NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|292495084|sp|Q12887|]
View 

RecName: Full=Protoheme IX farnesyltransferase, mitochondrial; AltName: Full=Heme O synthase; Flags: Precursor

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 160-415 1.05e-111

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: 329.40  E-value: 1.05e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:cd13957    3 LTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHALI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGI 317
Cdd:cd13957   83 FGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPlKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFLI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 318 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRV-ALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYLG 396
Cdd:cd13957  163 LFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYLA 242

                        250
                 ....*....|....*....
gi 292495084 397 FRFYVDADRRSSRRLFFCS 415
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 ...
 160-415 1.05e-111

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: 329.40  E-value: 1.05e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:cd13957    3 LTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHALI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGI 317
Cdd:cd13957   83 FGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPlKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFLI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 318 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRV-ALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYLG 396
Cdd:cd13957  163 LFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYLA 242

                        250
                 ....*....|....*....
gi 292495084 397 FRFYVDADRRSSRRLFFCS 415
Cdd:cd13957  243 IKLYRSPDDKWARKLFFAS 261
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 160-415 5.38e-104

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: 310.33  E-value: 5.38e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  160 LSKIKLTALVVSTTAAGFALAPGP--FDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 237
Cdd:TIGR01473   6 LTKPRIISLLLITAFAGMWLAPGGalVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPREAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  238 SFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGG 316
Cdd:TIGR01473  86 AFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWLLFA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  317 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHP--GLCRRVALRhCLALLVLSAAAPVLDITTWTFPIMALPINAYISY 394
Cdd:TIGR01473 166 IIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIALY-TAALLPVSLLLAFLGGTGWLYLIVATLLGALFLY 244

                         250       260
                  ....*....|....*....|..
gi 292495084  395 LGFRFYVDADRRS-SRRLFFCS 415
Cdd:TIGR01473 245 LAFKFYRDPTDRKkARKLFKFS 266
PLN02776 PLN02776
prenyltransferase
 160-415 3.06e-102

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 308.21  E-value: 3.06e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALAPGP-FDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:PLN02776   1 LSKARLSALVVATSGAGFVLGSGEaIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGIL 318
Cdd:PLN02776  81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 319 YSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCR--RVALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYLG 396
Cdd:PLN02776 161 YFWQMPHFMALAYMCRDDYAAGGYRMLSLADATGRRtaLVALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAYLAASA 240

                        250
                 ....*....|....*....
gi 292495084 397 FRFYVDADRRSSRRLFFCS 415
Cdd:PLN02776 241 ASFYREPTNANARKMFHGS 259
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 160-415 4.17e-78

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 244.66  E-value: 4.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:COG0109   22 LTKPRIILLLLFTALAGMLLAAGGLpDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPREALI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGI 317
Cdd:COG0109  102 FGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLLFLI 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 318 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLALLVLSAAAPVL----DITTWTFPIMALPINAYIS 393
Cdd:COG0109  182 IFLWTPPHFWALALKRRDDYARAGVPMLPVVKG---ERRTKRQILLYTLLLVPVSLLpyllGMAGLIYLVVALVLGAWFL 258

                        250       260
                 ....*....|....*....|..
gi 292495084 394 YLGFRFYVDADRRSSRRLFFCS 415
Cdd:COG0109  259 YLAVRLYRRPDRKWARKLFKFS 280
UbiA pfam01040
UbiA prenyltransferase family;
169-413 5.12e-55

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 183.20  E-value: 5.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  169 VVSTTAAGFALA-PGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPG 247
Cdd:pfam01040   1 LLIPALAGLALAaGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  248 VAILtLGVNPLTGALGLFNIFLYTcCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGILYSWQFPHF 326
Cdd:pfam01040  81 LLLL-LLLNPLTALLGLAALLLYV-LYTlRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  327 NALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLA---LLVLSAAAPVLDITTWTFPIMALPINAYISYLGFRFYVDA 403
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVVLG---RKAARILLALllaVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLR 235

                         250
                  ....*....|
gi 292495084  404 DRRSSRRLFF 413
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 ...
 160-415 1.05e-111

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: 329.40  E-value: 1.05e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:cd13957    3 LTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHALI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGI 317
Cdd:cd13957   83 FGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPlKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFLI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 318 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRV-ALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYLG 396
Cdd:cd13957  163 LFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYLA 242

                        250
                 ....*....|....*....
gi 292495084 397 FRFYVDADRRSSRRLFFCS 415
Cdd:cd13957  243 IKLYRSPDDKWARKLFFAS 261
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 160-415 5.38e-104

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: 310.33  E-value: 5.38e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  160 LSKIKLTALVVSTTAAGFALAPGP--FDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 237
Cdd:TIGR01473   6 LTKPRIISLLLITAFAGMWLAPGGalVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPREAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  238 SFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGG 316
Cdd:TIGR01473  86 AFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWLLFA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  317 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHP--GLCRRVALRhCLALLVLSAAAPVLDITTWTFPIMALPINAYISY 394
Cdd:TIGR01473 166 IIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIALY-TAALLPVSLLLAFLGGTGWLYLIVATLLGALFLY 244

                         250       260
                  ....*....|....*....|..
gi 292495084  395 LGFRFYVDADRRS-SRRLFFCS 415
Cdd:TIGR01473 245 LAFKFYRDPTDRKkARKLFKFS 266
PLN02776 PLN02776
prenyltransferase
 160-415 3.06e-102

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 308.21  E-value: 3.06e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALAPGP-FDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:PLN02776   1 LSKARLSALVVATSGAGFVLGSGEaIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGIL 318
Cdd:PLN02776  81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 319 YSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCR--RVALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYLG 396
Cdd:PLN02776 161 YFWQMPHFMALAYMCRDDYAAGGYRMLSLADATGRRtaLVALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAYLAASA 240

                        250
                 ....*....|....*....
gi 292495084 397 FRFYVDADRRSSRRLFFCS 415
Cdd:PLN02776 241 ASFYREPTNANARKMFHGS 259
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 160-415 4.17e-78

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 244.66  E-value: 4.17e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:COG0109   22 LTKPRIILLLLFTALAGMLLAAGGLpDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPREALI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGI 317
Cdd:COG0109  102 FGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLLFLI 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 318 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLALLVLSAAAPVL----DITTWTFPIMALPINAYIS 393
Cdd:COG0109  182 IFLWTPPHFWALALKRRDDYARAGVPMLPVVKG---ERRTKRQILLYTLLLVPVSLLpyllGMAGLIYLVVALVLGAWFL 258

                        250       260
                 ....*....|....*....|..
gi 292495084 394 YLGFRFYVDADRRSSRRLFFCS 415
Cdd:COG0109  259 YLAVRLYRRPDRKWARKLFKFS 280
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 160-415 7.08e-62

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 202.68  E-value: 7.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALAP-GPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:PRK04375  16 LTKPRVISLNLFTALGGMLLAPpGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRISPREALI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGI 317
Cdd:PRK04375  96 FGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWEALILFLI 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 318 LYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLALLVLSAAAPVL----DITTWTFPIMALPINAYIS 393
Cdd:PRK04375 176 IFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKG---IRVTKRQILLYTVLLVAVSLLpvllGMAGLLYLVVALLLGAWFL 252

                        250       260
                 ....*....|....*....|..
gi 292495084 394 YLGFRFYVDADRRSSRRLFFCS 415
Cdd:PRK04375 253 YYAWRLYRKDDRKWARKLFRYS 274
UbiA pfam01040
UbiA prenyltransferase family;
169-413 5.12e-55

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 183.20  E-value: 5.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  169 VVSTTAAGFALA-PGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPG 247
Cdd:pfam01040   1 LLIPALAGLALAaGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  248 VAILtLGVNPLTGALGLFNIFLYTcCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGILYSWQFPHF 326
Cdd:pfam01040  81 LLLL-LLLNPLTALLGLAALLLYV-LYTlRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084  327 NALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLA---LLVLSAAAPVLDITTWTFPIMALPINAYISYLGFRFYVDA 403
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVVLG---RKAARILLALllaVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLR 235

                         250
                  ....*....|
gi 292495084  404 DRRSSRRLFF 413
Cdd:pfam01040 236 DPKKDAKAFF 245
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 157-323 5.59e-22

4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate polyprenyltransferase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440151  Cd Length: 280  Bit Score: 95.30  E-value: 5.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 157 LARLSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLL 235
Cdd:COG0382    6 LLRLDRPIGILLLLWPTLWALFLAAGGLpDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 236 AVSFATCCAVPGVAILTLgVNPLTGALGLFNIFLyTCCYTP-LKRI-SIANTWVGAVVGaIPPVMGWTAATGSLDAGAFL 313
Cdd:COG0382   86 ALLLAIVLLLLALALALL-LNPLTFLLALAALAL-AWAYSLfLKRFtLLGNLVLGLLFG-LGILMGFAAVTGSLPLSAWL 162

