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Conserved domains on  [gi|12652629|gb|AAH00060|]
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COX10 homolog, cytochrome c oxidase assembly protein, heme A: farnesyltransferase (yeast) [Homo sapiens]

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 ...
 159-415 2.43e-112

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: 331.33  E-value: 2.43e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 159 QLSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 237
Cdd:cd13957   2 ELTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 238 SFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGG 316
Cdd:cd13957  82 IFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPlKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 317 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRV-ALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYL 395
Cdd:cd13957 162 ILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYL 241

                       250       260
                ....*....|....*....|
gi 12652629 396 GFRFYVDADRRSSRRLFFCS 415
Cdd:cd13957 242 AIKLYRSPDDKWARKLFFAS 261
 
Name Accession Description Interval E-value
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 159-415 2.43e-112

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: 331.33  E-value: 2.43e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 159 QLSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 237
Cdd:cd13957   2 ELTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 238 SFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGG 316
Cdd:cd13957  82 IFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPlKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 317 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRV-ALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYL 395
Cdd:cd13957 162 ILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYL 241

                       250       260
                ....*....|....*....|
gi 12652629 396 GFRFYVDADRRSSRRLFFCS 415
Cdd:cd13957 242 AIKLYRSPDDKWARKLFFAS 261
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 157-415 3.89e-105

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: 313.03  E-value: 3.89e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   157 LAQLSKIKLTALVVSTTAAGFALAPGP--FDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPL 234
Cdd:TIGR01473   3 YLQLTKPRIISLLLITAFAGMWLAPGGalVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   235 LAVSFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFL 313
Cdd:TIGR01473  83 EALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   314 LGGILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHP--GLCRRVALRhCLALLVLSAAAPVLDITTWTFPIMALPINAY 391
Cdd:TIGR01473 163 LFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIALY-TAALLPVSLLLAFLGGTGWLYLIVATLLGAL 241

                         250       260
                  ....*....|....*....|....*
gi 12652629   392 ISYLGFRFYVDADRRS-SRRLFFCS 415
Cdd:TIGR01473 242 FLYLAFKFYRDPTDRKkARKLFKFS 266
PLN02776 PLN02776
prenyltransferase
 160-415 2.83e-102

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 308.21  E-value: 2.83e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  160 LSKIKLTALVVSTTAAGFALAPGP-FDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:PLN02776   1 LSKARLSALVVATSGAGFVLGSGEaIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGIL 318
Cdd:PLN02776  81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  319 YSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCR--RVALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYLG 396
Cdd:PLN02776 161 YFWQMPHFMALAYMCRDDYAAGGYRMLSLADATGRRtaLVALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAYLAASA 240

                        250
                 ....*....|....*....
gi 12652629  397 FRFYVDADRRSSRRLFFCS 415
Cdd:PLN02776 241 ASFYREPTNANARKMFHGS 259
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 159-415 1.22e-78

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 245.81  E-value: 1.22e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 159 QLSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 237
Cdd:COG0109  21 ALTKPRIILLLLFTALAGMLLAAGGLpDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPREAL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 238 SFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGG 316
Cdd:COG0109 101 IFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLLFL 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 317 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLALLVLSAAAPVL----DITTWTFPIMALPINAYI 392
Cdd:COG0109 181 IIFLWTPPHFWALALKRRDDYARAGVPMLPVVKG---ERRTKRQILLYTLLLVPVSLLpyllGMAGLIYLVVALVLGAWF 257

                       250       260
                ....*....|....*....|...
gi 12652629 393 SYLGFRFYVDADRRSSRRLFFCS 415
Cdd:COG0109 258 LYLAVRLYRRPDRKWARKLFKFS 280
UbiA pfam01040
UbiA prenyltransferase family;
169-413 3.88e-55

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 183.58  E-value: 3.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   169 VVSTTAAGFALA-PGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPG 247
Cdd:pfam01040   1 LLIPALAGLALAaGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   248 VAILtLGVNPLTGALGLFNIFLYTcCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGILYSWQFPHF 326
Cdd:pfam01040  81 LLLL-LLLNPLTALLGLAALLLYV-LYTlRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   327 NALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLA---LLVLSAAAPVLDITTWTFPIMALPINAYISYLGFRFYVDA 403
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVVLG---RKAARILLALllaVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLR 235

