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Conserved domains on  [gi|663528510|gb|AIF18547|]
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protoheme IX farnesyltransferase (cyoE) [uncultured marine thaumarchaeote KM3_83_D12]

Protein Classification

protoheme IX farnesyltransferase( domain architecture ID 10785017)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 5-309 4.09e-85

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


:

Pssm-ID: 439879  Cd Length: 299  Bit Score: 257.75  E-value: 4.09e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   5 NTKSNIAVYYELTKPKIWYLLVFTAFGAAITASNVFnvpISLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNR 84
Cdd:COG0109   11 SLRSTLRDYLALTKPRIILLLLFTALAGMLLAAGGL---PDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  85 PIPSRRIyPPEKARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAP 164
Cdd:COG0109   88 PLPTGRI-SPREALIFGLVLGVLGLALLA-------LFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 165 ALIGYVAVTTTgLWDFGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFF 244
Cdd:COG0109  160 PLIGWAAVTGS-LSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYL 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663528510 245 LthdngePLMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIALMVDSVL 309
Cdd:COG0109  239 L------GMAGLIYLVVALVLGAWFLYLAVRLYRRPDRKWARKLFKFSILYLTLLFLALLVDHLL 297
 
Name Accession Description Interval E-value
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 5-309 4.09e-85

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 257.75  E-value: 4.09e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   5 NTKSNIAVYYELTKPKIWYLLVFTAFGAAITASNVFnvpISLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNR 84
Cdd:COG0109   11 SLRSTLRDYLALTKPRIILLLLFTALAGMLLAAGGL---PDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  85 PIPSRRIyPPEKARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAP 164
Cdd:COG0109   88 PLPTGRI-SPREALIFGLVLGVLGLALLA-------LFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 165 ALIGYVAVTTTgLWDFGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFF 244
Cdd:COG0109  160 PLIGWAAVTGS-LSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYL 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663528510 245 LthdngePLMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIALMVDSVL 309
Cdd:COG0109  239 L------GMAGLIYLVVALVLGAWFLYLAVRLYRRPDRKWARKLFKFSILYLTLLFLALLVDHLL 297
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 14-302 4.97e-73

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: 225.78  E-value: 4.97e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  14 YELTKPKIWYLLVFTAFGAAITASNVFNVPIslqTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIYP 93
Cdd:cd13957    1 LELTKPRITLLVLLTALAGYLLAPGGVPDLL---LLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  94 PEkARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAVT 173
Cdd:cd13957   78 KH-ALIFGLVLGILGLALLA-------LFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAAT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 174 TTGLWDfGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLThdngepL 253
Cdd:cd13957  150 GSLDLG-AWLLFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLG------L 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 663528510 254 MHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIA 302
Cdd:cd13957  223 TGWIYLVVALLLGLYFLYLAIKLYRSPDDKWARKLFFASLIYLPLLFLL 271
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 13-309 8.54e-69

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 215.77  E-value: 8.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  13 YYELTKPKIWYLLVFTAFGAAITASnVFNVPISLQTWALLlgGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIy 92
Cdd:PRK04375  13 YLALTKPRVISLNLFTALGGMLLAP-PGVPPLLLLLLTLL--GIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRI- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  93 PPEKARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAV 172
Cdd:PRK04375  89 SPREALIFGLVLGVLGFLLLG-------LFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 173 TTTGLWDfGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLTHdngep 252
Cdd:PRK04375 162 TGSLSWE-ALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGM----- 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663528510 253 lMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIALMVDSVL 309
Cdd:PRK04375 236 -AGLLYLVVALLLGAWFLYYAWRLYRKDDRKWARKLFRYSINYLTLLFVALLVDHLL 291
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 13-306 1.03e-65