                        170
                 ....*....|
gi 292495084 314 LGGILYSWQF 323
Cdd:COG0382  163 LALAAFLWTL 172
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
 158-321 5.55e-18

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: 83.67  E-value: 5.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 158 ARLSKIKLTALVVSTTAAGFALA---PGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPL 234
Cdd:cd13959    1 MRLDKPIGTLLLLPPALWGLLLAaggLPLPLLKLLLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 235 LAVSFATCCAVPGVAILTLgVNPLTGALGLFNIFLyTCCYtPL-KRIS-IANTWVGAVVGaIPPVMGWTAATGSLDAGAF 312
Cdd:cd13959   81 EALLFLAVQLLLGLALLLQ-LNPLTILLSPIALLL-VLIY-PLmKRFTyWPQLVLGLAFG-WGPLMGWAAVTGSLPLPAL 156


                 ....*....
gi 292495084 313 LLGGILYSW 321
Cdd:cd13959  157 LLYLAVIFW 165
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 158-414 2.59e-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: 63.91  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 158 ARLSKIKLTALVVSTTAAGFALAPGPFDWPC--FLLTSVGTGLASCAANSINQFFEVPFDSNMNRtkNRPLVRGQISPLL 235
Cdd:cd13956    1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLPalLLLALLAVFLGAGAGYALNDYTDRELDAINKP--DRPLPSGRLSPRQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 236 AVSFATCCAVPGVAiLTLGVNPLTGALGLFNIFLYTcCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATG---SLDAGA 311
Cdd:cd13956   79 ALAFAAALLLVGLA-LALALGPLALLLLLAGLLLGL-AYSlGLKRLKLGGWGVLGYATGLALLPGLGAVAAgglVPLALL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 312 FLLGGILYSWQFPHFNALsWGLREDySRGGYCMMSVThpgLCRRVALRHCLALLVLSAAAPVL--DITTWTFPIMALPIN 389
Cdd:cd13956  157 LALVFLLLGLGINLYNDL-PDVEGD-RAAGIRTLPVR---LGPRRARRLAAGLLLAALILVVLlaVAGLLGPLALLALLA 231

                        250       260
                 ....*....|....*....|....*
gi 292495084 390 AYISYLGFRFYVDADRRSSRRLFFC 414
Cdd:cd13956  232 VALLALRARFARADRLPALPRGFLL 256
PLN02809 PLN02809
4-hydroxybenzoate nonaprenyltransferase
 157-313 2.53e-08

4-hydroxybenzoate nonaprenyltransferase


Pssm-ID: 178405  Cd Length: 289  Bit Score: 55.08  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 157 LARLSKIKLTALVVSTTAAGFALAPGPFDWPCF-LLTSVGTG--LASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISP 233
Cdd:PLN02809  12 LARLDKPIGTWLLAWPCMWSIALAAPPGSLPDLkMLALFGCGalLLRGAGCTINDLLDRDIDKKVERTKLRPIASGALTP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 234 LLAVSFATCCAVPGVAILtLGVNPLTGALGLFNIFLyTCCYTPLKRISianTWVGAVV------GAIppvMGWTAATGSL 307
Cdd:PLN02809  92 FQGVGFLGAQLLLGLGIL-LQLNNYSRILGASSLLL-VFTYPLMKRFT---FWPQAFLgltfnwGAL---LGWAAVKGSL 163


                 ....*.
gi 292495084 308 DAGAFL 313
Cdd:PLN02809 164 DPAVVL 169
ubiA PRK12882
prenyltransferase; Reviewed
 175-322 9.22e-08

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 53.05  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 175 AGFALAPGPFDWPCFLLTSVGTGlascAANSINQFFEVPFDSnMNRtKNRPLVRGQISPLLAVSFATCCAVPGVAiLTLG 254
Cdd:PRK12882  30 AGGILSSPSLTGLAFAAVFLATG----AGNAINDYFDREIDR-INR-PDRPIPSGAVSPRGALAFSILLFAAGVA-LAFL 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292495084 255 VNPLTGALGLFN---IFLYTccyTPLKRIS-IANTWVGAVVGAIppvmgwtaatgsldagaFLLGGILYSWQ 322
Cdd:PRK12882 103 LPPLCLAIALFNsllLVLYA---ETLKGTPgLGNASVAYLTGST-----------------FLFGGAAVGTE 154
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 165-318 1.71e-06

