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Conserved domains on  [gi|1945432715|ref|WP_197995854|]
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UbiA family prenyltransferase [Gimesia algae]

Protein Classification

UbiA family prenyltransferase( domain architecture ID 10195487)

UbiA family prenyltransferase catalyzes the Mg2+-dependent transfer of a hydrophobic polyprenyl chain onto a variety of acceptor molecules and is involved in the synthesis of molecules that mediate electron transport, including Vitamin K and Coenzyme Q

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
7-295 5.29e-88

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: 264.06  E-value: 5.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   7 YFQLMRLPAVFTALSDIILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAA 86
Cdd:cd13964     1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  87 TLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKTFLAPLMMGICRFLNVMLGASAVSreiNLWVKPQLRIAA 166
Cdd:cd13964    81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715 167 ALGLFIVGLTWFARMEAKNSNRGQL--VGGLLVINSGLGALAWMLATYPWPretnlsMVLAALGVVALTINRRLVQAILN 244
Cdd:cd13964   158 ALGVYIAGVTYIARGEVHGGPRRLLplALLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1945432715 245 PVPQNVQVAVKTMLMSYVMLNAIMVFVWtANPQYAILTAALLLPTILLSRW 295
Cdd:cd13964   232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
 
Name Accession Description Interval E-value
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
7-295 5.29e-88

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: 264.06  E-value: 5.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   7 YFQLMRLPAVFTALSDIILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAA 86
Cdd:cd13964     1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  87 TLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKTFLAPLMMGICRFLNVMLGASAVSreiNLWVKPQLRIAA 166
Cdd:cd13964    81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715 167 ALGLFIVGLTWFARMEAKNSNRGQL--VGGLLVINSGLGALAWMLATYPWPretnlsMVLAALGVVALTINRRLVQAILN 244
Cdd:cd13964   158 ALGVYIAGVTYIARGEVHGGPRRLLplALLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1945432715 245 PVPQNVQVAVKTMLMSYVMLNAIMVFVWtANPQYAILTAALLLPTILLSRW 295
Cdd:cd13964   232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
prenyl_rel_EboC NF035940
UbiA-like protein EboC;
6-299 2.37e-54

UbiA-like protein EboC;


Pssm-ID: 468273  Cd Length: 292  Bit Score: 178.50  E-value: 2.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   6 AYFQLMRLPAVFTALSDIILGF------LLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGR 79
Cdd:NF035940    1 AYLQLMRPANIVTAWADILAGFaisgflTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  80 ISTQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKK-TFLAPLMMGICRFLNVMLGASAVSreinlwv 158
Cdd:NF035940   81 VSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKHhAIFGPLNMGLCRGGNLLLGMSVVP------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715 159 kPQLRIAAALGL----FIVGLTWFARMEAKNSNRGQLVGGLLVINSGLGALaWMLATYPWpreTNLSMVLAALGVVALTI 234
Cdd:NF035940  154 -EALSEYWFLALipivYIAAITMISRGEVHGGKKSTLIIALLLYALVIASL-LGLAFLQN---GNLLIALPFVLLFAILI 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1945432715 235 NRRLVQAILNPVPQNVQVAVKTMLMSYVMLNAIMVFVWtANPQYAILTAALLLPTILLSRWMSVT 299
Cdd:NF035940  229 FPPLIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGF-GGWPYGLLVLLLLPLSLLLAKIFAVT 292
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
5-158 3.61e-15

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: 74.11  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   5 LAYFQLMRLPA---VFTALSDIILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDA--EERPSRPIPSGR 79
Cdd:COG0382     1 RAYLRLLRLDRpigILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRinERKPNRPLASGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  80 ISTQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKTFLAP-LMMGICRFLNVMLGASAVSREINLWV 158
Cdd:COG0382    81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRFTLLGnLVLGLLFGLGILMGFAAVTGSLPLSA 160
ubiA PRK12884
prenyltransferase; Reviewed
4-152 6.26e-14

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 70.37  E-value: 6.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   4 LLAYFQLMRLPAVFTALSDIILGFLLTHGsFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQ 83
Cdd:PRK12884    4 MKAYLELLRPEHGLMAGIAVVLGAIIALG-GLPLDEALLGFLTAFFASGSANALNDYFDYEVDRINRPDRPIPSGRISRR 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  84 KAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKT-FLAPLMMGICRFLNVMLGASAVSR 152
Cdd:PRK12884   83 EALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKLKEYgLIGNLYVAFLTGMTFIFGGIAVGE 152
UbiA pfam01040
UbiA prenyltransferase family;
23-178 1.45e-13

