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Conserved domains on  [gi|1718823346|ref|WP_145211418|]
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UbiA family prenyltransferase [Gimesia alba]

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 1.12e-87

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: 263.29  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   7 YFQLMRLPAVFTAMSDIILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAA 86
Cdd:cd13964     1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  87 ALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKTFLGPVMMGICRFLNVMLGASAVAreiNLWVKPQLRIAA 166
Cdd:cd13964    81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 167 ALGLFILGLTWFARMEAKQSHRGHLI--GGMLVINAGLGALVWMLATYPWPqqlnltMVLAATGVVILTINRRLVQAVLN 244
Cdd:cd13964   158 ALGVYIAGVTYIARGEVHGGPRRLLPlaLLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1718823346 245 PIPQNVQIAVKTMLTSYVMLNAIMVFVWtANPQYAIITAALLLPTILLSRW 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 1.12e-87

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: 263.29  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   7 YFQLMRLPAVFTAMSDIILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAA 86
Cdd:cd13964     1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  87 ALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKTFLGPVMMGICRFLNVMLGASAVAreiNLWVKPQLRIAA 166
Cdd:cd13964    81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 167 ALGLFILGLTWFARMEAKQSHRGHLI--GGMLVINAGLGALVWMLATYPWPqqlnltMVLAATGVVILTINRRLVQAVLN 244
Cdd:cd13964   158 ALGVYIAGVTYIARGEVHGGPRRLLPlaLLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1718823346 245 PIPQNVQIAVKTMLTSYVMLNAIMVFVWtANPQYAIITAALLLPTILLSRW 295
Cdd:cd13964   232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
prenyl_rel_EboC NF035940
UbiA-like protein EboC;
6-299 1.11e-53

UbiA-like protein EboC;


Pssm-ID: 468273  Cd Length: 292  Bit Score: 176.58  E-value: 1.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   6 AYFQLMRLPAVFTAMSDIILGF------LLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGR 79
Cdd:NF035940    1 AYLQLMRPANIVTAWADILAGFaisgflTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  80 ISTQKAAALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKK-TFLGPVMMGICRFLNVMLGASAvareinlwV 158
Cdd:NF035940   81 VSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKHhAIFGPLNMGLCRGGNLLLGMSV--------V 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 159 KPQLRIAAALGL----FILGLTWFARMEAKQSHRGHLIGGMLVInAGLGALVWMLATYPWPqqlNLTMVLAATGVVILTI 234
Cdd:NF035940  153 PEALSEYWFLALipivYIAAITMISRGEVHGGKKSTLIIALLLY-ALVIASLLGLAFLQNG---NLLIALPFVLLFAILI 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718823346 235 NRRLVQAVLNPIPQNVQIAVKTMLTSYVMLNAIMVFVWtANPQYAIITAALLLPTILLSRWMSVT 299
Cdd:NF035940  229 FPPLIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGF-GGWPYGLLVLLLLPLSLLLAKIFAVT 292
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
5-175 6.80e-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: 72.95  E-value: 6.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   5 LAYFQLMRLPA---VFTAMSDIILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDA--EERPSRPIPSGR 79
Cdd:COG0382     1 RAYLRLLRLDRpigILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRinERKPNRPLASGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  80 ISTQKAAALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKK-TFLGPVMMGICRFLNVMLGASAVAREINLWV 158
Cdd:COG0382    81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRfTLLGNLVLGLLFGLGILMGFAAVTGSLPLSA 160
                         170
                  ....*....|....*..
gi 1718823346 159 kpqLRIAAALGLFILGL 175
Cdd:COG0382   161 ---WLLALAAFLWTLAY 174
ubiA PRK12884
prenyltransferase; Reviewed
1-152 8.91e-15

