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Conserved domains on  [gi|1496472626|ref|NP_001353864|]
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protein prenyltransferase alpha subunit repeat-containing protein 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 98-129 1.93e-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: 41.08  E-value: 1.93e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1496472626  98 IQEEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 129
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 super family cl44255
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 42-242 7.39e-04

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: 41.01  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626  42 KDLHLGKLALTKF--PKSPET---WIHRRWVLQQLiqetslpsfvtkgnlgTIPTERAQRLIQEEMEVCGEAAGRYPSNY 116
Cdd:COG5536    45 KEYSVRALKLTQEliDKNPEFytiWNYRFSILKHV----------------QMVSEDKEHLLDNELDFLDEALKDNPKNY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626 117 NAWSHRIWVLQHLAKldvKILLDELSSTKHWASMHVSDHSGFHYRQFLlkslisqtvidssvmeqnplrsepalvppkde 196
Cdd:COG5536   109 QIWHHRQWMLELFPK---PSWGRELFITKKLLDSDSRNYHVWSYRRWV-------------------------------- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1496472626 197 eaaVSTEEPRINLpHLLEEEVEFSTDLIDSYPGHETLWCHRRHIFY 242
Cdd:COG5536   154 ---LRTIEDLFNF-SDLKHELEYTTSLIETDIYNNSAWHHRYIWIE 195
 
Name Accession Description Interval E-value
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 98-129 1.93e-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: 41.08  E-value: 1.93e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1496472626  98 IQEEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 129
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 42-242 7.39e-04

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 41.01  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626  42 KDLHLGKLALTKF--PKSPET---WIHRRWVLQQLiqetslpsfvtkgnlgTIPTERAQRLIQEEMEVCGEAAGRYPSNY 116
Cdd:COG5536    45 KEYSVRALKLTQEliDKNPEFytiWNYRFSILKHV----------------QMVSEDKEHLLDNELDFLDEALKDNPKNY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626 117 NAWSHRIWVLQHLAKldvKILLDELSSTKHWASMHVSDHSGFHYRQFLlkslisqtvidssvmeqnplrsepalvppkde 196
Cdd:COG5536   109 QIWHHRQWMLELFPK---PSWGRELFITKKLLDSDSRNYHVWSYRRWV-------------------------------- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1496472626 197 eaaVSTEEPRINLpHLLEEEVEFSTDLIDSYPGHETLWCHRRHIFY 242
Cdd:COG5536   154 ---LRTIEDLFNF-SDLKHELEYTTSLIETDIYNNSAWHHRYIWIE 195
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 213-241 1.05e-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: 36.08  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 1496472626 213 LEEEVEFSTDLIDSYPGHETLWCHRRHIF 241
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLL 29
PLN02789 PLN02789
farnesyltranstransferase
 44-168 4.18e-03

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 38.57  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626  44 LHLGKLALTKFPKSPETWIHRRWVLQQLiqetslpsfvtkgnlgtipteraQRLIQEEMEVCGEAAGRYPSNYNAWSHRI 123
Cdd:PLN02789   57 LDLTADVIRLNPGNYTVWHFRRLCLEAL-----------------------DADLEEELDFAEDVAEDNPKNYQIWHHRR 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1496472626 124 WVLQhlaKLDVKILLDELSSTKHWASMHVSDHSGFHYRQFLLKSL 168
Cdd:PLN02789  114 WLAE---KLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTL 155
 
Name Accession Description Interval E-value
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 98-129 1.93e-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: 41.08  E-value: 1.93e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1496472626  98 IQEEMEVCGEAAGRYPSNYNAWSHRIWVLQHL 129
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 42-242 7.39e-04

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 41.01  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626  42 KDLHLGKLALTKF--PKSPET---WIHRRWVLQQLiqetslpsfvtkgnlgTIPTERAQRLIQEEMEVCGEAAGRYPSNY 116
Cdd:COG5536    45 KEYSVRALKLTQEliDKNPEFytiWNYRFSILKHV----------------QMVSEDKEHLLDNELDFLDEALKDNPKNY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626 117 NAWSHRIWVLQHLAKldvKILLDELSSTKHWASMHVSDHSGFHYRQFLlkslisqtvidssvmeqnplrsepalvppkde 196
Cdd:COG5536   109 QIWHHRQWMLELFPK---PSWGRELFITKKLLDSDSRNYHVWSYRRWV-------------------------------- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1496472626 197 eaaVSTEEPRINLpHLLEEEVEFSTDLIDSYPGHETLWCHRRHIFY 242
Cdd:COG5536   154 ---LRTIEDLFNF-SDLKHELEYTTSLIETDIYNNSAWHHRYIWIE 195
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 213-241 1.05e-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: 36.08  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 1496472626 213 LEEEVEFSTDLIDSYPGHETLWCHRRHIF 241
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLL 29
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 137-168 1.12e-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: 36.08  E-value: 1.12e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1496472626 137 LLDELSSTKHWASMHVSDHSGFHYRQFLLKSL 168
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PLN02789 PLN02789
farnesyltranstransferase
 44-168 4.18e-03

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 38.57  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626  44 LHLGKLALTKFPKSPETWIHRRWVLQQLiqetslpsfvtkgnlgtipteraQRLIQEEMEVCGEAAGRYPSNYNAWSHRI 123
Cdd:PLN02789   57 LDLTADVIRLNPGNYTVWHFRRLCLEAL-----------------------DADLEEELDFAEDVAEDNPKNYQIWHHRR 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1496472626 124 WVLQhlaKLDVKILLDELSSTKHWASMHVSDHSGFHYRQFLLKSL 168
Cdd:PLN02789  114 WLAE---KLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTL 155
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 50-251 6.87e-03

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 37.93  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626  50 ALTKFPKSPETWIHRRWVLQqLIQETSLPS--FVTKGNL-----------------GTIPTERAQRLIQEEMEVCGEAAG 110
Cdd:COG5536   100 ALKDNPKNYQIWHHRQWMLE-LFPKPSWGRelFITKKLLdsdsrnyhvwsyrrwvlRTIEDLFNFSDLKHELEYTTSLIE 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626 111 RYPSNYNAWSHR-IWVLQHLAKLDV---KILLDELSSTKHWASMHVSDHSGFHY-RQFLLKSLISQTVIDSSV------- 178
Cdd:COG5536   179 TDIYNNSAWHHRyIWIERRFNRGDVisqKYLEKELEYIFDKIFTDPDNQSVWGYlRGVSSEFATDIVMIGEKVedlgkyi 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496472626 179 -------MEQNPLRSEPALVPPKDEEAAVSTEEPrinLPHLLEEEVEFSTDLIDSY-PGHETLWchrrhifylqHHLNGR 250
Cdd:COG5536   259 viingkeLDLGPKENLPCLHSLLELEFLCHAEKA---LLTERDIEQKALVELAIKVdPARRNLY----------STLHER 325


                  .
gi 1496472626 251 F 251
Cdd:COG5536   326 F 326
 
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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