                         250
                  ....*....|
gi 12652629   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 ...
 159-415 2.43e-112

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: 331.33  E-value: 2.43e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 159 QLSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 237
Cdd:cd13957   2 ELTKPRITLLVLLTALAGYLLAPGGVpDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKHAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 238 SFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGG 316
Cdd:cd13957  82 IFGLVLGILGLALLALFVNPLTALLGLLGIFLYVFVYTPlKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWLLFL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 317 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRV-ALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYL 395
Cdd:cd13957 162 ILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRqILLYTLLLVPLSLLLYLLGLTGWIYLVVALLLGLYFLYL 241

                       250       260
                ....*....|....*....|
gi 12652629 396 GFRFYVDADRRSSRRLFFCS 415
Cdd:cd13957 242 AIKLYRSPDDKWARKLFFAS 261
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 157-415 3.89e-105

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: 313.03  E-value: 3.89e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   157 LAQLSKIKLTALVVSTTAAGFALAPGP--FDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPL 234
Cdd:TIGR01473   3 YLQLTKPRIISLLLITAFAGMWLAPGGalVNPPLLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   235 LAVSFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFL 313
Cdd:TIGR01473  83 EALAFGLLLGVLGVAILAAFVNPLAALLGLFGIFFYVIVYTiWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   314 LGGILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHP--GLCRRVALRhCLALLVLSAAAPVLDITTWTFPIMALPINAY 391
Cdd:TIGR01473 163 LFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGerITKRQIALY-TAALLPVSLLLAFLGGTGWLYLIVATLLGAL 241

                         250       260
                  ....*....|....*....|....*
gi 12652629   392 ISYLGFRFYVDADRRS-SRRLFFCS 415
Cdd:TIGR01473 242 FLYLAFKFYRDPTDRKkARKLFKFS 266
PLN02776 PLN02776
prenyltransferase
 160-415 2.83e-102

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 308.21  E-value: 2.83e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  160 LSKIKLTALVVSTTAAGFALAPGP-FDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVS 238
Cdd:PLN02776   1 LSKARLSALVVATSGAGFVLGSGEaIDLPGLGWTCAGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  239 FATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGIL 318
Cdd:PLN02776  81 WAVVVGAAGVALLAYKTNMLTAGLGAGNILLYAFVYTPLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVLAAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  319 YSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCR--RVALRHCLALLVLSAAAPVLDITTWTFPIMALPINAYISYLG 396
Cdd:PLN02776 161 YFWQMPHFMALAYMCRDDYAAGGYRMLSLADATGRRtaLVALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAYLAASA 240

                        250
                 ....*....|....*....
gi 12652629  397 FRFYVDADRRSSRRLFFCS 415
Cdd:PLN02776 241 ASFYREPTNANARKMFHGS 259
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 159-415 1.22e-78

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 245.81  E-value: 1.22e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 159 QLSKIKLTALVVSTTAAGFALAPGPF-DWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 237
Cdd:COG0109  21 ALTKPRIILLLLFTALAGMLLAAGGLpDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPREAL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 238 SFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGG 316
Cdd:COG0109 101 IFGLVLGVLGLALLALFVNPLAALLGLLGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALLLFL 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 317 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLALLVLSAAAPVL----DITTWTFPIMALPINAYI 392
Cdd:COG0109 181 IIFLWTPPHFWALALKRRDDYARAGVPMLPVVKG---ERRTKRQILLYTLLLVPVSLLpyllGMAGLIYLVVALVLGAWF 257

                       250       260
                ....*....|....*....|...
gi 12652629 393 SYLGFRFYVDADRRSSRRLFFCS 415
Cdd:COG0109 258 LYLAVRLYRRPDRKWARKLFKFS 280
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 159-415 1.59e-62

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 204.22  E-value: 1.59e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  159 QLSKIKLTALVVSTTAAGFALAP-GPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAV 237
Cdd:PRK04375  15 ALTKPRVISLNLFTALGGMLLAPpGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRISPREAL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  238 SFATCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTP-LKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGG 316
Cdd:PRK04375  95 IFGLVLGVLGFLLLGLFVNPLAAWLTLAGIFFYVVVYTLwLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWEALILFL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  317 ILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLALLVLSAAAPVL----DITTWTFPIMALPINAYI 392
Cdd:PRK04375 175 IIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKG---IRVTKRQILLYTVLLVAVSLLpvllGMAGLLYLVVALLLGAWF 251

