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Conserved domains on  [gi|6325085|ref|NP_015153|]
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protoheme IX farnesyltransferase [Saccharomyces cerevisiae S288C]

Protein Classification

protoheme IX farnesyltransferase( domain architecture ID 10797061)

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
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 147-442 1.54e-108

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: 322.66  E-value: 1.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    147 MPYLQLTKPRLTILVMLSAICSYALSPYPASVNE--LLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVT 224
Cdd:TIGR01473   1 KDYLQLTKPRIISLLLITAFAGMWLAPGGALVNPplLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    225 PTQAFEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYT-SMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGS 303
Cdd:TIGR01473  81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    304 WCLAGLLFAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNP--LLNARVSLrYSILMFPLCFGLSYFNITDWYYQIDSGLIN 381
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIAL-YTAALLPVSLLLAFLGGTGWLYLIVATLLG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325085    382 AWLTFWAFKFYWQQRinysaktlkDNVKfnkglsvaniyARKTFMASVLHLPAILILAIIH 442
Cdd:TIGR01473 240 ALFLYLAFKFYRDPT---------DRKK-----------ARKLFKFSLIYLALLFVALLID 280
 
Name Accession Description Interval E-value
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 147-442 1.54e-108

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: 322.66  E-value: 1.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    147 MPYLQLTKPRLTILVMLSAICSYALSPYPASVNE--LLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVT 224
Cdd:TIGR01473   1 KDYLQLTKPRIISLLLITAFAGMWLAPGGALVNPplLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    225 PTQAFEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYT-SMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGS 303
Cdd:TIGR01473  81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    304 WCLAGLLFAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNP--LLNARVSLrYSILMFPLCFGLSYFNITDWYYQIDSGLIN 381
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIAL-YTAALLPVSLLLAFLGGTGWLYLIVATLLG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325085    382 AWLTFWAFKFYWQQRinysaktlkDNVKfnkglsvaniyARKTFMASVLHLPAILILAIIH 442
Cdd:TIGR01473 240 ALFLYLAFKFYRDPT---------DRKK-----------ARKLFKFSLIYLALLFVALLID 280
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 150-438 8.15e-99

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: 297.43  E-value: 8.15e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  150 LQLTKPRLTILVMLSAICSYALSPYPA-SVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQA 228
Cdd:cd13957   1 LELTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  229 FEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYTSMKRKH-IINTWLGALVGMVPPLMGWAAASPLSHPGSWCLA 307
Cdd:cd13957  81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTtPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  308 GLLFAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNPLLNARV-SLRYSILMFPLCFGLSYFNITDWYYQIDSGLINAWLTF 386
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLY 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6325085  387 WAFKFYWQQRinysaktlkdnvkfnkglsvaNIYARKTFMASVLHLPAILIL 438
Cdd:cd13957 241 LAIKLYRSPD---------------------DKWARKLFFASLIYLPLLFLL 271
PLN02776 PLN02776
prenyltransferase
 152-444 1.14e-73

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 235.41  E-value: 1.14e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   152 LTKPRLTILVMLSAICSYAL-SPYPASVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQAFE 230
Cdd:PLN02776   1 LSKARLSALVVATSGAGFVLgSGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   231 FAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYTSMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGSWCLAGLL 310
Cdd:PLN02776  81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   311 FAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNPL--LNARVSLRYSILMFPLCFGLSYFNITDWYYQIDSGLINAWLTFWA 388
Cdd:PLN02776 161 YFWQMPHFMALAYMCRDDYAAGGYRMLSLADATgrRTALVALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAYLAASA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6325085   389 FKFYWQQrinysaktlkdnvkfnkglSVANiyARKTFMASVLHLPAILILAIIHKK 444
Cdd:PLN02776 241 ASFYREP-------------------TNAN--ARKMFHGSLLYLPAFMALLLLHRV 275
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 149-441 1.93e-70

Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 439879  Cd Length: 299  Bit Score: 225.40  E-value: 1.93e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  149 YLQLTKPRLTILVMLSAICSYAL-SPYPASVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQ 227
Cdd:COG0109  19 YLALTKPRIILLLLFTALAGMLLaAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPRE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  228 AFEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYT-SMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGSWCL 306
Cdd:COG0109  99 ALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTlWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLL 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  307 AGLLFAWQFPHFNTLSHNIRNEYKNAGY-VMTAWKNPLLNARVSLRYSILMFPLCFGLSYFNITDWYYQIDSGLINAWLT 385
Cdd:COG0109 179 FLIIFLWTPPHFWALALKRRDDYARAGVpMLPVVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLGAWFL 258

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6325085  386 FWAFKFYWqqriNYSAKTlkdnvkfnkglsvaniyARKTFMASVLHLPAILILAII 441
Cdd:COG0109 259 YLAVRLYR----RPDRKW-----------------ARKLFKFSILYLTLLFLALLV 293
UbiA pfam01040
UbiA prenyltransferase family;
161-396 3.44e-39

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 141.98  E-value: 3.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    161 VMLSAICSYALSPY-PASVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQAFEFAALIGTLG 239
Cdd:pfam01040   1 LLIPALAGLALAAGgVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    240 VSILYFgVNPTVAILGASNIALYgWAYTS-MKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGSWCLAGLLFAWQFPHF 318
Cdd:pfam01040  81 LLLLLL-LNPLTALLGLAALLLY-VLYTLrLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    319 NTLSHNIRNEYKNAGYVMTAwknPLLNARVSLRYSILMFPLCF----GLSYFNITDWYYQIDSGLINAWLtFWAFKFYWQ 394
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLP---VVLGRKAARILLALLLAVALllllLLLLLLLGGLYLLLALLLAALAL-LYAARLLRL 234


                  ..
gi 6325085    395 QR 396
Cdd:pfam01040 235 RD 236
 
Name Accession Description Interval E-value
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 147-442 1.54e-108

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: 322.66  E-value: 1.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    147 MPYLQLTKPRLTILVMLSAICSYALSPYPASVNE--LLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVT 224
Cdd:TIGR01473   1 KDYLQLTKPRIISLLLITAFAGMWLAPGGALVNPplLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    225 PTQAFEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYT-SMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGS 303
Cdd:TIGR01473  81 PREALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    304 WCLAGLLFAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNP--LLNARVSLrYSILMFPLCFGLSYFNITDWYYQIDSGLIN 381
Cdd:TIGR01473 161 WLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIAL-YTAALLPVSLLLAFLGGTGWLYLIVATLLG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325085    382 AWLTFWAFKFYWQQRinysaktlkDNVKfnkglsvaniyARKTFMASVLHLPAILILAIIH 442
Cdd:TIGR01473 240 ALFLYLAFKFYRDPT---------DRKK-----------ARKLFKFSLIYLALLFVALLID 280
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 150-438 8.15e-99

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: 297.43  E-value: 8.15e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  150 LQLTKPRLTILVMLSAICSYALSPYPA-SVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQA 228
Cdd:cd13957   1 LELTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  229 FEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYTSMKRKH-IINTWLGALVGMVPPLMGWAAASPLSHPGSWCLA 307
Cdd:cd13957  81 LIFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRTtPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  308 GLLFAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNPLLNARV-SLRYSILMFPLCFGLSYFNITDWYYQIDSGLINAWLTF 386
Cdd:cd13957 161 LILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLY 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6325085  387 WAFKFYWQQRinysaktlkdnvkfnkglsvaNIYARKTFMASVLHLPAILIL 438
Cdd:cd13957 241 LAIKLYRSPD---------------------DKWARKLFFASLIYLPLLFLL 271
PLN02776 PLN02776
prenyltransferase
 152-444 1.14e-73

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 235.41  E-value: 1.14e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   152 LTKPRLTILVMLSAICSYAL-SPYPASVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQAFE 230
Cdd:PLN02776   1 LSKARLSALVVATSGAGFVLgSGEAIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   231 FAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYTSMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGSWCLAGLL 310
Cdd:PLN02776  81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   311 FAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNPL--LNARVSLRYSILMFPLCFGLSYFNITDWYYQIDSGLINAWLTFWA 388
Cdd:PLN02776 161 YFWQMPHFMALAYMCRDDYAAGGYRMLSLADATgrRTALVALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAYLAASA 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6325085   389 FKFYWQQrinysaktlkdnvkfnkglSVANiyARKTFMASVLHLPAILILAIIHKK 444
Cdd:PLN02776 241 ASFYREP-------------------TNAN--ARKMFHGSLLYLPAFMALLLLHRV 275
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 149-441 1.93e-70

Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 439879  Cd Length: 299  Bit Score: 225.40  E-value: 1.93e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  149 YLQLTKPRLTILVMLSAICSYAL-SPYPASVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQ 227
Cdd:COG0109  19 YLALTKPRIILLLLFTALAGMLLaAGGLPDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPRE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  228 AFEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYT-SMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGSWCL 306
Cdd:COG0109  99 ALIFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTlWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLL 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  307 AGLLFAWQFPHFNTLSHNIRNEYKNAGY-VMTAWKNPLLNARVSLRYSILMFPLCFGLSYFNITDWYYQIDSGLINAWLT 385
Cdd:COG0109 179 FLIIFLWTPPHFWALALKRRDDYARAGVpMLPVVKGERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLGAWFL 258

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6325085  386 FWAFKFYWqqriNYSAKTlkdnvkfnkglsvaniyARKTFMASVLHLPAILILAII 441
Cdd:COG0109 259 YLAVRLYR----RPDRKW-----------------ARKLFKFSILYLTLLFLALLV 293
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 138-441 8.73e-56

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 187.27  E-value: 8.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   138 MKTLKKKVIMPYLQLTKPRLTILVMLSAICSYALSPYPASVNELLCLT-VGTTLCSGSANAINMGREPEFDRQMVRTQAR 216
Cdd:PRK04375   2 SSSSSRATLKDYLALTKPRVISLNLFTALGGMLLAPPGVPPLLLLLLTlLGIALVAGAAGALNNYIDRDIDAKMERTKNR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   217 PVVRGDVTPTQAFEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYTS-MKRKHIINTWLGALVGMVPPLMGWAAA 295
Cdd:PRK04375  82 PLVTGRISPREALIFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   296 SPLSHPGSWCLAGLLFAWQFPHFNTLSHNIRNEYKNAGY-VMTAWKNPLLNARVSLRYSILMFPLCFGLSYFNITDWYYQ 374
Cdd:PRK04375 162 TGSLSWEALILFLIIFLWTPPHFWALAIFRKDDYAAAGIpMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGMAGLLYL 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325085   375 IDSGLINAWLTFWAFKFYwqqrinysaktlkdnvkfnkgLSVANIYARKTFMASVLHLpAILILAII 441
Cdd:PRK04375 242 VVALLLGAWFLYYAWRLY---------------------RKDDRKWARKLFRYSINYL-TLLFVALL 286
UbiA pfam01040
UbiA prenyltransferase family;
161-396 3.44e-39

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 141.98  E-value: 3.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    161 VMLSAICSYALSPY-PASVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQAFEFAALIGTLG 239
Cdd:pfam01040   1 LLIPALAGLALAAGgVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    240 VSILYFgVNPTVAILGASNIALYgWAYTS-MKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGSWCLAGLLFAWQFPHF 318
Cdd:pfam01040  81 LLLLLL-LNPLTALLGLAALLLY-VLYTLrLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085    319 NTLSHNIRNEYKNAGYVMTAwknPLLNARVSLRYSILMFPLCF----GLSYFNITDWYYQIDSGLINAWLtFWAFKFYWQ 394
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLP---VVLGRKAARILLALLLAVALllllLLLLLLLGGLYLLLALLLAALAL-LYAARLLRL 234


                  ..
gi 6325085    395 QR 396
Cdd:pfam01040 235 RD 236
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 147-315 8.68e-21

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: 91.83  E-value: 8.68e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  147 MPYLQLT---KPRLTILVMLSAICSYALS-PYPASVNELLCLTVGTTLCSGSANAIN--MGREpeFDRQMVRTQARPVVR 220
Cdd:COG0382   1 RAYLRLLrldRPIGILLLLWPTLWALFLAaGGLPDLLLLLLAVLGTVLMRSAGYVINdyFDRE--IDRINERKPNRPLAS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  221 GDVTPTQAFEFAALIGTLGVSILYFgVNPTVAILGASNIALyGWAYTS-MKRKHII-NTWLGALVGMvPPLMGWAAASPL 298
Cdd:COG0382  79 GRISLREALLLAIVLLLLALALALL-LNPLTFLLALAALAL-AWAYSLfLKRFTLLgNLVLGLLFGL-GILMGFAAVTGS 155

                       170
                ....*....|....*..
gi 6325085  299 SHPGSWCLAGLLFAWQF 315
Cdd:COG0382 156 LPLSAWLLALAAFLWTL 172
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
 150-313 4.92e-14

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: 72.11  E-value: 4.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  150 LQLTKPRLTILVMLSAICSYALSPY---PASVNELLCLTVGTTLCSGSANAIN--MGREpeFDRQMVRTQARPVVRGDVT 224
Cdd:cd13959   1 MRLDKPIGTLLLLPPALWGLLLAAGglpLPLLKLLLLFLLGAFLMRSAGCTINdiADRD--IDAKVPRTKNRPLASGAIS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  225 PTQAFEFAALIGTLGVSILYFgVNPTVAILGASNIALYgWAYTSMKRK----HIintWLGALVGMvPPLMGWAAASPLSH 300
Cdd:cd13959  79 VKEALLFLAVQLLLGLALLLQ-LNPLTILLSPIALLLV-LIYPLMKRFtywpQL---VLGLAFGW-GPLMGWAAVTGSLP 152

                       170
                ....*....|...
gi 6325085  301 PGSWCLAGLLFAW 313
Cdd:cd13959 153 LPALLLYLAVIFW 165
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 150-313 2.03e-12

UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260119 [Multi-domain]  Cd Length: 271  Bit Score: 67.37  E-value: 2.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  150 LQLTKPRLTILVMLSAICSYALSPYPASVNE--LLCLTVGTTLCSGSANAINMGREPEFDRqmVRTQARPVVRGDVTPTQ 227
Cdd:cd13956   1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLPalLLLALLAVFLGAGAGYALNDYTDRELDA--INKPDRPLPSGRLSPRQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  228 AFEFAALIGTLGVsILYFGVNPTVAILGASNIALyGWAYTSMK--RKHIINTWLGALVGMVPpLMGWAAASPLSHPGSWC 305
Cdd:cd13956  79 ALAFAAALLLVGL-ALALALGPLALLLLLAGLLL-GLAYSLGLkrLKLGGWGVLGYATGLAL-LPGLGAVAAGGLVPLAL 155


                ....*...
gi 6325085  306 LAGLLFAW 313
Cdd:cd13956 156 LLALVFLL 163
PLN02809 PLN02809
4-hydroxybenzoate nonaprenyltransferase
 148-294 4.20e-11

4-hydroxybenzoate nonaprenyltransferase


Pssm-ID: 178405  Cd Length: 289  Bit Score: 63.56  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   148 PYLQLT---KPRLTILVMLSAICSYALSPYPASVNELLCLT---VGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRG 221
Cdd:PLN02809   8 PYAKLArldKPIGTWLLAWPCMWSIALAAPPGSLPDLKMLAlfgCGALLLRGAGCTINDLLDRDIDKKVERTKLRPIASG 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325085   222 DVTPTQAFEFAALIGTLGVSILyFGVNPTVAILGASNIALYGwAYTSMKRkhiINTWLGALVGMV---PPLMGWAA 294
Cdd:PLN02809  88 ALTPFQGVGFLGAQLLLGLGIL-LQLNNYSRILGASSLLLVF-TYPLMKR---FTFWPQAFLGLTfnwGALLGWAA 158
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 148-311 1.30e-05

