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Conserved domains on  [gi|2201784377|ref|XP_046769766|]
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tetratricopeptide repeat protein 7A isoform X2 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TTC7_N pfam19440
Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a ...
1-399 1.99e-167

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: 486.21  E-value: 1.99e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377   1 MAAKGPLSHVKLEGEIERCRAEGHWGQLRLLVqqqllppartrrKVAAGGTEETEDYGSMLLAEALLEECLKENFAKLKD 80
Cdd:pfam19440   1 MTSRISFSGYRLETEIERCRSECQWDKVPELV------------EQLKAKRIANDDMANLLLGEGKLEQYLKENPPILEN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377  81 SiplTERNEPKLSEAKQHLTNVLIRGKLRPKYMTEAMLILGKLHYVEGSYRDAISMYAKAGIDDLSTKDEPLYMLRLVAE 160
Cdd:pfam19440  69 S---TEKNQPKLSEAKKHLTSALDRGNLKPEFLQEAHLLLAKLNYVEGDYREALNMYARAGLDDLTLKELPVYRLRLLAE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 161 AFVIKGLSLERSTNSIASRARLCEREEEVMTCFETACVITQVYLQELEKTLNNTHSRSIKGSnMTYSEFELSYFLEAALQ 240
Cdd:pfam19440 146 AYAIKGLCLEKQAVSSSSRVRLAEREEEMITCYEKAGDIALLYLQELERINSNTQNRSPKPG-PPSQEQELGFFLETALQ 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 241 SAYVTHLKKGNIVKGVRSLREVLRTVETKATQTFKMTAAKQLGQVLLHSLSEDCYWSPLSDPLPE--FMNKEDQSYISNL 318
Cdd:pfam19440 225 RAYVLYFKKGNLARGVGRYREILRAVETRTTQNLRMTIARQLAEVLLRGVCEQSYWNPLEDPPPQslLDEPLKGTNTKNY 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 319 -LCRKPELYTEENVYCPQDNVEEALLLLLISESMANRDAVISRAPDQQDDRAVSLRDASEVYDLLSITLGRRGQYVMLSE 397
Cdd:pfam19440 305 tPSRKPRVYSGENIFCPQDNVEEALLLLLISESMANRDAVLSRSPEHREARIISLQNATAVYDLLTIAMGRRGQYEMLSE 384

                  ..
gi 2201784377 398 CL 399
Cdd:pfam19440 385 CL 386
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
363-624 1.31e-11

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: 65.91  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 363 DQQDDRAVSL--------RDASEVYDLLSITLGRRGQYVMLSECLERAMKFAFDEFHLWYQLALSMVACGKSAYAVSVLK 434
Cdd:COG2956    21 NGQPDKAIDLleealeldPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 435 ECAKLRPTDPTVPLLAAKVCIGSLHWLEEGEYFAKMvidlgEDAGESLAKGYLALGLTYSLQatdatlkstqDEYnKKAL 514
Cdd:COG2956   101 KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERL-----LKLGPENAHAYCELAELYLEQ----------GDY-DEAI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 515 QTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAEYPE 594
Cdd:COG2956   165 EALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 2201784377 595 SfSLLFTKVKLEWMHKGPEEALVTCRHMLQ 624
Cdd:COG2956   245 D-DLLLALADLLERKEGLEAALALLERQLR 273
 
Name Accession Description Interval E-value
TTC7_N pfam19440
Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a ...
1-399 1.99e-167