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: 49.42  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 165 LTALVVSTTAAGFALapgPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSnMNRtKNRPLVRGQISPLLAVSFATCCA 244
Cdd:cd13961   16 LAQYLGALFALGPLL---SLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDR-INK-PDRPIPSGRISRREALILSILLN 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292495084 245 VPGVaILTLGVNPLTGALGLFNIFL---YTccyTPLKRISIANTWVGAVVGAIPPVMGWtAATGSLDAGAFLLGGIL 318
Cdd:cd13961   91 ALGL-ILAFLLSPLALLIALLNSLLlwlYS---HKLKRTPLIGNLLVALLTGLPFLFGG-LAAGNLLLIILLLALFA 162
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
 159-315 6.55e-06

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


Pssm-ID: 260125  Cd Length: 283  Bit Score: 47.51  E-value: 6.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 159 RLSKIKLTALVVSTTAAGFALA---PGPFDWPCFLLTSVGTGLASCAANSINQFFEvpF----DSNMNRTKNRPLVRGQI 231
Cdd:cd13962    2 LAARPRTLPASLAPVLLGTALAyylGGFFNWLLFLLALLAALLLQIGVNLANDYFD--YkkgtDTEPRSGPSRVLVSGLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 232 SP----LLAVSFATCCAVPGVAILTLGVNPLT--GALGLFNIFLYTccyTPLKRIS------IAntwVGAVVGAIPPVMG 299
Cdd:cd13962   80 SPrqvlRAALVLLLLAALLGLYLVALGGWLLLllGLLGILAGYFYT---GGPFPLSyrglgeLF---VFLFFGLLAVLGT 153

                        170
                 ....*....|....*.
gi 292495084 300 WTAATGSLDAGAFLLG 315
Cdd:cd13962  154 YYVQTGSLSWEVLLAA 169
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 175-282 3.77e-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: 45.16  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 175 AGFALAPGPFDWPCFLLTSVGTGLASCAANS---INQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPGVAiL 251
Cdd:cd13963   18 APLLFAGQLFDPDLLLAALLAFVAFCLAASAvyiLNDLLDLEADRLHPTKRNRPIASGRLSIPAALALAVVLLLAGLA-L 96

                         90       100       110
                 ....*....|....*....|....*....|..
gi 292495084 252 TLGVNPLTGALGLFNIFLyTCCYT-PLKRISI 282
Cdd:cd13963   97 ALLLSPAFLLVLLAYLVL-NLAYSlKLKRIPL 127
ubiA PRK12886
prenyltransferase; Reviewed
 160-321 2.18e-04

prenyltransferase; Reviewed


Pssm-ID: 237247  Cd Length: 291  Bit Score: 43.14  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 160 LSKIKLTALVVSTTAAGFALapgPFDWPCFLLTSVGTGLAS-------------CAANSINQFFEVPFDSNMNRTKNRPL 226
Cdd:PRK12886   5 LTKLKVFLEMIKFSHTLFAL---PFAGIGAVLAALGLPGASqldwilmamvgarTAAMGFNRLIDAEIDARNPRTAGRAI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 227 VRGQISPLLAVSFaTCCAVPGVAILTLGVNPLTGAL---GLFNIFLYTCCytplKRIsianTWVGAVV-G---AIPPVMG 299
Cdd:PRK12886  82 PAGLISKGSAILF-IVLSSLLMLFAAWFLNPLCLYLsppALFFLLLYSYC----KRF----TALAHVVlGfclALAPLGA 152

                        170       180
                 ....*....|....*....|..
gi 292495084 300 WTAATGSLDAGAFLLGGILYSW 321
Cdd:PRK12886 153 WIAIRGTIELPAILLGLAVLFW 174
ubiA PRK12873
4-hydroxybenzoate polyprenyltransferase;
199-315 2.96e-04

