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Conserved domains on  [gi|149050469|gb|EDM02642|]
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tetratricopeptide repeat domain 7 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TTC7_N super family cl44857
Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a ...
11-404 2.47e-146

Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a protein that forms the regulatory subunit of the PI4KIIIalpha complex (also known as PI4KA). This complex is composed of PI4KIIIalpha, TTC7 and FAM126A and catalyzes the first step in plasma membrane phosphoinositide synthesis. This TTC7 N-terminal domain contains basic residues suitable for interaction with the acidic inner leaflet of the plasma membrane and is required for localising the active site near its substrate. TTC7 acts as a bridge between PI4KA and EFR3B-FAM126A, via direct interactions. ERF3B is not part of the complex but contributes to its recruitment to the membrane.


The actual alignment was detected with superfamily member pfam19440:

Pssm-ID: 466084  Cd Length: 386  Bit Score: 429.58  E-value: 2.47e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469   11 LKVESEMERCRAEGQWDRMFQLVRHLqvlgisgggssnrrssPSGRfisLDTDDFGKLLLAEALLEQCLKDNHDKIKNSI 90
Cdd:pfam19440  10 YRLETEIERCRSECQWDKVPELVEQL----------------KAKR---IANDDMANLLLGEGKLEQYLKENPPILENST 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469   91 pllEKTDSRLNEARDHLSSILNNGKLPPQYMCEAMLILGKLHYVEGSYRDAVSMYARAGIDDISVEDKPLYQMRLLSEAF 170
Cdd:pfam19440  71 ---EKNQPKLSEAKKHLTSALDRGNLKPEFLQEAHLLLAKLNYVEGDYREALNMYARAGLDDLTLKELPVYRLRLLAEAY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469  171 VIKGLSLERLPNSVASHIRLTEREEEVVACFERASWVAQVFLQELEKTSNNSTSRHLKGSL-SVDYELSYFLEAALQSAY 249
Cdd:pfam19440 148 AIKGLCLEKQAVSSSSRVRLAEREEEMITCYEKAGDIALLYLQELERINSNTQNRSPKPGPpSQEQELGFFLETALQRAY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469  250 VKNLKKGNIVKGMRELREILRTVETKATQNFKVVAAKHLAGVLLHSLSEDCYWSPLSHPLPEFM----SKEENSFITQTL 325
Cdd:pfam19440 228 VLYFKKGNLARGVGRYREILRAVETRTTQNLRMTIARQLAEVLLRGVCEQSYWNPLEDPPPQSLldepLKGTNTKNYTPS 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149050469  326 RKPHLYEGDNLYCPKDNIEEALLLLLISESMATRDVVLSRAPEQEEDRKVSLQNASAIYDLLSITLGRRGQYVMLSECL 404
Cdd:pfam19440 308 RKPRVYSGENIFCPQDNVEEALLLLLISESMANRDAVLSRSPEHREARIISLQNATAVYDLLTIAMGRRGQYEMLSECL 386
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
461-630 1.43e-06

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


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.53  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 461 GSLHWLEEAEHFAMVVIGLGEEAGEFLPKGYLALGLTYSLQATDATLKSKQDelHRKALQTLERALELAPDDPQIIFYVS 540
Cdd:COG3914   42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGR--YEEALALYRRALALNPDNAEALFNLG 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 541 LQLALVRQISSAIERLQEALTVCRDDANALHLLALLFSAQKHHQHALDVINMAITEHPENFNLMFTKVKLEQVLKGPEEA 620
Cdd:COG3914  120 NLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEA 199
                        170
                 ....*....|
gi 149050469 621 LVTCRQMLRL 630
Cdd:COG3914  200 IAAYRRALEL 209
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
378-473 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: 41.33  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 378 QNASAiYDLLSITLGRRGQYVMLSECLERAMKYAFGEFHLWYQVALSMVACGKSAYAVSLLRECMKLQPSNPTVPLMAAK 457
Cdd:COG4783   36 DNPEA-FALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLAR 114
                         90
                 ....*....|....*.
gi 149050469 458 VCIGSLHWLEEAEHFA 473
Cdd:COG4783  115 AYRALGRPDEAIAALE 130
 
Name Accession Description Interval E-value
TTC7_N pfam19440
Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a ...
11-404 2.47e-146

Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a protein that forms the regulatory subunit of the PI4KIIIalpha complex (also known as PI4KA). This complex is composed of PI4KIIIalpha, TTC7 and FAM126A and catalyzes the first step in plasma membrane phosphoinositide synthesis. This TTC7 N-terminal domain contains basic residues suitable for interaction with the acidic inner leaflet of the plasma membrane and is required for localising the active site near its substrate. TTC7 acts as a bridge between PI4KA and EFR3B-FAM126A, via direct interactions. ERF3B is not part of the complex but contributes to its recruitment to the membrane.