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: 207.48  E-value: 1.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   13 YYELTKPKIWYLLVFTAFGAAITASNVFNVPISLQTWALLlgGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIy 92
Cdd:TIGR01473   3 YLQLTKPRIISLLLITAFAGMWLAPGGALVNPPLLLLTLL--GTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRI- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   93 PPEKARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAV 172
Cdd:TIGR01473  80 SPREALAFGLLLGVLGVAILA-------AFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  173 TTTGLWdFGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLThdngep 252
Cdd:TIGR01473 153 TGSISL-GAWLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFLG------ 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 663528510  253 LMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWV-LFKFSSPYLAVLFIALMVD 306
Cdd:TIGR01473 226 GTGWLYLIVATLLGALFLYLAFKFYRDPTDRKKARkLFKFSLIYLALLFVALLID 280
UbiA pfam01040
UbiA prenyltransferase family;
24-291 1.55e-31

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 118.10  E-value: 1.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   24 LLVFTAFGAAITASNVFnvpiSLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIyPPEKARNFGLI 103
Cdd:pfam01040   1 LLIPALAGLALAAGGVP----DLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRI-SPREALIFALV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  104 LAVISLACAfgicftasFWQGILAGSFMAFGLVdNILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAVTTTGLWDFgLV 183
Cdd:pfam01040  76 LLALGLLLL--------LLLNPLTALLGLAALL-LYVLYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA-LL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  184 IAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLTHDNgeplmheVYLYTAI 263
Cdd:pfam01040 146 LALALFLWTWAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGG-------LYLLLAL 218

                         250       260
                  ....*....|....*....|....*...
gi 663528510  264 ASGVLMVILSFWVVAKPSEKASWVLFKF 291
Cdd:pfam01040 219 LLAALALLYAARLLRLRDPKKDAKAFFF 246
 
Name Accession Description Interval E-value
CyoE COG0109
Polyprenyltransferase (heme O synthase) [Coenzyme transport and metabolism, Lipid transport ...
 5-309 4.09e-85

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


Pssm-ID: 439879  Cd Length: 299  Bit Score: 257.75  E-value: 4.09e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   5 NTKSNIAVYYELTKPKIWYLLVFTAFGAAITASNVFnvpISLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNR 84
Cdd:COG0109   11 SLRSTLRDYLALTKPRIILLLLFTALAGMLLAAGGL---PDLLLLLLTLLGGALAAGAANALNNYIDRDIDALMKRTKNR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  85 PIPSRRIyPPEKARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAP 164
Cdd:COG0109   88 PLPTGRI-SPREALIFGLVLGVLGLALLA-------LFVNPLAALLGLLGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 165 ALIGYVAVTTTgLWDFGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFF 244
Cdd:COG0109  160 PLIGWAAVTGS-LSLEALLLFLIIFLWTPPHFWALALKRRDDYARAGVPMLPVVKGERRTKRQILLYTLLLVPVSLLPYL 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663528510 245 LthdngePLMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIALMVDSVL 309
Cdd:COG0109  239 L------GMAGLIYLVVALVLGAWFLYLAVRLYRRPDRKWARKLFKFSILYLTLLFLALLVDHLL 297
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
 14-302 4.97e-73

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: 225.78  E-value: 4.97e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  14 YELTKPKIWYLLVFTAFGAAITASNVFNVPIslqTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIYP 93
Cdd:cd13957    1 LELTKPRITLLVLLTALAGYLLAPGGVPDLL---LLLLTLLGTALVSASANALNQYIERDIDAKMKRTRNRPLPSGRISP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  94 PEkARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAVT 173
Cdd:cd13957   78 KH-ALIFGLVLGILGLALLA-------LFVNPLTALLGLLGIFLYVFVYTPLKKRTTPLNTVIGGIAGAIPPLIGWAAAT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 174 TTGLWDfGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLThdngepL 253
Cdd:cd13957  150 GSLDLG-AWLLFLILFLWQPPHFWALAILYRDDYARAGIPMLPVVKGERRTKRQILLYTLLLVPLSLLLYLLG------L 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 663528510 254 MHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIA 302
Cdd:cd13957  223 TGWIYLVVALLLGLYFLYLAIKLYRSPDDKWARKLFFASLIYLPLLFLL 271
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
 13-309 8.54e-69