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 72.68  E-value: 8.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   1 MKKCLAYFQLMRLPAVFTAMSDIILGFLLTHGsFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGRI 80
Cdd:PRK12884    1 RTKMKAYLELLRPEHGLMAGIAVVLGAIIALG-GLPLDEALLGFLTAFFASGSANALNDYFDYEVDRINRPDRPIPSGRI 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718823346  81 STQKAAALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKT-FLGPVMMGICRFLNVMLGASAVAR 152
Cdd:PRK12884   80 SRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKLKEYgLIGNLYVAFLTGMTFIFGGIAVGE 152
UbiA pfam01040
UbiA prenyltransferase family;
23-178 3.53e-14

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 70.72  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  23 IILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDA--EERPSRPIPSGRISTQKAAALGGLLMLAGVGAA 100
Cdd:pfam01040   5 ALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAimPRTPNRPLPSGRISPREALIFALVLLALGLLLL 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718823346 101 QTVGTQSLIVAGLLVVAILGYDTILKK-TFLGPVMMGICRFLNVMLGASAVAREINLWVkpqLRIAAALGLFILGLTWF 178
Cdd:pfam01040  85 LLLNPLTALLGLAALLLYVLYTLRLKRrTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA---LLLALALFLWTWAIALA 160
chlor_syn_BchG TIGR01476
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family ...
41-138 2.18e-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: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  41 ALLLVASAGLYLSGM--VFNDVFDRKVDAEERPSRPIPSGRISTQKAAALGGLLMLAGVGAAQTVGTQS---LIVAGLLV 115
Cdd:TIGR01476  39 MLLGMLMAGPLGTGFsqSINDYFDRDVDAINEPQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLivlFTVVGIVL 118
                          90       100
                  ....*....|....*....|....*
gi 1718823346 116 VAILGYDTI-LKKTF-LGPVMMGIC 138
Cdd:TIGR01476 119 AVIYSMPPIkLKRNGwLGPPAVGLS 143
 
Name Accession Description Interval E-value
PT_UbiA_1 cd13964
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
7-295 1.12e-87

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: 263.29  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   7 YFQLMRLPAVFTAMSDIILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAA 86
Cdd:cd13964     1 YLQLVRLPNLFTVPADVLAGAALAGGGLGPVLRLALLLLASVLLYAAGMVLNDVFDAELDARERPERPIPSGRVSRGAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  87 ALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKTFLGPVMMGICRFLNVMLGASAVAreiNLWVKPQLRIAA 166
Cdd:cd13964    81 ALGAGLLAAGVALAALVGRLSGLVALLLAAAILLYDAWLKHTPLGPLLMGLCRGLNLLLGASAAA---AGGLGPALLAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 167 ALGLFILGLTWFARMEAKQSHRGHLI--GGMLVINAGLGALVWMLATYPWPqqlnltMVLAATGVVILTINRRLVQAVLN 244
Cdd:cd13964   158 ALGVYIAGVTYIARGEVHGGPRRLLPlaLLAVLLVIGLALALAAPRGGRVL------LALLFLALFAAWVGRPLLRAYRD 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1718823346 245 PIPQNVQIAVKTMLTSYVMLNAIMVFVWtANPQYAIITAALLLPTILLSRW 295
Cdd:cd13964   232 PSPPNIGKAVGAGILSLIPLDAALAAAF-GGPALALLVLALLPLALLLARK 281
prenyl_rel_EboC NF035940
UbiA-like protein EboC;
6-299 1.11e-53

UbiA-like protein EboC;


