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Conserved domains on  [gi|30410008|ref|NP_848466|]
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protoheme IX farnesyltransferase, mitochondrial [Mus musculus]

Protein Classification

protoheme IX farnesyltransferase( domain architecture ID 10195468)

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
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 159-414 3.17e-118

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: 345.96  E-value: 3.17e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 159 LSKIKLTALVVSTTSAGFALAPGPF-DWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 237
Cdd:cd13957   3 LTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHALI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 238 FATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTPLKRV-SITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGI 316
Cdd:cd13957  83 FGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRtTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFLI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 317 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPALCRRV-ALRHCLALIALSTAAPVLDITTWVFPVISLPINLYISYLG 395
Cdd:cd13957 163 LFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYLA 242

                       250
                ....*....|....*....
gi 30410008 396 FRFYVDADRRSSRKLFFCS 414
Cdd:cd13957 243 IKLYRSPDDKWARKLFFAS 261
 
Name Accession Description Interval E-value
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 159-414 3.17e-118

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: 345.96  E-value: 3.17e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 159 LSKIKLTALVVSTTSAGFALAPGPF-DWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 237
Cdd:cd13957   3 LTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHALI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 238 FATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTPLKRV-SITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGI 316
Cdd:cd13957  83 FGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRtTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFLI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 317 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPALCRRV-ALRHCLALIALSTAAPVLDITTWVFPVISLPINLYISYLG 395
Cdd:cd13957 163 LFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYLA 242

                       250
                ....*....|....*....
gi 30410008 396 FRFYVDADRRSSRKLFFCS 414
Cdd:cd13957 243 IKLYRSPDDKWARKLFFAS 261
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 159-414 3.84e-106

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: 315.72  E-value: 3.84e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   159 LSKIKLTALVVSTTSAGFALAPGP--FDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 236
Cdd:TIGR01473   6 LTKPRIISLLLITAFAGMWLAPGGalVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPREAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   237 SFATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYT-PLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGG 315
Cdd:TIGR01473  86 AFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWLLFA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   316 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHP--ALCRRVALRhCLALIALSTAAPVLDITTWVFPVISLPINLYISY 393
Cdd:TIGR01473 166 IIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIALY-TAALLPVSLLLAFLGGTGWLYLIVATLLGALFLY 244

                         250       260
                  ....*....|....*....|..
gi 30410008   394 LGFRFYVDADRRS-SRKLFFCS 414
Cdd:TIGR01473 245 LAFKFYRDPTDRKkARKLFKFS 266
PLN02776 PLN02776
prenyltransferase
 159-414 1.47e-103

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 311.29  E-value: 1.47e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  159 LSKIKLTALVVSTTSAGFALAPGP-FDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 237
Cdd:PLN02776   1 LSKARLSALVVATSGAGFVLGSGEaIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  238 FATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTPLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGIL 317
Cdd:PLN02776  81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  318 YSWQFPHFNALSWGLREDYSRGGYCMMSVTHPALCR--RVALRHCLALIALSTAAPVLDITTWVFPVISLPINLYISYLG 395
Cdd:PLN02776 161 YFWQMPHFMALAYMCRDDYAAGGYRMLSLADATGRRtaLVALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAYLAASA 240

                        250
                 ....*....|....*....
gi 30410008  396 FRFYVDADRRSSRKLFFCS 414
Cdd:PLN02776 241 ASFYREPTNANARKMFHGS 259
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 159-414 2.81e-84

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 260.45  E-value: 2.81e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 159 LSKIKLTALVVSTTSAGFALAPGPF-DWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 237
Cdd:COG0109  22 LTKPRIILLLLFTALAGMLLAAGGLpDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPREALI 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 238 FATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTP-LKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGI 316
Cdd:COG0109 102 FGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLLFLI 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 317 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTH-PALCRRVALRHCLALIALSTAAPVLDITTWVFPVISLPINLYISYLG 395
Cdd:COG0109 182 IFLWTPPHFWALALKRRDDYARAGVPMLPVVKgERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLGAWFLYLA 261