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 68.79  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  23 IILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDA--EERPSRPIPSGRISTQKAATLGGLLILAGVGAA 100
Cdd:pfam01040   5 ALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAimPRTPNRPLPSGRISPREALIFALVLLALGLLLL 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1945432715 101 QTVGTQSLIVASLLVVAILSYDMLLKKTFLAP-LMMGICRFLNVMLGASAVSREINLWVkpqLRIAAALGLFIVGLTWF 178
Cdd:pfam01040  85 LLLNPLTALLGLAALLLYVLYTLRLKRRTLLGqLVGGLAFGLPPLLGWAAVTGSLSPLA---LLLALALFLWTWAIALA 160
chlor_syn_BchG TIGR01476
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family ...
56-138 2.14e-06

bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family of polyprenyltransferases (pfam01040) that also includes 4-hydroxybenzoate octaprenyltransferase and protoheme IX farnesyltransferase (heme O synthase). Members of this family are found exclusively in photosynthetic organisms, including a single copy in Arabidopsis thaliana. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 130541  Cd Length: 283  Bit Score: 48.24  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  56 VFNDVFDRKVDAEERPSRPIPSGRISTQKAATLGGLLILAGVGAAQTVGTQSLIVASLL-VVAILSYDM---LLKKTF-L 130
Cdd:TIGR01476  56 SINDYFDRDVDAINEPQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLIVLFTVVgIVLAVIYSMppiKLKRNGwL 135

                  ....*...
gi 1945432715 131 APLMMGIC 138
Cdd:TIGR01476 136 GPPAVGLS 143
 
Name Accession Description Interval E-value
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
7-295 5.29e-88

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: 264.06  E-value: 5.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   7 YFQLMRLPAVFTALSDIILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAA 86
Cdd:cd13964     1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  87 TLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKTFLAPLMMGICRFLNVMLGASAVSreiNLWVKPQLRIAA 166
Cdd:cd13964    81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715 167 ALGLFIVGLTWFARMEAKNSNRGQL--VGGLLVINSGLGALAWMLATYPWPretnlsMVLAALGVVALTINRRLVQAILN 244
Cdd:cd13964   158 ALGVYIAGVTYIARGEVHGGPRRLLplALLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1945432715 245 PVPQNVQVAVKTMLMSYVMLNAIMVFVWtANPQYAILTAALLLPTILLSRW 295
Cdd:cd13964   232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
prenyl_rel_EboC NF035940
UbiA-like protein EboC;
6-299 2.37e-54

UbiA-like protein EboC;


Pssm-ID: 468273  Cd Length: 292  Bit Score: 178.50  E-value: 2.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   6 AYFQLMRLPAVFTALSDIILGF------LLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGR 79
Cdd:NF035940    1 AYLQLMRPANIVTAWADILAGFaisgflTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  80 ISTQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKK-TFLAPLMMGICRFLNVMLGASAVSreinlwv 158
Cdd:NF035940   81 VSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKHhAIFGPLNMGLCRGGNLLLGMSVVP------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715 159 kPQLRIAAALGL----FIVGLTWFARMEAKNSNRGQLVGGLLVINSGLGALaWMLATYPWpreTNLSMVLAALGVVALTI 234
Cdd:NF035940  154 -EALSEYWFLALipivYIAAITMISRGEVHGGKKSTLIIALLLYALVIASL-LGLAFLQN---GNLLIALPFVLLFAILI 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1945432715 235 NRRLVQAILNPVPQNVQVAVKTMLMSYVMLNAIMVFVWtANPQYAILTAALLLPTILLSRWMSVT 299
Cdd:NF035940  229 FPPLIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGF-GGWPYGLLVLLLLPLSLLLAKIFAVT 292
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
5-158 3.61e-15

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: 74.11  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   5 LAYFQLMRLPA---VFTALSDIILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDA--EERPSRPIPSGR 79
Cdd:COG0382     1 RAYLRLLRLDRpigILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRinERKPNRPLASGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  80 ISTQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKTFLAP-LMMGICRFLNVMLGASAVSREINLWV 158
Cdd:COG0382    81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRFTLLGnLVLGLLFGLGILMGFAAVTGSLPLSA 160
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
6-130 9.97e-15

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: 72.54  E-value: 9.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   6 AYFQLMRLP-AVFTALSDIILGFLLTHGSFSPPVSFALLLVASASLYL-SGMVFNDVFDRKVDAEERPSRPIPSGRISTQ 83
Cdd:cd13961     1 AYLELIRPPnLLMAALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAaAGYIINDYFDVEIDRINKPDRPIPSGRISRR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1945432715  84 KAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKTFL 130
Cdd:cd13961    81 EALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTPL 127
ubiA PRK12884
prenyltransferase; Reviewed
4-152 6.26e-14