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: 486.21  E-value: 1.99e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377   1 MAAKGPLSHVKLEGEIERCRAEGHWGQLRLLVqqqllppartrrKVAAGGTEETEDYGSMLLAEALLEECLKENFAKLKD 80
Cdd:pfam19440   1 MTSRISFSGYRLETEIERCRSECQWDKVPELV------------EQLKAKRIANDDMANLLLGEGKLEQYLKENPPILEN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377  81 SiplTERNEPKLSEAKQHLTNVLIRGKLRPKYMTEAMLILGKLHYVEGSYRDAISMYAKAGIDDLSTKDEPLYMLRLVAE 160
Cdd:pfam19440  69 S---TEKNQPKLSEAKKHLTSALDRGNLKPEFLQEAHLLLAKLNYVEGDYREALNMYARAGLDDLTLKELPVYRLRLLAE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 161 AFVIKGLSLERSTNSIASRARLCEREEEVMTCFETACVITQVYLQELEKTLNNTHSRSIKGSnMTYSEFELSYFLEAALQ 240
Cdd:pfam19440 146 AYAIKGLCLEKQAVSSSSRVRLAEREEEMITCYEKAGDIALLYLQELERINSNTQNRSPKPG-PPSQEQELGFFLETALQ 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 241 SAYVTHLKKGNIVKGVRSLREVLRTVETKATQTFKMTAAKQLGQVLLHSLSEDCYWSPLSDPLPE--FMNKEDQSYISNL 318
Cdd:pfam19440 225 RAYVLYFKKGNLARGVGRYREILRAVETRTTQNLRMTIARQLAEVLLRGVCEQSYWNPLEDPPPQslLDEPLKGTNTKNY 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 319 -LCRKPELYTEENVYCPQDNVEEALLLLLISESMANRDAVISRAPDQQDDRAVSLRDASEVYDLLSITLGRRGQYVMLSE 397
Cdd:pfam19440 305 tPSRKPRVYSGENIFCPQDNVEEALLLLLISESMANRDAVLSRSPEHREARIISLQNATAVYDLLTIAMGRRGQYEMLSE 384

                  ..
gi 2201784377 398 CL 399
Cdd:pfam19440 385 CL 386
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
363-624 1.31e-11

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: 65.91  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 363 DQQDDRAVSL--------RDASEVYDLLSITLGRRGQYVMLSECLERAMKFAFDEFHLWYQLALSMVACGKSAYAVSVLK 434
Cdd:COG2956    21 NGQPDKAIDLleealeldPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 435 ECAKLRPTDPTVPLLAAKVCIGSLHWLEEGEYFAKMvidlgEDAGESLAKGYLALGLTYSLQatdatlkstqDEYnKKAL 514
Cdd:COG2956   101 KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERL-----LKLGPENAHAYCELAELYLEQ----------GDY-DEAI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 515 QTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAEYPE 594
Cdd:COG2956   165 EALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 2201784377 595 SfSLLFTKVKLEWMHKGPEEALVTCRHMLQ 624
Cdd:COG2956   245 D-DLLLALADLLERKEGLEAALALLERQLR 273
YPP1 cd23270
cargo-transport protein YPP1; This family includes YGR198w (named YPP1, also called ...
480-586 3.51e-07

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: 53.82  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 480 ESLAKGYLALGLTYSLQATDATLKSTQDEYNKKALQTLERARELDREDHQIILY-LSLQLALVRQISDAIEHLQEAL-QL 557
Cdd:cd23270   391 KILSKAWYALYEYYSYLLIYTSNESELELNSNDLLSYLKNSLIVNPTGNSDLLFqYAYTLAQQREIEPAIKLLKFILlKK 470
                          90       100
                  ....*....|....*....|....*....
gi 2201784377 558 CKDDMNSLHLLALLFSAQKHYQHALEVIN 586
Cdd:cd23270   471 NPESFKSWHLLALCLSIQEDKEESFKIIN 499
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
312-474 2.88e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.21  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 312 QSYISNLLCRKPELYTEENVYCPQDNVEEALLLLLISESMANRDAVISRAPDQQDD--------RAVSLR-DASEVYDLL 382
Cdd:COG3914    39 AALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYeealalyrRALALNpDNAEALFNL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 383 SITLGRRGQYVMLSECLERAMKFAFDEFHLWYQLALSMVACGKSAYAVSVLKECAKLRPTDPTVPLLAAKVCIgSLHWLE 462
Cdd:COG3914   119 GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQ-DLGRLE 197
                         170
                  ....*....|..
gi 2201784377 463 EGEYFAKMVIDL 474
Cdd:COG3914   198 EAIAAYRRALEL 209
 