Pssm-ID: 468273  Cd Length: 292  Bit Score: 176.58  E-value: 1.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   6 AYFQLMRLPAVFTAMSDIILGF------LLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGR 79
Cdd:NF035940    1 AYLQLMRPANIVTAWADILAGFaisgflTLTWSSAPNDISLIWLLLATIGLYGGGVVFNDVFDAELDAVERPERPIPSGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  80 ISTQKAAALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKK-TFLGPVMMGICRFLNVMLGASAvareinlwV 158
Cdd:NF035940   81 VSKQAALLLGSLLLLIGILAAFQVSLLSGVIALAIALAALLYDRFGKHhAIFGPLNMGLCRGGNLLLGMSV--------V 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 159 KPQLRIAAALGL----FILGLTWFARMEAKQSHRGHLIGGMLVInAGLGALVWMLATYPWPqqlNLTMVLAATGVVILTI 234
Cdd:NF035940  153 PEALSEYWFLALipivYIAAITMISRGEVHGGKKSTLIIALLLY-ALVIASLLGLAFLQNG---NLLIALPFVLLFAILI 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718823346 235 NRRLVQAVLNPIPQNVQIAVKTMLTSYVMLNAIMVFVWtANPQYAIITAALLLPTILLSRWMSVT 299
Cdd:NF035940  229 FPPLIKAIQNPIPPNIGKAVKAGVLSLIVLNAALAAGF-GGWPYGLLVLLLLPLSLLLAKIFAVT 292
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
5-175 6.80e-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: 72.95  E-value: 6.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   5 LAYFQLMRLPA---VFTAMSDIILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDA--EERPSRPIPSGR 79
Cdd:COG0382     1 RAYLRLLRLDRpigILLLLWPTLWALFLAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFDREIDRinERKPNRPLASGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  80 ISTQKAAALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKK-TFLGPVMMGICRFLNVMLGASAVAREINLWV 158
Cdd:COG0382    81 ISLREALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRfTLLGNLVLGLLFGLGILMGFAAVTGSLPLSA 160
                         170
                  ....*....|....*..
gi 1718823346 159 kpqLRIAAALGLFILGL 175
Cdd:COG0382   161 ---WLLALAAFLWTLAY 174
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
6-150 8.13e-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: 72.92  E-value: 8.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   6 AYFQLMRLP-AVFTAMSDIILGFLLTHGSFNPPVSFALLLVASAGLYL-SGMVFNDVFDRKVDAEERPSRPIPSGRISTQ 83
Cdd:cd13961     1 AYLELIRPPnLLMAALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAaAGYIINDYFDVEIDRINKPDRPIPSGRISRR 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718823346  84 KAAALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKT-FLGPVMMGICRFLNVMLGASAV 150
Cdd:cd13961    81 EALILSILLNALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTpLIGNLLVALLTGLPFLFGGLAA 148
ubiA PRK12884
prenyltransferase; Reviewed
1-152 8.91e-15

prenyltransferase; Reviewed


Pssm-ID: 183812  Cd Length: 279  Bit Score: 72.68  E-value: 8.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   1 MKKCLAYFQLMRLPAVFTAMSDIILGFLLTHGsFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGRI 80
Cdd:PRK12884    1 RTKMKAYLELLRPEHGLMAGIAVVLGAIIALG-GLPLDEALLGFLTAFFASGSANALNDYFDYEVDRINRPDRPIPSGRI 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718823346  81 STQKAAALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKT-FLGPVMMGICRFLNVMLGASAVAR 152
Cdd:PRK12884   80 SRREALLLAILLFILGLIAAYLISPLAFLVVILVSVLGILYNWKLKEYgLIGNLYVAFLTGMTFIFGGIAVGE 152
ubiA PRK12882
prenyltransferase; Reviewed
6-180 2.02e-14

prenyltransferase; Reviewed


Pssm-ID: 183811  Cd Length: 276  Bit Score: 71.93  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   6 AYFQLMRLPAVFTAMSDIILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKA 85
Cdd:PRK12882    6 GYLELTRPVNAVVAGVAAFIGAFIAGGILSSPSLTGLAFAAVFLATGAGNAINDYFDREIDRINRPDRPIPSGAVSPRGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  86 AALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKT-FLGPVMMGICRFLNVMLGASAVAREinlwvkpqlRI 164
Cdd:PRK12882   86 LAFSILLFAAGVALAFLLPPLCLAIALFNSLLLVLYAETLKGTpGLGNASVAYLTGSTFLFGGAAVGTE---------GL 156
                         170
                  ....*....|....*..
gi 1718823346 165 AAALGLFIL-GLTWFAR 180
Cdd:PRK12882  157 LALLVLFALaALATLAR 173
UbiA pfam01040
UbiA prenyltransferase family;
23-178 3.53e-14

