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Conserved domains on  [gi|1985662627|emb|CAE6076765|]
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unnamed protein product [Arabidopsis arenosa]

Protein Classification

protein prenyltransferase subunit alpha family protein( domain architecture ID 11477143)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
4-324 0e+00

farnesyltranstransferase


:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 571.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627   4 DETVPLSQRSEWADVVPLTQDDGPNPVVPIAYKEEFRETMDYFRAIYFSDERSPRSLRLTEETLRLNSGNYTVWHFRRLV 83
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  84 LEALNHDLFEELEFIERIAEDNSKNYQLWHHRRWVAEKLGPDVVGRELEFTRRVLSLDAKHYHAWSHRQWTLRALGGWED 163
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 164 ELDYCHELLEADVFNNSAWNQRYYVITRSPLLGGLEAMRESEVSYTIKAILANPANESSWRYLKALYKDDKESWISDPSV 243
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 244 SSVCLNVLSRTDCFHgFALSTLLDLLCDGLKPTNEHKDSVRALANEEPDTSLANLVCTILGRVDPIRANYWAWRKSKITV 323
Cdd:PLN02789  241 SSVCLEVLSKDSNHV-FALSDLLDLLCEGLQPTAEFRDTVDTLAEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKLPK 319

                  .
gi 1985662627 324 A 324
Cdd:PLN02789  320 A 320
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
4-324 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 571.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627   4 DETVPLSQRSEWADVVPLTQDDGPNPVVPIAYKEEFRETMDYFRAIYFSDERSPRSLRLTEETLRLNSGNYTVWHFRRLV 83
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  84 LEALNHDLFEELEFIERIAEDNSKNYQLWHHRRWVAEKLGPDVVGRELEFTRRVLSLDAKHYHAWSHRQWTLRALGGWED 163
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 164 ELDYCHELLEADVFNNSAWNQRYYVITRSPLLGGLEAMRESEVSYTIKAILANPANESSWRYLKALYKDDKESWISDPSV 243
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 244 SSVCLNVLSRTDCFHgFALSTLLDLLCDGLKPTNEHKDSVRALANEEPDTSLANLVCTILGRVDPIRANYWAWRKSKITV 323
Cdd:PLN02789  241 SSVCLEVLSKDSNHV-FALSDLLDLLCEGLQPTAEFRDTVDTLAEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKLPK 319

                  .
gi 1985662627 324 A 324
Cdd:PLN02789  320 A 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
21-321 3.36e-42

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 148.86  E-value: 3.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  21 LTQDDGPNPVVPIAYKEEFRETMDYFRAIYFSDERSPRSLRLTEETLRLNSGNYTVWHFRR-------LVLEALNHDLFE 93
Cdd:COG5536    13 PIQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFsilkhvqMVSEDKEHLLDN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  94 ELEFIERIAEDNSKNYQLWHHRRWVAEKLGPDVVGRELEFTRRVLSLDAKHYHAWSHRQW---TLRALGGWED---ELDY 167
Cdd:COG5536    93 ELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWvlrTIEDLFNFSDlkhELEY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 168 CHELLEADVFNNSAWNQRYYVITRSPLLG--GLEAMRESEVSYTIKAILANPANESSWRYLKALYKDDKESWISDPS--- 242
Cdd:COG5536   173 TTSLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVMIGEkve 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 243 ---VSSVCLNV----LSRTDCFHGFALSTLLDLLCDGLKPTNEHKDSVRALANEEpdtslanlvctiLGRVDPIRANYWA 315
Cdd:COG5536   253 dlgKYIVIINGkeldLGPKENLPCLHSLLELEFLCHAEKALLTERDIEQKALVEL------------AIKVDPARRNLYS 320

                  ....*.
gi 1985662627 316 WRKSKI 321
Cdd:COG5536   321 TLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
93-122 4.69e-06

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: 42.62  E-value: 4.69e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1985662627  93 EELEFIERIAEDNSKNYQLWHHRRWVAEKL 122
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
4-324 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 571.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627   4 DETVPLSQRSEWADVVPLTQDDGPNPVVPIAYKEEFRETMDYFRAIYFSDERSPRSLRLTEETLRLNSGNYTVWHFRRLV 83
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  84 LEALNHDLFEELEFIERIAEDNSKNYQLWHHRRWVAEKLGPDVVGRELEFTRRVLSLDAKHYHAWSHRQWTLRALGGWED 163
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 164 ELDYCHELLEADVFNNSAWNQRYYVITRSPLLGGLEAMRESEVSYTIKAILANPANESSWRYLKALYKDDKESWISDPSV 243
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 244 SSVCLNVLSRTDCFHgFALSTLLDLLCDGLKPTNEHKDSVRALANEEPDTSLANLVCTILGRVDPIRANYWAWRKSKITV 323
Cdd:PLN02789  241 SSVCLEVLSKDSNHV-FALSDLLDLLCEGLQPTAEFRDTVDTLAEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKLPK 319

                  .
gi 1985662627 324 A 324
Cdd:PLN02789  320 A 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
21-321 3.36e-42

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 148.86  E-value: 3.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  21 LTQDDGPNPVVPIAYKEEFRETMDYFRAIYFSDERSPRSLRLTEETLRLNSGNYTVWHFRR-------LVLEALNHDLFE 93
Cdd:COG5536    13 PIQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFsilkhvqMVSEDKEHLLDN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  94 ELEFIERIAEDNSKNYQLWHHRRWVAEKLGPDVVGRELEFTRRVLSLDAKHYHAWSHRQW---TLRALGGWED---ELDY 167
Cdd:COG5536    93 ELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWvlrTIEDLFNFSDlkhELEY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 168 CHELLEADVFNNSAWNQRYYVITRSPLLG--GLEAMRESEVSYTIKAILANPANESSWRYLKALYKDDKESWISDPS--- 242
Cdd:COG5536   173 TTSLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVMIGEkve 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627 243 ---VSSVCLNV----LSRTDCFHGFALSTLLDLLCDGLKPTNEHKDSVRALANEEpdtslanlvctiLGRVDPIRANYWA 315
Cdd:COG5536   253 dlgKYIVIINGkeldLGPKENLPCLHSLLELEFLCHAEKALLTERDIEQKALVEL------------AIKVDPARRNLYS 320

                  ....*.
gi 1985662627 316 WRKSKI 321
Cdd:COG5536   321 TLHERF 326
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
49-185 1.63e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.46  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  49 IYFSDERSPRSLRLTEETLRLNSGNYTVWHFRRLVLEALNHdlFEE-LEFIERIAEDNSKNYQLWHHRRWVAEKLG-PDv 126
Cdd:COG0457    17 AYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGR--YEEaLADYEQALELDPDDAEALNNLGLALQALGrYE- 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1985662627 127 vgRELEFTRRVLSLDAKHYHAWSHRQWTLRALGGWEDELDYCHELLEADVFNNSAWNQR 185
Cdd:COG0457    94 --EALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
93-122 4.69e-06

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: 42.62  E-value: 4.69e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1985662627  93 EELEFIERIAEDNSKNYQLWHHRRWVAEKL 122
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
129-158 1.13e-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: 41.47  E-value: 1.13e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1985662627 129 RELEFTRRVLSLDAKHYHAWSHRQWTLRAL 158
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
49-175 2.86e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 44.61  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985662627  49 IYFSDERSPRSLRLTEETLRLNSGNYTVWHFRRLVLEALNHdlFEE-LEFIERIAEDNSKNYQLWHHRRWVAEKLGPdvV 127
Cdd:COG0457    51 AYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGR--YEEaLEDYDKALELDPDDAEALYNLGLALLELGR--Y 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1985662627 128 GRELEFTRRVLSLDAKHYHAWSHRQWTLRALGGWEDELDYCHELLEAD 175
Cdd:COG0457   127 DEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAA 174
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
161-191 1.95e-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: 35.31  E-value: 1.95e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1985662627 161 WEDELDYCHELLEADVFNNSAWNQRYYVITR 191
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
 
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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