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: 46.73  E-value: 1.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  148 PYLQLTKPRLTILVMLSAICSY--ALSPYPASVNELLCLTVGTTLC-SGSANAINmgrePEFDRQMVRTQA--RPVVRGD 222
Cdd:cd13961   1 AYLELIRPPNLLMAALAQYLGAlfALGPLLSLNDLELLLLFLSVFLiAAAGYIIN----DYFDVEIDRINKpdRPIPSGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  223 VTPTQAFEFAALIGTLGVSILYFgVNPTVAILGASNIALyGWAYtSMKRKHIIntWLG-----ALVGMvPPLMGWAAASP 297
Cdd:cd13961  77 ISRREALILSILLNALGLILAFL-LSPLALLIALLNSLL-LWLY-SHKLKRTP--LIGnllvaLLTGL-PFLFGGLAAGN 150

                       170
                ....*....|....
gi 6325085  298 LSHPgSWCLAGLLF 311
Cdd:cd13961 151 LLLI-ILLLALFAF 163
ubiA PRK12882
prenyltransferase; Reviewed
 149-284 1.66e-04

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 43.42  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   149 YLQLTKPRLTI----LVMLSAICSYALSPYPASVNELLCLTVgttLCSGSANAINMGREPEFDRqmVRTQARPVVRGDVT 224
Cdd:PRK12882   7 YLELTRPVNAVvagvAAFIGAFIAGGILSSPSLTGLAFAAVF---LATGAGNAINDYFDREIDR--INRPDRPIPSGAVS 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325085   225 PTQAFEFAALIGTLGVsILYFGVNPTVAILGASNIALYgWAYTS-MKRKHII-NTWLGALVG 284
Cdd:PRK12882  82 PRGALAFSILLFAAGV-ALAFLLPPLCLAIALFNSLLL-VLYAEtLKGTPGLgNASVAYLTG 141
ubiA PRK12884
prenyltransferase; Reviewed
 148-311 3.94e-04

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 42.25  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   148 PYLQLTKPRLTIL----VMLSAICSYA-LSPYPASvneLLCLTVgtTLCSGSANAINmgrePEFDRQMVRTQA--RPVVR 220
Cdd:PRK12884   6 AYLELLRPEHGLMagiaVVLGAIIALGgLPLDEAL---LGFLTA--FFASGSANALN----DYFDYEVDRINRpdRPIPS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085   221 GDVTPTQAFEFAALIGTLGVSILYF-GVNPTVAILGASNIA-LYGWaytSMKRKHII-NTWLGALVGMVPPLMGWAAASP 297
Cdd:PRK12884  77 GRISRREALLLAILLFILGLIAAYLiSPLAFLVVILVSVLGiLYNW---KLKEYGLIgNLYVAFLTGMTFIFGGIAVGEL 153

                        170
                 ....*....|....
gi 6325085   298 LShpGSWCLAGLLF 311
Cdd:PRK12884 154 NE--AVILLAAMAF 165
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 216-312 3.59e-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: 39.10  E-value: 3.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325085  216 RPVVRGDVTPTQAFEFAALIGTLGVsILYFGVNPTVAILG---ASNIALY-GWAytsmkrKHiinTWLGALV-----GMV 286
Cdd:cd13964  67 RPIPSGRVSRGAALALGAGLLAAGV-ALAALVGRLSGLVAlllAAAILLYdAWL------KH---TPLGPLLmglcrGLN 136

                        90       100
                ....*....|....*....|....*.
gi 6325085  287 pPLMGWAAASPLSHPGSWCLAGLLFA 312
Cdd:cd13964 137 -LLLGASAAAAGGLGPALLAALALGV 161
 
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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