                       250
                ....*....|....*....
gi 30410008 396 FRFYVDADRRSSRKLFFCS 414
Cdd:COG0109 262 VRLYRRPDRKWARKLFKFS 280
UbiA pfam01040
UbiA prenyltransferase family;
168-412 3.30e-57

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 188.98  E-value: 3.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   168 VVSTTSAGFALA-PGPFDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPG 246
Cdd:pfam01040   1 LLIPALAGLALAaGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   247 VALLtWGVNPLTGALGVFNIFLYTcCYT-PLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGILYSWQFPHF 325
Cdd:pfam01040  81 LLLL-LLLNPLTALLGLAALLLYV-LYTlRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   326 NALSWGLREDYSRGGYCMMSVTHPalcRRVALRHCLALIALSTAAP---VLDITTWVFPVISLPINLYISYLGFRFYVDA 402
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVVLG---RKAARILLALLLAVALLLLlllLLLLLGGLYLLLALLLAALALLYAARLLRLR 235

                         250
                  ....*....|
gi 30410008   403 DRRSSRKLFF 412
Cdd:pfam01040 236 DPKKDAKAFF 245
 
Name Accession Description Interval E-value
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 159-414 3.17e-118

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: 345.96  E-value: 3.17e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 159 LSKIKLTALVVSTTSAGFALAPGPF-DWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 237
Cdd:cd13957   3 LTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHALI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 238 FATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTPLKRV-SITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGI 316
Cdd:cd13957  83 FGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPLKKRtTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFLI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 317 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPALCRRV-ALRHCLALIALSTAAPVLDITTWVFPVISLPINLYISYLG 395
Cdd:cd13957 163 LFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYLA 242

                       250
                ....*....|....*....
gi 30410008 396 FRFYVDADRRSSRKLFFCS 414
Cdd:cd13957 243 IKLYRSPDDKWARKLFFAS 261
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 159-414 3.84e-106

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: 315.72  E-value: 3.84e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   159 LSKIKLTALVVSTTSAGFALAPGP--FDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 236
Cdd:TIGR01473   6 LTKPRIISLLLITAFAGMWLAPGGalVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPREAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   237 SFATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYT-PLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGG 315
Cdd:TIGR01473  86 AFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWLLFA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   316 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHP--ALCRRVALRhCLALIALSTAAPVLDITTWVFPVISLPINLYISY 393
Cdd:TIGR01473 166 IIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIALY-TAALLPVSLLLAFLGGTGWLYLIVATLLGALFLY 244

                         250       260
                  ....*....|....*....|..
gi 30410008   394 LGFRFYVDADRRS-SRKLFFCS 414
Cdd:TIGR01473 245 LAFKFYRDPTDRKkARKLFKFS 266
PLN02776 PLN02776
prenyltransferase
 159-414 1.47e-103

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 311.29  E-value: 1.47e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  159 LSKIKLTALVVSTTSAGFALAPGP-FDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 237
Cdd:PLN02776   1 LSKARLSALVVATSGAGFVLGSGEaIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  238 FATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTPLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGIL 317
Cdd:PLN02776  81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  318 YSWQFPHFNALSWGLREDYSRGGYCMMSVTHPALCR--RVALRHCLALIALSTAAPVLDITTWVFPVISLPINLYISYLG 395
Cdd:PLN02776 161 YFWQMPHFMALAYMCRDDYAAGGYRMLSLADATGRRtaLVALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAYLAASA 240

                        250
                 ....*....|....*....
gi 30410008  396 FRFYVDADRRSSRKLFFCS 414
Cdd:PLN02776 241 ASFYREPTNANARKMFHGS 259
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 159-414 2.81e-84

