NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|258613904|ref|NP_082484|]
View 

protein prenyltransferase alpha subunit repeat-containing protein 1 [Mus musculus]

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
PubMed:  1918005
SCOP:  4001331

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02789 super family cl33568
farnesyltranstransferase
89-315 8.89e-09

farnesyltranstransferase


The actual alignment was detected with superfamily member PLN02789:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 56.68  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904  89 DVTCTLLLLNPDFTTAWNVRKeLILSGTLSPI-KDLHL-GKLALTKfPKSPETWIHRRWVLQQLSqetflpSSVAKGSLg 166
Cdd:PLN02789  58 DLTADVIRLNPGNYTVWHFRR-LCLEALDADLeEELDFaEDVAEDN-PKNYQIWHHRRWLAEKLG------PDAANKEL- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904 167 avpaERTQRIIQEEmevcseaagryPSNYNAWSHRIWVLQNVAKLDlkillDELSSTKHWASMHVSDHSGFHYRQFLLKs 246
Cdd:PLN02789 129 ----EFTRKILSLD-----------AKNYHAWSHRQWVLRTLGGWE-----DELEYCHQLLEEDVRNNSAWNQRYFVIT- 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613904 247 lisqttidsAVPQHNSLKsepkdeaaaasteepsvnlpQLLEEEVEFCTDLIDSYPGHETLWCHRRHVF 315
Cdd:PLN02789 188 ---------RSPLLGGLE--------------------AMRDSELKYTIDAILANPRNESPWRYLRGLF 227
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
89-315 8.89e-09

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 56.68  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904  89 DVTCTLLLLNPDFTTAWNVRKeLILSGTLSPI-KDLHL-GKLALTKfPKSPETWIHRRWVLQQLSqetflpSSVAKGSLg 166
Cdd:PLN02789  58 DLTADVIRLNPGNYTVWHFRR-LCLEALDADLeEELDFaEDVAEDN-PKNYQIWHHRRWLAEKLG------PDAANKEL- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904 167 avpaERTQRIIQEEmevcseaagryPSNYNAWSHRIWVLQNVAKLDlkillDELSSTKHWASMHVSDHSGFHYRQFLLKs 246
Cdd:PLN02789 129 ----EFTRKILSLD-----------AKNYHAWSHRQWVLRTLGGWE-----DELEYCHQLLEEDVRNNSAWNQRYFVIT- 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613904 247 lisqttidsAVPQHNSLKsepkdeaaaasteepsvnlpQLLEEEVEFCTDLIDSYPGHETLWCHRRHVF 315
Cdd:PLN02789 188 ---------RSPLLGGLE--------------------AMRDSELKYTIDAILANPRNESPWRYLRGLF 227
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
91-240 5.88e-06

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 47.94  E-value: 5.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904  91 TCTLLLLNPDFTTAWNVRKELILSGTL-SPIKDLHLGK------LALTKFPKSPETWIHRRWVLQQlsqetflpssvakg 163
Cdd:COG5536   55 TQELIDKNPEFYTIWNYRFSILKHVQMvSEDKEHLLDNeldfldEALKDNPKNYQIWHHRQWMLEL-------------- 120
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258613904 164 slgaVPAERTQRiiqeEMEVCSEAAGRYPSNYNAWSHRIWVLQNVAKLDLKILL-DELSSTKHWASMHVSDHSGFHYR 240
Cdd:COG5536  121 ----FPKPSWGR----ELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNFSDLkHELEYTTSLIETDIYNNSAWHHR 190
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
177-207 8.50e-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: 39.54  E-value: 8.50e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 258613904  177 IQEEMEVCSEAAGRYPSNYNAWSHRIWVLQN 207
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
89-315 8.89e-09

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 56.68  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904  89 DVTCTLLLLNPDFTTAWNVRKeLILSGTLSPI-KDLHL-GKLALTKfPKSPETWIHRRWVLQQLSqetflpSSVAKGSLg 166
Cdd:PLN02789  58 DLTADVIRLNPGNYTVWHFRR-LCLEALDADLeEELDFaEDVAEDN-PKNYQIWHHRRWLAEKLG------PDAANKEL- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904 167 avpaERTQRIIQEEmevcseaagryPSNYNAWSHRIWVLQNVAKLDlkillDELSSTKHWASMHVSDHSGFHYRQFLLKs 246
Cdd:PLN02789 129 ----EFTRKILSLD-----------AKNYHAWSHRQWVLRTLGGWE-----DELEYCHQLLEEDVRNNSAWNQRYFVIT- 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258613904 247 lisqttidsAVPQHNSLKsepkdeaaaasteepsvnlpQLLEEEVEFCTDLIDSYPGHETLWCHRRHVF 315
Cdd:PLN02789 188 ---------RSPLLGGLE--------------------AMRDSELKYTIDAILANPRNESPWRYLRGLF 227
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
91-240 5.88e-06

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 47.94  E-value: 5.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904  91 TCTLLLLNPDFTTAWNVRKELILSGTL-SPIKDLHLGK------LALTKFPKSPETWIHRRWVLQQlsqetflpssvakg 163
Cdd:COG5536   55 TQELIDKNPEFYTIWNYRFSILKHVQMvSEDKEHLLDNeldfldEALKDNPKNYQIWHHRQWMLEL-------------- 120
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258613904 164 slgaVPAERTQRiiqeEMEVCSEAAGRYPSNYNAWSHRIWVLQNVAKLDLKILL-DELSSTKHWASMHVSDHSGFHYR 240
Cdd:COG5536  121 ----FPKPSWGR----ELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNFSDLkHELEYTTSLIETDIYNNSAWHHR 190
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
177-207 8.50e-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: 39.54  E-value: 8.50e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 258613904  177 IQEEMEVCSEAAGRYPSNYNAWSHRIWVLQN 207
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
121-316 9.69e-05

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 44.09  E-value: 9.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904 121 KDLHLGKLALTKF--PKSPET---WIHRRWVLQQLSQEtflpssvakgslgavpAERTQRIIQEEMEVCSEAAGRYPSNY 195
Cdd:COG5536   45 KEYSVRALKLTQEliDKNPEFytiWNYRFSILKHVQMV----------------SEDKEHLLDNELDFLDEALKDNPKNY 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613904 196 NAWSHRIWVLQNVAKLDLKillDELSSTKHWASMHVSDHSGFHYRQFLLkslisqttidsavpqhnslksepkdeaaaaS 275
Cdd:COG5536  109 QIWHHRQWMLELFPKPSWG---RELFITKKLLDSDSRNYHVWSYRRWVL------------------------------R 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 258613904 276 TEEPSVNLpQLLEEEVEFCTDLIDSYPGHETLWCHRRHVFY 316
Cdd:COG5536  156 TIEDLFNF-SDLKHELEYTTSLIETDIYNNSAWHHRYIWIE 195
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
287-315 5.18e-04

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: 37.23  E-value: 5.18e-04
                          10        20
                  ....*....|....*....|....*....
gi 258613904  287 LEEEVEFCTDLIDSYPGHETLWCHRRHVF 315
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLL 29
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
216-247 1.91e-03

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: 35.69  E-value: 1.91e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 258613904  216 LLDELSSTKHWASMHVSDHSGFHYRQFLLKSL 247
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH