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Conserved domains on  [gi|1216253007|ref|XP_021610338|]
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protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha [Manihot esculenta]

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
 10-331 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 1216253007  10 EEMLPLSQRPEWSDVVPIPQDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLV 89
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  90 LEALNADLDEELDYVARIAKKNTKNYQIWHHRRWVAEKLGTNAMAKELQFTRKILSLDAKNYHAWSHRQWVLQALGGWED 169
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 170 ELDYCGQLLQDDVFNNSAWNQRYFVITRSPLLGGLKSMRESEVKYTVEAILANPENESPWRYLRGLYKGDSQSWINDLQV 249
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 250 SSVCLKVLNSKTNYIFALSVLLDLLCDGFQANQEFIDAVTALrtsNADPLDTDLAKAVCSVLEHVDPIRVNYWTYRKSNL 329
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1216253007 330 PV 331
Cdd:PLN02789  318 PK 319
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 10-331 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 1216253007  10 EEMLPLSQRPEWSDVVPIPQDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLV 89
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  90 LEALNADLDEELDYVARIAKKNTKNYQIWHHRRWVAEKLGTNAMAKELQFTRKILSLDAKNYHAWSHRQWVLQALGGWED 169
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 170 ELDYCGQLLQDDVFNNSAWNQRYFVITRSPLLGGLKSMRESEVKYTVEAILANPENESPWRYLRGLYKGDSQSWINDLQV 249
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 250 SSVCLKVLNSKTNYIFALSVLLDLLCDGFQANQEFIDAVTALrtsNADPLDTDLAKAVCSVLEHVDPIRVNYWTYRKSNL 329
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1216253007 330 PV 331
Cdd:PLN02789  318 PK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 22-329 5.03e-47

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 161.58  E-value: 5.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  22 SDVVPIP-QDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRR-------LVLEAL 93
Cdd:COG5536     7 RRVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFsilkhvqMVSEDK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  94 NADLDEELDYVARIAKKNTKNYQIWHHRRWVAEKLGTNAMAKELQFTRKILSLDAKNYHAWSHRQWVL---QALGGWED- 169
Cdd:COG5536    87 EHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtiEDLFNFSDl 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 170 --ELDYCGQLLQDDVFNNSAWNQRYFVITRSPLLG--GLKSMRESEVKYTVEAILANPENESPWRYLRGLYK---GDSQS 242
Cdd:COG5536   167 khELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSefaTDIVM 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 243 W---INDLQVSSVCLKV----LNSKTNYIFALSVL-LDLLCDGFQANQEFIDAVTalrtsnadpldtdlaKAVCSVLEHV 314
Cdd:COG5536   247 IgekVEDLGKYIVIINGkeldLGPKENLPCLHSLLeLEFLCHAEKALLTERDIEQ---------------KALVELAIKV 311

                         330
                  ....*....|....*
gi 1216253007 315 DPIRVNYWTYRKSNL 329
Cdd:COG5536   312 DPARRNLYSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 135-164 4.83e-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: 4.83e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1216253007 135 KELQFTRKILSLDAKNYHAWSHRQWVLQAL 164
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 10-331 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 1216253007  10 EEMLPLSQRPEWSDVVPIPQDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLV 89
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  90 LEALNADLDEELDYVARIAKKNTKNYQIWHHRRWVAEKLGTNAMAKELQFTRKILSLDAKNYHAWSHRQWVLQALGGWED 169
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 170 ELDYCGQLLQDDVFNNSAWNQRYFVITRSPLLGGLKSMRESEVKYTVEAILANPENESPWRYLRGLYKGDSQSWINDLQV 249
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 250 SSVCLKVLNSKTNYIFALSVLLDLLCDGFQANQEFIDAVTALrtsNADPLDTDLAKAVCSVLEHVDPIRVNYWTYRKSNL 329
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1216253007 330 PV 331
Cdd:PLN02789  318 PK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 22-329 5.03e-47

