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Conserved domains on  [gi|225433858|ref|XP_002264387|]
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protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha [Vitis vinifera]

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
7-329 0e+00

farnesyltranstransferase


:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 591.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858   7 GEERPLSQRPEWSDVTPVPQDDGPNPVVPIAYKDDFTETMDYFRAVYFADERSLRSLHVTAEAIHMNAGNYTVWHFRRLI 86
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  87 LGALNADLHEELNFIKKVANGNPKNYQIWHHRRWVAEKLGSDATSKELDFTKKILSLDAKNYHAWSHRQWVLQELGGWED 166
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 167 ELDYCKQLLEDDIFNNSAWNQRYFVITKSPFLGGLEAMRESEVNYTVGAIIAKPENESPWRYLRGLYKDDAQSWVNDPQV 246
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 247 SSVCLTVLSAKRNTVFALSTLLDLLCHGFQPSQDFINAVDALktpDLDQSDSNLATAVCSVLGHMDPMRVNYWAWRKNKL 326
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                 ...
gi 225433858 327 PAQ 329
Cdd:PLN02789 318 PKA 320
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
7-329 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 591.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858   7 GEERPLSQRPEWSDVTPVPQDDGPNPVVPIAYKDDFTETMDYFRAVYFADERSLRSLHVTAEAIHMNAGNYTVWHFRRLI 86
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  87 LGALNADLHEELNFIKKVANGNPKNYQIWHHRRWVAEKLGSDATSKELDFTKKILSLDAKNYHAWSHRQWVLQELGGWED 166
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 167 ELDYCKQLLEDDIFNNSAWNQRYFVITKSPFLGGLEAMRESEVNYTVGAIIAKPENESPWRYLRGLYKDDAQSWVNDPQV 246
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 247 SSVCLTVLSAKRNTVFALSTLLDLLCHGFQPSQDFINAVDALktpDLDQSDSNLATAVCSVLGHMDPMRVNYWAWRKNKL 326
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                 ...
gi 225433858 327 PAQ 329
Cdd:PLN02789 318 PKA 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
19-326 1.58e-43

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 152.33  E-value: 1.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  19 SDVTPVP-QDDGPNPVVPIAYKDDFTETMDYFRAVYFADERSLRSLHVTAEAIHMNAGNYTVWHFRRLILGALNADLHE- 96
Cdd:COG5536    7 RRVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDk 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  97 ------ELNFIKKVANGNPKNYQIWHHRRWVAEKLGSDATSKELDFTKKILSLDAKNYHAWSHRQWVL---QELGGWED- 166
Cdd:COG5536   87 ehlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtiEDLFNFSDl 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 167 --ELDYCKQLLEDDIFNNSAWNQRYFVITKSPFLG--GLEAMRESEVNYTVGAIIAKPENESPWRYLRGLYKD---DAQS 239
Cdd:COG5536  167 khELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEfatDIVM 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 240 W---VNDPQVSSVCLTV----LSAKRNTVFALSTL-LDLLCHGFQPSQDFInavdalktpdldqsdSNLATAVCSVLGHM 311
Cdd:COG5536  247 IgekVEDLGKYIVIINGkeldLGPKENLPCLHSLLeLEFLCHAEKALLTER---------------DIEQKALVELAIKV 311
                        330
                 ....*....|....*
gi 225433858 312 DPMRVNYWAWRKNKL 326
Cdd:COG5536  312 DPARRNLYSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
131-161 2.44e-07

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: 46.48  E-value: 2.44e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 225433858  131 SKELDFTKKILSLDAKNYHAWSHRQWVLQEL 161
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
7-329 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 591.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858   7 GEERPLSQRPEWSDVTPVPQDDGPNPVVPIAYKDDFTETMDYFRAVYFADERSLRSLHVTAEAIHMNAGNYTVWHFRRLI 86
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  87 LGALNADLHEELNFIKKVANGNPKNYQIWHHRRWVAEKLGSDATSKELDFTKKILSLDAKNYHAWSHRQWVLQELGGWED 166
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 167 ELDYCKQLLEDDIFNNSAWNQRYFVITKSPFLGGLEAMRESEVNYTVGAIIAKPENESPWRYLRGLYKDDAQSWVNDPQV 246
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 247 SSVCLTVLSAKRNTVFALSTLLDLLCHGFQPSQDFINAVDALktpDLDQSDSNLATAVCSVLGHMDPMRVNYWAWRKNKL 326
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                 ...
gi 225433858 327 PAQ 329
Cdd:PLN02789 318 PKA 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
19-326 1.58e-43

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 152.33  E-value: 1.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  19 SDVTPVP-QDDGPNPVVPIAYKDDFTETMDYFRAVYFADERSLRSLHVTAEAIHMNAGNYTVWHFRRLILGALNADLHE- 96
Cdd:COG5536    7 RRVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDk 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  97 ------ELNFIKKVANGNPKNYQIWHHRRWVAEKLGSDATSKELDFTKKILSLDAKNYHAWSHRQWVL---QELGGWED- 166
Cdd:COG5536   87 ehlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtiEDLFNFSDl 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 167 --ELDYCKQLLEDDIFNNSAWNQRYFVITKSPFLG--GLEAMRESEVNYTVGAIIAKPENESPWRYLRGLYKD---DAQS 239
Cdd:COG5536  167 khELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEfatDIVM 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858 240 W---VNDPQVSSVCLTV----LSAKRNTVFALSTL-LDLLCHGFQPSQDFInavdalktpdldqsdSNLATAVCSVLGHM 311
Cdd:COG5536  247 IgekVEDLGKYIVIINGkeldLGPKENLPCLHSLLeLEFLCHAEKALLTER---------------DIEQKALVELAIKV 311
                        330
                 ....*....|....*
gi 225433858 312 DPMRVNYWAWRKNKL 326
Cdd:COG5536  312 DPARRNLYSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
131-161 2.44e-07

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: 46.48  E-value: 2.44e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 225433858  131 SKELDFTKKILSLDAKNYHAWSHRQWVLQEL 161
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
36-188 2.80e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.78  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  36 IAYKDDFTETMDYFRAVYFADERSLRSLHVTAEAIHMNAGNYTVWHFRRLILGALNaDLHEELNFIKKVANGNPKNYQIW 115
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLG-RYEEALADYEQALELDPDDAEAL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225433858 116 HHRRWVAEKLGSDATSKELdfTKKILSLDAKNYHAWSHRQWVLQELGGWEDELDYCKQLLEDDIFNNSAWNQR 188
Cdd:COG0457   80 NNLGLALQALGRYEEALED--YDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
94-125 1.04e-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: 44.55  E-value: 1.04e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 225433858   94 LHEELNFIKKVANGNPKNYQIWHHRRWVAEKL 125
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
68-179 2.96e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 44.61  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225433858  68 EAIHMNAGNYTVWHFRRLILGALNaDLHEELNFIKKVANGNPKNYQIWHHRRWVAEKLG--SDAtskeLDFTKKILSLDA 145
Cdd:COG0457   67 QALELDPDDAEALNNLGLALQALG-RYEEALEDYDKALELDPDDAEALYNLGLALLELGryDEA----IEAYERALELDP 141
                         90       100       110
                 ....*....|....*....|....*....|....
gi 225433858 146 KNYHAWSHRQWVLQELGGWEDELDYCKQLLEDDI 179
Cdd:COG0457  142 DDADALYNLGIALEKLGRYEEALELLEKLEAAAL 175
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
164-194 1.15e-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: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 225433858  164 WEDELDYCKQLLEDDIFNNSAWNQRYFVITK 194
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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