                        250       260
                 ....*....|....*....|...
gi 12652629  393 SYLGFRFYVDADRRSSRRLFFCS 415
Cdd:PRK04375 252 LYYAWRLYRKDDRKWARKLFRYS 274
UbiA pfam01040
UbiA prenyltransferase family;
169-413 3.88e-55

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 183.58  E-value: 3.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   169 VVSTTAAGFALA-PGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPG 247
Cdd:pfam01040   1 LLIPALAGLALAaGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVLLALG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   248 VAILtLGVNPLTGALGLFNIFLYTcCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATGSLDAGAFLLGGILYSWQFPHF 326
Cdd:pfam01040  81 LLLL-LLLNPLTALLGLAALLLYV-LYTlRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLALLLALALFLWTWAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629   327 NALSWGLREDYSRGGYCMMSVTHPglcRRVALRHCLA---LLVLSAAAPVLDITTWTFPIMALPINAYISYLGFRFYVDA 403
Cdd:pfam01040 159 LANDLRDREDDRKAGIKTLPVVLG---RKAARILLALllaVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRLR 235

                         250
                  ....*....|
gi 12652629   404 DRRSSRRLFF 413
Cdd:pfam01040 236 DPKKDAKAFF 245
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 163-323 4.57e-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: 92.60  E-value: 4.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 163 IKLTALVVSTTAAGFALAPGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATC 242
Cdd:COG0382  13 IGILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISLREALLLAIV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 243 CAVPGVAILTLgVNPLTGALGLFNIFLyTCCYTP-LKRI-SIANTWVGAVVGaIPPVMGWTAATGSLDAGAFLLGGILYS 320
Cdd:COG0382  93 LLLLALALALL-LNPLTFLLALAALAL-AWAYSLfLKRFtLLGNLVLGLLFG-LGILMGFAAVTGSLPLSAWLLALAAFL 169


                ...
gi 12652629 321 WQF 323
Cdd:COG0382 170 WTL 172
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
 158-321 8.32e-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: 80.20  E-value: 8.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 158 AQLSKIKLTALVVSTTAAGFALA---PGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPL 234
Cdd:cd13959   1 MRLDKPIGTLLLLPPALWGLLLAaggLPLPLLKLLLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 235 LAVSFATCCAVPGVAILTLgVNPLTGALGLFNIFLyTCCYtPL-KRIS-IANTWVGAVVGaIPPVMGWTAATGSLDAGAF 312
Cdd:cd13959  81 EALLFLAVQLLLGLALLLQ-LNPLTILLSPIALLL-VLIY-PLmKRFTyWPQLVLGLAFG-WGPLMGWAAVTGSLPLPAL 156


                ....*....
gi 12652629 313 LLGGILYSW 321
Cdd:cd13959 157 LLYLAVIFW 165
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 158-414 4.47e-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: 63.14  E-value: 4.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 158 AQLSKIKLTALVVSTTAAGFALAPGPFDWPC--FLLTSVGTGLASCAANSINQFFEVPFDSNMNRtkNRPLVRGQISPLL 235
Cdd:cd13956   1 LRLMRPYTLLYVLAPALAGAALAGAFAGPLPalLLLALLAVFLGAGAGYALNDYTDRELDAINKP--DRPLPSGRLSPRQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 236 AVSFATCCAVPGVAiLTLGVNPLTGALGLFNIFLYTcCYT-PLKRISIANTWVGAVVGAIPPVMGWTAATG---SLDAGA 311
Cdd:cd13956  79 ALAFAAALLLVGLA-LALALGPLALLLLLAGLLLGL-AYSlGLKRLKLGGWGVLGYATGLALLPGLGAVAAgglVPLALL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 312 FLLGGILYSWQFPHFNALsWGLREDySRGGYCMMSVThpgLCRRVALRHCLALLVLSAAAPVL--DITTWTFPIMALPIN 389
Cdd:cd13956 157 LALVFLLLGLGINLYNDL-PDVEGD-RAAGIRTLPVR---LGPRRARRLAAGLLLAALILVVLlaVAGLLGPLALLALLA 231

                       250       260
                ....*....|....*....|....*
gi 12652629 390 AYISYLGFRFYVDADRRSSRRLFFC 414
Cdd:cd13956 232 VALLALRARFARADRLPALPRGFLL 256
ubiA PRK12882
prenyltransferase; Reviewed
 175-322 8.65e-08

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 53.44  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  175 AGFALAPGPFDWPCFLLTSVGTGlascAANSINQFFEVPFDSnMNRtKNRPLVRGQISPLLAVSFATCCAVPGVAiLTLG 254
Cdd:PRK12882  30 AGGILSSPSLTGLAFAAVFLATG----AGNAINDYFDREIDR-INR-PDRPIPSGAVSPRGALAFSILLFAAGVA-LAFL 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12652629  255 VNPLTGALGLFN---IFLYTccyTPLKRIS-IANTWVGAVVGAIppvmgwtaatgsldagaFLLGGILYSWQ 322
Cdd:PRK12882 103 LPPLCLAIALFNsllLVLYA---ETLKGTPgLGNASVAYLTGST-----------------FLFGGAAVGTE 154
PLN02809 PLN02809
4-hydroxybenzoate nonaprenyltransferase
 186-313 1.97e-07

4-hydroxybenzoate nonaprenyltransferase


Pssm-ID: 178405  Cd Length: 289  Bit Score: 52.39  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  186 WPCF----------------LLTSVGTG--LASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPG 247
Cdd:PLN02809  26 WPCMwsialaappgslpdlkMLALFGCGalLLRGAGCTINDLLDRDIDKKVERTKLRPIASGALTPFQGVGFLGAQLLLG 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12652629  248 VAILtLGVNPLTGALGLFNIFLyTCCYTPLKRISianTWVGAVV------GAIppvMGWTAATGSLDAGAFL 313
Cdd:PLN02809 106 LGIL-LQLNNYSRILGASSLLL-VFTYPLMKRFT---FWPQAFLgltfnwGAL---LGWAAVKGSLDPAVVL 169
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 165-318 1.69e-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: 1.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 165 LTALVVSTTAAGFALapgPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSnMNRtKNRPLVRGQISPLLAVSFATCCA 244
Cdd:cd13961  16 LAQYLGALFALGPLL---SLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDR-INK-PDRPIPSGRISRREALILSILLN 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12652629 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 4.78e-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: 47.89  E-value: 4.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 159 QLSKIKLTALVVSTTAAGFALA---PGPFDWPCFLLTSVGTGLASCAANSINQFFEvpF----DSNMNRTKNRPLVRGQI 231
Cdd:cd13962   2 LAARPRTLPASLAPVLLGTALAyylGGFFNWLLFLLALLAALLLQIGVNLANDYFD--YkkgtDTEPRSGPSRVLVSGLL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 232 SP----LLAVSFATCCAVPGVAILTLGVNPLT--GALGLFNIFLYTccyTPLKRIS------IAntwVGAVVGAIPPVMG 299
Cdd:cd13962  80 SPrqvlRAALVLLLLAALLGLYLVALGGWLLLllGLLGILAGYFYT---GGPFPLSyrglgeLF---VFLFFGLLAVLGT 153

                       170
                ....*....|....*.
gi 12652629 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 3.60e-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: 3.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 175 AGFALAPGPFDWPCFLLTSVGTGLASCAANS---INQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFATCCAVPGVAiL 251
Cdd:cd13963  18 APLLFAGQLFDPDLLLAALLAFVAFCLAASAvyiLNDLLDLEADRLHPTKRNRPIASGRLSIPAALALAVVLLLAGLA-L 96

                        90       100       110
                ....*....|....*....|....*....|..
gi 12652629 252 TLGVNPLTGALGLFNIFLyTCCYT-PLKRISI 282
Cdd:cd13963  97 ALLLSPAFLLVLLAYLVL-NLAYSlKLKRIPL 127
ubiA PRK12886
prenyltransferase; Reviewed
 160-321 2.10e-04

prenyltransferase; Reviewed


Pssm-ID: 237247  Cd Length: 291  Bit Score: 43.14  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  160 LSKIKLTALVVSTTAAGFALapgPFDWPCFLLTSVGTGLAS-------------CAANSINQFFEVPFDSNMNRTKNRPL 226
Cdd:PRK12886   5 LTKLKVFLEMIKFSHTLFAL---PFAGIGAVLAALGLPGASqldwilmamvgarTAAMGFNRLIDAEIDARNPRTAGRAI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  227 VRGQISPLLAVSFaTCCAVPGVAILTLGVNPLTGAL---GLFNIFLYTCCytplKRIsianTWVGAVV-G---AIPPVMG 299
Cdd:PRK12886  82 PAGLISKGSAILF-IVLSSLLMLFAAWFLNPLCLYLsppALFFLLLYSYC----KRF----TALAHVVlGfclALAPLGA 152