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 260.45  E-value: 2.81e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 159 LSKIKLTALVVSTTSAGFALAPGPF-DWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 237
Cdd:COG0109  22 LTKPRIILLLLFTALAGMLLAAGGLpDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPREALI 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 238 FATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTP-LKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGI 316
Cdd:COG0109 102 FGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLLFLI 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 317 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTH-PALCRRVALRHCLALIALSTAAPVLDITTWVFPVISLPINLYISYLG 395
Cdd:COG0109 182 IFLWTPPHFWALALKRRDDYARAGVPMLPVVKgERRTKRQILLYTLLLVPVSLLPYLLGMAGLIYLVVALVLGAWFLYLA 261

                       250
                ....*....|....*....
gi 30410008 396 FRFYVDADRRSSRKLFFCS 414
Cdd:COG0109 262 VRLYRRPDRKWARKLFKFS 280
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 159-414 1.48e-64

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 209.61  E-value: 1.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  159 LSKIKLTALVVSTTSAGFALAP-GPFDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 237
Cdd:PRK04375  16 LTKPRVISLNLFTALGGMLLAPpGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRISPREALI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  238 FATCCAVPGVALLTWGVNPLTGALGVFNIFLYTCCYTP-LKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGI 316
Cdd:PRK04375  96 FGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWEALILFLI 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  317 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPAlcrRVALRHCL----ALIALSTAAPVLDITTWVFPVISLPINLYIS 392
Cdd:PRK04375 176 IFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGI---RVTKRQILlytvLLVAVSLLPVLLGMAGLLYLVVALLLGAWFL 252

                        250       260
                 ....*....|....*....|..
gi 30410008  393 YLGFRFYVDADRRSSRKLFFCS 414
Cdd:PRK04375 253 YYAWRLYRKDDRKWARKLFRYS 274
UbiA pfam01040
UbiA prenyltransferase family;
168-412 3.30e-57

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 188.98  E-value: 3.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   168 VVSTTSAGFALA-PGPFDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPG 246
Cdd:pfam01040   1 LLIPALAGLALAaGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   247 VALLtWGVNPLTGALGVFNIFLYTcCYT-PLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLLGGILYSWQFPHF 325
Cdd:pfam01040  81 LLLL-LLLNPLTALLGLAALLLYV-LYTlRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008   326 NALSWGLREDYSRGGYCMMSVTHPalcRRVALRHCLALIALSTAAP---VLDITTWVFPVISLPINLYISYLGFRFYVDA 402
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVVLG---RKAARILLALLLAVALLLLlllLLLLLGGLYLLLALLLAALALLYAARLLRLR 235

                         250
                  ....*....|
gi 30410008   403 DRRSSRKLFF 412
Cdd:pfam01040 236 DPKKDAKAFF 245
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 156-322 7.87e-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: 7.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 156 LARLSKIKLTALVVSTTSAGFALAPGPF-DWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLL 234
Cdd:COG0382   6 LLRLDRPIGILLLLWPTLWALFLAAGGLpDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISLRE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 235 AVSFATCCAVPGVALLTWgVNPLTGALGVFNIFLyTCCYTP-LKRvsitNTWVGAVV----GAIPPVMGWTAATGSLDAG 309
Cdd:COG0382  86 ALLLAIVLLLLALALALL-LNPLTFLLALAALAL-AWAYSLfLKR----FTLLGNLVlgllFGLGILMGFAAVTGSLPLS 159

                       170
                ....*....|...
gi 30410008 310 ALLLGGILYSWQF 322
Cdd:COG0382 160 AWLLALAAFLWTL 172
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
 157-320 1.31e-17

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: 82.51  E-value: 1.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 157 ARLSKIKLTALVVSTTSAGFALA---PGPFDWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPL 233
Cdd:cd13959   1 MRLDKPIGTLLLLPPALWGLLLAaggLPLPLLKLLLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 234 LAVSFATCCAVPGVALLtWGVNPLTGALGVFNIFLyTCCYtPL-KRVSItntWVGAVVG---AIPPVMGWTAATGSLDAG 309
Cdd:cd13959  81 EALLFLAVQLLLGLALL-LQLNPLTILLSPIALLL-VLIY-PLmKRFTY---WPQLVLGlafGWGPLMGWAAVTGSLPLP 154