Pssm-ID: 466084  Cd Length: 386  Bit Score: 429.58  E-value: 2.47e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469   11 LKVESEMERCRAEGQWDRMFQLVRHLqvlgisgggssnrrssPSGRfisLDTDDFGKLLLAEALLEQCLKDNHDKIKNSI 90
Cdd:pfam19440  10 YRLETEIERCRSECQWDKVPELVEQL----------------KAKR---IANDDMANLLLGEGKLEQYLKENPPILENST 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469   91 pllEKTDSRLNEARDHLSSILNNGKLPPQYMCEAMLILGKLHYVEGSYRDAVSMYARAGIDDISVEDKPLYQMRLLSEAF 170
Cdd:pfam19440  71 ---EKNQPKLSEAKKHLTSALDRGNLKPEFLQEAHLLLAKLNYVEGDYREALNMYARAGLDDLTLKELPVYRLRLLAEAY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469  171 VIKGLSLERLPNSVASHIRLTEREEEVVACFERASWVAQVFLQELEKTSNNSTSRHLKGSL-SVDYELSYFLEAALQSAY 249
Cdd:pfam19440 148 AIKGLCLEKQAVSSSSRVRLAEREEEMITCYEKAGDIALLYLQELERINSNTQNRSPKPGPpSQEQELGFFLETALQRAY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469  250 VKNLKKGNIVKGMRELREILRTVETKATQNFKVVAAKHLAGVLLHSLSEDCYWSPLSHPLPEFM----SKEENSFITQTL 325
Cdd:pfam19440 228 VLYFKKGNLARGVGRYREILRAVETRTTQNLRMTIARQLAEVLLRGVCEQSYWNPLEDPPPQSLldepLKGTNTKNYTPS 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149050469  326 RKPHLYEGDNLYCPKDNIEEALLLLLISESMATRDVVLSRAPEQEEDRKVSLQNASAIYDLLSITLGRRGQYVMLSECL 404
Cdd:pfam19440 308 RKPRVYSGENIFCPQDNVEEALLLLLISESMANRDAVLSRSPEHREARIISLQNATAVYDLLTIAMGRRGQYEMLSECL 386
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
461-630 1.43e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.53  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 461 GSLHWLEEAEHFAMVVIGLGEEAGEFLPKGYLALGLTYSLQATDATLKSKQDelHRKALQTLERALELAPDDPQIIFYVS 540
Cdd:COG3914   42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGR--YEEALALYRRALALNPDNAEALFNLG 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 541 LQLALVRQISSAIERLQEALTVCRDDANALHLLALLFSAQKHHQHALDVINMAITEHPENFNLMFTKVKLEQVLKGPEEA 620
Cdd:COG3914  120 NLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEA 199
                        170
                 ....*....|
gi 149050469 621 LVTCRQMLRL 630
Cdd:COG3914  200 IAAYRRALEL 209
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
378-473 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: 41.33  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 378 QNASAiYDLLSITLGRRGQYVMLSECLERAMKYAFGEFHLWYQVALSMVACGKSAYAVSLLRECMKLQPSNPTVPLMAAK 457
Cdd:COG4783   36 DNPEA-FALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLAR 114
                         90
                 ....*....|....*.
gi 149050469 458 VCIGSLHWLEEAEHFA 473
Cdd:COG4783  115 AYRALGRPDEAIAALE 130
TPR_20 pfam14561
Tetratricopeptide repeat;
519-556 3.77e-03

Tetratricopeptide repeat;


Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 37.10  E-value: 3.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 149050469  519 LQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERL 556
Cdd:pfam14561   8 LAALEARLAADPDDLDARLDLALALHAAGRNEEALELL 45
YPP1 cd23270
cargo-transport protein YPP1; This family includes YGR198w (named YPP1, also called ...
485-554 4.28e-03

cargo-transport protein YPP1; This family includes YGR198w (named YPP1, also called alpha-synuclein protective protein 1), which is essential in Saccharomyces cerevisiae. It has also been shown to perform fundamental functions in human and mouse. YPP1 is a cargo-transport protein involved in endocytosis. It interacts with genes involved in protein sorting and secretion, and plays a role in the assembly and recruitment of multiple copies of the kinase into phosphoinositide kinase (PIK) patches at the plasma membrane. It has been found to suppress the toxicity of alpha-synuclein (alpha-syn) mutant (A30P) that is associated with early onset of Parkinson's disease (PD) in humans, but not wild-type or the A53T mutant (also associated with early onset PD).


