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Conserved domains on  [gi|2131043842|ref|XP_044898639|]
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protein prenyltransferase alpha subunit repeat-containing protein 1 isoform X2 [Felis catus]

Protein Classification

protein prenyltransferase subunit alpha family protein( domain architecture ID 1002166)

protein prenyltransferase subunit alpha family protein such as Homo sapiens GGTase-I-alpha, which contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X

CATH:  1.25.40.120
EC:  2.5.1.58|2.5.1.59
Gene Ontology:  GO:0018343|GO:0018342|GO:0004661|GO:0004660
PubMed:  1918005
SCOP:  4001331

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02789 super family cl33568
farnesyltranstransferase
 88-219 1.56e-08

farnesyltranstransferase


The actual alignment was detected with superfamily member PLN02789:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 54.37  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131043842  88 IDVTCTLLLLNPDFTTAWNVRKELI--LSGTLNPIKDLhLGKLALTKfPKSPETWIHRRWVLQQLiqetslpsfvtkgnl 165
Cdd:PLN02789   57 LDLTADVIRLNPGNYTVWHFRRLCLeaLDADLEEELDF-AEDVAEDN-PKNYQIWHHRRWLAEKL--------------- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131043842 166 GTIPAERtqrlireEMEVCGEAAGRYPSNYNAWSHRIWVLQHL----AKLDVKEEIIK 219
Cdd:PLN02789  120 GPDAANK-------ELEFTRKILSLDAKNYHAWSHRQWVLRTLggweDELEYCHQLLE 170
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 88-219 1.56e-08

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 54.37  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131043842  88 IDVTCTLLLLNPDFTTAWNVRKELI--LSGTLNPIKDLhLGKLALTKfPKSPETWIHRRWVLQQLiqetslpsfvtkgnl 165
Cdd:PLN02789   57 LDLTADVIRLNPGNYTVWHFRRLCLeaLDADLEEELDF-AEDVAEDN-PKNYQIWHHRRWLAEKL--------------- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131043842 166 GTIPAERtqrlireEMEVCGEAAGRYPSNYNAWSHRIWVLQHL----AKLDVKEEIIK 219
Cdd:PLN02789  120 GPDAANK-------ELEFTRKILSLDAKNYHAWSHRQWVLRTLggweDELEYCHQLLE 170
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 177-208 3.14e-05

Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) recognize a CaaX motif on their substrates where 'a' stands for preferably aliphatic residues, whereas GGT2 recognizes a completely different motif. Important substrates for FT include, amongst others, many members of the Ras superfamily. GGT1 substrates include some of the other small GTPases and GGT2 substrates include the Rab family.


Pssm-ID: 460128 [Multi-domain]  Cd Length: 32  Bit Score: 39.93  E-value: 3.14e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2131043842 177 IREEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 208
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 91-205 3.36e-04

Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 41.39  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131043842  91 TCTLLLLNPDFTTAWNVRKELILSGTLNPI-------KDLHLGKLALTKFPKSPETWIHRRWVLQQLiqetslpsfvtkg 163
Cdd:COG5536    55 TQELIDKNPEFYTIWNYRFSILKHVQMVSEdkehlldNELDFLDEALKDNPKNYQIWHHRQWMLELF------------- 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2131043842 164 nlgtiPAERTQRlireEMEVCGEAAGRYPSNYNAWSHRIWVL 205
Cdd:COG5536   122 -----PKPSWGR----ELFITKKLLDSDSRNYHVWSYRRWVL 154
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 88-219 1.56e-08

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 54.37  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131043842  88 IDVTCTLLLLNPDFTTAWNVRKELI--LSGTLNPIKDLhLGKLALTKfPKSPETWIHRRWVLQQLiqetslpsfvtkgnl 165
Cdd:PLN02789   57 LDLTADVIRLNPGNYTVWHFRRLCLeaLDADLEEELDF-AEDVAEDN-PKNYQIWHHRRWLAEKL--------------- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2131043842 166 GTIPAERtqrlireEMEVCGEAAGRYPSNYNAWSHRIWVLQHL----AKLDVKEEIIK 219
Cdd:PLN02789  120 GPDAANK-------ELEFTRKILSLDAKNYHAWSHRQWVLRTLggweDELEYCHQLLE 170
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 177-208 3.14e-05

Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) recognize a CaaX motif on their substrates where 'a' stands for preferably aliphatic residues, whereas GGT2 recognizes a completely different motif. Important substrates for FT include, amongst others, many members of the Ras superfamily. GGT1 substrates include some of the other small GTPases and GGT2 substrates include the Rab family.


Pssm-ID: 460128 [Multi-domain]  Cd Length: 32  Bit Score: 39.93  E-value: 3.14e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2131043842 177 IREEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 208
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 91-205 3.36e-04

Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 41.39  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131043842  91 TCTLLLLNPDFTTAWNVRKELILSGTLNPI-------KDLHLGKLALTKFPKSPETWIHRRWVLQQLiqetslpsfvtkg 163
Cdd:COG5536    55 TQELIDKNPEFYTIWNYRFSILKHVQMVSEdkehlldNELDFLDEALKDNPKNYQIWHHRQWMLELF------------- 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2131043842 164 nlgtiPAERTQRlireEMEVCGEAAGRYPSNYNAWSHRIWVL 205
Cdd:COG5536   122 -----PKPSWGR----ELFITKKLLDSDSRNYHVWSYRRWVL 154
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 121-216 1.97e-03

Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 39.08  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131043842 121 KDLHLGKLALTKF--PKSPET---WIHRRWVLQQLiqetslpsfvtkgnlgTIPAERTQRLIREEMEVCGEAAGRYPSNY 195
Cdd:COG5536    45 KEYSVRALKLTQEliDKNPEFytiWNYRFSILKHV----------------QMVSEDKEHLLDNELDFLDEALKDNPKNY 108

                          90       100
                  ....*....|....*....|.
gi 2131043842 196 NAWSHRIWVLQHLAKLDVKEE 216
Cdd:COG5536   109 QIWHHRQWMLELFPKPSWGRE 129
 
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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