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Conserved domains on  [gi|2789617066|ref|WP_370876314|]
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heme o synthase [Bacillus pumilus]

Protein Classification

protoheme IX farnesyltransferase( domain architecture ID 10792362)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
15-293 2.13e-97

protoheme IX farnesyltransferase; Provisional


:

Pssm-ID: 235293  Cd Length: 296  Bit Score: 288.58  E-value: 2.13e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  15 QTVKSGIIKSNLIPMCAGLTLALYTyqidiLHKSIEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVN 94
Cdd:PRK04375   15 ALTKPRVISLNLFTALGGMLLAPPG-----VPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRIS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  95 PKKVLWLSILMSVLGLGFLAFTT-YLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPA 173
Cdd:PRK04375   90 PREALIFGLVLGVLGFLLLGLFVnPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWEA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 174 IMgLFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLG 250
Cdd:PRK04375  170 LI-LFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLpvlLGMAGLLYLVVALLLG 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2789617066 251 LIWICLSILGYKRMhSEKWASIMFVYSLIYMTTLYSTVIIYSL 293
Cdd:PRK04375  249 AWFLYYAWRLYRKD-DRKWARKLFRYSINYLTLLFVALLVDHL 290
 
Name Accession Description Interval E-value
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
15-293 2.13e-97

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 288.58  E-value: 2.13e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  15 QTVKSGIIKSNLIPMCAGLTLALYTyqidiLHKSIEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVN 94
Cdd:PRK04375   15 ALTKPRVISLNLFTALGGMLLAPPG-----VPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRIS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  95 PKKVLWLSILMSVLGLGFLAFTT-YLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPA 173
Cdd:PRK04375   90 PREALIFGLVLGVLGFLLLGLFVnPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWEA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 174 IMgLFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLG 250
Cdd:PRK04375  170 LI-LFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLpvlLGMAGLLYLVVALLLG 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2789617066 251 LIWICLSILGYKRMhSEKWASIMFVYSLIYMTTLYSTVIIYSL 293
Cdd:PRK04375  249 AWFLYYAWRLYRKD-DRKWARKLFRYSINYLTLLFVALLVDHL 290
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
18-293 1.46e-93

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 278.94  E-value: 1.46e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  18 KSGIIKSNLIPMCAGLTLALYTYqIDILhksiEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKK 97
Cdd:COG0109    24 KPRIILLLLFTALAGMLLAAGGL-PDLL----LLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPRE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  98 VLWLSILMSVLGLGFLA-FTTYLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMg 176
Cdd:COG0109    99 ALIFGLVLGVLGLALLAlFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALL- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 177 LFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLGLIW 253
Cdd:COG0109   178 LFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLpylLGMAGLIYLVVALVLGAWF 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2789617066 254 ICLSILGYKRMhSEKWASIMFVYSLIYMTTLYSTVIIYSL 293
Cdd:COG0109   258 LYLAVRLYRRP-DRKWARKLFKFSILYLTLLFLALLVDHL 296
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
18-284 1.54e-87

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: 262.38  E-value: 1.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  18 KSGIIKSNLIPMCAGLTLALYTyqidiLHKSIEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKK 97
Cdd:cd13957     5 KPRITLLVLLTALAGYLLAPGG-----VPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  98 VLWLSILMSVLGLGFLAFTT-YLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMg 176
Cdd:cd13957    80 ALIFGLVLGILGLALLALFVnPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWL- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 177 LFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLGLIW 253
Cdd:cd13957   159 LFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLlylLGLTGWIYLVVALLLGLYF 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2789617066 254 ICLSILGYKRMhSEKWASIMFVYSLIYMTTL 284
Cdd:cd13957   239 LYLAIKLYRSP-DDKWARKLFFASLIYLPLL 268
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
18-290 4.59e-81

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: 246.39  E-value: 4.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  18 KSGIIKSNLIPMCAGLTLALYTYQIDILhksiEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKK 97
Cdd:TIGR01473   8 KPRIISLLLITAFAGMWLAPGGALVNPP----LLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPRE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  98 VLWLSILMSVLGLGFLA-FTTYLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMg 176
Cdd:TIGR01473  84 ALAFGLLLGVLGVAILAaFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWL- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 177 LFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLGLIW 253
Cdd:TIGR01473 163 LFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLlafLGGTGWLYLIVATLLGALF 242
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2789617066 254 ICLSILGYKRMHSEKWASIMFVYSLIYMTTLYSTVII 290
Cdd:TIGR01473 243 LYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLI 279
UbiA pfam01040
UbiA prenyltransferase family;
26-279 5.81e-47