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 215.77  E-value: 8.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  13 YYELTKPKIWYLLVFTAFGAAITASnVFNVPISLQTWALLlgGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIy 92
Cdd:PRK04375  13 YLALTKPRVISLNLFTALGGMLLAP-PGVPPLLLLLLTLL--GIALVAGAAGALNNYIDRDIDAKMERTKNRPLVTGRI- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  93 PPEKARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAV 172
Cdd:PRK04375  89 SPREALIFGLVLGVLGFLLLG-------LFVNPLAAWLTLAGIFFYVVVYTLWLKRRTPQNIVIGGAAGAMPPLIGWAAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 173 TTTGLWDfGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLTHdngep 252
Cdd:PRK04375 162 TGSLSWE-ALILFLIIFLWTPPHFWALAIFRKDDYAAAGIPMLPVVKGIRVTKRQILLYTVLLVAVSLLPVLLGM----- 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663528510 253 lMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIALMVDSVL 309
Cdd:PRK04375 236 -AGLLYLVVALLLGAWFLYYAWRLYRKDDRKWARKLFRYSINYLTLLFVALLVDHLL 291
cyoE_ctaB TIGR01473
protoheme IX farnesyltransferase; This model describes protoheme IX farnesyltransferase, also ...
 13-306 1.03e-65

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: 207.48  E-value: 1.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   13 YYELTKPKIWYLLVFTAFGAAITASNVFNVPISLQTWALLlgGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIy 92
Cdd:TIGR01473   3 YLQLTKPRIISLLLITAFAGMWLAPGGALVNPPLLLLTLL--GTTLAAASANAFNMYIDRDIDKKMKRTRNRPLVTGRI- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   93 PPEKARNFGLILAVISLACAFgicftasFWQGILAGSFMAFGLVDNILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAV 172
Cdd:TIGR01473  80 SPREALAFGLLLGVLGVAILA-------AFVNPLAALLGLFGIFFYVIVYTIWLKRRTPQNTVIGGFAGAVPPLIGWAAV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  173 TTTGLWdFGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLThdngep 252
Cdd:TIGR01473 153 TGSISL-GAWLLFAIIFLWQPPHFWALALKYKDDYRAAGIPMLPVVKGERITKRQIALYTAALLPVSLLLAFLG------ 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 663528510  253 LMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWV-LFKFSSPYLAVLFIALMVD 306
Cdd:TIGR01473 226 GTGWLYLIVATLLGALFLYLAFKFYRDPTDRKKARkLFKFSLIYLALLFVALLID 280
UbiA pfam01040
UbiA prenyltransferase family;
24-291 1.55e-31

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 118.10  E-value: 1.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   24 LLVFTAFGAAITASNVFnvpiSLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIyPPEKARNFGLI 103
Cdd:pfam01040   1 LLIPALAGLALAAGGVP----DLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRTPNRPLPSGRI-SPREALIFALV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  104 LAVISLACAfgicftasFWQGILAGSFMAFGLVdNILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAVTTTGLWDFgLV 183
Cdd:pfam01040  76 LLALGLLLL--------LLLNPLTALLGLAALL-LYVLYTLRLKRRTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA-LL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  184 IAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLTHDNgeplmheVYLYTAI 263
Cdd:pfam01040 146 LALALFLWTWAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLLLLLLGG-------LYLLLAL 218

                         250       260
                  ....*....|....*....|....*...
gi 663528510  264 ASGVLMVILSFWVVAKPSEKASWVLFKF 291
Cdd:pfam01040 219 LLAALALLYAARLLRLRDPKKDAKAFFF 246
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
 16-303 2.26e-14

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: 71.80  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  16 LTKPKIWYLLVFTAFGAAITASNVFnvpISLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIYPPE 95
Cdd:COG0382    9 LDRPIGILLLLWPTLWALFLAAGGL---PDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRINERKPNRPLASGRISLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  96 karnfGLILAVISLACAFGICFTASFWQGILAGSFMAFglvdnILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAVTTT 175
Cdd:COG0382   86 -----ALLLAIVLLLLALALALLLNPLTFLLALAALAL-----AWAYSLFLKRFTLLGNLVLGLLFGLGILMGFAAVTGS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 176 GLWDFgLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLTHDNgeplmh 255
Cdd:COG0382  156 LPLSA-WLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIIAGVLYALAVLLLLLLGLLAGLG------ 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 663528510 256 eVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIAL 303
Cdd:COG0382  229 -LLYLLGLLAALLLLYLSQLWLLRPRKKDPARALKLFKLNMLLGLLLF 275
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
 15-305 1.36e-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: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  15 ELTKPKIW-YLLVFTAFGAAITASNVFNVPISLqtwALLLGGVAAGSAAANTLTNYHDRDIDAImeRTKNRPIPSRRIyP 93
Cdd:cd13956    2 RLMRPYTLlYVLAPALAGAALAGAFAGPLPALL---LLALLAVFLGAGAGYALNDYTDRELDAI--NKPDRPLPSGRL-S 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  94 PEKARNFGLILAVISLACAFgicftASFWQGILAGSFMAFGlvdnILVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAVT 173
Cdd:cd13956   76 PRQALAFAAALLLVGLALAL-----ALGPLALLLLLAGLLL----GLAYSLGLKRLKLGGWGVLGYATGLALLPGLGAVA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 174 TTGLWDFGLVIAGLVFVWIPMHIWALTLHFKDDYKKVNVPMLTAVQSEKTSARIIAGttLMMVLFSIVPFFLTHDNGEPL 253
Cdd:cd13956  147 AGGLVPLALLLALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLGPRRARRLAAG--LLLAALILVVLLAVAGLLGPL 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663528510 254 mhevYLYTAIASGVLMVILSFWvvAKPSEKASWVLFKFSSPYLAVLFIALMV 305
Cdd:cd13956  225 ----ALLALLAVALLALRARFA--RADRLPALPRGFLLLAVYRLLLFAALLL 270
PLN02776 PLN02776
prenyltransferase
 64-308 7.45e-11

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 62.07  E-value: 7.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  64 NTLTNYHDRDIDAIMERTKNRPIPSRRIYPPeKARNFGLILAVIslacafGICFTASFWQGILAGsFMAFGLVDNILVYS 143
Cdd:PLN02776  46 NTLNQVFEVKNDSKMKRTMRRPLPSGRISVP-HAVAWAVVVGAA------GVALLAYKTNMLTAG-LGAGNILLYAFVYT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 144 YgLKRKSRTNIVLGGFSGGAPALIGYVAvtTTGLWDFG-LVIAGLVFVW-IPmHIWALTLHFKDDYKKVNVPMLTAVQSe 221
Cdd:PLN02776 118 P-LKQIHPANTWVGAVVGAIPPLMGWAA--ASGQLDAGaMVLAAALYFWqMP-HFMALAYMCRDDYAAGGYRMLSLADA- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 222 ktSARIIAGTTLMMVLFSIVPFFLTHDNGepLMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFI 301
Cdd:PLN02776 193 --TGRRTALVALRNCLYLAPLGFLAYDWG--VTSSPFALEAALLTAYLAASAASFYREPTNANARKMFHGSLLYLPAFMA 268


                 ....*..
gi 663528510 302 ALMVDSV 308
Cdd:PLN02776 269 LLLLHRV 275
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
 21-306 4.48e-10

