NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|255587054|ref|XP_002534116|]
View 

protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha isoform X2 [Ricinus communis]

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
 10-332 0e+00

farnesyltranstransferase


:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 590.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  10 EETVPLSQRPEWSDVIPVQQDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLV 89
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  90 LEALNAELYEELDYIERVAKKNTKNYQIWHHRRWVAEKLGTDAAAKELQFTRKILSLDAKNYHAWSHRQWVLQALGGWED 169
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 170 ELDYCRQLLEHDVFNNSAWNQRYFIITRSPLLGGLKAVRESEMKFTVEAILANPENESPWRYLRGLYQGDTQSWINDPQV 249
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 250 SSVCLKVLSAKTNHIFALSMLLDLLCHGFQANQEIRDSVDALrtsNCDPPEPDLAKAVCSLLEHVDPMRANYWIWRKSKL 329
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                 ...
gi 255587054 330 PVL 332
Cdd:PLN02789 318 PKA 320
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 10-332 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 590.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  10 EETVPLSQRPEWSDVIPVQQDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLV 89
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  90 LEALNAELYEELDYIERVAKKNTKNYQIWHHRRWVAEKLGTDAAAKELQFTRKILSLDAKNYHAWSHRQWVLQALGGWED 169
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 170 ELDYCRQLLEHDVFNNSAWNQRYFIITRSPLLGGLKAVRESEMKFTVEAILANPENESPWRYLRGLYQGDTQSWINDPQV 249
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 250 SSVCLKVLSAKTNHIFALSMLLDLLCHGFQANQEIRDSVDALrtsNCDPPEPDLAKAVCSLLEHVDPMRANYWIWRKSKL 329
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                 ...
gi 255587054 330 PVL 332
Cdd:PLN02789 318 PKA 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 29-329 1.26e-45

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 158.11  E-value: 1.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  29 QDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNAELYE-------EL 101
Cdd:COG5536   15 QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDkehlldnEL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 102 DYIERVAKKNTKNYQIWHHRRWVAEKLGTDAAAKELQFTRKILSLDAKNYHAWSHRQWVL---QALGGWED---ELDYCR 175
Cdd:COG5536   95 DFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtiEDLFNFSDlkhELEYTT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 176 QLLEHDVFNNSAWNQRYFIITRSPLLG--GLKAVRESEMKFTVEAILANPENESPWRYLRGL---YQGDTQSW---INDP 247
Cdd:COG5536  175 SLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVsseFATDIVMIgekVEDL 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 248 QVSSVCLKV----LSAKTNHIFALSML-LDLLCHGFQAnqeirdsvdalrtsncDPPEPDLA-KAVCSLLEHVDPMRANY 321
Cdd:COG5536  255 GKYIVIINGkeldLGPKENLPCLHSLLeLEFLCHAEKA----------------LLTERDIEqKALVELAIKVDPARRNL 318


                 ....*...
gi 255587054 322 WIWRKSKL 329
Cdd:COG5536  319 YSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 135-164 7.80e-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: 7.80e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 255587054  135 KELQFTRKILSLDAKNYHAWSHRQWVLQAL 164
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
 10-332 0e+00

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 590.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  10 EETVPLSQRPEWSDVIPVQQDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLV 89
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  90 LEALNAELYEELDYIERVAKKNTKNYQIWHHRRWVAEKLGTDAAAKELQFTRKILSLDAKNYHAWSHRQWVLQALGGWED 169
Cdd:PLN02789  81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPDAANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 170 ELDYCRQLLEHDVFNNSAWNQRYFIITRSPLLGGLKAVRESEMKFTVEAILANPENESPWRYLRGLYQGDTQSWINDPQV 249
Cdd:PLN02789 161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPLLGGLEAMRDSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPEV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 250 SSVCLKVLSAKTNHIFALSMLLDLLCHGFQANQEIRDSVDALrtsNCDPPEPDLAKAVCSLLEHVDPMRANYWIWRKSKL 329
Cdd:PLN02789 241 SSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTL---AEELSDSTLAQAVCSELEVADPMRRNYWAWRKSKL 317


                 ...
gi 255587054 330 PVL 332
Cdd:PLN02789 318 PKA 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 29-329 1.26e-45