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 157.77  E-value: 5.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  26 LIPMCAGLTLALYtyqidILHKSIEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILM 105
Cdd:pfam01040   2 LIPALAGLALAAG-----GVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 106 SVLGLGFLAFTTYLAAIIGLIGLFFYIFpYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDIShPAIMGLFFITIIWQ 185
Cdd:pfam01040  77 LALGLLLLLLLNPLTALLGLAALLLYVL-YTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLS-PLALLLALALFLWT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 186 MPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNL--YILAITLSSFLFHSLSIGLVLVSFFLGLIWICLSILGYKR 263
Cdd:pfam01040 155 WAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALllAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRL 234
                         250
                  ....*....|....*.
gi 2789617066 264 MHSEKWASIMFVYSLI 279
Cdd:pfam01040 235 RDPKKDAKAFFFLSSL 250
 
Name Accession Description Interval E-value
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
15-293 2.13e-97

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 288.58  E-value: 2.13e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  15 QTVKSGIIKSNLIPMCAGLTLALYTyqidiLHKSIEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVN 94
Cdd:PRK04375   15 ALTKPRVISLNLFTALGGMLLAPPG-----VPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRIS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  95 PKKVLWLSILMSVLGLGFLAFTT-YLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPA 173
Cdd:PRK04375   90 PREALIFGLVLGVLGFLLLGLFVnPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSWEA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 174 IMgLFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLG 250
Cdd:PRK04375  170 LI-LFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLpvlLGMAGLLYLVVALLLG 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2789617066 251 LIWICLSILGYKRMhSEKWASIMFVYSLIYMTTLYSTVIIYSL 293
Cdd:PRK04375  249 AWFLYYAWRLYRKD-DRKWARKLFRYSINYLTLLFVALLVDHL 290
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
18-293 1.46e-93

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 278.94  E-value: 1.46e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  18 KSGIIKSNLIPMCAGLTLALYTYqIDILhksiEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKK 97
Cdd:COG0109    24 KPRIILLLLFTALAGMLLAAGGL-PDLL----LLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNRPLPTGRISPRE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  98 VLWLSILMSVLGLGFLA-FTTYLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMg 176
Cdd:COG0109    99 ALIFGLVLGVLGLALLAlFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAVTGSLSLEALL- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 177 LFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLGLIW 253
Cdd:COG0109   178 LFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLpylLGMAGLIYLVVALVLGAWF 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2789617066 254 ICLSILGYKRMhSEKWASIMFVYSLIYMTTLYSTVIIYSL 293
Cdd:COG0109   258 LYLAVRLYRRP-DRKWARKLFKFSILYLTLLFLALLVDHL 296
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
18-284 1.54e-87

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: 262.38  E-value: 1.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  18 KSGIIKSNLIPMCAGLTLALYTyqidiLHKSIEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKK 97
Cdd:cd13957     5 KPRITLLVLLTALAGYLLAPGG-----VPDLLLLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISPKH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  98 VLWLSILMSVLGLGFLAFTT-YLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMg 176
Cdd:cd13957    80 ALIFGLVLGILGLALLALFVnPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAATGSLDLGAWL- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 177 LFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLGLIW 253
Cdd:cd13957   159 LFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLlylLGLTGWIYLVVALLLGLYF 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2789617066 254 ICLSILGYKRMhSEKWASIMFVYSLIYMTTL 284
Cdd:cd13957   239 LYLAIKLYRSP-DDKWARKLFFASLIYLPLL 268
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
18-290 4.59e-81

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: 246.39  E-value: 4.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  18 KSGIIKSNLIPMCAGLTLALYTYQIDILhksiEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKK 97
Cdd:TIGR01473   8 KPRIISLLLITAFAGMWLAPGGALVNPP----LLLLTLLGTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRISPRE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  98 VLWLSILMSVLGLGFLA-FTTYLAAIIGLIGLFFYIFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMg 176
Cdd:TIGR01473  84 ALAFGLLLGVLGVAILAaFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAVTGSISLGAWL- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 177 LFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---FHSLSIGLVLVSFFLGLIW 253
Cdd:TIGR01473 163 LFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLlafLGGTGWLYLIVATLLGALF 242
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2789617066 254 ICLSILGYKRMHSEKWASIMFVYSLIYMTTLYSTVII 290
Cdd:TIGR01473 243 LYLAFKFYRDPTDRKKARKLFKFSLIYLALLFVALLI 279
UbiA pfam01040
UbiA prenyltransferase family;
26-279 5.81e-47