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 70.72  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  23 IILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDA--EERPSRPIPSGRISTQKAAALGGLLMLAGVGAA 100
Cdd:pfam01040   5 ALAGLALAAGGVPDLLLLLLALLGTVLARAAANALNDYYDRDIDAimPRTPNRPLPSGRISPREALIFALVLLALGLLLL 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718823346 101 QTVGTQSLIVAGLLVVAILGYDTILKK-TFLGPVMMGICRFLNVMLGASAVAREINLWVkpqLRIAAALGLFILGLTWF 178
Cdd:pfam01040  85 LLLNPLTALLGLAALLLYVLYTLRLKRrTLLGQLVGGLAFGLPPLLGWAAVTGSLSPLA---LLLALALFLWTWAIALA 160
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
8-178 8.50e-12

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: 64.29  E-value: 8.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   8 FQLMRLPAVFTAMSDIILGFLL-THGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAA 86
Cdd:cd13956     1 LRLMRPYTLLYVLAPALAGAALaGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLPSGRLSPRQAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  87 ALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKT-FLGPVMMGICRFLNVMLGASAVAREINLWvkPQLRIA 165
Cdd:cd13956    81 AFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLkLGGWGVLGYATGLALLPGLGAVAAGGLVP--LALLLA 158
                         170
                  ....*....|...
gi 1718823346 166 AALGLFILGLTWF 178
Cdd:cd13956   159 LVFLLLGLGINLY 171
PRK09573 PRK09573
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; Reviewed
6-128 9.20e-11

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


Pssm-ID: 181963  Cd Length: 279  Bit Score: 61.13  E-value: 9.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   6 AYFQLMRLPAVFTAMSDIILGFLLTHGsFNPPVSFALLLVASAGLYLS-GMVFNDVFDRKVDAEERPSRPIPSGRISTQK 84
Cdd:PRK09573    5 AYFELIRPKNCIGASIGAIIGYLIASN-FKIDLKGIILAALVVFLVCAgGNVINDIYDIEIDKINKPERPIPSGRISLKE 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1718823346  85 AAALGGLLMLAGVGAAQTVGTQSLIVAGLLVVAILGYDTILKKT 128
Cdd:PRK09573   84 AKIFSITLFIVGLILSIFINIYAFLIALLNSILLYLYAKDLKKT 127
PT_UbiA_COQ2 cd13959
4-Hydroxybenzoate polyprenyltransferase; 4-Hydroxybenzoate polyprenyltransferase, also known ...
24-177 5.44e-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: 5.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  24 ILGFLLTHGSFNPPV--SFALLLVASAGLYLSGMVFNDVFDRKVDAE-ERP-SRPIPSGRISTQKAAALGGLLMLAGVGA 99
Cdd:cd13959    17 LWGLLLAAGGLPLPLlkLLLLFLLGAFLMRSAGCTINDIADRDIDAKvPRTkNRPLASGAISVKEALLFLAVQLLLGLAL 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718823346 100 AQTVGTQSLIVAGLLVVAILGYDTILKKTFLGPVMMGICRFLNVMLGASAVAREINLwvkpqlriaAALGLFILGLTW 177
Cdd:cd13959    97 LLQLNPLTILLSPIALLLVLIYPLMKRFTYWPQLVLGLAFGWGPLMGWAAVTGSLPL---------PALLLYLAVIFW 165
PT_UbiA_Cox10 cd13957
Protoheme IX farnesyltransferase; Protoheme IX farnesyltransferase (also called heme O ...
16-136 4.76e-08

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: 53.21  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  16 VFTAMSdiilGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAE-ERPS-RPIPSGRISTQKAAALGGLLM 93
Cdd:cd13957    13 LLTALA----GYLLAPGGVPDLLLLLLTLLGTALVSASANALNQYIERDIDAKmKRTRnRPLPSGRISPKHALIFGLVLG 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1718823346  94 LAGVGAAQTvgTQSLIVAGLLVVAILGYD---TILKK------TFLG------PVMMG 136
Cdd:cd13957    89 ILGLALLAL--FVNPLTALLGLLGIFLYVfvyTPLKKrttplnTVIGgiagaiPPLIG 144
PT_UbiA_chlorophyll cd13958
Bacteriochlorophyll/chlorophyll synthetase; Chlorophyll synthase catalyzes the last step of ...
32-295 6.16e-08

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: 52.62  E-value: 6.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  32 GSFNPPVSFALLLVASAGLYLSGM--VFNDVFDRKVDAEERPSRPIPSGRISTQKAAALGGLLMLAGVGAAQTVGtqSLI 109
Cdd:cd13958    28 QWSNWDVWLLLLGMLLAGPLLTGTsqTINDYYDREVDAINEPYRPIPSGRISEREALWNIWVLLLLSLLVALFLD--GPW 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 110 VAGLLVVAIlgydtilkktflgpvmmgicrFLNVMLGASAVAREINLWVKPqlriaAALGLFILGLTWFArmeakqshrG 189
Cdd:cd13958   106 VFAAAVVGL---------------------VLAYIYSAPPLKLKQNGWWGN-----AAVGLSYEGLPWWA---------G 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 190 HLIggmlvinaglgalvwmLATYPWPQQLNLTMVLAATGVVILTIN--------RRLVqavLNPIPqnVQIAVKT-MLTS 260
Cdd:cd13958   151 AAA----------------FAGLLTWESLALALLYSIGAHGIMTLNdfksiegdRQLG---LRSLP--VALGVDTaAWIA 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1718823346 261 YVMLN-----AIMVFVWTANPQYAIITAALLLPTILLSRW 295
Cdd:cd13958   210 CGVIDvpqlaVAALLLAWGETWYAAVVGALLLAQIPLQFK 249
PRK07566 PRK07566
chlorophyll synthase ChlG;
32-292 3.86e-07

chlorophyll synthase ChlG;


Pssm-ID: 236052  Cd Length: 314  Bit Score: 50.69  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  32 GSFNPPVSFALLLVAS---AGLYLSGM--VFNDVFDRKVDAEERPSRPIPSGRISTQKAAALGGLLMLAGVGAAqtvgtq 106
Cdd:PRK07566   54 GAFGWTLENVLKLLAGmllAGPLLCGTsqTLNDYFDREVDAINEPYRPIPSGAISLRWVLYLIAVLTVLGLAVA------ 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 107 slivagllvvailgydtilkkTFLGPVMMGICrFLNVMLGASAVAREI----NLWVKPqlriaAALGLFILGLTWFArme 182
Cdd:PRK07566  128 ---------------------YLLGPWVFLAA-LLGLFLAWIYSAPPLrlkqNGWLGN-----YAVGLSYEGLPWWA--- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346 183 akqshrghligGMLVINAGLgaLVWMLATypwpqqLNLTMVLAATGvvILTIN--------RRLvqaVLNPIPqnVQIAV 254
Cdd:PRK07566  178 -----------GAAAFGAGL--PSWPIVI------LALLYSLGAHG--IMTLNdfksvegdRQL---GLRSLP--VVFGE 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1718823346 255 KTM-LTSYVMLN-----AIMVFVWTANPQYAIITAALLLPTILL 292
Cdd:PRK07566  232 KNAaRIACVVIDlfqlaVIALLLAWGQPLYAAIVGLLLIPQITL 275
chlor_syn_BchG TIGR01476
bacteriochlorophyll/chlorophyll synthetase; This model describes a subfamily of a large family ...
41-138 2.18e-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: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  41 ALLLVASAGLYLSGM--VFNDVFDRKVDAEERPSRPIPSGRISTQKAAALGGLLMLAGVGAAQTVGTQS---LIVAGLLV 115
Cdd:TIGR01476  39 MLLGMLMAGPLGTGFsqSINDYFDRDVDAINEPQRPIPSGIISLREVRWNWLVLTVAGLLVALVLGNWLivlFTVVGIVL 118
                          90       100
                  ....*....|....*....|....*
gi 1718823346 116 VAILGYDTI-LKKTF-LGPVMMGIC 138
Cdd:TIGR01476 119 AVIYSMPPIkLKRNGwLGPPAVGLS 143
PRK12324 PRK12324
decaprenyl-phosphate phosphoribosyltransferase;
23-126 3.09e-06