                       170
                ....*....|.
gi 30410008 310 ALLLGGILYSW 320
Cdd:cd13959 155 ALLLYLAVIFW 165
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 157-413 1.51e-11

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


Pssm-ID: 260119 [Multi-domain]  Cd Length: 271  Bit Score: 64.68  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 157 ARLSKIKLTALVVSTTSAGFALAPGPFDWSC--FLLTSLGTGLASCAANSINQFFEVPFDSNMNRtkNRPLVRGQISPLL 234
Cdd:cd13956   1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLPalLLLALLAVFLGAGAGYALNDYTDRELDAINKP--DRPLPSGRLSPRQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 235 AVSFATCCAVPGVALLTWgVNPLTGALGVFNIFLYTcCYT-PLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLL 313
Cdd:cd13956  79 ALAFAAALLLVGLALALA-LGPLALLLLLAGLLLGL-AYSlGLKRLKLGGWGVLGYATGLALLPGLGAVAAGGLVPLALL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 314 GGILYSWQFPHFNalSWGLREDY---SRGGYCMMSVThpaLCRRVALRHCLALIALSTAAPVL--DITTWVFPVISLPIN 388
Cdd:cd13956 157 LALVFLLLGLGIN--LYNDLPDVegdRAAGIRTLPVR---LGPRRARRLAAGLLLAALILVVLlaVAGLLGPLALLALLA 231

                       250       260
                ....*....|....*....|....*
gi 30410008 389 LYISYLGFRFYVDADRRSSRKLFFC 413
Cdd:cd13956 232 VALLALRARFARADRLPALPRGFLL 256
ubiA PRK12882
prenyltransferase; Reviewed
 174-293 1.81e-07

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 52.28  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  174 AGFALAPGPFDWSCFLLTSLGTGlascAANSINQFFEVPFDSnMNRtKNRPLVRGQISPLLAVSFATCCAVPGVAlLTWG 253
Cdd:PRK12882  30 AGGILSSPSLTGLAFAAVFLATG----AGNAINDYFDREIDR-INR-PDRPIPSGAVSPRGALAFSILLFAAGVA-LAFL 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 30410008  254 VNPLTGALGVFN---IFLYTccyTPLKRVS-ITNTWVGAVVGAI 293
Cdd:PRK12882 103 LPPLCLAIALFNsllLVLYA---ETLKGTPgLGNASVAYLTGST 143
PLN02809 PLN02809
4-hydroxybenzoate nonaprenyltransferase
 156-312 3.52e-07

4-hydroxybenzoate nonaprenyltransferase


Pssm-ID: 178405  Cd Length: 289  Bit Score: 51.62  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  156 LARLSKIKLTALVVSTT--SAGFALAPGPF-DWSCFLLTSLGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISP 232
Cdd:PLN02809  12 LARLDKPIGTWLLAWPCmwSIALAAPPGSLpDLKMLALFGCGALLLRGAGCTINDLLDRDIDKKVERTKLRPIASGALTP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  233 LLAVSFATCCAVPGVALLTwGVNPLTGALGVFNIFLyTCCYTPLKRvsITNtWVGAVV------GAIppvMGWTAATGSL 306
Cdd:PLN02809  92 FQGVGFLGAQLLLGLGILL-QLNNYSRILGASSLLL-VFTYPLMKR--FTF-WPQAFLgltfnwGAL---LGWAAVKGSL 163


                 ....*.
gi 30410008  307 DAGALL 312
Cdd:PLN02809 164 DPAVVL 169
ubiA PRK12886
prenyltransferase; Reviewed
 159-320 6.37e-06

prenyltransferase; Reviewed


Pssm-ID: 237247  Cd Length: 291  Bit Score: 47.76  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  159 LSKIKLTALVVSTTSAGFALapgPFDWSCFLLTSLGTGLAS-------------CAANSINQFFEVPFDSNMNRTKNRPL 225
Cdd:PRK12886   5 LTKLKVFLEMIKFSHTLFAL---PFAGIGAVLAALGLPGASqldwilmamvgarTAAMGFNRLIDAEIDARNPRTAGRAI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  226 VRGQISPLLAVSFaTCCAVPGVALLTWGVNPLTGAL---GVFNIFLYTCCytplKRVsitnTWVGAVV-G---AIPPVMG 298
Cdd:PRK12886  82 PAGLISKGSAILF-IVLSSLLMLFAAWFLNPLCLYLsppALFFLLLYSYC----KRF----TALAHVVlGfclALAPLGA 152

                        170       180
                 ....*....|....*....|..
gi 30410008  299 WTAATGSLDAGALLLGGILYSW 320
Cdd:PRK12886 153 WIAIRGTIELPAILLGLAVLFW 174
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 164-302 1.53e-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: 46.34  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 164 LTALVVSTTSAGFALAPGP-FDWSCFLLTSLGTGLASCAANSINQFFEVPFDSnMNRtKNRPLVRGQISPLLAVSFATCC 242
Cdd:cd13961  12 LMAALAQYLGALFALGPLLsLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDR-INK-PDRPIPSGRISRREALILSILL 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30410008 243 AVPGVaLLTWGVNPLTGALGVFNIFL---YTccyTPLKRVSITNTWVGAVVGAIPPVMGWTAA 302
Cdd:cd13961  90 NALGL-ILAFLLSPLALLIALLNSLLlwlYS---HKLKRTPLIGNLLVALLTGLPFLFGGLAA 148
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
 164-314 1.93e-05

1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260125  Cd Length: 283  Bit Score: 45.97  E-value: 1.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 164 LTALVVSTTsAGFALA---PGPFDWSCFLLTSLGTGLASCAANSINQFFEvpF----DSNMNRTKNRPLVRGQISP---- 232
Cdd:cd13962   9 LPASLAPVL-LGTALAyylGGFFNWLLFLLALLAALLLQIGVNLANDYFD--YkkgtDTEPRSGPSRVLVSGLLSPrqvl 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 233 LLAVSFATCCAVPGVALLTWGVNPLT--GALGVFNIFLYTC-----CYTPLKRVSitntwVGAVVGAIPPVMGWTAATGS 305
Cdd:cd13962  86 RAALVLLLLAALLGLYLVALGGWLLLllGLLGILAGYFYTGgpfplSYRGLGELF-----VFLFFGLLAVLGTYYVQTGS 160


                ....*....
gi 30410008 306 LDAGALLLG 314
Cdd:cd13962 161 LSWEVLLAA 169
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 174-281 1.95e-05

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


Pssm-ID: 260126  Cd Length: 278  Bit Score: 45.93  E-value: 1.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 174 AGFALAPGPFDWSCFLLTSLGTGLASCAANS---INQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPGVAlL 250
Cdd:cd13963  18 APLLFAGQLFDPDLLLAALLAFVAFCLAASAvyiLNDLLDLEADRLHPTKRNRPIASGRLSIPAALALAVVLLLAGLA-L 96

                        90       100       110
                ....*....|....*....|....*....|..
gi 30410008 251 TWGVNPLTGALGVFNIFLyTCCYT-PLKRVSI 281
Cdd:cd13963  97 ALLLSPAFLLVLLAYLVL-NLAYSlKLKRIPL 127
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
 164-314 1.33e-03

1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441183  Cd Length: 290  Bit Score: 40.51  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 164 LTALVVSTTsAGFALA---PGPFDWSCFLLTSLGTGLASCAANSINQFF--EVPFDSNMNRTKNRPLVRGQISP----LL 234
Cdd:COG1575  11 LPAAVAPVL-LGTALAyyeTGSFNWLLFLLALLAALLLQIGVNLANDYFdyKKGTDTEERVGPSRVIVSGLLSPkqvlRA 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 235 AVSFATCCAVPGVALLT---WGVNPLtGALGVFNIFLYTC-----CYTPLKRVSitntwVGAVVGAIPPVMGWTAATGSL 306
Cdd:COG1575  90 ALLLLALALLLGLYLVLlsgWPLLLL-GLLGILAAIFYTGgpfplGYRGLGELF-----VFLFFGLVAVLGTYYVQTGTL 163