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 157.77  E-value: 5.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  26 LIPMCAGLTLALYtyqidILHKSIEILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILM 105
Cdd:pfam01040   2 LIPALAGLALAAG-----GVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRISPREALIFALVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 106 SVLGLGFLAFTTYLAAIIGLIGLFFYIFpYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDIShPAIMGLFFITIIWQ 185
Cdd:pfam01040  77 LALGLLLLLLLNPLTALLGLAALLLYVL-YTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLS-PLALLLALALFLWT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 186 MPHFYSIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNL--YILAITLSSFLFHSLSIGLVLVSFFLGLIWICLSILGYKR 263
Cdd:pfam01040 155 WAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALllAVALLLLLLLLLLLLGGLYLLLALLLAALALLYAARLLRL 234
                         250
                  ....*....|....*.
gi 2789617066 264 MHSEKWASIMFVYSLI 279
Cdd:pfam01040 235 RDPKKDAKAFFFLSSL 250
PLN02776 PLN02776
prenyltransferase
56-296 3.69e-30

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 116.38  E-value: 3.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  56 AGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILMSVLGLGFLAF-TTYLAAIIGLIGLFFYIFP 134
Cdd:PLN02776   36 AGTMLCAASANTLNQVFEVKNDSKMKRTMRRPLPSGRISVPHAVAWAVVVGAAGVALLAYkTNMLTAGLGAGNILLYAFV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 135 YTiWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIM---GLFFitiiWQMPHFYSIAIRKQNEYKAANIPMLPVV 211
Cdd:PLN02776  116 YT-PLKQIHPANTWVGAVVGAIPPLMGWAAASGQLDAGAMVlaaALYF----WQMPHFMALAYMCRDDYAAGGYRMLSLA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 212 -KGMKRT---YLQTNLYILAITLSSFLFHSLSIGLVLVSFFLGLIwICLSILGYKRMHSEKWASIMFVYSLIYMTTLYST 287
Cdd:PLN02776  191 dATGRRTalvALRNCLYLAPLGFLAYDWGVTSSPFALEAALLTAY-LAASAASFYREPTNANARKMFHGSLLYLPAFMAL 269

                  ....*....
gi 2789617066 288 VIIYSLTRQ 296
Cdd:PLN02776  270 LLLHRVPND 278
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
26-186 1.70e-19

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: 85.98  E-value: 1.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  26 LIPMCAGLTLALYTYQIDILHKsieILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILM 105
Cdd:cd13959    13 LPPALWGLLLAAGGLPLPLLKL---LLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVKEALLFLAVQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 106 SVLGLGFLAFTTYLAAIIGLIGLFFYIF-PYTiwsKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMgLFFITIIW 184
Cdd:cd13959    90 LLLGLALLLQLNPLTILLSPIALLLVLIyPLM---KRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPLPALL-LYLAVIFW 165

                  ..
gi 2789617066 185 QM 186
Cdd:cd13959   166 TA 167
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
26-280 2.65e-19

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: 85.67  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  26 LIPMCAGLTLAlYTYQIDILHksieILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILM 105
Cdd:COG0382    19 LWPTLWALFLA-AGGLPDLLL----LLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISLREALLLAIVL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 106 SVLGLGFLAFTTYLAAIIGLIGLFFYIFpYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMgLFFITIIWQ 185
Cdd:COG0382    94 LLLALALALLLNPLTFLLALAALALAWA-YSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGSLPLSAWL-LALAAFLWT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 186 MphfySIAIRK----QNEYKAANIPMLPVVKGMKRTYLQ-TNLYILAITLSSFLFHSLSIG---LVLVSFFLGLIWICLS 257
Cdd:COG0382   172 L----AYDTIYdledREGDRKIGIKTLAILFGVRDALIIaGVLYALAVLLLLLLGLLAGLGllyLLGLLAALLLLYLSQL 247
                         250       260
                  ....*....|....*....|...
gi 2789617066 258 ILGYKRMHSEKWASIMFVYSLIY 280
Cdd:COG0382   248 WLLRPRKKDPARALKLFKLNMLL 270
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
52-245 1.22e-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: 63.52  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  52 LLAFAGSILLIGAAGALNNLYDRDIDSVMNRtkNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIGLFFy 131
Cdd:cd13956    35 LLALLAVFLGAGAGYALNDYTDRELDAINKP--DRPLPSGRLSPRQALAFAAALLLVGLALALALGPLALLLLLAGLLL- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 132 IFPYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMgLFFITIIWQMPHFYSIAIRKQNEY-KAANIPMLPV 210
Cdd:cd13956   112 GLAYSLGLKRLKLGGWGVLGYATGLALLPGLGAVAAGGLVPLAL-LLALVFLLLGLGINLYNDLPDVEGdRAAGIRTLPV 190
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2789617066 211 VKGMKRT-YLQTNLYILAITLSSFLFHSLSIGLVLV 245
Cdd:cd13956   191 RLGPRRArRLAAGLLLAALILVVLLAVAGLLGPLAL 226
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
31-266 1.60e-11

