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Conserved domains on  [gi|308338667|gb|EFP27518|]
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cytochrome C oxidase assembly factor ctaB [Mycobacterium tuberculosis SUMu005]

Protein Classification

protoheme IX farnesyltransferase( domain architecture ID 10792362)

protoheme IX farnesyltransferase acts in step 1 of the conversion protoheme IX to heme O in heme O biosynthesis

Graphical summary

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List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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