LLGLLAALLL 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 308338667 260 LTMAHQLYAGVRAGEPVRPLRLFLQSNNYLAVVFCALAV 298
Cdd:COG0382 242 LYLSQLWLLRPRKKDPARALKLFKLNMLLGLLLFLGIAL 280
|
|
| PT_UbiA_COQ2 |
cd13959 |
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ... |
34-299 |
1.80e-16 |
|
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: 77.51 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 34 LLLVTAIPAMLLADRGAIHPLLMLNTLVG-GMMAA-AGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALALGLTLT 111
Cdd:cd13959 11 LLLPPALWGLLLAAGGLPLPLLKLLLLFLlGAFLMrSAGCTINDIADRDIDAKVPRTKNRPLASGAISVKEALLFLAVQL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 112 VISFFWLWcATNLLAGVLALVTVAFyVFVYTLwLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMFAIIFFWTP 191
Cdd:cd13959 91 LLGLALLL-QLNPLTILLSPIALLL-VLIYPL-MKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPALLLYLAVIFWTA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 192 PHTWALAMRYKQDYQVAGVPMLPAVATERqvtkqILIYTWLTVAATLVLALATSWLY--GAVALVAGGWFLTMAHQLYAG 269
Cdd:cd13959 168 GYDTIYAHQDREDDRKIGVKSTAVLFGDR-----TKLILALLLHLFVALLLLAGGLAglGWPYYLGLGAAAHLLWQEHRL 242
|
250 260 270
....*....|....*....|....*....|
gi 308338667 270 VRAGEPVRPLRLFLQSNNYLAVVFCALAVD 299
Cdd:cd13959 243 DLPDPLRSCLAFFLSNGWVGLLLFAGLLLD 272
|
|
| PT_UbiA |
cd13956 |
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ... |
24-298 |
1.83e-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: 60.44 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 24 LALTKPRVIELLLVTAIPAMLLADRGAI-HPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRtaRRPLAREAVPTRN 102
Cdd:cd13956 1 LRLMRPYTLLYVLAPALAGAALAGAFAGpLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKP--DRPLPSGRLSPRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 103 ALALGLTLTVISFfWLWCATNLLAGVLALVTVAFyVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAI-TGTIAWPALA 181
Cdd:cd13956 79 ALAFAAALLLVGL-ALALALGPLALLLLLAGLLL-GLAYSLGLKRLKLGGWGVLGYATGLALLPGLGAVaAGGLVPLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 182 MFAIIFFWTPPHTWALAMRYKQDYQVAGVPMLPAVATERQVTKqiLIYTWLTVAATLVLALATSWLYGAVALVAGGWFLT 261
Cdd:cd13956 157 LALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGPRRARR--LAAGLLLAALILVVLLAVAGLLGPLALLALLAVAL 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 308338667 262 MAhQLYAGVRAGEPVRPLRLFLQSNNYLAVVFCALAV 298
Cdd:cd13956 235 LA-LRARFARADRLPALPRGFLLLAVYRLLLFAALLL 270
|
|
| PT_UbiA_DGGGPS |
cd13961 |
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ... |
22-148 |
1.06e-04 |
|
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: 42.88 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 22 AYLALTKPrviELLLVTAIpAMLLADRGAIHPLLMLNTL------VGGMMAAAGANTLNCVADADIDKVMKrtARRPLAR 95
Cdd:cd13961 1 AYLELIRP---PNLLMAAL-AQYLGALFALGPLLSLNDLellllfLSVFLIAAAGYIINDYFDVEIDRINK--PDRPIPS 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 308338667 96 EAVPTRNALALGLTLTVISFFwLWCATNLLAGVLALVTVAFYVFvYTLWLKRR 148
Cdd:cd13961 75 GRISRREALILSILLNALGLI-LAFLLSPLALLIALLNSLLLWL-YSHKLKRT 125
|
|
| ubiA |
PRK12873 |
4-hydroxybenzoate polyprenyltransferase; |
17-190 |
1.92e-04 |
|
4-hydroxybenzoate polyprenyltransferase;
Pssm-ID: 171787 [Multi-domain] Cd Length: 294 Bit Score: 42.34 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 17 MSTLLAYLALTKPRVIELLLVTAIPAMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLARE 96
Cdd:PRK12873 7 LSPWFELLRWNKPTGRLILLIPAGWSLWLTPSAPPSLLLLLLIILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLARG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 97 AVPTRNALALGLTLTVISFF----------WLwcatNLLAGVLALVTVAFYVFVytlwlKR--RTSQNVV---WGGAagc 161
Cdd:PRK12873 87 KISLKTAYSLLIVLLLLSLFvvlslpqpsrNL----CLSLAFLALPPILIYPSA-----KRwfAYPQAILalcWGFA--- 154
|
170 180 190
....*....|....*....|....*....|.
gi 308338667 162 mpVMIGWSAITGTIA--WPALAMFAIIFFWT 190
Cdd:PRK12873 155 --VLIPWAAAEGSLNggWPLLFCWLATLLWT 183
|
|
| ubiA |
PRK12886 |
prenyltransferase; Reviewed |
54-189 |
2.02e-04 |
|
prenyltransferase; Reviewed
Pssm-ID: 237247 Cd Length: 291 Bit Score: 42.37 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 54 LLMLNTLVGGMMAAAGantLNCVADADIDKVMKRTARRPLAREAVPTRNALaLGLTLTVISFFWLWCATNLLAGVLALVT 133
Cdd:PRK12886 45 DWILMAMVGARTAAMG---FNRLIDAEIDARNPRTAGRAIPAGLISKGSAI-LFIVLSSLLMLFAAWFLNPLCLYLSPPA 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 308338667 134 VaFYVFVYTLwLKRRTS-QNVVWGGAAGCMPvMIGWSAITGTIAWPALAMFAIIFFW 189
Cdd:PRK12886 121 L-FFLLLYSY-CKRFTAlAHVVLGFCLALAP-LGAWIAIRGTIELPAILLGLAVLFW 174
|
|
| PLN02809 |
PLN02809 |
4-hydroxybenzoate nonaprenyltransferase |
44-190 |
1.06e-03 |
|
4-hydroxybenzoate nonaprenyltransferase
Pssm-ID: 178405 Cd Length: 289 Bit Score: 40.06 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 44 LLADRGAIHPLLMLNTLVGGMMAAAGAN-TLNCVADADIDKVMKRTARRPLAREAVPTRNALA---------LGLTLTVI 113
Cdd:PLN02809 34 LAAPPGSLPDLKMLALFGCGALLLRGAGcTINDLLDRDIDKKVERTKLRPIASGALTPFQGVGflgaqlllgLGILLQLN 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 308338667 114 SFFWLWCATNLlagvlalvtvaFYVFVYTLwLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPA-LAMFAIIFFWT 190
Cdd:PLN02809 114 NYSRILGASSL-----------LLVFTYPL-MKRFTFWPQAFLGLTFNWGALLGWAAVKGSLDPAVvLPLYASGVCWT 179
|
|
| ubiA |
PRK12888 |
4-hydroxybenzoate octaprenyltransferase; |
36-189 |
2.21e-03 |
|
4-hydroxybenzoate octaprenyltransferase;
Pssm-ID: 183814 Cd Length: 284 Bit Score: 38.93 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 36 LVTAIPAMLLADRgAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALALGLTLTVIsf 115
Cdd:PRK12888 22 YIAALTAMFASDG-SVHWADLLLVTVAMVGARTFAMAANRIIDREIDARNPRTAGRELVTGAVSVRTAWTGALVALAV-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308338667 116 fWLWCATNLLAGVLALVTVAFYVFVYTLWLKRRTSQNVVWGGAAGCMPVMIGWSAITGTIAWPALAMFAIIFFW 189
Cdd:PRK12888 99 -FLGAAALLNPLCLALAPLAVAPLVVYPYAKRFTNFPHAILGLAQAVGPVGAWIAVTGTWSWPAVLLGLAVGLW 171
|
|
| PRK12324 |
PRK12324 |
decaprenyl-phosphate phosphoribosyltransferase; |
65-146 |
3.65e-03 |
|
decaprenyl-phosphate phosphoribosyltransferase;
Pssm-ID: 237058 Cd Length: 295 Bit Score: 38.30 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 65 MAAAGANTLNCVADADIDKVMKRTARRPLAREAVPTRNALALGLTLTVISFFWLWCATNLLAGVLA---LVTVAfyvfvY 141
Cdd:PRK12324 57 LASSAVYLVNDIRDVEADRLHPTKRNRPIASGVVSVSLAYILAVVLLVASLALAYLLSPKLALVLLvylVLNLA-----Y 131
|
....*
gi 308338667 142 TLWLK 146
Cdd:PRK12324 132 SFKLK 136
|
|
| PT_UbiA_1 |
cd13964 |
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ... |
36-190 |
5.06e-03 |
|
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: 37.95 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308338667 36 LVTAIP----AMLLADRGAIHPLLMLNTLVGGMMAAAGANTLNCVADADIDKVMKRTarRPLAREAVPTRNALALGLTLT 111
Cdd:cd13964 10 LFTVPAdvlaGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPE--RPIPSGRVSRGAALALGAGLL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308338667 112 VISFFWLWCAtNLLAGVLALVTVAFyVFVYTLWLKRRTSQNVVWGGAAGcMPVMIGWSAITGTIAWPALAMFAIIFFWT 190
Cdd:cd13964 88 AAGVALAALV-GRLSGLVALLLAAA-ILLYDAWLKHTPLGPLLMGLCRG-LNLLLGASAAAAGGLGPALLAALALGVYI 163
|
|
|