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: 63.29  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  31 AGLTLALYTYQIDILHKSIEILLAFAGSILLIGAAGALNNLYDRDIDSVmNRtKNRPTVTGEVNPKKVLWLSILMSVLGL 110
Cdd:cd13961    17 AQYLGALFALGPLLSLNDLELLLLFLSVFLIAAAGYIINDYFDVEIDRI-NK-PDRPIPSGRISRREALILSILLNALGL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 111 GFLAFTTYLAAIIGLIGLFFYIFpYTIWSKRKTVYNTEIGSISGAMPPLIGWAAISPDIShpaIMGLFFITIiwqmphFY 190
Cdd:cd13961    95 ILAFLLSPLALLIALLNSLLLWL-YSHKLKRTPLIGNLLVALLTGLPFLFGGLAAGNLLL---IILLLALFA------FL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 191 SIAIR---KQNEY----KAANIPMLPVVKGMKRTYLQTNLYILAITLSSFL---------FHSLSIGLVLVSFFLGLIWI 254
Cdd:cd13961   165 ITLGReivKDIEDvegdRAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLpyllgglgiLYLILIIIADLLFLYSAIRL 244
                         250
                  ....*....|..
gi 2789617066 255 CLSILGYKRMHS 266
Cdd:cd13961   245 AKSPKDYSKLSK 256
PLN02809 PLN02809
4-hydroxybenzoate nonaprenyltransferase
56-184 1.69e-09

4-hydroxybenzoate nonaprenyltransferase


Pssm-ID: 178405  Cd Length: 289  Bit Score: 57.39  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  56 AGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKK-VLWLSILMSvLGLGFLAFTTYLAAIIGLIGLFFyIFP 134
Cdd:PLN02809   52 CGALLLRGAGCTINDLLDRDIDKKVERTKLRPIASGALTPFQgVGFLGAQLL-LGLGILLQLNNYSRILGASSLLL-VFT 129
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2789617066 135 YTIWsKRKTVYNTEIGSISGAMPPLIGWAAISPDISHPAIMGLFFITIIW 184
Cdd:PLN02809  130 YPLM-KRFTFWPQAFLGLTFNWGALLGWAAVKGSLDPAVVLPLYASGVCW 178
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
26-293 1.70e-07

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: 51.36  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  26 LIPMCAGLTLALYTYQIDILhksIEILLAFAGSILLIGAAGALNNLYD--RDIDSVMNRTKNRPTVTGEVNPKKVLWLSI 103
Cdd:cd13962    13 LAPVLLGTALAYYLGGFFNW---LLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRSGPSRVLVSGLLSPRQVLRAAL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 104 LMSVL----GLGFLAFTTYLAAIIGLIGLFFYIFpYTIWSKRKtvYNTEIGSIS-----GAMPPLIGWAAISPDISHPAI 174
Cdd:cd13962    90 VLLLLaallGLYLVALGGWLLLLLGLLGILAGYF-YTGGPFPL--SYRGLGELFvflffGLLAVLGTYYVQTGSLSWEVL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 175 -----MGLFFITIIWqmphfySIAIRKQNEYKAANIPMLPVVKGMKRTYLQTNLYILAITLSSFLFHSLsiGLVLVSFFL 249
Cdd:cd13962   167 laalpLGLLIAAILL------ANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLVLL--GLLPLWSLL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2789617066 250 GLIWICLSILGYKRMHSEKWASIMFVYSLIYMTTLYSTVIIYSL 293
Cdd:cd13962   239 ALLSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLLLAL 282
ubiA PRK12882
prenyltransferase; Reviewed
53-128 5.17e-07