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 161.58  E-value: 5.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  22 SDVVPIP-QDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRR-------LVLEAL 93
Cdd:COG5536     7 RRVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFsilkhvqMVSEDK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  94 NADLDEELDYVARIAKKNTKNYQIWHHRRWVAEKLGTNAMAKELQFTRKILSLDAKNYHAWSHRQWVL---QALGGWED- 169
Cdd:COG5536    87 EHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtiEDLFNFSDl 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 170 --ELDYCGQLLQDDVFNNSAWNQRYFVITRSPLLG--GLKSMRESEVKYTVEAILANPENESPWRYLRGLYK---GDSQS 242
Cdd:COG5536   167 khELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSefaTDIVM 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007 243 W---INDLQVSSVCLKV----LNSKTNYIFALSVL-LDLLCDGFQANQEFIDAVTalrtsnadpldtdlaKAVCSVLEHV 314
Cdd:COG5536   247 IgekVEDLGKYIVIINGkeldLGPKENLPCLHSLLeLEFLCHAEKALLTERDIEQ---------------KALVELAIKV 311

                         330
                  ....*....|....*
gi 1216253007 315 DPIRVNYWTYRKSNL 329
Cdd:COG5536   312 DPARRNLYSTLHERF 326
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
39-191 3.86e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 56.55  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  39 IAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNaDLDEELDYVARIAKKNTKNYQIW 118
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLG-RYEEALADYEQALELDPDDAEAL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1216253007 119 HHRRWVAEKLGTNAMAKELQftRKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCGQLLQDDVFNNSAWNQR 191
Cdd:COG0457    80 NNLGLALQALGRYEEALEDY--DKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
39-181 1.04e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 52.32  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  39 IAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNaDLDEELDYVARIAKKNTKNYQIW 118
Cdd:COG0457    35 LELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALG-RYEEALEDYDKALELDPDDAEAL 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1216253007 119 HHRRWVAEKLGTNAMAkeLQFTRKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCGQLLQDD 181
Cdd:COG0457   114 YNLGLALLELGRYDEA--IEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAA 174
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 135-164 4.83e-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: 4.83e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1216253007 135 KELQFTRKILSLDAKNYHAWSHRQWVLQAL 164
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 97-128 9.04e-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: 44.55  E-value: 9.04e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1216253007  97 LDEELDYVARIAKKNTKNYQIWHHRRWVAEKL 128
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 39-179 4.58e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.07  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  39 IAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNaDLDEELDYVARIAKKNTKNYQIW 118
Cdd:COG3914   105 LALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG-RLEEAIAALRRALELDPDNAEAL 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1216253007 119 HHRRWVAEKLGTNAMAkeLQFTRKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCGQLLQ 179
Cdd:COG3914   184 NNLGNALQDLGRLEEA--IAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELLAA 242
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 54-181 2.68e-04

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: 40.56  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  54 AIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNaDLDEELDYVARIAKKNTKNYQIWHHRRWVAEKLGtnAM 133
Cdd:COG4783    12 QALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLG-DLDEAIVLLHEALELDPDEPEARLNLGLALLKAG--DY 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1216253007 134 AKELQFTRKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCGQLLQDD 181
Cdd:COG4783    89 DEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 64-93 6.11e-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: 36.85  E-value: 6.11e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1216253007  64 RALQLTHLVILLNPGNYTVWHFRRLVLEAL 93
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 39-150 2.44e-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: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216253007  39 IAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNaDLDEELDYVARIAKKNTKNYQIW 118
Cdd:COG4783    31 LELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAG-DYDEALALLEKALKLDPEHPEAY 109

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1216253007 119 HHRRWVAEKLGTNAMAKELQftRKILSLDAKN 150
Cdd:COG4783   110 LRLARAYRALGRPDEAIAAL--EKALELDPDD 139
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 167-197 5.48e-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: 34.15  E-value: 5.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1216253007 167 WEDELDYCGQLLQDDVFNNSAWNQRYFVITR 197
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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