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 158.11  E-value: 1.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  29 QDDGPNPVVPIAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNAELYE-------EL 101
Cdd:COG5536   15 QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDkehlldnEL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 102 DYIERVAKKNTKNYQIWHHRRWVAEKLGTDAAAKELQFTRKILSLDAKNYHAWSHRQWVL---QALGGWED---ELDYCR 175
Cdd:COG5536   95 DFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtiEDLFNFSDlkhELEYTT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 176 QLLEHDVFNNSAWNQRYFIITRSPLLG--GLKAVRESEMKFTVEAILANPENESPWRYLRGL---YQGDTQSW---INDP 247
Cdd:COG5536  175 SLIETDIYNNSAWHHRYIWIERRFNRGdvISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVsseFATDIVMIgekVEDL 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 248 QVSSVCLKV----LSAKTNHIFALSML-LDLLCHGFQAnqeirdsvdalrtsncDPPEPDLA-KAVCSLLEHVDPMRANY 321
Cdd:COG5536  255 GKYIVIINGkeldLGPKENLPCLHSLLeLEFLCHAEKA----------------LLTERDIEqKALVELAIKVDPARRNL 318


                 ....*...
gi 255587054 322 WIWRKSKL 329
Cdd:COG5536  319 YSTLHERF 326
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
39-191 6.36e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.56  E-value: 6.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  39 IAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALnaELYEE-LDYIERVAKKNTKNYQI 117
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRL--GRYEEaLADYEQALELDPDDAEA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255587054 118 WHHRRWVAEKLGTDAAAKELQftRKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCRQLLEHDVFNNSAWNQR 191
Cdd:COG0457   79 LNNLGLALQALGRYEEALEDY--DKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
39-179 2.05e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.24  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  39 IAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNaeLYEE-LDYIERVAKKNTKNYQI 117
Cdd:COG0457   35 LELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALG--RYEEaLEDYDKALELDPDDAEA 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255587054 118 WHHRRWVAEKLGTDAAAkeLQFTRKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCRQLLE 179
Cdd:COG0457  113 LYNLGLALLELGRYDEA--IEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEA 172
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 135-164 7.80e-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: 7.80e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 255587054  135 KELQFTRKILSLDAKNYHAWSHRQWVLQAL 164
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 97-128 2.12e-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: 43.78  E-value: 2.12e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 255587054   97 LYEELDYIERVAKKNTKNYQIWHHRRWVAEKL 128
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 39-177 2.84e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.84  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  39 IAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNaELYEELDYIERVAKKNTKNYQIW 118
Cdd:COG3914  105 LALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG-RLEEAIAALRRALELDPDNAEAL 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255587054 119 HHRRWVAEKLGTDAAAkeLQFTRKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCRQL 177
Cdd:COG3914  184 NNLGNALQDLGRLEEA--IAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELL 240
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 54-181 6.48e-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: 45.18  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  54 AIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLeaLNAELYEE-LDYIERVAKKNTKNYQIWHHRRWVAEKLG-TD 131
Cdd:COG4783   12 QALLLAGDYDEAEALLEKALELDPDNPEAFALLGEIL--LQLGDLDEaIVLLHEALELDPDEPEARLNLGLALLKAGdYD 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 255587054 132 AAAKELQftrKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCRQLLEHD 181
Cdd:COG4783   90 EALALLE---KALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 167-197 4.01e-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: 4.01e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 255587054  167 WEDELDYCRQLLEHDVFNNSAWNQRYFIITR 197
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 64-93 9.15e-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: 9.15e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 255587054   64 RALQLTHLVILLNPGNYTVWHFRRLVLEAL 93
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
111-237 1.69e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054 111 NTKNYQIWHHRRWVAEKLGTDAAAkeLQFTRKILSLDAKNYHAWSHRQWVLQALGGWEDELDYCRQLLEHDVFNNSAWNQ 190
Cdd:COG0457    4 DPDDAEAYNNLGLAYRRLGRYEEA--IEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255587054 191 RYFIitrsplLGGLKAVRESEMKFTvEAILANPENESPWRYLRGLYQ 237
Cdd:COG0457   82 LGLA------LQALGRYEEALEDYD-KALELDPDDAEALYNLGLALL 121
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 39-150 9.45e-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: 35.94  E-value: 9.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255587054  39 IAYKPEFEETMNYFRAIYLSDERSPRALQLTHLVILLNPGNYTVWHFRRLVLEALNaELYEELDYIERVAKKNTKNYQIW 118
Cdd:COG4783   31 LELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAG-DYDEALALLEKALKLDPEHPEAY 109

                         90       100       110
                 ....*....|....*....|....*....|...
gi 255587054 119 HHRRWVAEKLG-TDAAAKELQftrKILSLDAKN 150
Cdd:COG4783  110 LRLARAYRALGrPDEAIAALE---KALELDPDD 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