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Conserved domains on  [gi|1334313529|gb|PNT28576|]
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hypothetical protein POPTR_007G127500v4 [Populus trichocarpa]

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
 5-326 0e+00

farnesyltranstransferase


:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 591.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529   5 EHKLRLSQDPEWADVTPIPQDDGPNPVVPIDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  85 LDALGIDLNEELNFMSGISESNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 165 ELDYCHQLLEKDVFNNSAWNQRYFVVTRSPFLGGLEATRESEVKYTIETILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDIAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1334313529 325 PS 326
Cdd:PLN02789  318 PK 319
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 5-326 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 591.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529   5 EHKLRLSQDPEWADVTPIPQDDGPNPVVPIDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  85 LDALGIDLNEELNFMSGISESNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 165 ELDYCHQLLEKDVFNNSAWNQRYFVVTRSPFLGGLEATRESEVKYTIETILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDIAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1334313529 325 PS 326
Cdd:PLN02789  318 PK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 18-324 7.84e-49

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 166.20  E-value: 7.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  18 DVTPIP-QDDGPNPVVPIDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGIDLNE-- 94
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  95 -----ELNFMSGISESNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN----- 164
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlk 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 165 -ELDYCHQLLEKDVFNNSAWNQRYFVVTRSpFLGGLEATR---ESEVKYTIETILGNPGNESPWRYLRGLYKNDPKSWIS 240
Cdd:COG5536   168 hELEYTTSLIETDIYNNSAWHHRYIWIERR-FNRGDVISQkylEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVM 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 241 DPQvssvclKVLSAEANHVFALSTLLDLLS-HGFQANQEFRDAVDSLRPSNSDPADSDIA-KTICSILRHVDPMRVNYWT 318
Cdd:COG5536   247 IGE------KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNLYS 320


                  ....*.
gi 1334313529 319 WRKSKL 324
Cdd:COG5536   321 TLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 129-159 2.36e-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: 2.36e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1334313529 129 SKELEFTRRMLSLDAKNYHAWSHRQWVLQAL 159
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 5-326 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 591.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529   5 EHKLRLSQDPEWADVTPIPQDDGPNPVVPIDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  85 LDALGIDLNEELNFMSGISESNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 165 ELDYCHQLLEKDVFNNSAWNQRYFVVTRSPFLGGLEATRESEVKYTIETILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDIAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1334313529 325 PS 326
Cdd:PLN02789  318 PK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 18-324 7.84e-49

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 166.20  E-value: 7.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  18 DVTPIP-QDDGPNPVVPIDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGIDLNE-- 94
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  95 -----ELNFMSGISESNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWEN----- 164
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlk 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 165 -ELDYCHQLLEKDVFNNSAWNQRYFVVTRSpFLGGLEATR---ESEVKYTIETILGNPGNESPWRYLRGLYKNDPKSWIS 240
Cdd:COG5536   168 hELEYTTSLIETDIYNNSAWHHRYIWIERR-FNRGDVISQkylEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVM 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529 241 DPQvssvclKVLSAEANHVFALSTLLDLLS-HGFQANQEFRDAVDSLRPSNSDPADSDIA-KTICSILRHVDPMRVNYWT 318
Cdd:COG5536   247 IGE------KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNLYS 320


                  ....*.
gi 1334313529 319 WRKSKL 324
Cdd:COG5536   321 TLHERF 326
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-186 1.14e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.09  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  34 IDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISESNPKNYQIW 113
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLG-RYEEALADYEQALELDPDDAEAL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334313529 114 HHRRWIAEKLG-TDAAskeLEFTRRMLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEKDVFNNSAWNQR 186
Cdd:COG0457    80 NNLGLALQALGrYEEA---LEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-176 9.59e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 52.32  E-value: 9.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  34 IDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISESNPKNYQIW 113
Cdd:COG0457    35 LELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALG-RYEEALEDYDKALELDPDDAEAL 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334313529 114 HHRRWIAEKLG-TDAAskeLEFTRRMLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEKD 176
Cdd:COG0457   114 YNLGLALLELGrYDEA---IEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAA 174
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 129-159 2.36e-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: 2.36e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1334313529 129 SKELEFTRRMLSLDAKNYHAWSHRQWVLQAL 159
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 92-123 1.16e-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: 1.16e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1334313529  92 LNEELNFMSGISESNPKNYQIWHHRRWIAEKL 123
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 59-176 8.46e-06

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: 44.80  E-value: 8.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  59 RALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISESNPKNYQIWHHRRWIAEKLG-TDAASKELEftrR 137
Cdd:COG4783    22 EAEALLEKALELDPDNPEAFALLGEILLQLG-DLDEAIVLLHEALELDPDEPEARLNLGLALLKAGdYDEALALLE---K 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1334313529 138 MLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEKD 176
Cdd:COG4783    98 ALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 34-172 1.27e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.83  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  34 IDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISESNPKNYQIW 113
Cdd:COG3914   105 LALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG-RLEEAIAALRRALELDPDNAEAL 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1334313529 114 HHRRWIAEKLGTDAASkeLEFTRRMLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQL 172
Cdd:COG3914   184 NNLGNALQDLGRLEEA--IAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELL 240
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 59-88 2.38e-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: 38.00  E-value: 2.38e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1334313529  59 RALQLTHQAILLNPGNYTVWHFRRLILDAL 88
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 162-192 3.02e-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: 37.62  E-value: 3.02e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1334313529 162 WENELDYCHQLLEKDVFNNSAWNQRYFVVTR 192
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 34-145 4.40e-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: 39.79  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  34 IDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISESNPKNYQIW 113
Cdd:COG4783    31 LELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAG-DYDEALALLEKALKLDPEHPEAY 109

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1334313529 114 HHRRWIAEKLG-TDAASKELEftrRMLSLDAKN 145
Cdd:COG4783   110 LRLARAYRALGrPDEAIAALE---KALELDPDD 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 60-176 1.35e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 40.36  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  60 ALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISESNPKNYQIWHHRRWIAEKLG-TDAAskeLEFTRRM 138
Cdd:COG3914    97 ALALYRRALALNPDNAEALFNLGNLLLALG-RLEEALAALRRALALNPDFAEAYLNLGEALRRLGrLEEA---IAALRRA 172

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1334313529 139 LSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEKD 176
Cdd:COG3914   173 LELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELD 210
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-187 4.72e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.06  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334313529  34 IDYKPDFIETMGYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISESNPKNYQIW 113
Cdd:COG0457    69 LELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELG-RYDEAIEAYERALELDPDDADAL 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334313529 114 HHRRWIAEKLGTDAASKELEFTRRMLSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEKDVFNNSAWNQRY 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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