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: 59.02  E-value: 4.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  21 IWYLLVFTAFGAAITASNVfnVPISLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNRPIPSRRIYPPEkarnf 100
Cdd:cd13959    9 TLLLLPPALWGLLLAAGGL--PLPLLKLLLLFLLGAFLMRSAGCTINDIADRDIDAKVPRTKNRPLASGAISVKE----- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 101 GLILAVISLACAFGICFTASFWQGILAGSFMAFglvdnILVYSYGlKRKSR-TNIVLgGFSGGAPALIGYVAVTTTgLWD 179
Cdd:cd13959   82 ALLFLAVQLLLGLALLLQLNPLTILLSPIALLL-----VLIYPLM-KRFTYwPQLVL-GLAFGWGPLMGWAAVTGS-LPL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 180 FGLVIAGLVFVWipmhiwalTLHF--------KDDYKKVNVpMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLTHdnge 251
Cdd:cd13959  154 PALLLYLAVIFW--------TAGYdtiyahqdREDDRKIGV-KSTAVLFGDRTKLILALLLHLFVALLLLAGGLAG---- 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663528510 252 plMHEVYLYTAIASGVLMVILSFWVVAKPsEKASWVLFKFSSPYLAVLFIALMVD 306
Cdd:cd13959  221 --LGWPYYLGLGAAAHLLWQEHRLDLPDP-LRSCLAFFLSNGWVGLLLFAGLLLD 272
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
 22-282 2.43e-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: 47.88  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  22 WYLLVFTAFGAAITASNVFNVPISLQTWALLLGGVAAGSAAA--NTLTNYHDRDIDAImerTK-NRPIPSRRIyppekAR 98
Cdd:cd13961    8 PPNLLMAALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAAagYIINDYFDVEIDRI---NKpDRPIPSGRI-----SR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  99 NFGLILAVISLACAFGICFTASFWQGILAGSFMAFGlvdniLVYSYGLKRKSRTNIVLGGFSGGAPALIGYVAVttTGLW 178
Cdd:cd13961   80 REALILSILLNALGLILAFLLSPLALLIALLNSLLL-----WLYSHKLKRTPLIGNLLVALLTGLPFLFGGLAA--GNLL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 179 DFGLVIAGLVFVwipmhiwaLTLH---FKD--DY---KKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVPFFLTHDNg 250
Cdd:cd13961  153 LIILLLALFAFL--------ITLGreiVKDieDVegdRAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPYLLGGLG- 223

                        250       260       270
                 ....*....|....*....|....*....|..
gi 663528510 251 eplmhEVYLYTAIASGVLMVILSFWVVAKPSE 282
Cdd:cd13961  224 -----ILYLILIIIADLLFLYSAIRLAKSPKD 250
ubiA_proteo TIGR01474
4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of ...
 18-306 8.23e-06

4-hydroxybenzoate polyprenyl transferase, proteobacterial; This model represents a family of integral membrane proteins that condenses para-hydroxybenzoate with any of several polyprenyldiphosphates. Heterologous expression studies suggest that for, many but not all members, the activity seen (e.g. octaprenyltransferase in E. coli) reflects available host isoprenyl pools rather than enzyme specificity. A fairly deep split by both clustering (UPGMA) and phylogenetics (NJ tree) separates this group (mostly Proteobacterial and mitochondrial), with several characterized members, from another group (mostly archaeal and Gram-positive bacterial) lacking characterized members. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 130539  Cd Length: 281  Bit Score: 46.54  E-value: 8.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   18 KPKIWYLLVFTAFGAAITASNVFNVPislqTWALLLGGVAAGSAAAN---TLTNYHDRDIDAIMERTKNRPIPSRRIYPP 94
Cdd:TIGR01474  12 KPIGTLLLLWPCLWSLLLAAQAGGIP----PLYLLGLFTVGAILMRGagcVINDIWDRDFDPQVERTKSRPLASGAVSVR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   95 EkarnfGLILAVISLACAFGICFTASfWQGILAGsfmAFGLvdnILVYSY-GLKRKSRTNIVLGGFSGGAPALIGYVAVt 173
Cdd:TIGR01474  88 Q-----AILFLLVQLLVALGVLLQLN-PLTILLG---VASL---ALVATYpFMKRITYWPQLVLGLAFGWGALMGWAAV- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  174 tTGLWDfgLVIAGLVFVWIpmhIWALT------LHFKDDYKKVNVPMLTAVQSEKTSARIIAGTTLMMVLFSIVpfflth 247
Cdd:TIGR01474 155 -TGDLS--TAAWVLYLANI---LWTLGydtiyaMQDKEDDIKIGVKSTALRFGDNTKPWLGGLYALMILLLALA------ 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 663528510  248 dnGEPLMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIALMVD 306
Cdd:TIGR01474 223 --GLIAGLGPVYYLGLAAAALLLIRQIATLDIRDPENCLKLFKANNYVGLLLFAGIALG 279
PT_UbiA_chlorophyll cd13958
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ...
 15-286 1.15e-05

Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of chlorophyll (Chl) biosynthesis, the addition of the tetraprenyl (phytyl or geranylgeranyl) side chain. In plant chloroplast, the chlorophyll synthase is located in thylakoid membrane and has been shown to also have a regulatory or channeling function. 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: 260121  Cd Length: 277  Bit Score: 46.07  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  15 ELTKPKIWYLLVFTAFGAAITASN-VFNVPISLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMErtKNRPIPSRRIyp 93
Cdd:cd13958    3 ELLKPVTWFPPMWAFLCGAAASGAfQWSNWDVWLLLLGMLLAGPLLTGTSQTINDYYDREVDAINE--PYRPIPSGRI-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  94 PEKArnfGLILAVISLACAFGICFTASFWQGILA---GSFMAFglvdnilVYSYG---LKRksrtNIVLG----GFS-GG 162
Cdd:cd13958   79 SERE---ALWNIWVLLLLSLLVALFLDGPWVFAAavvGLVLAY-------IYSAPplkLKQ----NGWWGnaavGLSyEG 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 163 APALIGYVAVTTTGLWDFgLVIAGLVFvwipmhIWALTLHFKDDYK------KVNVPMLTAVQSEKTSARIIAGTtlMMV 236
Cdd:cd13958  145 LPWWAGAAAFAGLLTWES-LALALLYS------IGAHGIMTLNDFKsiegdrQLGLRSLPVALGVDTAAWIACGV--IDV 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663528510 237 LFSIVPFFLthdngepLMHEVYLYTAIASGVLM--VILSFWVVAKPSEKASW 286
Cdd:cd13958  216 PQLAVAALL-------LAWGETWYAAVVGALLLaqIPLQFKLLLDPPAKAVW 260
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 65-203 9.18e-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: 260127  Cd Length: 282  Bit Score: 43.34  E-value: 9.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  65 TLTNYHDRDIDAImERtKNRPIPSRRIyPPEKARNFGLILAVISLACAFGICFTASFWQGILAGSfmafglvdnILVYSY 144
Cdd:cd13964   50 VLNDVFDAELDAR-ER-PERPIPSGRV-SRGAALALGAGLLAAGVALAALVGRLSGLVALLLAAA---------ILLYDA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 145 GLKRKS---------RTNIVLGGFSG-----------GAPALIGYVA-VTT---------------TGLWDFGLVIAGLV 188
Cdd:cd13964  118 WLKHTPlgpllmglcRGLNLLLGASAaaagglgpallAALALGVYIAgVTYiargevhggprrllpLALLAVLLVIGLAL 197

                        170
                 ....*....|....*.
gi 663528510 189 FVWIPM-HIWALTLHF 203
Cdd:cd13964  198 ALAAPRgGRVLLALLF 213
PRK07566 PRK07566
chlorophyll synthase ChlG;
6-133 1.37e-04

chlorophyll synthase ChlG;


