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Conserved domains on  [gi|743841171|ref|XP_011026393|]
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PREDICTED: protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha [Populus euphratica]

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
 5-327 0e+00

farnesyltranstransferase


:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 585.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171   5 EHILRLSQDPEWADLTPIPQDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  85 LDALGIDLNEELNFMLGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171 165 ELDYCHQLLEEDVFNNSAWNQRYFVVTRSPLLGGLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDLAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                 ...
gi 743841171 325 PSA 327
Cdd:PLN02789 318 PKA 320
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 5-327 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 585.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171   5 EHILRLSQDPEWADLTPIPQDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  85 LDALGIDLNEELNFMLGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171 165 ELDYCHQLLEEDVFNNSAWNQRYFVVTRSPLLGGLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDLAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                 ...
gi 743841171 325 PSA 327
Cdd:PLN02789 318 PKA 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 24-324 4.03e-47

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 161.96  E-value: 4.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  24 QDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGIDLNE-------EL 96
Cdd:COG5536   15 QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDkehlldnEL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  97 NFMLGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN------ELDYCH 170
Cdd:COG5536   95 DFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlkhELEYTT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171 171 QLLEEDVFNNSAWNQRYFVVTRSPLLG--GLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISDPQvssvc 248
Cdd:COG5536  175 SLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVMIGE----- 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743841171 249 lKVLSAEANHVFALSTLLDLLS-HGFQANQEFRDAVDSLRPSNSDPADSDLA-KTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:COG5536  250 -KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNLYSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 129-159 3.29e-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: 46.09  E-value: 3.29e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 743841171  129 SKELEFTRRMLSLDAKNYHAWSHRQWVLQAL 159
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 5-327 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 585.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171   5 EHILRLSQDPEWADLTPIPQDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  85 LDALGIDLNEELNFMLGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171 165 ELDYCHQLLEEDVFNNSAWNQRYFVVTRSPLLGGLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDLAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                 ...
gi 743841171 325 PSA 327
Cdd:PLN02789 318 PKA 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 24-324 4.03e-47

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 161.96  E-value: 4.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  24 QDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGIDLNE-------EL 96
Cdd:COG5536   15 QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDkehlldnEL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  97 NFMLGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN------ELDYCH 170
Cdd:COG5536   95 DFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlkhELEYTT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171 171 QLLEEDVFNNSAWNQRYFVVTRSPLLG--GLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISDPQvssvc 248
Cdd:COG5536  175 SLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVMIGE----- 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743841171 249 lKVLSAEANHVFALSTLLDLLS-HGFQANQEFRDAVDSLRPSNSDPADSDLA-KTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:COG5536  250 -KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNLYSTLHERF 326
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-186 1.24e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.01  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMLGISERNPKNYQIW 113
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLG-RYEEALADYEQALELDPDDAEAL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743841171 114 HHRRWIAEKLG-TDAAskeLEFTRRMLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEEDVFNNSAWNQR 186
Cdd:COG0457   80 NNLGLALQALGrYEEA---LEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 129-159 3.29e-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: 46.09  E-value: 3.29e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 743841171  129 SKELEFTRRMLSLDAKNYHAWSHRQWVLQAL 159
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-176 6.33e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 49.62  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMLGISERNPKNYQIW 113
Cdd:COG0457   35 LELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALG-RYEEALEDYDKALELDPDDAEAL 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743841171 114 HHRRWIAEKLG-TDAAskeLEFTRRMLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEED 176
Cdd:COG0457  114 YNLGLALLELGrYDEA---IEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAA 174
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 92-123 1.23e-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: 1.23e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 743841171   92 LNEELNFMLGISERNPKNYQIWHHRRWIAEKL 123
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 59-176 2.21e-05

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: 43.64  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  59 RALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMLGISERNPKNYQIWHHRRWIAEKLG-TDAASKELEftrR 137
Cdd:COG4783   22 EAEALLEKALELDPDNPEAFALLGEILLQLG-DLDEAIVLLHEALELDPDEPEARLNLGLALLKAGdYDEALALLE---K 97

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 743841171 138 MLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEED 176
Cdd:COG4783   98 ALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 34-172 3.30e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 45.37  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMLGISERNPKNYQIW 113
Cdd:COG3914  105 LALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG-RLEEAIAALRRALELDPDNAEAL 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 743841171 114 HHRRWIAEKLGTDAASkeLEFTRRMLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQL 172
Cdd:COG3914  184 NNLGNALQDLGRLEEA--IAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELL 240
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 59-88 3.17e-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: 37.62  E-value: 3.17e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 743841171   59 RALQLTHQAILLNPGNYTVWHFRRLILDAL 88
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 34-145 6.21e-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: 39.40  E-value: 6.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMLGISERNPKNYQIW 113
Cdd:COG4783   31 LELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAG-DYDEALALLEKALKLDPEHPEAY 109

                         90       100       110
                 ....*....|....*....|....*....|...
gi 743841171 114 HHRRWIAEKLG-TDAASKELEftrRMLSLDAKN 145
Cdd:COG4783  110 LRLARAYRALGrPDEAIAALE---KALELDPDD 139
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 162-192 8.89e-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: 36.08  E-value: 8.89e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 743841171  162 WENELDYCHQLLEEDVFNNSAWNQRYFVVTR 192
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 60-174 3.79e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 38.82  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  60 ALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMLGISERNPKNYQIWHHRRWIAEKLG-TDAAskeLEFTRRM 138
Cdd:COG3914   97 ALALYRRALALNPDNAEALFNLGNLLLALG-RLEEALAALRRALALNPDFAEAYLNLGEALRRLGrLEEA---IAALRRA 172

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 743841171 139 LSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLE 174
Cdd:COG3914  173 LELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALE 208
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-187 9.46e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 36.91  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743841171  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMLGISERNPKNYQIW 113
Cdd:COG0457   69 LELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELG-RYDEAIEAYERALELDPDDADAL 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743841171 114 HHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEEDVFNNSAWNQRY 187
Cdd:COG0457  148 YNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAE 221
 
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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