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 70.37  E-value: 6.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   4 LLAYFQLMRLPAVFTALSDIILGFLLTHGsFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQ 83
Cdd:PRK12884    4 MKAYLELLRPEHGLMAGIAVVLGAIIALG-GLPLDEALLGFLTAFFASGSANALNDYFDYEVDRINRPDRPIPSGRISRR 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  84 KAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKT-FLAPLMMGICRFLNVMLGASAVSR 152
Cdd:PRK12884   83 EALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKLKEYgLIGNLYVAFLTGMTFIFGGIAVGE 152
ubiA PRK12882
prenyltransferase; Reviewed
1-128 7.79e-14

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 70.00  E-value: 7.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   1 MKTLLAYFQLMRLPAVFTALSDIILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGRI 80
Cdd:PRK12882    1 GMTVRGYLELTRPVNAVVAGVAAFIGAFIAGGILSSPSLTGLAFAAVFLATGAGNAINDYFDREIDRINRPDRPIPSGAV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1945432715  81 STQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKT 128
Cdd:PRK12882   81 SPRGALAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYAETLKGT 128
UbiA pfam01040
UbiA prenyltransferase family;
23-178 1.45e-13

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 68.79  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  23 IILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDA--EERPSRPIPSGRISTQKAATLGGLLILAGVGAA 100
Cdd:pfam01040   5 ALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAimPRTPNRPLPSGRISPREALIFALVLLALGLLLL 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1945432715 101 QTVGTQSLIVASLLVVAILSYDMLLKKTFLAP-LMMGICRFLNVMLGASAVSREINLWVkpqLRIAAALGLFIVGLTWF 178
Cdd:pfam01040  85 LLLNPLTALLGLAALLLYVLYTLRLKRRTLLGqLVGGLAFGLPPLLGWAAVTGSLSPLA---LLLALALFLWTWAIALA 160
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
4-128 2.13e-11

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


Pssm-ID: 181963  Cd Length: 279  Bit Score: 63.05  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   4 LLAYFQLMRLPAVFTALSDIILGFLLTHGS--FSPPVSFALLLVASASLYlsGMVFNDVFDRKVDAEERPSRPIPSGRIS 81
Cdd:PRK09573    3 IKAYFELIRPKNCIGASIGAIIGYLIASNFkiDLKGIILAALVVFLVCAG--GNVINDIYDIEIDKINKPERPIPSGRIS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1945432715  82 TQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKT 128
Cdd:PRK09573   81 LKEAKIFSITLFIVGLILSIFINIYAFLIALLNSILLYLYAKDLKKT 127
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
8-178 2.54e-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: 62.75  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   8 FQLMRLPAVFTALSDIILGFLL-THGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAA 86
Cdd:cd13956     1 LRLMRPYTLLYVLAPALAGAALaGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRLSPRQAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  87 TLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKKTFLA-PLMMGICRFLNVMLGASAVSREINLWvkPQLRIA 165
Cdd:cd13956    81 AFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLKLGgWGVLGYATGLALLPGLGAVAAGGLVP--LALLLA 158
                         170
                  ....*....|...
gi 1945432715 166 AALGLFIVGLTWF 178
Cdd:cd13956   159 LVFLLLGLGINLY 171
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
24-177 6.34e-11

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: 61.71  E-value: 6.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  24 ILGFLLTHGSFSPPV--SFALLLVASASLYLSGMVFNDVFDRKVDAE-ERP-SRPIPSGRISTQKAATLGGLLILAGVGA 99
Cdd:cd13959    17 LWGLLLAAGGLPLPLlkLLLLFLLGAFLMRSAGCTINDIADRDIDAKvPRTkNRPLASGAISVKEALLFLAVQLLLGLAL 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1945432715 100 AQTVGTQSLIVASLLVVAILSYDMLLKKTFLAPLMMGICRFLNVMLGASAVSREINLwvkpqlriaAALGLFIVGLTW 177
Cdd:cd13959    97 LLQLNPLTILLSPIALLLVLIYPLMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPL---------PALLLYLAVIFW 165
PRK12324 PRK12324
decaprenyl-phosphate phosphoribosyltransferase;
1-126 7.58e-07

decaprenyl-phosphate phosphoribosyltransferase;


Pssm-ID: 237058  Cd Length: 295  Bit Score: 49.48  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   1 MKTLLAYFQLMR----LPAVFTALSDIILGFLLTHGSFSP-PVSFALLLVASASLYLsgmvFNDVFDRKVDAE--ERPSR 73
Cdd:PRK12324    8 KNLLAGYLKLLRpkqwIKNLFVFAAPIFAGNLLNPGALLKvLLAFVLFCLASSAVYL----VNDIRDVEADRLhpTKRNR 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1945432715  74 PIPSGRISTQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLK 126
Cdd:PRK12324   84 PIASGVVSVSLAYILAVVLLVASLALAYLLSPKLALVLLVYLVLNLAYSFKLK 136
PT_UbiA_chlorophyll cd13958
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ...
32-121 1.17e-06

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: 48.76  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  32 GSFSPPVSFALLLVASASLYLSGM--VFNDVFDRKVDAEERPSRPIPSGRISTQKAATLGGLLILAGVGAAQTVGTQsLI 109
Cdd:cd13958    28 QWSNWDVWLLLLGMLLAGPLLTGTsqTINDYYDREVDAINEPYRPIPSGRISEREALWNIWVLLLLSLLVALFLDGP-WV 106
                          90
                  ....*....|..
gi 1945432715 110 VASLLVVAILSY 121
Cdd:cd13958   107 FAAAVVGLVLAY 118
PRK07566 PRK07566
chlorophyll synthase ChlG;
52-100 1.27e-06

chlorophyll synthase ChlG;


Pssm-ID: 236052  Cd Length: 314  Bit Score: 49.15  E-value: 1.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1945432715  52 LSGM--VFNDVFDRKVDAEERPSRPIPSGRISTQKAATLGGLLILAGVGAA 100
Cdd:PRK07566   77 LCGTsqTLNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAVA 127
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
16-128 1.39e-06

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: 48.59  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  16 VFTALSdiilGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAE-ERPS-RPIPSGRISTQKAATLGGLLI 93
Cdd:cd13957    13 LLTALA----GYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKmKRTRnRPLPSGRISPKHALIFGLVLG 88
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1945432715  94 LAGVGAAQTvgTQSLIVASLLVVAILS----YDMLLKKT 128
Cdd:cd13957    89 ILGLALLAL--FVNPLTALLGLLGIFLyvfvYTPLKKRT 125
chlor_syn_BchG TIGR01476
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family ...
56-138 2.14e-06

bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family of polyprenyltransferases (pfam01040) that also includes 4-hydroxybenzoate octaprenyltransferase and protoheme IX farnesyltransferase (heme O synthase). Members of this family are found exclusively in photosynthetic organisms, including a single copy in Arabidopsis thaliana. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 130541  Cd Length: 283  Bit Score: 48.24  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  56 VFNDVFDRKVDAEERPSRPIPSGRISTQKAATLGGLLILAGVGAAQTVGTQSLIVASLL-VVAILSYDM---LLKKTF-L 130
Cdd:TIGR01476  56 SINDYFDRDVDAINEPQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLIVLFTVVgIVLAVIYSMppiKLKRNGwL 135

                  ....*...
gi 1945432715 131 APLMMGIC 138
Cdd:TIGR01476 136 GPPAVGLS 143
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
3-126 1.21e-05

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 45.90  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   3 TLLAYFQL-----MRLpAVFTAlsdiILGFLLTHGSFSPPVSFALLLVASASLYLSGMVFNDVFDRKVDAE-ERPS-RPI 75
Cdd:PRK04375    9 TLKDYLALtkprvISL-NLFTA----LGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKmERTKnRPL 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1945432715  76 PSGRISTQKAATLGGLLILAGV---GAAQTVGTQSLIVASLLVVAILsYDMLLK 126
Cdd:PRK04375   84 VTGRISPREALIFGLVLGVLGFlllGLFVNPLAAWLTLAGIFFYVVV-YTLWLK 136
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
7-127 1.46e-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: 45.54  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   7 YFQLMRLP------AVFTALsdiILGFLLTHGSFSPPVSFALL---LVASASlYlsgmVFNDVFDRKVDAE--ERPSRPI 75
Cdd:cd13963     1 LLKLLRPHqwvknlLVFAPL---LFAGQLFDPDLLLAALLAFVafcLAASAV-Y----ILNDLLDLEADRLhpTKRNRPI 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1945432715  76 PSGRISTQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKK 127
Cdd:cd13963    73 ASGRLSIPAALALAVVLLLAGLALALLLSPAFLLVLLAYLVLNLAYSLKLKR 124
PLN00012 PLN00012
chlorophyll synthetase; Provisional
58-103 4.15e-05

chlorophyll synthetase; Provisional


Pssm-ID: 215028  Cd Length: 375  Bit Score: 44.47  E-value: 4.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1945432715  58 NDVFDRKVDAEERPSRPIPSGRISTQKAATLGGLLILAGVGAAQTV 103
Cdd:PLN00012  143 NDWYDREIDAINEPYRPIPSGAISENEVITQIWVLLLGGLGLAYTL 188
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
8-119 8.84e-05

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


Pssm-ID: 260125  Cd Length: 283  Bit Score: 43.27  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   8 FQLMRLPAVFTALSDIILGFLLT--HGSFSPPVSFALLLVASASLYLSGMVFNDVFD--RKVDAEER--PSRPIPSGRIS 81
Cdd:cd13962     1 LLAARPRTLPASLAPVLLGTALAyyLGGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRsgPSRVLVSGLLS 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1945432715  82 TQKAATLG-GLLILAGVGAAQTVGTQSLIVASLLVVAIL 119
Cdd:cd13962    81 PRQVLRAAlVLLLLAALLGLYLVALGGWLLLLLGLLGIL 119
PRK12392 PRK12392
bacteriochlorophyll c synthase; Provisional
58-121 1.50e-04

bacteriochlorophyll c synthase; Provisional


Pssm-ID: 171463  Cd Length: 331  Bit Score: 42.76  E-value: 1.50e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  58 NDVFDRKVDAEERPSRPIPSGRISTQKAATLGGLLILAGVGAAQTVGTQS------LIVASLLVVAILSY 121
Cdd:PRK12392   70 NDYFDLELDRVNEPTRPIPSGRLSEKEALWNSIIVLLLAIGLGVWLGLHIggergmVIISSILAGLFVAY 139
ubiA PRK12883
prenyltransferase UbiA-like protein; Reviewed
24-126 2.88e-04

prenyltransferase UbiA-like protein; Reviewed


Pssm-ID: 171796  Cd Length: 277  Bit Score: 41.64  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  24 ILGFLLTHGSFsPPVSFALLLVASASLYLS-GMVFNDVFDRKVDAEERPSRPIPSGRISTQKAATLGGLLILAGVGAAQT 102
Cdd:PRK12883   23 ILGSLVALGGI-PPIKTLILIFLVVYLGCSgGNTINDYFDYEIDKINRPNRPLPRGAMSRKAALYYSLLLFAVGLALAYL 101
                          90       100
                  ....*....|....*....|....
gi 1945432715 103 VGTQSLIVASLLVVAILSYDMLLK 126
Cdd:PRK12883  102 INIEAFLFALGAYVLMFLYAWKLK 125
ubiA PRK12874
4-hydroxybenzoate polyprenyltransferase;
13-157 1.06e-03

4-hydroxybenzoate polyprenyltransferase;


Pssm-ID: 237242  Cd Length: 291  Bit Score: 39.99  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  13 LPAVFTALSDIILGFLLTHGSFSPPVSFALLLVASASLYLSG---------------------MVFNDVFDRKVDAE--E 69
Cdd:PRK12874    1 MKKFTKKLKDISELVVFKHSIFSLPFIFIAMIVASKQKNDTGwfgfkllilgilaavsarnfaMAFNRLVDRDIDKDnpR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715  70 RPSRPIPSGRISTqkaatlGGLLILAGVGAAQTVGTQSLIVA-----SLLVVAIL-SYDMLLKKTFLAPLMMGICRFLNV 143
Cdd:PRK12874   81 TANRPSVDGRISV------KSMVLFIVLNALIFIGVSYFINPlafklSFPFLIVLgGYSYFKRFSSLAHLVLGLSLGLAP 154
                         170
                  ....*....|....
gi 1945432715 144 MLGASAVSREINLW 157
Cdd:PRK12874  155 IAGVVAVLGEIPLW 168
PRK08238 PRK08238
UbiA family prenyltransferase;
4-127 3.84e-03

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 38.70  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945432715   4 LLAYFQLMRLPAVFTALsdiiLGFLlthgSFSppvsfallLVASASlYlsgmVFNDVFDRKVDaEERPS---RPIPSGRI 80
Cdd:PRK08238  213 LLAAHQFGDLQALLAAL----LAFL----AFS--------LCASAV-Y----ILNDLLDLEAD-RAHPRkrrRPFASGAL 270
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1945432715  81 STQKAATLGGLLILAGVGAAQTVGTQSLIVASLLVVAILSYDMLLKK 127
Cdd:PRK08238  271 PIPFGLAAAPLLLLAGLALALALGPAFLLVLLAYLALTLAYSLRLKR 317
 
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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