Name Accession Description Interval E-value
TTC7_N pfam19440
Tetratricopeptide repeat protein 7 N-terminal; This is the N-terminal domain of TTC7, a ...
1-399 1.99e-167

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: 486.21  E-value: 1.99e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377   1 MAAKGPLSHVKLEGEIERCRAEGHWGQLRLLVqqqllppartrrKVAAGGTEETEDYGSMLLAEALLEECLKENFAKLKD 80
Cdd:pfam19440   1 MTSRISFSGYRLETEIERCRSECQWDKVPELV------------EQLKAKRIANDDMANLLLGEGKLEQYLKENPPILEN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377  81 SiplTERNEPKLSEAKQHLTNVLIRGKLRPKYMTEAMLILGKLHYVEGSYRDAISMYAKAGIDDLSTKDEPLYMLRLVAE 160
Cdd:pfam19440  69 S---TEKNQPKLSEAKKHLTSALDRGNLKPEFLQEAHLLLAKLNYVEGDYREALNMYARAGLDDLTLKELPVYRLRLLAE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 161 AFVIKGLSLERSTNSIASRARLCEREEEVMTCFETACVITQVYLQELEKTLNNTHSRSIKGSnMTYSEFELSYFLEAALQ 240
Cdd:pfam19440 146 AYAIKGLCLEKQAVSSSSRVRLAEREEEMITCYEKAGDIALLYLQELERINSNTQNRSPKPG-PPSQEQELGFFLETALQ 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 241 SAYVTHLKKGNIVKGVRSLREVLRTVETKATQTFKMTAAKQLGQVLLHSLSEDCYWSPLSDPLPE--FMNKEDQSYISNL 318
Cdd:pfam19440 225 RAYVLYFKKGNLARGVGRYREILRAVETRTTQNLRMTIARQLAEVLLRGVCEQSYWNPLEDPPPQslLDEPLKGTNTKNY 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 319 -LCRKPELYTEENVYCPQDNVEEALLLLLISESMANRDAVISRAPDQQDDRAVSLRDASEVYDLLSITLGRRGQYVMLSE 397
Cdd:pfam19440 305 tPSRKPRVYSGENIFCPQDNVEEALLLLLISESMANRDAVLSRSPEHREARIISLQNATAVYDLLTIAMGRRGQYEMLSE 384

                  ..
gi 2201784377 398 CL 399
Cdd:pfam19440 385 CL 386
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
363-624 1.31e-11

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: 65.91  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 363 DQQDDRAVSL--------RDASEVYDLLSITLGRRGQYVMLSECLERAMKFAFDEFHLWYQLALSMVACGKSAYAVSVLK 434
Cdd:COG2956    21 NGQPDKAIDLleealeldPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 435 ECAKLRPTDPTVPLLAAKVCIGSLHWLEEGEYFAKMvidlgEDAGESLAKGYLALGLTYSLQatdatlkstqDEYnKKAL 514
Cdd:COG2956   101 KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERL-----LKLGPENAHAYCELAELYLEQ----------GDY-DEAI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 515 QTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAEYPE 594
Cdd:COG2956   165 EALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 2201784377 595 SfSLLFTKVKLEWMHKGPEEALVTCRHMLQ 624
Cdd:COG2956   245 D-DLLLALADLLERKEGLEAALALLERQLR 273
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
413-624 1.31e-08

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: 56.66  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 413 WYQLALSMVACGKSAYAVSVLKECAKLRPTDPTVPLLAAKVcigslhWLEEGEY-----FAKMVIDLGEDAGES---LAK 484
Cdd:COG2956    11 WYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNL------YRRRGEYdrairIHQKLLERDPDRAEAlleLAQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 485 GYLALGLTyslqatdatlkstqdeynKKALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNS 564
Cdd:COG2956    85 DYLKAGLL------------------DRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHA 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 565 LHLLALLFSAQKHYQHALEVINMAVAEYPESFSLLFTKVKLEWMHKGPEEALVTCRHMLQ 624
Cdd:COG2956   147 YCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALE 206
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
447-625 1.72e-08

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 57.70  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 447 PLLAAKVCIGSLHWLEEGEYFAKMVIDLGEDAGESLAKGYLALGLTYSLQATDATLKSTQDEYNKkALQTLERARELDRE 526
Cdd:COG3914    32 LEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEE-ALALYRRALALNPD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 527 DHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAEYPESFSLLFTKVK-L 605
Cdd:COG3914   111 NAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNaL 190
                         170       180
                  ....*....|....*....|
gi 2201784377 606 EWMHKgPEEALVTCRHMLQM 625
Cdd:COG3914   191 QDLGR-LEEAIAAYRRALEL 209
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
511-625 4.43e-08

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: 52.50  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 511 KKALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVA 590
Cdd:COG4783    21 DEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALK 100
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2201784377 591 EYPESFSLLFTKVKLEWMHKGPEEALVTCRHMLQM 625
Cdd:COG4783   101 LDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
511-616 1.82e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 52.70  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 511 KKALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVA 590
Cdd:COG0457    59 EEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALE 138
                          90       100
                  ....*....|....*....|....*.
gi 2201784377 591 EYPESFSLLFTKVKLEWMHKGPEEAL 616
Cdd:COG0457   139 LDPDDADALYNLGIALEKLGRYEEAL 164
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
483-595 2.12e-07

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: 50.39  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 483 AKGYLALGLTYSLQatdatlkstqDEYnKKALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDM 562
Cdd:COG4235    17 AEGWLLLGRAYLRL----------GRY-DEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNP 85
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2201784377 563 NSLHLLALLFSAQKHYQHALEVINMAVAEYPES 595
Cdd:COG4235    86 EALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
YPP1 cd23270
cargo-transport protein YPP1; This family includes YGR198w (named YPP1, also called ...
480-586 3.51e-07

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: 53.82  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 480 ESLAKGYLALGLTYSLQATDATLKSTQDEYNKKALQTLERARELDREDHQIILY-LSLQLALVRQISDAIEHLQEAL-QL 557
Cdd:cd23270   391 KILSKAWYALYEYYSYLLIYTSNESELELNSNDLLSYLKNSLIVNPTGNSDLLFqYAYTLAQQREIEPAIKLLKFILlKK 470
                          90       100
                  ....*....|....*....|....*....
gi 2201784377 558 CKDDMNSLHLLALLFSAQKHYQHALEVIN 586
Cdd:cd23270   471 NPESFKSWHLLALCLSIQEDKEESFKIIN 499
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
512-595 3.94e-07

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: 49.81  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 512 KALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAE 591
Cdd:COG4783    56 EAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135

                  ....
gi 2201784377 592 YPES 595
Cdd:COG4783   136 DPDD 139
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
512-593 8.11e-07

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: 49.57  E-value: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 512 KALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAE 591
Cdd:COG5010    72 ESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151

                  ..
gi 2201784377 592 YP 593
Cdd:COG5010   152 SP 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
374-594 1.11e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.39  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 374 DASEVYDLLSITLGRRGQYVMLSECLERAMKFAFDEFHLWYQLALSMVACGKSAYAVSVLKECAKLRPTDPTVpllaakv 453
Cdd:COG0457     6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEA------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 454 cigslhwleegeyfakmvidlgedageslakgYLALGLTYSlqatdatlksTQDEYnKKALQTLERARELDREDHQIILY 533
Cdd:COG0457    79 --------------------------------LNNLGLALQ----------ALGRY-EEALEDYDKALELDPDDAEALYN 115
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201784377 534 LSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAEYPE 594
Cdd:COG0457   116 LGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
482-625 1.30e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.39  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 482 LAKGYLALGLTYSLQatdatlkstqDEYnKKALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDD 561
Cdd:COG0457     7 DAEAYNNLGLAYRRL----------GRY-EEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201784377 562 MNSLHLLALLFSAQKHYQHALEVINMAVAEYPESFSLLFTKVKLEWMHKGPEEALVTCRHMLQM 625
Cdd:COG0457    76 AEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
512-599 1.44e-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: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 512 KALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVA- 590
Cdd:COG3914   130 EALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEl 209
                          90
                  ....*....|.
gi 2201784377 591 --EYPESFSLL 599
Cdd:COG3914   210 dpDNADAHSNL 220
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
512-625 2.30e-05

