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Conserved domains on  [gi|2015345506|gb|KAG5242110|]
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protein farnesyltransferase/geranylgeranyltransferase type [Salix suchowensis]

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
5-325 0e+00

farnesyltranstransferase


:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 580.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506   5 EHKLPLSQNPEWADVTPIPQDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTLQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506  85 LDALGIDLNEELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKEMLFLDAKNYHAWSYRQWVLQTLGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 165 ELNYCHQLLEEDVFNNSAWNQRYFVVTGSPLLGGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 245 SSVCLKVLSAKANHVFALSTLLDLLSHGFQANQEFKDSVDSLrpsNSDPPDSDLAKAICSILRHVDPMRVNYWTWRKNRL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                  .
gi 2015345506 325 P 325
Cdd:PLN02789  318 P 318
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
5-325 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 580.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506   5 EHKLPLSQNPEWADVTPIPQDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTLQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506  85 LDALGIDLNEELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKEMLFLDAKNYHAWSYRQWVLQTLGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 165 ELNYCHQLLEEDVFNNSAWNQRYFVVTGSPLLGGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 245 SSVCLKVLSAKANHVFALSTLLDLLSHGFQANQEFKDSVDSLrpsNSDPPDSDLAKAICSILRHVDPMRVNYWTWRKNRL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                  .
gi 2015345506 325 P 325
Cdd:PLN02789  318 P 318
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
18-324 3.39e-48

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 164.66  E-value: 3.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506  18 DVTPIP-QDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTLQAILLNPGNYTVWHFRRLILDALGIDLNE-- 94
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506  95 -----ELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKEMLFLDAKNYHAWSYRQWVLQTLGGWEN----- 164
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 165 -ELNYCHQLLEEDVFNNSAWNQRYFVV-----TGSPllgGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSW 238
Cdd:COG5536   168 hELEYTTSLIETDIYNNSAWHHRYIWIerrfnRGDV---ISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 239 ISDPQvssvclKVLSAKANHVFALSTLLDLLS-HGFQANQEFKDSVDSLRPSNSDPPDSDLA-KAICSILRHVDPMRVNY 316
Cdd:COG5536   245 VMIGE------KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNL 318

                  ....*...
gi 2015345506 317 WTWRKNRL 324
Cdd:COG5536   319 YSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
129-159 6.32e-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: 45.32  E-value: 6.32e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2015345506 129 SKELDFTKEMLFLDAKNYHAWSYRQWVLQTL 159
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
5-325 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 580.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506   5 EHKLPLSQNPEWADVTPIPQDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTLQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506  85 LDALGIDLNEELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKEMLFLDAKNYHAWSYRQWVLQTLGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 165 ELNYCHQLLEEDVFNNSAWNQRYFVVTGSPLLGGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 245 SSVCLKVLSAKANHVFALSTLLDLLSHGFQANQEFKDSVDSLrpsNSDPPDSDLAKAICSILRHVDPMRVNYWTWRKNRL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                  .
gi 2015345506 325 P 325
Cdd:PLN02789  318 P 318
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
18-324 3.39e-48

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 164.66  E-value: 3.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506  18 DVTPIP-QDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTLQAILLNPGNYTVWHFRRLILDALGIDLNE-- 94
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506  95 -----ELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKEMLFLDAKNYHAWSYRQWVLQTLGGWEN----- 164
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 165 -ELNYCHQLLEEDVFNNSAWNQRYFVV-----TGSPllgGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSW 238
Cdd:COG5536   168 hELEYTTSLIETDIYNNSAWHHRYIWIerrfnRGDV---ISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506 239 ISDPQvssvclKVLSAKANHVFALSTLLDLLS-HGFQANQEFKDSVDSLRPSNSDPPDSDLA-KAICSILRHVDPMRVNY 316
Cdd:COG5536   245 VMIGE------KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNL 318

                  ....*...
gi 2015345506 317 WTWRKNRL 324
Cdd:COG5536   319 YSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
129-159 6.32e-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: 45.32  E-value: 6.32e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2015345506 129 SKELDFTKEMLFLDAKNYHAWSYRQWVLQTL 159
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
92-123 1.48e-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: 44.17  E-value: 1.48e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2015345506  92 LNEELEFMSGISENNPKNYQIWHHRRWIAEKL 123
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-186 9.27e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.15  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015345506  34 IAYKPEFIETMDYFRAVYKANEFSPRALQLTLQAILLNPGNYTVWHFRRLILDALGiDLNEELEFMSGISENNPKNYQIW 113
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLG-RYEEALADYEQALELDPDDAEAL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015345506 114 HHRRWIAEKLG-TDVASKELDftkEMLFLDAKNYHAWSYRQWVLQTLGGWENELNYCHQLLEEDVFNNSAWNQR 186
Cdd:COG0457    80 NNLGLALQALGrYEEALEDYD---KALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
59-88 4.02e-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: 4.02e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2015345506  59 RALQLTLQAILLNPGNYTVWHFRRLILDAL 88
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 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.
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