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Conserved domains on  [gi|1860389516|ref|XP_034892555|]
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protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha [Populus alba]

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: 584.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516   5 EHQWRLSQDPEWADVTPIPQDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  85 LDALGIDLNEELNFMSGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMFSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 165 ELDYCHQLLEEDVFNNSAWNQRYFVVTRSPLLGGLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDLAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1860389516 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: 584.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516   5 EHQWRLSQDPEWADVTPIPQDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  85 LDALGIDLNEELNFMSGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMFSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 165 ELDYCHQLLEEDVFNNSAWNQRYFVVTRSPLLGGLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDLAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1860389516 325 PS 326
Cdd:PLN02789  318 PK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 18-324 5.26e-47

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 161.58  E-value: 5.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  18 DVTPIP-QDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGIDLNE-- 94
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  95 -----ELNFMSGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMFSLDAKNYHAWSHRQWVLQALGGWEN----- 164
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlk 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 165 -ELDYCHQLLEEDVFNNSAWNQRYFVVTRSPLLG--GLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISD 241
Cdd:COG5536   168 hELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVMI 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 242 PQvssvclKVLSAEANHVFALSTLLDLLS-HGFQANQEFRDAVDSLRPSNSDPADSDLA-KTICSILRHVDPMRVNYWTW 319
Cdd:COG5536   248 GE------KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNLYST 321


                  ....*
gi 1860389516 320 RKSKL 324
Cdd:COG5536   322 LHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 92-123 8.70e-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: 8.70e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1860389516  92 LNEELNFMSGISERNPKNYQIWHHRRWIAEKL 123
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 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: 584.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516   5 EHQWRLSQDPEWADVTPIPQDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLI 84
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  85 LDALGIDLNEELNFMSGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMFSLDAKNYHAWSHRQWVLQALGGWEN 164
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 165 ELDYCHQLLEEDVFNNSAWNQRYFVVTRSPLLGGLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISDPQV 244
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 245 SSVCLKVLSAEANHVFALSTLLDLLSHGFQANQEFRDAVDSLrpsNSDPADSDLAKTICSILRHVDPMRVNYWTWRKSKL 324
Cdd:PLN02789  241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                  ..
gi 1860389516 325 PS 326
Cdd:PLN02789  318 PK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 18-324 5.26e-47

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 161.58  E-value: 5.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  18 DVTPIP-QDDGPNPVVPIAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGIDLNE-- 94
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  95 -----ELNFMSGISERNPKNYQIWHHRRWIAEKLGTDAASKELEFTRRMFSLDAKNYHAWSHRQWVLQALGGWEN----- 164
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDLFNfsdlk 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 165 -ELDYCHQLLEEDVFNNSAWNQRYFVVTRSPLLG--GLEATRESEVKYTIEAILGNPGNESPWRYLRGLYKNDPKSWISD 241
Cdd:COG5536   168 hELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFATDIVMI 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516 242 PQvssvclKVLSAEANHVFALSTLLDLLS-HGFQANQEFRDAVDSLRPSNSDPADSDLA-KTICSILRHVDPMRVNYWTW 319
Cdd:COG5536   248 GE------KVEDLGKYIVIINGKELDLGPkENLPCLHSLLELEFLCHAEKALLTERDIEqKALVELAIKVDPARRNLYST 321


                  ....*
gi 1860389516 320 RKSKL 324
Cdd:COG5536   322 LHERF 326
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-186 2.00e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.24  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISERNPKNYQIW 113
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLG-RYEEALADYEQALELDPDDAEAL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860389516 114 HHRRWIAEKLG-TDAAskeLEFTRRMFSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEEDVFNNSAWNQR 186
Cdd:COG0457    80 NNLGLALQALGrYEEA---LEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-176 6.87e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 49.62  E-value: 6.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISERNPKNYQIW 113
Cdd:COG0457    35 LELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALG-RYEEALEDYDKALELDPDDAEAL 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860389516 114 HHRRWIAEKLG-TDAAskeLEFTRRMFSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEED 176
Cdd:COG0457   114 YNLGLALLELGrYDEA---IEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAA 174
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 92-123 8.70e-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: 8.70e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1860389516  92 LNEELNFMSGISERNPKNYQIWHHRRWIAEKL 123
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 129-159 1.31e-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: 1.31e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1860389516 129 SKELEFTRRMFSLDAKNYHAWSHRQWVLQAL 159
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 59-176 4.05e-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: 42.87  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  59 RALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISERNPKNYQIWHHRRWIAEKLG-TDAASKELEftrR 137
Cdd:COG4783    22 EAEALLEKALELDPDNPEAFALLGEILLQLG-DLDEAIVLLHEALELDPDEPEARLNLGLALLKAGdYDEALALLE---K 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1860389516 138 MFSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEED 176
Cdd:COG4783    98 ALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 34-172 1.13e-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: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISERNPKNYQIW 113
Cdd:COG3914   105 LALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG-RLEEAIAALRRALELDPDNAEAL 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1860389516 114 HHRRWIAEKLGTDAASkeLEFTRRMFSLDAKNYHAWSHRQWVLQALGGWENELDYCHQL 172
Cdd:COG3914   184 NNLGNALQDLGRLEEA--IAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELL 240
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 59-88 3.14e-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: 3.14e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1860389516  59 RALQLTHQAILLNPGNYTVWHFRRLILDAL 88
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 34-133 5.70e-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: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISERNPKNYQIW 113
Cdd:COG4783    31 LELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAG-DYDEALALLEKALKLDPEHPEAY 109

                          90       100
                  ....*....|....*....|.
gi 1860389516 114 HHRRWIAEKLG-TDAASKELE 133
Cdd:COG4783   110 LRLARAYRALGrPDEAIAALE 130
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 162-192 8.72e-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: 36.46  E-value: 8.72e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1860389516 162 WENELDYCHQLLEEDVFNNSAWNQRYFVVTR 192
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-187 2.14e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860389516  34 IAYKPDFIETMDYFRAVYKANEFSPRALQLTHQAILLNPGNYTVWHFRRLILDALGiDLNEELNFMSGISERNPKNYQIW 113
Cdd:COG0457    69 LELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELG-RYDEAIEAYERALELDPDDADAL 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860389516 114 HHRRWIAEKLGTDAASKELEFTRRMFSLDAKNYHAWSHRQWVLQALGGWENELDYCHQLLEEDVFNNSAWNQRY 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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