NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462624622|ref|XP_054218903|]
View 

protein prenyltransferase alpha subunit repeat-containing protein 1 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 105-136 2.88e-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: 40.70  E-value: 2.88e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462624622 105 IQEEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 136
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 super family cl44255
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 49-249 1.03e-03

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


The actual alignment was detected with superfamily member COG5536:

Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 40.62  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622  49 KDLHLGKLALTKF--PKSPET---WIHRRWVLQQLiqetslpsfvtkgnlgTIPTERAQRLIQEEMEVCGEAAGRYPSNY 123
Cdd:COG5536    45 KEYSVRALKLTQEliDKNPEFytiWNYRFSILKHV----------------QMVSEDKEHLLDNELDFLDEALKDNPKNY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622 124 NAWSHRIWVLQHLAKldvKILLDELSSTKHWASMHVSDHSGFHYRQFLlkslisqtvidssvmeqnplrsepalvppkde 203
Cdd:COG5536   109 QIWHHRQWMLELFPK---PSWGRELFITKKLLDSDSRNYHVWSYRRWV-------------------------------- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462624622 204 eaaVSTEEPRINLpHLLEEEVEFSTDLIDSYPGHETLWCHRRHIFY 249
Cdd:COG5536   154 ---LRTIEDLFNF-SDLKHELEYTTSLIETDIYNNSAWHHRYIWIE 195
 
Name Accession Description Interval E-value
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 105-136 2.88e-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: 40.70  E-value: 2.88e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462624622 105 IQEEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 136
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 49-249 1.03e-03

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 40.62  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622  49 KDLHLGKLALTKF--PKSPET---WIHRRWVLQQLiqetslpsfvtkgnlgTIPTERAQRLIQEEMEVCGEAAGRYPSNY 123
Cdd:COG5536    45 KEYSVRALKLTQEliDKNPEFytiWNYRFSILKHV----------------QMVSEDKEHLLDNELDFLDEALKDNPKNY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622 124 NAWSHRIWVLQHLAKldvKILLDELSSTKHWASMHVSDHSGFHYRQFLlkslisqtvidssvmeqnplrsepalvppkde 203
Cdd:COG5536   109 QIWHHRQWMLELFPK---PSWGRELFITKKLLDSDSRNYHVWSYRRWV-------------------------------- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462624622 204 eaaVSTEEPRINLpHLLEEEVEFSTDLIDSYPGHETLWCHRRHIFY 249
Cdd:COG5536   154 ---LRTIEDLFNF-SDLKHELEYTTSLIETDIYNNSAWHHRYIWIE 195
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 220-248 1.47e-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: 1.47e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462624622 220 LEEEVEFSTDLIDSYPGHETLWCHRRHIF 248
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLL 29
PLN02789 PLN02789
farnesyltranstransferase
 51-175 4.43e-03

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 38.57  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622  51 LHLGKLALTKFPKSPETWIHRRWVLQQLiqetslpsfvtkgnlgtipteraQRLIQEEMEVCGEAAGRYPSNYNAWSHRI 130
Cdd:PLN02789   57 LDLTADVIRLNPGNYTVWHFRRLCLEAL-----------------------DADLEEELDFAEDVAEDNPKNYQIWHHRR 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462624622 131 WVLQhlaKLDVKILLDELSSTKHWASMHVSDHSGFHYRQFLLKSL 175
Cdd:PLN02789  114 WLAE---KLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTL 155
 
Name Accession Description Interval E-value
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 105-136 2.88e-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: 40.70  E-value: 2.88e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462624622 105 IQEEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 136
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 49-249 1.03e-03

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 40.62  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622  49 KDLHLGKLALTKF--PKSPET---WIHRRWVLQQLiqetslpsfvtkgnlgTIPTERAQRLIQEEMEVCGEAAGRYPSNY 123
Cdd:COG5536    45 KEYSVRALKLTQEliDKNPEFytiWNYRFSILKHV----------------QMVSEDKEHLLDNELDFLDEALKDNPKNY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622 124 NAWSHRIWVLQHLAKldvKILLDELSSTKHWASMHVSDHSGFHYRQFLlkslisqtvidssvmeqnplrsepalvppkde 203
Cdd:COG5536   109 QIWHHRQWMLELFPK---PSWGRELFITKKLLDSDSRNYHVWSYRRWV-------------------------------- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462624622 204 eaaVSTEEPRINLpHLLEEEVEFSTDLIDSYPGHETLWCHRRHIFY 249
Cdd:COG5536   154 ---LRTIEDLFNF-SDLKHELEYTTSLIETDIYNNSAWHHRYIWIE 195
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 220-248 1.47e-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: 1.47e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462624622 220 LEEEVEFSTDLIDSYPGHETLWCHRRHIF 248
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLL 29
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 144-175 1.62e-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: 1.62e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462624622 144 LLDELSSTKHWASMHVSDHSGFHYRQFLLKSL 175
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PLN02789 PLN02789
farnesyltranstransferase
 51-175 4.43e-03

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 38.57  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622  51 LHLGKLALTKFPKSPETWIHRRWVLQQLiqetslpsfvtkgnlgtipteraQRLIQEEMEVCGEAAGRYPSNYNAWSHRI 130
Cdd:PLN02789   57 LDLTADVIRLNPGNYTVWHFRRLCLEAL-----------------------DADLEEELDFAEDVAEDNPKNYQIWHHRR 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462624622 131 WVLQhlaKLDVKILLDELSSTKHWASMHVSDHSGFHYRQFLLKSL 175
Cdd:PLN02789  114 WLAE---KLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTL 155
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 57-243 9.08e-03

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 37.54  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622  57 ALTKFPKSPETWIHRRWVLQqLIQETSLPS--FVTKGNL-----------------GTIPTERAQRLIQEEMEVCGEAAG 117
Cdd:COG5536   100 ALKDNPKNYQIWHHRQWMLE-LFPKPSWGRelFITKKLLdsdsrnyhvwsyrrwvlRTIEDLFNFSDLKHELEYTTSLIE 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624622 118 RYPSNYNAWSHR-IWVLQHLAKLDV---KILLDELSSTKHWASMHVSDHSGFHY-RQFLLKSLISQTVIDSSV------- 185
Cdd:COG5536   179 TDIYNNSAWHHRyIWIERRFNRGDVisqKYLEKELEYIFDKIFTDPDNQSVWGYlRGVSSEFATDIVMIGEKVedlgkyi 258

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462624622 186 -------MEQNPLRSEPALVPPKDEEAAVSTEEPrinLPHLLEEEVEFSTDLIDSY-PGHETLWCH 243
Cdd:COG5536   259 viingkeLDLGPKENLPCLHSLLELEFLCHAEKA---LLTERDIEQKALVELAIKVdPARRNLYST 321
 
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