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 49.97  E-value: 5.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2789617066  53 LAFAGSILLIGAAGALNNLYDRDIDSVmNRtKNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIGL 128
Cdd:PRK12882   42 LAFAAVFLATGAGNAINDYFDREIDRI-NR-PDRPIPSGAVSPRGALAFSILLFAAGVALAFLLPPLCLAIALFNS 115
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
48-141 1.01e-06

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: 49.12  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  48 SIEILLAFAGSILLIGAAGALNNLYDRDIDSVmNRtKNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIg 127
Cdd:cd13964    31 VLRLALLLLASVLLYAAGMVLNDVFDAELDAR-ER-PERPIPSGRVSRGAALALGAGLLAAGVALAALVGRLSGLVALL- 107
                          90
                  ....*....|....
gi 2789617066 128 LFFYIFPYTIWSKR 141
Cdd:cd13964   108 LAAAILLYDAWLKH 121
ubiA PRK12884
prenyltransferase; Reviewed
49-132 2.45e-06

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 48.03  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  49 IEILLAFAGSILLIGAAGALNNLYDRDIDSVmNRTkNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIGL 128
Cdd:PRK12884   37 DEALLGFLTAFFASGSANALNDYFDYEVDRI-NRP-DRPIPSGRISRREALLLAILLFILGLIAAYLISPLAFLVVILVS 114

                  ....
gi 2789617066 129 FFYI 132
Cdd:PRK12884  115 VLGI 118
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
26-136 6.70e-06

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: 46.67  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  26 LIPMCAGLTLALYTY-QIDILHksieILLAFAGSILLIGAAGALNNLYD--RDIDSVMNRTKNRPTVTGEVNPKKVLWLS 102
Cdd:COG1575    15 VAPVLLGTALAYYETgSFNWLL----FLLALLAALLLQIGVNLANDYFDykKGTDTEERVGPSRVIVSGLLSPKQVLRAA 90
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2789617066 103 ILMSVL----GLGFLAFTTYLAAIIGLIGLFFYIFpYT 136
Cdd:COG1575    91 LLLLALalllGLYLVLLSGWPLLLLGLLGILAAIF-YT 127
ubiA PRK13106
prenyltransferase; Reviewed
50-154 9.81e-06

prenyltransferase; Reviewed


Pssm-ID: 237283  Cd Length: 300  Bit Score: 46.26  E-value: 9.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  50 EILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIGLF 129
Cdd:PRK13106   50 TLILIFLALFFLRTAGMTNDNLADLEIDAKNPRTKNRPLVTGAIKISEAKALITAGLILFFASAYLVNRWALLLSPIVAL 129
                          90       100
                  ....*....|....*....|....*..
gi 2789617066 130 FYI-FPYtiwSKRKTVY-NTEIGSISG 154
Cdd:PRK13106  130 IAMsYPY---MKRYTAFaNYHLASIQG 153
ubiA PRK12888
4-hydroxybenzoate octaprenyltransferase;
65-175 4.09e-05

4-hydroxybenzoate octaprenyltransferase;


Pssm-ID: 183814  Cd Length: 284  Bit Score: 44.33  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  65 AGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIGLF-FYIFPYtiwSKRKT 143
Cdd:PRK12888   55 AMAANRIIDREIDARNPRTAGRELVTGAVSVRTAWTGALVALAVFLGAAALLNPLCLALAPLAVApLVVYPY---AKRFT 131
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2789617066 144 VYNTEIGSISGAMPPLIGWAAISPDISHPAIM 175
Cdd:PRK12888  132 NFPHAILGLAQAVGPVGAWIAVTGTWSWPAVL 163
ubiA PRK12886
prenyltransferase; Reviewed
64-261 9.16e-05