Pssm-ID: 438014 [Multi-domain]  Cd Length: 740  Bit Score: 40.34  E-value: 4.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149050469 485 EFLPKGYLALGLTYSLQATDATLKSKQDELHRKALQTLERALELAPD-DPQIIFYVSLQLALVRQISSAIE 554
Cdd:cd23270  391 KILSKAWYALYEYYSYLLIYTSNESELELNSNDLLSYLKNSLIVNPTgNSDLLFQYAYTLAQQREIEPAIK 461
 
Name Accession Description Interval E-value
TTC7_N pfam19440
Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a ...
11-404 2.47e-146

Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a protein that forms the regulatory subunit of the PI4KIIIalpha complex (also known as PI4KA). This complex is composed of PI4KIIIalpha, TTC7 and FAM126A and catalyzes the first step in plasma membrane phosphoinositide synthesis. This TTC7 N-terminal domain contains basic residues suitable for interaction with the acidic inner leaflet of the plasma membrane and is required for localising the active site near its substrate. TTC7 acts as a bridge between PI4KA and EFR3B-FAM126A, via direct interactions. ERF3B is not part of the complex but contributes to its recruitment to the membrane.


Pssm-ID: 466084  Cd Length: 386  Bit Score: 429.58  E-value: 2.47e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469   11 LKVESEMERCRAEGQWDRMFQLVRHLqvlgisgggssnrrssPSGRfisLDTDDFGKLLLAEALLEQCLKDNHDKIKNSI 90
Cdd:pfam19440  10 YRLETEIERCRSECQWDKVPELVEQL----------------KAKR---IANDDMANLLLGEGKLEQYLKENPPILENST 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469   91 pllEKTDSRLNEARDHLSSILNNGKLPPQYMCEAMLILGKLHYVEGSYRDAVSMYARAGIDDISVEDKPLYQMRLLSEAF 170
Cdd:pfam19440  71 ---EKNQPKLSEAKKHLTSALDRGNLKPEFLQEAHLLLAKLNYVEGDYREALNMYARAGLDDLTLKELPVYRLRLLAEAY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469  171 VIKGLSLERLPNSVASHIRLTEREEEVVACFERASWVAQVFLQELEKTSNNSTSRHLKGSL-SVDYELSYFLEAALQSAY 249
Cdd:pfam19440 148 AIKGLCLEKQAVSSSSRVRLAEREEEMITCYEKAGDIALLYLQELERINSNTQNRSPKPGPpSQEQELGFFLETALQRAY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469  250 VKNLKKGNIVKGMRELREILRTVETKATQNFKVVAAKHLAGVLLHSLSEDCYWSPLSHPLPEFM----SKEENSFITQTL 325
Cdd:pfam19440 228 VLYFKKGNLARGVGRYREILRAVETRTTQNLRMTIARQLAEVLLRGVCEQSYWNPLEDPPPQSLldepLKGTNTKNYTPS 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149050469  326 RKPHLYEGDNLYCPKDNIEEALLLLLISESMATRDVVLSRAPEQEEDRKVSLQNASAIYDLLSITLGRRGQYVMLSECL 404
Cdd:pfam19440 308 RKPRVYSGENIFCPQDNVEEALLLLLISESMANRDAVLSRSPEHREARIISLQNATAVYDLLTIAMGRRGQYEMLSECL 386
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
461-630 1.43e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.53  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 461 GSLHWLEEAEHFAMVVIGLGEEAGEFLPKGYLALGLTYSLQATDATLKSKQDelHRKALQTLERALELAPDDPQIIFYVS 540
Cdd:COG3914   42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGR--YEEALALYRRALALNPDNAEALFNLG 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 541 LQLALVRQISSAIERLQEALTVCRDDANALHLLALLFSAQKHHQHALDVINMAITEHPENFNLMFTKVKLEQVLKGPEEA 620
Cdd:COG3914  120 NLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEA 199
                        170
                 ....*....|
gi 149050469 621 LVTCRQMLRL 630
Cdd:COG3914  200 IAAYRRALEL 209
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
418-630 3.36e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.96  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 418 WYQVALSMVACGKSAYAVSLLRECMKLQPSNPtvplmAAKVCIGSLHW----LEEAEHFAMVVIGLGEEAgeflPKGYLA 493
Cdd:COG2956   11 WYFKGLNYLLNGQPDKAIDLLEEALELDPETV-----EAHLALGNLYRrrgeYDRAIRIHQKLLERDPDR----AEALLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 494 LGLTYSLQatdatlkskqdELHRKALQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERLQEALTVCRDDANALHLL 573
Cdd:COG2956   82 LAQDYLKA-----------GLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCEL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149050469 574 ALLFSAQKHHQHALDVINMAITEHPENFNLMFTKVKLEQVLKGPEEALVTCRQMLRL 630
Cdd:COG2956  151 AELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ 207
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
393-629 7.76e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.19  E-value: 7.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 393 RRGQYVMLSECLERAMKYAFGEFHLWYQVALSMVACGKSAYAVSLLRECMKLQPSNPTVPLMAAKVCIGSLHWlEEAEHF 472
Cdd:COG2956   54 RRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDW-EKAIEV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 473 AMVVIGLGEEAGEFlpkgYLALGLTYslqatdatLKSKQDElhrKALQTLERALELAPDDPqiifYVSLQLALV----RQ 548
Cdd:COG2956  133 LERLLKLGPENAHA----YCELAELY--------LEQGDYD---EAIEALEKALKLDPDCA----RALLLLAELyleqGD 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 549 ISSAIERLQEALTVCRDDANALHLLALLFSAQKHHQHALDVINMAITEHPENfNLMFTKVKLEQVLKGPEEALVTCRQML 628
Cdd:COG2956  194 YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSD-DLLLALADLLERKEGLEAALALLERQL 272

                 .
gi 149050469 629 R 629
Cdd:COG2956  273 R 273
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
491-626 2.99e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.15  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 491 YLALGLTYSLQatdatlkskqdELHRKALQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERLQEALTVCRDDANAL 570
Cdd:COG0457   45 LYNLGLAYLRL-----------GRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEAL 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149050469 571 HLLALLFSAQKHHQHALDVINMAITEHPENFNLMFTKVKLEQVLKGPEEALVTCRQ 626
Cdd:COG0457  114 YNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEK 169
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
515-630 4.26e-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: 4.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 515 HRKALQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERLQEALTVCRDDANALHLLALLFSAQKHHQHALDVINMAI 594
Cdd:COG4783   20 YDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKAL 99
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 149050469 595 TEHPENFNLMFTKVKLEQVLKGPEEALVTCRQMLRL 630
Cdd:COG4783  100 KLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
515-598 1.39e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 42.64  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 515 HRKALQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERLQEALTVCRDDANALHLLALLFSAQKHHQHALDVINMAI 594
Cdd:COG5010   70 FEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRAL 149

                 ....
gi 149050469 595 TEHP 598
Cdd:COG5010  150 GTSP 153
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
378-473 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: 41.33  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 378 QNASAiYDLLSITLGRRGQYVMLSECLERAMKYAFGEFHLWYQVALSMVACGKSAYAVSLLRECMKLQPSNPTVPLMAAK 457
Cdd:COG4783   36 DNPEA-FALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLAR 114
                         90
                 ....*....|....*.
gi 149050469 458 VCIGSLHWLEEAEHFA 473
Cdd:COG4783  115 AYRALGRPDEAIAALE 130
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
515-640 2.75e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.07  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 515 HRKALQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERLQEALTVCRDDANALHLLALLFSAQKHHQHALDVINMAI 594
Cdd:COG0457   24 YEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKAL 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 149050469 595 TEHPENFNLMFTKVKLEQVLKGPEEALVTCRQMLRL----WQALYNFSQL 640
Cdd:COG0457  104 ELDPDDAEALYNLGLALLELGRYDEAIEAYERALELdpddADALYNLGIA 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
384-560 5.62e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.92  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 384 YDLLSITLGRRGQYVMLSECLERAMKYAFGEFHLWYQVALSMVACGKSAYAVSLLRECMKLQPSNPTVPLMAAKVCIgSL 463
Cdd:COG0457   11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQ-AL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 464 HWLEEAEHFAMVVIGLGEEagefLPKGYLALGLTYSLQatdatlkskqdELHRKALQTLERALELAPDDPQIIFYVSLQL 543
Cdd:COG0457   90 GRYEEALEDYDKALELDPD----DAEALYNLGLALLEL-----------GRYDEAIEAYERALELDPDDADALYNLGIAL 154
                        170
                 ....*....|....*..
gi 149050469 544 ALVRQISSAIERLQEAL 560
Cdd:COG0457  155 EKLGRYEEALELLEKLE 171
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
488-612 9.65e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 39.60  E-value: 9.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 488 PKGYLALGLTYSLQatdatlkskqdELHRKALQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERLQEALTVCRDDA 567
Cdd:COG4235   17 AEGWLLLGRAYLRL-----------GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNP 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 149050469 568 NALHLLALLFSAQKHHQHALDVINMAITEHPENFNLMFTKVKLEQ 612
Cdd:COG4235   86 EALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLLEASIAE 130
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
379-566 1.04e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.29  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 379 NASAIYDLLSITLGRRGQYVMLSECLERAMKYAFGEFHLWYQVALSMVACGKSAYAVSLLRECMKLQPSNPTVplmaakv 458
Cdd:COG3914  110 DNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA------- 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 459 cigslhwleeaehfamvviglgeeageflpkgYLALGLTYSLQAtdatlkskqdeLHRKALQTLERALELAPDDPQIIFY 538
Cdd:COG3914  183 --------------------------------LNNLGNALQDLG-----------RLEEAIAAYRRALELDPDNADAHSN 219
                        170       180
                 ....*....|....*....|....*...
gi 149050469 539 VsLQLALVRQISSAIERLQEALTVCRDD 566
Cdd:COG3914  220 L-LFALRQACDWEVYDRFEELLAALARG 246
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
488-639 1.22e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.90  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 488 PKGYLALGLTYSLQatdatlkskqdELHRKALQTLERALELAPDDPQIifYVSLQLALVRQ--ISSAIERLQEALTVCRD 565
Cdd:COG3914  112 AEALFNLGNLLLAL-----------GRLEEALAALRRALALNPDFAEA--YLNLGEALRRLgrLEEAIAALRRALELDPD 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 566 DANALHLLALLFSAQKHHQHALDVINMAITEHPENF----NLMFTKVKLE--QVLKGPEEALVTCRQMLRLWQALYNFSQ 639
Cdd:COG3914  179 NAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNAdahsNLLFALRQACdwEVYDRFEELLAALARGPSELSPFALLYL 258
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
517-600 2.17e-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: 39.02  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149050469 517 KALQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERLQEALTVCRDDANALHLLALLFSAQKHHQHALDVINMAITE 596
Cdd:COG4783   56 EAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135

                 ....
gi 149050469 597 HPEN 600
Cdd:COG4783  136 DPDD 139
TPR_20 pfam14561
Tetratricopeptide repeat;
519-556 3.77e-03

Tetratricopeptide repeat;


Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 37.10  E-value: 3.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 149050469  519 LQTLERALELAPDDPQIIFYVSLQLALVRQISSAIERL 556
Cdd:pfam14561   8 LAALEARLAADPDDLDARLDLALALHAAGRNEEALELL 45
YPP1 cd23270
cargo-transport protein YPP1; This family includes YGR198w (named YPP1, also called ...
485-554 4.28e-03

cargo-transport protein YPP1; This family includes YGR198w (named YPP1, also called alpha-synuclein protective protein 1), which is essential in Saccharomyces cerevisiae. It has also been shown to perform fundamental functions in human and mouse. YPP1 is a cargo-transport protein involved in endocytosis. It interacts with genes involved in protein sorting and secretion, and plays a role in the assembly and recruitment of multiple copies of the kinase into phosphoinositide kinase (PIK) patches at the plasma membrane. It has been found to suppress the toxicity of alpha-synuclein (alpha-syn) mutant (A30P) that is associated with early onset of Parkinson's disease (PD) in humans, but not wild-type or the A53T mutant (also associated with early onset PD).


Pssm-ID: 438014 [Multi-domain]  Cd Length: 740  Bit Score: 40.34  E-value: 4.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149050469 485 EFLPKGYLALGLTYSLQATDATLKSKQDELHRKALQTLERALELAPD-DPQIIFYVSLQLALVRQISSAIE 554
Cdd:cd23270  391 KILSKAWYALYEYYSYLLIYTSNESELELNSNDLLSYLKNSLIVNPTgNSDLLFQYAYTLAQQREIEPAIK 461
 
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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