                        170       180
                 ....*....|....*....|..
gi 12652629  300 WTAATGSLDAGAFLLGGILYSW 321
Cdd:PRK12886 153 WIAIRGTIELPAILLGLAVLFW 174
ubiA PRK12873
4-hydroxybenzoate polyprenyltransferase;
199-315 2.85e-04

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 171787 [Multi-domain]  Cd Length: 294  Bit Score: 42.73  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  199 ASCAANSInqfFEVPFDSNMNRTKNRPLVRGQISP---------LLAVSFATCCAVPG-VAILTLGVnpltGALGLFNIF 268
Cdd:PRK12873  59 AGCIANDL---WDRRIDRKVERTKNRPLARGKISLktaysllivLLLLSLFVVLSLPQpSRNLCLSL----AFLALPPIL 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 12652629  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 6.89e-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: 41.28  E-value: 6.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 159 QLSKIKLTALVVSTTAAGFALA---PGPFDWPCFLLTSVGTGLASCAANSINQFF--EVPFDSNMNRTKNRPLVRGQISP 233
Cdd:COG1575   4 EAARPRTLPAAVAPVLLGTALAyyeTGSFNWLLFLLALLAALLLQIGVNLANDYFdyKKGTDTEERVGPSRVIVSGLLSP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629 234 ----LLAVSFATCCAVPGVAILTLGVNPLT--GALGLFNIFLYTC-----CYTPLKRISiantwVGAVVGAIPPVMGWTA 302
Cdd:COG1575  84 kqvlRAALLLLALALLLGLYLVLLSGWPLLllGLLGILAAIFYTGgpfplGYRGLGELF-----VFLFFGLVAVLGTYYV 158

                       170
                ....*....|...
gi 12652629 303 ATGSLDAGAFLLG 315
Cdd:COG1575 159 QTGTLSWAALLAS 171
ubiA PRK12884
prenyltransferase; Reviewed
 190-313 3.66e-03

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 39.17  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  190 LLTSVGTGLASCAANSINQFFEVPFDSnMNRTkNRPLVRGQISPLLAVSFATCCAVPGVaILTLGVNPLTGALGLFNIFL 269
Cdd:PRK12884  40 LLGFLTAFFASGSANALNDYFDYEVDR-INRP-DRPIPSGRISRREALLLAILLFILGL-IAAYLISPLAFLVVILVSVL 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 12652629  270 yTCCYT-PLKRISIA-NTWVGAVVGAiPPVMGWTAATGSLDAGAFL 313
Cdd:PRK12884 117 -GILYNwKLKEYGLIgNLYVAFLTGM-TFIFGGIAVGELNEAVILL 160
ubiA PRK12874
4-hydroxybenzoate polyprenyltransferase;
165-322 5.93e-03

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 237242  Cd Length: 291  Bit Score: 38.45  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  165 LTALVVsttAAGFALAPGPFDWPCFLLtsvGTGLASCAAN---SINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFAT 241
Cdd:PRK12874  28 FIAMIV---ASKQKNDTGWFGFKLLIL---GILAAVSARNfamAFNRLVDRDIDKDNPRTANRPSVDGRISVKSMVLFIV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12652629  242 CCAVPGVAILTLgVNPLTGALGlFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGWTAATGS-------LDAG-AFL 313
Cdd:PRK12874 102 LNALIFIGVSYF-INPLAFKLS-FPFLIVLGGYSYFKRFSSLAHLVLGLSLGLAPIAGVVAVLGEiplwsvfLALGvMFW 179

                        170
                 ....*....|.
gi 12652629  314 LGG--ILYSWQ 322
Cdd:PRK12874 180 VAGfdLLYSLQ 190
 
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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