prenyltransferase; Reviewed


Pssm-ID: 237247  Cd Length: 291  Bit Score: 43.14  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  64 AAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLwLSILMSVLGLGFLA-FTTYLAAIIGLIGLFFyIFPYTiWSKRK 142
Cdd:PRK12886   57 AAMGFNRLIDAEIDARNPRTAGRAIPAGLISKGSAI-LFIVLSSLLMLFAAwFLNPLCLYLSPPALFF-LLLYS-YCKRF 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 143 TVYNTEIGSISGAMPPLIGWAAISPDISHPAIMgLFFITIIWQMPHFYSIAIRKQNEYKAANIPMLPVVKGMKRT-YLQT 221
Cdd:PRK12886  134 TALAHVVLGFCLALAPLGAWIAIRGTIELPAIL-LGLAVLFWVAGFDILYALQDLEFDRKEGLHSIPAKLGVNGSlWIAR 212
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2789617066 222 NLYILAITLSSFLFHSLSIGLVlvsFFLGLIwICLSILGY 261
Cdd:PRK12886  213 VFHLLMIGFLFALGISAGLGPW---FLAGLA-VTGILLLY 248
ubiA PRK12873
4-hydroxybenzoate polyprenyltransferase;
51-184 1.17e-04

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 171787 [Multi-domain]  Cd Length: 294  Bit Score: 43.11  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  51 ILLAFAGSILLIGAAGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIGLFF 130
Cdd:PRK12873   46 LLLIILGGLAVSGAGCIANDLWDRRIDRKVERTKNRPLARGKISLKTAYSLLIVLLLLSLFVVLSLPQPSRNLCLSLAFL 125
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2789617066 131 YIFPYTIW--SKRKTVYNTEIGSISGAMPPLIGWAAISPDISH-PAIMGLFFITIIW 184
Cdd:PRK12873  126 ALPPILIYpsAKRWFAYPQAILALCWGFAVLIPWAAAEGSLNGgWPLLFCWLATLLW 182
ubiA PRK12874
4-hydroxybenzoate polyprenyltransferase;
53-169 1.42e-04

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 237242  Cd Length: 291  Bit Score: 42.69  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  53 LAFAGSILLIGA---AGALNNLYDRDIDSVMNRTKNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIGLF 129
Cdd:PRK12874   48 LLILGILAAVSArnfAMAFNRLVDRDIDKDNPRTANRPSVDGRISVKSMVLFIVLNALIFIGVSYFINPLAFKLSFPFLI 127
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2789617066 130 FyIFPYTIWsKRKTVYNTEIGSISGAMPPLIGWAAISPDI 169
Cdd:PRK12874  128 V-LGGYSYF-KRFSSLAHLVLGLSLGLAPIAGVVAVLGEI 165
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
49-281 1.35e-03

(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed


Pssm-ID: 181963  Cd Length: 279  Bit Score: 39.56  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  49 IEILLAFAGSILLIGAAGALNNLYDRDIDSVmnRTKNRPTVTGEVNPKKVLWLSILMSVLGLGFLAFTTYLAAIIGLIGL 128
Cdd:PRK09573   37 KGIILAALVVFLVCAGGNVINDIYDIEIDKI--NKPERPIPSGRISLKEAKIFSITLFIVGLILSIFINIYAFLIALLNS 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 129 FFYIFPYTIWSKRKTVYNTEIGSISGamppligwaaiSPDISHPAIMGLFFITIIWQMPHFYSIAIRK-------QNEYK 201
Cdd:PRK09573  115 ILLYLYAKDLKKTGLIGNLIVAYLTG-----------LSFIFGGLAVFNVLRIIILFLCAFFSTWSREivkdiedIEGDL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066 202 AANIPMLPVVKGMKRT-YLQTNLYILAITLSS--FLFHSLSIGLVLVSFFLGLIWICLSILGYKRmHSEKWASIMFVYSL 278
Cdd:PRK09573  184 KENVITLPIKYGIKKSwYIAKILLILAIVLSPlpYFLGIFGIYYLIVVIICDILFIIAMLILLKN-PSIEGASKASKYLK 262

                  ...
gi 2789617066 279 IYM 281
Cdd:PRK09573  263 IIM 265
PRK07566 PRK07566
chlorophyll synthase ChlG;
48-131 2.46e-03

chlorophyll synthase ChlG;


Pssm-ID: 236052  Cd Length: 314  Bit Score: 38.75  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2789617066  48 SIEILLAFAGSILLIG--AAG---ALNNLYDRDIDSVmnRTKNRPTVTGEVNPKKVLWLSILMSVLGLG---FLAFTTYL 119
Cdd:PRK07566   59 TLENVLKLLAGMLLAGplLCGtsqTLNDYFDREVDAI--NEPYRPIPSGAISLRWVLYLIAVLTVLGLAvayLLGPWVFL 136
                          90
                  ....*....|..
gi 2789617066 120 AAIIGLIGLFFY 131
Cdd:PRK07566  137 AALLGLFLAWIY 148
 
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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