NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1764611504|gb|KAB5548422|]
View 

hypothetical protein DKX38_011828 [Salix brachista]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 571.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504   5 EHKLPLSQNPEWADVTPIPQDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  85 LDALGIDLNEELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKRMLFLDAKNYHAWSYRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 165 ELSYCHQLLEEDVFNNSAWNQRYFVVTGSPLLGGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 245 SSVCLKVLSAKANHVFALSTLLDLLSHGFQANQEFKDAVDSLrpsSSDPPDSDLAKAICSILRHVDPMRVNYWTWRENKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                  .
gi 1764611504 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: 571.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504   5 EHKLPLSQNPEWADVTPIPQDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  85 LDALGIDLNEELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKRMLFLDAKNYHAWSYRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 165 ELSYCHQLLEEDVFNNSAWNQRYFVVTGSPLLGGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 245 SSVCLKVLSAKANHVFALSTLLDLLSHGFQANQEFKDAVDSLrpsSSDPPDSDLAKAICSILRHVDPMRVNYWTWRENKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                  .
gi 1764611504 325 P 325
Cdd:PLN02789  318 P 318
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
18-324 1.81e-46

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 160.04  E-value: 1.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  18 DVTPIP-QDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGIDLNE-- 94
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  95 -----ELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKRMLFLDAKNYHAWSYRQWVLQALGGWEN----- 164
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 165 -ELSYCHQLLEEDVFNNSAWNQRYFVV-----TGSPllgGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSW 238
Cdd:COG5536   168 hELEYTTSLIETDIYNNSAWHHRYIWIerrfnRGDV---ISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 239 ISDPQvssvclKVLSAKANHVFALSTLLDLLS-HGFQANQEFKDAVDSLRPSSSDPPDSDLA-KAICSILRHVDPMRVNY 316
Cdd:COG5536   245 VMIGE------KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNL 318

                  ....*...
gi 1764611504 317 WTWRENKL 324
Cdd:COG5536   319 YSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
129-159 6.97e-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: 44.94  E-value: 6.97e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1764611504 129 SKELDFTKRMLFLDAKNYHAWSYRQWVLQAL 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: 571.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504   5 EHKLPLSQNPEWADVTPIPQDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  85 LDALGIDLNEELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKRMLFLDAKNYHAWSYRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 165 ELSYCHQLLEEDVFNNSAWNQRYFVVTGSPLLGGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 245 SSVCLKVLSAKANHVFALSTLLDLLSHGFQANQEFKDAVDSLrpsSSDPPDSDLAKAICSILRHVDPMRVNYWTWRENKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317

                  .
gi 1764611504 325 P 325
Cdd:PLN02789  318 P 318
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
18-324 1.81e-46

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 160.04  E-value: 1.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  18 DVTPIP-QDDGPNPVVPIAYKPEFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGIDLNE-- 94
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  95 -----ELEFMSGISENNPKNYQIWHHRRWIAEKLGTDVASKELDFTKRMLFLDAKNYHAWSYRQWVLQALGGWEN----- 164
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 165 -ELSYCHQLLEEDVFNNSAWNQRYFVV-----TGSPllgGLEAMRESEVKYTVEAILRSPENESPWRYLRGLYKNDPKSW 238
Cdd:COG5536   168 hELEYTTSLIETDIYNNSAWHHRYIWIerrfnRGDV---ISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504 239 ISDPQvssvclKVLSAKANHVFALSTLLDLLS-HGFQANQEFKDAVDSLRPSSSDPPDSDLA-KAICSILRHVDPMRVNY 316
Cdd:COG5536   245 VMIGE------KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNL 318

                  ....*...
gi 1764611504 317 WTWRENKL 324
Cdd:COG5536   319 YSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
129-159 6.97e-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: 44.94  E-value: 6.97e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1764611504 129 SKELDFTKRMLFLDAKNYHAWSYRQWVLQAL 159
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
92-123 2.30e-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: 43.40  E-value: 2.30e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1764611504  92 LNEELEFMSGISENNPKNYQIWHHRRWIAEKL 123
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-186 2.59e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.08  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  34 IAYKPEFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELEFMSGISENNPKNYQIW 113
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLG-RYEEALADYEQALELDPDDAEAL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1764611504 114 HHRRWIAEKLG-TDVASKELDftkRMLFLDAKNYHAWSYRQWVLQALGGWENELSYCHQLLEEDVFNNSAWNQR 186
Cdd:COG0457    80 NNLGLALQALGrYEEALEDYD---KALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
58-176 1.51e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.77  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  58 PRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELEFMSGISENNPKNYQIWHHRRWIAEKLG-TDVAskeLDFTK 136
Cdd:COG0457    59 EEALADYEQALELDPDDAEALNNLGLALQALG-RYEEALEDYDKALELDPDDAEALYNLGLALLELGrYDEA---IEAYE 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1764611504 137 RMLFLDAKNYHAWSYRQWVLQALGGWENELSYCHQLLEED 176
Cdd:COG0457   135 RALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAA 174
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
59-88 3.87e-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: 3.87e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1764611504  59 RALQLTHQAILLNPGNYTVWHFRRLILDAL 88
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
59-176 1.90e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 37.86  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  59 RALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELEFMSGISENNPKNYQIWHHRRWIAEKLG-TDVASKELdftKR 137
Cdd:COG4783    22 EAEALLEKALELDPDNPEAFALLGEILLQLG-DLDEAIVLLHEALELDPDEPEARLNLGLALLKAGdYDEALALL---EK 97
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1764611504 138 MLFLDAKNYHAWSYRQWVLQALGGWENELSYCHQLLEED 176
Cdd:COG4783    98 ALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
34-145 8.43e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 36.32  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764611504  34 IAYKPEFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELEFMSGISENNPKNYQIW 113
Cdd:COG4783    31 LELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAG-DYDEALALLEKALKLDPEHPEAY 109
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1764611504 114 HHRRWIAEKLG-TDVASKELdftKRMLFLDAKN 145
Cdd:COG4783   110 LRLARAYRALGrPDEAIAAL---EKALELDPDD 139
 
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