Pssm-ID: 236052  Cd Length: 314  Bit Score: 42.99  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   6 TKSNIAVYYELTKPKIWYLLVFtAFGAAITASNVFNVPISLQTWALL--LGGVAAGSAAANTLTNYHDRDIDAIMErtKN 83
Cdd:PRK07566  23 TTSIWKARLQLMKPITWFPPMW-AFLCGAVSSGAFGWTLENVLKLLAgmLLAGPLLCGTSQTLNDYFDREVDAINE--PY 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663528510  84 RPIPSRRIypPEKArnfGLILAVISLACAFGICFTASFWQGILA--GSFMAF 133
Cdd:PRK07566 100 RPIPSGAI--SLRW---VLYLIAVLTVLGLAVAYLLGPWVFLAAllGLFLAW 146
ubiA PRK12882
prenyltransferase; Reviewed
 9-302 7.70e-04

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 40.34  E-value: 7.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   9 NIAVYYELTKPKIWYLLVFTAFGAAITASNVFNVPISLqtwALLLGGVAAGSAAANTLTNYHDRDIDAIMErtKNRPIPS 88
Cdd:PRK12882   3 TVRGYLELTRPVNAVVAGVAAFIGAFIAGGILSSPSLT---GLAFAAVFLATGAGNAINDYFDREIDRINR--PDRPIPS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  89 RRIYPPEkARNFGLILAVISLACAFGIcftasfwqGILAGSFMAFGLVdnILV-YSYGLKRKSRTNIVLGGFSGGAPALI 167
Cdd:PRK12882  78 GAVSPRG-ALAFSILLFAAGVALAFLL--------PPLCLAIALFNSL--LLVlYAETLKGTPGLGNASVAYLTGSTFLF 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 168 GYVAVTTTGLWDfGLVIAGLVFVWIpmhiwaLTLHFKDDYKKV---------NVPMLTAVqseKTSARIIAGTTLMMVLF 238
Cdd:PRK12882 147 GGAAVGTEGLLA-LLVLFALAALAT------LAREIIKDVEDIegdraegarTLPILIGV---RKALYVAAAFLLVAVAA 216

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663528510 239 SIVPFFLThdngepLMHEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIA 302
Cdd:PRK12882 217 SPLPYLLS------TFGLWYLVLVAPADLVMLAAAYRSLKKTDPTASQKLLKYGMFLALAAFIV 274
PLN02809 PLN02809
4-hydroxybenzoate nonaprenyltransferase
 65-172 8.32e-04

4-hydroxybenzoate nonaprenyltransferase


Pssm-ID: 178405  Cd Length: 289  Bit Score: 40.44  E-value: 8.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  65 TLTNYHDRDIDAIMERTKNRPIPSRRIYPPEkarnfGLILAVISLACAFGICFTASFWQGILAGSFMAfglvdniLVYSY 144
Cdd:PLN02809  63 TINDLLDRDIDKKVERTKLRPIASGALTPFQ-----GVGFLGAQLLLGLGILLQLNNYSRILGASSLL-------LVFTY 130

                         90       100       110
                 ....*....|....*....|....*....|..
gi 663528510 145 GLkRKSRTN---IVLG-GFSGGapALIGYVAV 172
Cdd:PLN02809 131 PL-MKRFTFwpqAFLGlTFNWG--ALLGWAAV 159
PLN00012 PLN00012
chlorophyll synthetase; Provisional
 15-95 1.12e-03

chlorophyll synthetase; Provisional


Pssm-ID: 215028  Cd Length: 375  Bit Score: 40.23  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  15 ELTKPKIWYLLVF-TAFGAAITASNVFNVPISLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMErtKNRPIPSRRIYP 93
Cdd:PLN00012  90 QLTKPVTWPPLVWgVLCGAAASGNFHWTLEDVAKSIVCMLMSGPFLTGYTQTINDWYDREIDAINE--PYRPIPSGAISE 167


                 ..
gi 663528510  94 PE 95
Cdd:PLN00012 168 NE 169
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
 69-149 1.20e-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: 260126  Cd Length: 278  Bit Score: 39.76  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  69 YHDRDIDAIMERTKNRPIPSRRIYPPEkarnfGLILAVISLACAFGICFTASFWQGILAGSFMAFGlvdniLVYSYGLKR 148
Cdd:cd13963   55 LLDLEADRLHPTKRNRPIASGRLSIPA-----ALALAVVLLLAGLALALLLSPAFLLVLLAYLVLN-----LAYSLKLKR 124


                 .
gi 663528510 149 K 149
Cdd:cd13963  125 I 125
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
 9-308 5.79e-03

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


Pssm-ID: 181963  Cd Length: 279  Bit Score: 37.63  E-value: 5.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   9 NIAVYYELTKPKIWYLLVFTAFGAAITASNvFNVPISLQTWALLLGGVAAGSAaaNTLTNYHDRDIDAImeRTKNRPIPS 88
Cdd:PRK09573   2 SIKAYFELIRPKNCIGASIGAIIGYLIASN-FKIDLKGIILAALVVFLVCAGG--NVINDIYDIEIDKI--NKPERPIPS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  89 RRIyPPEKARNFGLILAVISLACafgicftaSFWQGILAgsfMAFGLVDNILVYSYGLKRKsRTNIVlGGFsggapalig 168
Cdd:PRK09573  77 GRI-SLKEAKIFSITLFIVGLIL--------SIFINIYA---FLIALLNSILLYLYAKDLK-KTGLI-GNL--------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 169 YVAVTTTGLWDFGLVIAGLVFVWIPMHIWALTLHF-----KD--DY---KKVNVPMLTAVQSEKTSARIIAGTTLMMVLF 238
Cdd:PRK09573 134 IVAYLTGLSFIFGGLAVFNVLRIIILFLCAFFSTWsreivKDieDIegdLKENVITLPIKYGIKKSWYIAKILLILAIVL 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510 239 SIVPFFLTHDNgeplmhEVYLYTAIASGVLMVILSFWVVAKPSEKASWVLFKFSSPYLAVLFIALMVDSV 308
Cdd:PRK09573 214 SPLPYFLGIFG------IYYLIVVIICDILFIIAMLILLKNPSIEGASKASKYLKIIMILGLIAFLIGSL 277
PRK12324 PRK12324
decaprenyl-phosphate phosphoribosyltransferase;
7-147 5.96e-03

decaprenyl-phosphate phosphoribosyltransferase;


Pssm-ID: 237058  Cd Length: 295  Bit Score: 37.92  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510   7 KSNIAVYYELTKPKIWY--LLVFtafgAAITASNVFNVPISLQTWALLLGGVAAGSAAANTLTNYHDRDIDAIMERTKNR 84
Cdd:PRK12324   8 KNLLAGYLKLLRPKQWIknLFVF----AAPIFAGNLLNPGALLKVLLAFVLFCLASSAVYLVNDIRDVEADRLHPTKRNR 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663528510  85 PIPSRRIYPPekarnFGLILAVISLACAFGICFTASFWQGILAGSFMAFglvdnILVYSYGLK 147
Cdd:PRK12324  84 PIASGVVSVS-----LAYILAVVLLVASLALAYLLSPKLALVLLVYLVL-----NLAYSFKLK 136
ubiA PRK12884
prenyltransferase; Reviewed
 64-174 7.39e-03

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 37.24  E-value: 7.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528510  64 NTLTNYHDRDIDAImERTkNRPIPSRRIYPPEkARNFGLILAVISLACAFGIcftaSFWQGILAGSFMAFGlvdniLVYS 143
Cdd:PRK12884  54 NALNDYFDYEVDRI-NRP-DRPIPSGRISRRE-ALLLAILLFILGLIAAYLI----SPLAFLVVILVSVLG-----ILYN 121

                         90       100       110
                 ....*....|....*....|....*....|.
gi 663528510 144 YGLKRKSRTNIVLGGFSGGAPALIGYVAVTT 174
Cdd:PRK12884 122 WKLKEYGLIGNLYVAFLTGMTFIFGGIAVGE 152
 
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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