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: 44.61  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 512 KALQTLERARELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAE 591
Cdd:COG4235     1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2201784377 592 YPESFSLLFTKVKLEWMHKGPEEALVTCRHMLQM 625
Cdd:COG4235    81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLAL 114
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
522-616 1.19e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 44.23  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 522 ELDREDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAEYPESFSLLFT 601
Cdd:COG0457     2 ELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNN 81
                          90
                  ....*....|....*
gi 2201784377 602 KVKLEWMHKGPEEAL 616
Cdd:COG0457    82 LGLALQALGRYEEAL 96
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
511-594 2.25e-04

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 40.54  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 511 KKALQTLERARELDREDHQIILYLSLQLALVRQISDAIEhLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVA 590
Cdd:COG3063     9 EEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALE 87

                  ....
gi 2201784377 591 EYPE 594
Cdd:COG3063    88 LDPS 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
374-477 2.74e-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: 41.72  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 374 DASEVYDLLSITLGRRGQYVMLSECLERAMKFAFDEFHLWYQLALSMVACGKSAYAVSVLKECAKLRPTDPTVPLLAAKV 453
Cdd:COG4783    36 DNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARA 115
                          90       100
                  ....*....|....*....|....
gi 2201784377 454 CIGSLHWLEEGEYFAKMVIDLGED 477
Cdd:COG4783   116 YRALGRPDEAIAALEKALELDPDD 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
312-474 2.88e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.21  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 312 QSYISNLLCRKPELYTEENVYCPQDNVEEALLLLLISESMANRDAVISRAPDQQDD--------RAVSLR-DASEVYDLL 382
Cdd:COG3914    39 AALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYeealalyrRALALNpDNAEALFNL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 383 SITLGRRGQYVMLSECLERAMKFAFDEFHLWYQLALSMVACGKSAYAVSVLKECAKLRPTDPTVPLLAAKVCIgSLHWLE 462
Cdd:COG3914   119 GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQ-DLGRLE 197
                         170
                  ....*....|..
gi 2201784377 463 EGEYFAKMVIDL 474
Cdd:COG3914   198 EAIAAYRRALEL 209
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
526-625 1.18e-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: 39.79  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 526 EDHQIILYLSLQLALVRQISDAIEHLQEALQLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAEYPESFSLLFTKVKL 605
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81
                          90       100
                  ....*....|....*....|
gi 2201784377 606 EWMHKGPEEALVTCRHMLQM 625
Cdd:COG4783    82 LLKAGDYDEALALLEKALKL 101
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
367-446 4.34e-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: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 367 DRAVSLR-DASEVYDLLSITLGRRGQYVMLSECLERAMKFAFDEFHLWYQLALSMVACGKSAYAVSVLKECAKLRPTDPT 445
Cdd:COG3914   136 RRALALNpDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNAD 215

                  .
gi 2201784377 446 V 446
Cdd:COG3914   216 A 216
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
476-629 6.77e-03

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: 38.02  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201784377 476 EDAGESLAKGYLALGLTYSLQATDATLKSTQDEYNKKALQTLERARELDREDHQIILYLSLQlalvRQISDAIEHLQEAL 555
Cdd:COG5010     6 GFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKL----GDFEESLALLEQAL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201784377 556 QLCKDDMNSLHLLALLFSAQKHYQHALEVINMAVAEYPESFSLLFTKVKLEWMHKGPEEALVTCRHMLQMWQMA 629
Cdd:COG5010    82 QLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSPLK 155
 
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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