                ....*...
gi 30410008 307 DAGALLLG 314
Cdd:COG1575 164 SWAALLAS 171
ubiA PRK12873
4-hydroxybenzoate polyprenyltransferase;
198-314 2.25e-03

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 171787 [Multi-domain]  Cd Length: 294  Bit Score: 39.64  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  198 ASCAANSInqfFEVPFDSNMNRTKNRPLVRGQISPLLAVS---FATCCAVPGVALLTWGVNPLTGALGVFN---IFLYTC 271
Cdd:PRK12873  59 AGCIANDL---WDRRIDRKVERTKNRPLARGKISLKTAYSlliVLLLLSLFVVLSLPQPSRNLCLSLAFLAlppILIYPS 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 30410008  272 C--YTPLKRVSITNTWVGAVVgaIPpvmgWTAATGSLDAGALLLG 314
Cdd:PRK12873 136 AkrWFAYPQAILALCWGFAVL--IP----WAAAEGSLNGGWPLLF 174
ubiA PRK12874
4-hydroxybenzoate polyprenyltransferase;
164-321 6.78e-03

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 237242  Cd Length: 291  Bit Score: 38.45  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  164 LTALVVSttsAGFALAPGPFDWSCFLLtslGTGLASCAAN---SINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFAT 240
Cdd:PRK12874  28 FIAMIVA---SKQKNDTGWFGFKLLIL---GILAAVSARNfamAFNRLVDRDIDKDNPRTANRPSVDGRISVKSMVLFIV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  241 CCAV--PGVALLtwgVNPLTGALGvFNIFLYTCCYTPLKRVSITNTWVGAVVGAIPPVMGWTAATGSLDAGALLL----- 313
Cdd:PRK12874 102 LNALifIGVSYF---INPLAFKLS-FPFLIVLGGYSYFKRFSSLAHLVLGLSLGLAPIAGVVAVLGEIPLWSVFLalgvm 177

                        170
                 ....*....|...
gi 30410008  314 ---GG--ILYSWQ 321
Cdd:PRK12874 178 fwvAGfdLLYSLQ 190
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 156-317 8.63e-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: 8.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 156 LARLSKIkLTalVVSTTSAGFALAPGPFDWSC-FLLTSLGTGLASCAANSINQFFEVPFDSNmNRtKNRPLVRGQISPLL 234
Cdd:cd13964   4 LVRLPNL-FT--VPADVLAGAALAGGGLGPVLrLALLLLASVLLYAAGMVLNDVFDAELDAR-ER-PERPIPSGRVSRGA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008 235 AVSFATCCAVPGVALLtWGVNPLTGALGVF---NIFLYTccyTPLKRvsitnTWVGAVVGAIPP----VMGWTAATGSLD 307
Cdd:cd13964  79 ALALGAGLLAAGVALA-ALVGRLSGLVALLlaaAILLYD---AWLKH-----TPLGPLLMGLCRglnlLLGASAAAAGGL 149

                       170
                ....*....|
gi 30410008 308 AGALLLGGIL 317
Cdd:cd13964 150 GPALLAALAL 159
ubiA PRK12884
prenyltransferase; Reviewed
 189-312 9.07e-03

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 38.01  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30410008  189 LLTSLGTGLASCAANSINQFFEVPFDSnMNRTkNRPLVRGQISPLLAVSFATCCAVPGV---ALLTWGvnPLTGALgVFN 265
Cdd:PRK12884  40 LLGFLTAFFASGSANALNDYFDYEVDR-INRP-DRPIPSGRISRREALLLAILLFILGLiaaYLISPL--AFLVVI-LVS 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30410008  266 IFLYTCCYTPLKRVSITNTWVGAVVGAiPPVMGWTAATGSLDAGALL 312
Cdd:PRK12884 115 VLGILYNWKLKEYGLIGNLYVAFLTGM-TFIFGGIAVGELNEAVILL 160
 
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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