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Conserved domains on  [gi|530391099|ref|XP_005252037|]
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protein prenyltransferase alpha subunit repeat-containing protein 1 isoform X4 [Homo sapiens]

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
 88-208 4.59e-08

farnesyltranstransferase


The actual alignment was detected with superfamily member PLN02789:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 52.82  E-value: 4.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530391099  88 IDVTCTLLLLNPDFTTAWNVRKELI--LSGTLNPIKDLhLGKLALTKfPKSPETWIHRRWVLQQLiqetsLPSFVTKgnl 165
Cdd:PLN02789  57 LDLTADVIRLNPGNYTVWHFRRLCLeaLDADLEEELDF-AEDVAEDN-PKNYQIWHHRRWLAEKL-----GPDAANK--- 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530391099 166 gtipteraqrliqeEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 208
Cdd:PLN02789 127 --------------ELEFTRKILSLDAKNYHAWSHRQWVLRTL 155
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 88-208 4.59e-08

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 52.82  E-value: 4.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530391099  88 IDVTCTLLLLNPDFTTAWNVRKELI--LSGTLNPIKDLhLGKLALTKfPKSPETWIHRRWVLQQLiqetsLPSFVTKgnl 165
Cdd:PLN02789  57 LDLTADVIRLNPGNYTVWHFRRLCLeaLDADLEEELDF-AEDVAEDN-PKNYQIWHHRRWLAEKL-----GPDAANK--- 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530391099 166 gtipteraqrliqeEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 208
Cdd:PLN02789 127 --------------ELEFTRKILSLDAKNYHAWSHRQWVLRTL 155
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 177-208 3.04e-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: 3.04e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530391099  177 IQEEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 208
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 91-205 1.15e-04

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 42.55  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530391099  91 TCTLLLLNPDFTTAWNVRKELILSGTLNPI-------KDLHLGKLALTKFPKSPETWIHRRWVLQQLiqetslpsfvtkg 163
Cdd:COG5536   55 TQELIDKNPEFYTIWNYRFSILKHVQMVSEdkehlldNELDFLDEALKDNPKNYQIWHHRQWMLELF------------- 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530391099 164 nlgtiPTERAQRliqeEMEVCGEAAGRYPSNYNAWSHRIWVL 205
Cdd:COG5536  122 -----PKPSWGR----ELFITKKLLDSDSRNYHVWSYRRWVL 154
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 88-208 4.59e-08

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 52.82  E-value: 4.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530391099  88 IDVTCTLLLLNPDFTTAWNVRKELI--LSGTLNPIKDLhLGKLALTKfPKSPETWIHRRWVLQQLiqetsLPSFVTKgnl 165
Cdd:PLN02789  57 LDLTADVIRLNPGNYTVWHFRRLCLeaLDADLEEELDF-AEDVAEDN-PKNYQIWHHRRWLAEKL-----GPDAANK--- 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530391099 166 gtipteraqrliqeEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 208
Cdd:PLN02789 127 --------------ELEFTRKILSLDAKNYHAWSHRQWVLRTL 155
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 177-208 3.04e-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: 3.04e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530391099  177 IQEEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 208
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 91-205 1.15e-04

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 42.55  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530391099  91 TCTLLLLNPDFTTAWNVRKELILSGTLNPI-------KDLHLGKLALTKFPKSPETWIHRRWVLQQLiqetslpsfvtkg 163
Cdd:COG5536   55 TQELIDKNPEFYTIWNYRFSILKHVQMVSEdkehlldNELDFLDEALKDNPKNYQIWHHRQWMLELF------------- 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530391099 164 nlgtiPTERAQRliqeEMEVCGEAAGRYPSNYNAWSHRIWVL 205
Cdd:COG5536  122 -----PKPSWGR----ELFITKKLLDSDSRNYHVWSYRRWVL 154
 
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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