decaprenyl-phosphate phosphoribosyltransferase;


Pssm-ID: 237058  Cd Length: 295  Bit Score: 47.93  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  23 IILGFLLTHGSFNPPV------SFALLLVASAGLYLsgmvFNDVFDRKVDAE--ERPSRPIPSGRISTQKAAALGGLLML 94
Cdd:PRK12324   29 VFAAPIFAGNLLNPGAllkvllAFVLFCLASSAVYL----VNDIRDVEADRLhpTKRNRPIASGVVSVSLAYILAVVLLV 104
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1718823346  95 AGVGAAQTVGTQSLIVAGLLVVAILGYDTILK 126
Cdd:PRK12324  105 ASLALAYLLSPKLALVLLVYLVLNLAYSFKLK 136
PRK04375 PRK04375
protoheme IX farnesyltransferase; Provisional
6-121 4.00e-06

protoheme IX farnesyltransferase; Provisional


Pssm-ID: 235293  Cd Length: 296  Bit Score: 47.44  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   6 AYFQL-----MRLpAVFTAmsdiILGFLLTHGSFNPPVSFALLLVASAGLYLSGMVFNDVFDRKVDAE-ERPS-RPIPSG 78
Cdd:PRK04375   12 DYLALtkprvISL-NLFTA----LGGMLLAPPGVPPLLLLLLTLLGIALVAGAAGALNNYIDRDIDAKmERTKnRPLVTG 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1718823346  79 RISTQKAAALGGLLMLAGVGA-AQTVgtqSLIVAGLLVVAILGY 121
Cdd:PRK04375   87 RISPREALIFGLVLGVLGFLLlGLFV---NPLAAWLTLAGIFFY 127
PT_UbiA_2 cd13963
UbiA family of prenyltransferases (PTases), Unknown subgroup; Many characterized members of ...
23-157 1.03e-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: 45.93  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  23 IILGFLLTHGSFNPPVSFALL---LVASAGlYlsgmVFNDVFDRKVDAE--ERPSRPIPSGRISTQKAAALGGLLMLAGV 97
Cdd:cd13963    20 LLFAGQLFDPDLLLAALLAFVafcLAASAV-Y----ILNDLLDLEADRLhpTKRNRPIASGRLSIPAALALAVVLLLAGL 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718823346  98 GAAQTVGTQSLIVAGLLVVAILGYDTILKKTFLGPVMM-GICRFLNVMLGASAVAREINLW 157
Cdd:cd13963    95 ALALLLSPAFLLVLLAYLVLNLAYSLKLKRIPLLDVFViAAGFVLRVLAGAVAIGVPLSPW 155
PLN00012 PLN00012
chlorophyll synthetase; Provisional
38-103 2.25e-05

chlorophyll synthetase; Provisional


Pssm-ID: 215028  Cd Length: 375  Bit Score: 45.24  E-value: 2.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718823346  38 VSFALLLVASAGLYLSG--MVFNDVFDRKVDAEERPSRPIPSGRISTQKAAALGGLLMLAGVGAAQTV 103
Cdd:PLN00012  121 VAKSIVCMLMSGPFLTGytQTINDWYDREIDAINEPYRPIPSGAISENEVITQIWVLLLGGLGLAYTL 188
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
8-120 1.50e-04

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: 42.50  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346   8 FQLMRLPAVFTAMSDIILGFLLT--HGSFNPPVSFALLLVASAGLYLSGMVFNDVFD--RKVDAEER--PSRPIPSGRIS 81
Cdd:cd13962     1 LLAARPRTLPASLAPVLLGTALAyyLGGFFNWLLFLLALLAALLLQIGVNLANDYFDykKGTDTEPRsgPSRVLVSGLLS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1718823346  82 TQKAAALG-GLLMLAGVGAAQTVGTQSLIVAGLLVVAILG 120
Cdd:cd13962    81 PRQVLRAAlVLLLLAALLGLYLVALGGWLLLLLGLLGILA 120
PRK12392 PRK12392
bacteriochlorophyll c synthase; Provisional
58-121 1.62e-04

bacteriochlorophyll c synthase; Provisional


Pssm-ID: 171463  Cd Length: 331  Bit Score: 42.76  E-value: 1.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  58 NDVFDRKVDAEERPSRPIPSGRISTQKAAALGGLLMLAGVGAAQTVGTQS------LIVAGLLVVAILGY 121
Cdd:PRK12392   70 NDYFDLELDRVNEPTRPIPSGRLSEKEALWNSIIVLLLAIGLGVWLGLHIggergmVIISSILAGLFVAY 139
PLN02776 PLN02776
prenyltransferase
26-137 3.55e-04

prenyltransferase


Pssm-ID: 215415  Cd Length: 341  Bit Score: 41.65  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  26 GFLLTHGSFnppVSFALLLVASAGLYL---SGMVFNDVFDRKVDAEERPS--RPIPSGRISTQKAAALGGLLMLAGVG-- 98
Cdd:PLN02776   17 GFVLGSGEA---IDLPGLGWTCAGTMLcaaSANTLNQVFEVKNDSKMKRTmrRPLPSGRISVPHAVAWAVVVGAAGVAll 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1718823346  99 AAQTVGTQSLIVAGLLVVAILGYdTILKK-----TFLGPVMMGI 137
Cdd:PLN02776   94 AYKTNMLTAGLGAGNILLYAFVY-TPLKQihpanTWVGAVVGAI 136
ubiA PRK12883
prenyltransferase UbiA-like protein; Reviewed
24-152 4.73e-04

prenyltransferase UbiA-like protein; Reviewed


Pssm-ID: 171796  Cd Length: 277  Bit Score: 40.87  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  24 ILGFLLTHGSFnPPVSFALL--LVASAGLYlSGMVFNDVFDRKVDAEERPSRPIPSGRISTQKAAALGGLLMLAGVGAAQ 101
Cdd:PRK12883   23 ILGSLVALGGI-PPIKTLILifLVVYLGCS-GGNTINDYFDYEIDKINRPNRPLPRGAMSRKAALYYSLLLFAVGLALAY 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1718823346 102 TVGTQSLIVAGLLVVAILGYDTILKKT-FLGPVMMGICRFLNVMLGASAVAR 152
Cdd:PRK12883  101 LINIEAFLFALGAYVLMFLYAWKLKPLpFIGNVVVALLTGATPIYGAIAVGR 152
PRK08238 PRK08238
UbiA family prenyltransferase;
40-157 1.86e-03

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 39.47  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718823346  40 FALLLVASAGlYlsgmVFNDVFDRKVDaEERPS---RPIPSGRISTQKAAALGGLLMLAGVGAAQTVGTQSLIVAGLLVV 116
Cdd:PRK08238  233 LAFSLCASAV-Y----ILNDLLDLEAD-RAHPRkrrRPFASGALPIPFGLAAAPLLLLAGLALALALGPAFLLVLLAYLA 306
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1718823346 117 AILGYDTILKKTFLGPVMMGICRF-LNVMLGASAVAREINLW 157
Cdd:PRK08238  307 LTLAYSLRLKRKVLVDVLTLAALYtLRIIAGAAAIGVALSFW 348
 
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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