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 171787 [Multi-domain]  Cd Length: 294  Bit Score: 42.73  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 199 ASCAANSInqfFEVPFDSNMNRTKNRPLVRGQISP---------LLAVSFATCCAVPG-VAILTLGVnpltGALGLFNIF 268
Cdd:PRK12873  59 AGCIANDL---WDRRIDRKVERTKNRPLARGKISLktaysllivLLLLSLFVVLSLPQpSRNLCLSL----AFLALPPIL 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 292495084 269 LYTCC--YTPLKRISIANTWVGAVVgaIPpvmgWTAATGSLDAGAFLLG 315
Cdd:PRK12873 132 IYPSAkrWFAYPQAILALCWGFAVL--IP----WAAAEGSLNGGWPLLF 174
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
 159-315 8.69e-04

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: 40.90  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 159 RLSKIKLTALVVSTTAAGFALA---PGPFDWPCFLLTSVGTGLASCAANSINQFF--EVPFDSNMNRTKNRPLVRGQISP 233
Cdd:COG1575    4 EAARPRTLPAAVAPVLLGTALAyyeTGSFNWLLFLLALLAALLLQIGVNLANDYFdyKKGTDTEERVGPSRVIVSGLLSP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 234 ----LLAVSFATCCAVPGVAILTLGVNPLT--GALGLFNIFLYTC-----CYTPLKRISiantwVGAVVGAIPPVMGWTA 302
Cdd:COG1575   84 kqvlRAALLLLALALLLGLYLVLLSGWPLLllGLLGILAAIFYTGgpfplGYRGLGELF-----VFLFFGLVAVLGTYYV 158

                        170
                 ....*....|...
gi 292495084 303 ATGSLDAGAFLLG 315
Cdd:COG1575  159 QTGTLSWAALLAS 171
ubiA PRK12884
prenyltransferase; Reviewed
 190-313 3.89e-03

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 39.17  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 190 LLTSVGTGLASCAANSINQFFEVPFDSnMNRTkNRPLVRGQISPLLAVSFATCCAVPGVaILTLGVNPLTGALGLFNIFL 269
Cdd:PRK12884  40 LLGFLTAFFASGSANALNDYFDYEVDR-INRP-DRPIPSGRISRREALLLAILLFILGL-IAAYLISPLAFLVVILVSVL 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 292495084 270 yTCCYT-PLKRISIA-NTWVGAVVGAiPPVMGWTAATGSLDAGAFL 313
Cdd:PRK12884 117 -GILYNwKLKEYGLIgNLYVAFLTGM-TFIFGGIAVGELNEAVILL 160
ubiA PRK12874
4-hydroxybenzoate polyprenyltransferase;
165-322 5.99e-03

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 237242  Cd Length: 291  Bit Score: 38.45  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 165 LTALVVsttAAGFALAPGPFDWPCFLLtsvGTGLASCAAN---SINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFAT 241
Cdd:PRK12874  28 FIAMIV---ASKQKNDTGWFGFKLLIL---GILAAVSARNfamAFNRLVDRDIDKDNPRTANRPSVDGRISVKSMVLFIV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 242 CCAVPGVAILTLgVNPLTGALGlFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGWTAATGS-------LDAG-AFL 313
Cdd:PRK12874 102 LNALIFIGVSYF-INPLAFKLS-FPFLIVLGGYSYFKRFSSLAHLVLGLSLGLAPIAGVVAVLGEiplwsvfLALGvMFW 179

                        170
                 ....*....|.
gi 292495084 314 LGG--ILYSWQ 322
Cdd:PRK12874 180 VAGfdLLYSLQ 190
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 157-315 8.18e-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: 8.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 157 LARLSKIkLTalVVSTTAAGFALAPGPFDWPC-FLLTSVGTGLASCAANSINQFFEVPFDSNmNRtKNRPLVRGQISPLL 235
Cdd:cd13964    4 LVRLPNL-FT--VPADVLAGAALAGGGLGPVLrLALLLLASVLLYAAGMVLNDVFDAELDAR-ER-PERPIPSGRVSRGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292495084 236 AVSFATCCAVPGVAILTLgVNPLTGALGLF---NIFLYTccyTPLKRISIA----------NTWVGAVVGAIPPVMGWTA 302
Cdd:cd13964   79 ALALGAGLLAAGVALAAL-VGRLSGLVALLlaaAILLYD---AWLKHTPLGpllmglcrglNLLLGASAAAAGGLGPALL 154

                        170
                 ....*....|...
gi 292495084 303 ATGSLdaGAFLLG 315
Cdd:cd13964  155 AALAL--GVYIAG 165
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH