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Conserved domains on  [gi|387511659|emb|CCH59100|]
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hypothetical protein TBLA_0B02580 [Tetrapisispora blattae CBS 6284]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
964-1131 3.51e-36

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


:

Pssm-ID: 463063  Cd Length: 130  Bit Score: 133.11  E-value: 3.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   964 ENAVVRRFKDIESLAKRYKKESKFRKSVLETY---KKEKITLKNFEIGDLALFLPMSDIsipidskassvnssfssVDLS 1040
Cdd:pfam10377    1 ESAVIKRFKDVETLAKKLTKENKSKREKLEKLqseAHEKITLKNFKVGDLALFLPTRRH-----------------NDLS 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659  1041 TPPtsemlmnkamssisidtssrrksnysWAAFTAygETKRYILKEDTKVPEGN-DWFLGRIVALQNKVVTEEEP--NRY 1117
Cdd:pfam10377   64 TPP--------------------------WAAFNV--GAPHYFLKADSLLALKSrEWFVGRITSIEERVVDLSDKdsNPF 115
                          170
                   ....*....|....
gi 387511659  1118 KLPLGSQWCKVSAT 1131
Cdd:pfam10377  116 KLSKGTVWYLVTAE 129
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
159-488 1.86e-26

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


:

Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 112.48  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   159 WLTALDIDIQYLTESIQSKMSDINKILKGLNVCSRYLDLYCMDSFDLFDSNIKYLNQLKDfeSFNKWEEFYESTLANLKG 238
Cdd:pfam04108   11 WANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLK--DLDAALERLEETLDKLRN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   239 ITNDP-----------LTSFLNKKSLDKKALEVKKLDVYLRKHFQKMQEIIDENANLQKTLNFEIVEL-------EKKYS 300
Cdd:pfam04108   89 TPVEPalppgeekqktLLDFIDEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELESLsspsesiSLIPT 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   301 PKTSKSTLEETMISKFYDILSTMKKQQSVLLSKKDDDLSWTNLSSKNEIynQLiyakDNQVKTLLTIAQALFSQYD---E 377
Cdd:pfam04108  169 LLKELESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDAR--EL----DDVVPELQDRLDEMENNYErlqK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   378 ITTLKKQLQIENIQKWGRIATIQINVSEIKkELLTNCNEELSIYK-SHQLVFAKLKD-------FPIVYGLYLIELLRRK 449
Cdd:pfam04108  243 LLEQKNSLIDELLSALQLIAEIQSRLPEYL-AALKEFEERWEEEKeTIEDYLSELEDlrefyegFPSAYGSLLLEVERRR 321
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 387511659   450 LWINFILKDGLNFATSYKLNSHNEEIKRKKWLDNFGHLL 488
Cdd:pfam04108  322 EWAEKMKKILRKLAEELDRLQEEERKRREKFLKEVGDFL 360
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
248-999 3.91e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 3.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   248 LNKKSLDKKALEVKKLDVYLRKHF--QKMQEIIDENANLQKTLN---FEIVELEKKYSPKTSKSTLEETMISKFYDILST 322
Cdd:pfam02463  288 LKLLAKEEEELKSELLKLERRKVDdeEKLKESEKEKKKAEKELKkekEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   323 MKKQQSVLLSKKDDDlsWTNLSSKNEIYNQLIYAKDNQVKTLLTIAQaLFSQYDEITTLKKQLQIENIQKWGRIATIQIN 402
Cdd:pfam02463  368 LEQLEEELLAKKKLE--SERLSSAAKLKEEELELKSEEEKEAQLLLE-LARQLEDLLKEEKKEELEILEEEEESIELKQG 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   403 VSEIKKELLtncnEELSIYKSHQLVFAKLKDFPIVYGLYLIELLRRKLWINFILKDGLNFATSYKLNSHNEEIKRKKWLD 482
Cdd:pfam02463  445 KLTEEKEEL----EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   483 NFGHLLNDFNLELPSE-KEDLKVINCFFGRDisnpATNPAVKLKNQQEETLTSVLEIENFLNKYISSLQDNDLFANSVDI 561
Cdd:pfam02463  521 GGRIISAHGRLGDLGVaVENYKVAISTAVIV----EVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   562 LTKNIEKVKYFQHNALLSENKNPLPTKFHKSLTQPVLPLDQNEIFLNNATGSGIDNNNKVLVNGFRDRISSMSNKMFQSN 641
Cdd:pfam02463  597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   642 VISNVSSNSLFPTVKPEIEREylQLKDEVRILRKENDMKTSKIQSLESQISDNNVEIHAYRETLTSLNKELSRLItEKED 721
Cdd:pfam02463  677 EIQELQEKAESELAKEEILRR--QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE-EEEE 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   722 NTALKRVKDAEFRDHIQKIINQNVILENKLISSSKysERLEIENKKLLSFVLNIKVELTHMREDFFNYFDKAKSQLNLIT 801
Cdd:pfam02463  754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV--EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   802 LKYTNFKNKLPKSLLQQLPNASKNASVIGINQvnffdqsltsQTDSYINSSNNMPLKLLEMivqifkanvCILENIGLLP 881
Cdd:pfam02463  832 EEELEELALELKEEQKLEKLAEEELERLEEEI----------TKEELLQELLLKEEELEEQ---------KLKDELESKE 892
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   882 TIDKTNNiQIIRVRGLRNNTLSDSTAGSISDSTFLIDQNEK----IKSTFFNNVFQEYSNMKNFEQQEVNSIvvnpiLQL 957
Cdd:pfam02463  893 EKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKyeeePEELLLEEADEKEKEENNKEEEEERNK-----RLL 966
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|..
gi 387511659   958 FKNHLLENAVVRRFKDIESLAKRYKKESKFRKSVLETYKKEK 999
Cdd:pfam02463  967 LAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
 
Name Accession Description Interval E-value
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
964-1131 3.51e-36

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


Pssm-ID: 463063  Cd Length: 130  Bit Score: 133.11  E-value: 3.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   964 ENAVVRRFKDIESLAKRYKKESKFRKSVLETY---KKEKITLKNFEIGDLALFLPMSDIsipidskassvnssfssVDLS 1040
Cdd:pfam10377    1 ESAVIKRFKDVETLAKKLTKENKSKREKLEKLqseAHEKITLKNFKVGDLALFLPTRRH-----------------NDLS 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659  1041 TPPtsemlmnkamssisidtssrrksnysWAAFTAygETKRYILKEDTKVPEGN-DWFLGRIVALQNKVVTEEEP--NRY 1117
Cdd:pfam10377   64 TPP--------------------------WAAFNV--GAPHYFLKADSLLALKSrEWFVGRITSIEERVVDLSDKdsNPF 115
                          170
                   ....*....|....
gi 387511659  1118 KLPLGSQWCKVSAT 1131
Cdd:pfam10377  116 KLSKGTVWYLVTAE 129
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
159-488 1.86e-26

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 112.48  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   159 WLTALDIDIQYLTESIQSKMSDINKILKGLNVCSRYLDLYCMDSFDLFDSNIKYLNQLKDfeSFNKWEEFYESTLANLKG 238
Cdd:pfam04108   11 WANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLK--DLDAALERLEETLDKLRN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   239 ITNDP-----------LTSFLNKKSLDKKALEVKKLDVYLRKHFQKMQEIIDENANLQKTLNFEIVEL-------EKKYS 300
Cdd:pfam04108   89 TPVEPalppgeekqktLLDFIDEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELESLsspsesiSLIPT 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   301 PKTSKSTLEETMISKFYDILSTMKKQQSVLLSKKDDDLSWTNLSSKNEIynQLiyakDNQVKTLLTIAQALFSQYD---E 377
Cdd:pfam04108  169 LLKELESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDAR--EL----DDVVPELQDRLDEMENNYErlqK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   378 ITTLKKQLQIENIQKWGRIATIQINVSEIKkELLTNCNEELSIYK-SHQLVFAKLKD-------FPIVYGLYLIELLRRK 449
Cdd:pfam04108  243 LLEQKNSLIDELLSALQLIAEIQSRLPEYL-AALKEFEERWEEEKeTIEDYLSELEDlrefyegFPSAYGSLLLEVERRR 321
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 387511659   450 LWINFILKDGLNFATSYKLNSHNEEIKRKKWLDNFGHLL 488
Cdd:pfam04108  322 EWAEKMKKILRKLAEELDRLQEEERKRREKFLKEVGDFL 360
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
248-999 3.91e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 3.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   248 LNKKSLDKKALEVKKLDVYLRKHF--QKMQEIIDENANLQKTLN---FEIVELEKKYSPKTSKSTLEETMISKFYDILST 322
Cdd:pfam02463  288 LKLLAKEEEELKSELLKLERRKVDdeEKLKESEKEKKKAEKELKkekEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   323 MKKQQSVLLSKKDDDlsWTNLSSKNEIYNQLIYAKDNQVKTLLTIAQaLFSQYDEITTLKKQLQIENIQKWGRIATIQIN 402
Cdd:pfam02463  368 LEQLEEELLAKKKLE--SERLSSAAKLKEEELELKSEEEKEAQLLLE-LARQLEDLLKEEKKEELEILEEEEESIELKQG 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   403 VSEIKKELLtncnEELSIYKSHQLVFAKLKDFPIVYGLYLIELLRRKLWINFILKDGLNFATSYKLNSHNEEIKRKKWLD 482
Cdd:pfam02463  445 KLTEEKEEL----EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   483 NFGHLLNDFNLELPSE-KEDLKVINCFFGRDisnpATNPAVKLKNQQEETLTSVLEIENFLNKYISSLQDNDLFANSVDI 561
Cdd:pfam02463  521 GGRIISAHGRLGDLGVaVENYKVAISTAVIV----EVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   562 LTKNIEKVKYFQHNALLSENKNPLPTKFHKSLTQPVLPLDQNEIFLNNATGSGIDNNNKVLVNGFRDRISSMSNKMFQSN 641
Cdd:pfam02463  597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   642 VISNVSSNSLFPTVKPEIEREylQLKDEVRILRKENDMKTSKIQSLESQISDNNVEIHAYRETLTSLNKELSRLItEKED 721
Cdd:pfam02463  677 EIQELQEKAESELAKEEILRR--QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE-EEEE 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   722 NTALKRVKDAEFRDHIQKIINQNVILENKLISSSKysERLEIENKKLLSFVLNIKVELTHMREDFFNYFDKAKSQLNLIT 801
Cdd:pfam02463  754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV--EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   802 LKYTNFKNKLPKSLLQQLPNASKNASVIGINQvnffdqsltsQTDSYINSSNNMPLKLLEMivqifkanvCILENIGLLP 881
Cdd:pfam02463  832 EEELEELALELKEEQKLEKLAEEELERLEEEI----------TKEELLQELLLKEEELEEQ---------KLKDELESKE 892
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   882 TIDKTNNiQIIRVRGLRNNTLSDSTAGSISDSTFLIDQNEK----IKSTFFNNVFQEYSNMKNFEQQEVNSIvvnpiLQL 957
Cdd:pfam02463  893 EKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKyeeePEELLLEEADEKEKEENNKEEEEERNK-----RLL 966
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|..
gi 387511659   958 FKNHLLENAVVRRFKDIESLAKRYKKESKFRKSVLETYKKEK 999
Cdd:pfam02463  967 LAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
658-819 9.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   658 EIEREYLQLKDEVRILRKENDMKTSKIQSLESQISDNNVEIHAYRETLTSLNKELSRLITEKEDNTALKRVKDAEFRDHI 737
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   738 QKIINQNVILENKLISSSKYSERLEIENKKLLSF---VLNIKVELTHMREDFFNyfdkAKSQLNLITLKYTNFKNKLpKS 814
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELkeeLESLEAELEELEAELEE----LESRLEELEEQLETLRSKV-AQ 390

                   ....*
gi 387511659   815 LLQQL 819
Cdd:TIGR02168  391 LELQI 395
 
Name Accession Description Interval E-value
ATG11 pfam10377
Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, ...
964-1131 3.51e-36

Autophagy-related protein 11; The function of this family is conflicting. In the fission yeast, Schizosaccharomyces pombe, this protein has been shown to interact with the telomere cap complex and it is also required for dimerization and kinase activation of Atg1. However, in budding yeast, Saccharomyces cerevisiae, this protein is called ATG11 and is shown to be involved in autophagy.


Pssm-ID: 463063  Cd Length: 130  Bit Score: 133.11  E-value: 3.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   964 ENAVVRRFKDIESLAKRYKKESKFRKSVLETY---KKEKITLKNFEIGDLALFLPMSDIsipidskassvnssfssVDLS 1040
Cdd:pfam10377    1 ESAVIKRFKDVETLAKKLTKENKSKREKLEKLqseAHEKITLKNFKVGDLALFLPTRRH-----------------NDLS 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659  1041 TPPtsemlmnkamssisidtssrrksnysWAAFTAygETKRYILKEDTKVPEGN-DWFLGRIVALQNKVVTEEEP--NRY 1117
Cdd:pfam10377   64 TPP--------------------------WAAFNV--GAPHYFLKADSLLALKSrEWFVGRITSIEERVVDLSDKdsNPF 115
                          170
                   ....*....|....
gi 387511659  1118 KLPLGSQWCKVSAT 1131
Cdd:pfam10377  116 KLSKGTVWYLVTAE 129
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
159-488 1.86e-26

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 112.48  E-value: 1.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   159 WLTALDIDIQYLTESIQSKMSDINKILKGLNVCSRYLDLYCMDSFDLFDSNIKYLNQLKDfeSFNKWEEFYESTLANLKG 238
Cdd:pfam04108   11 WANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLK--DLDAALERLEETLDKLRN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   239 ITNDP-----------LTSFLNKKSLDKKALEVKKLDVYLRKHFQKMQEIIDENANLQKTLNFEIVEL-------EKKYS 300
Cdd:pfam04108   89 TPVEPalppgeekqktLLDFIDEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELESLsspsesiSLIPT 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   301 PKTSKSTLEETMISKFYDILSTMKKQQSVLLSKKDDDLSWTNLSSKNEIynQLiyakDNQVKTLLTIAQALFSQYD---E 377
Cdd:pfam04108  169 LLKELESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDAR--EL----DDVVPELQDRLDEMENNYErlqK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   378 ITTLKKQLQIENIQKWGRIATIQINVSEIKkELLTNCNEELSIYK-SHQLVFAKLKD-------FPIVYGLYLIELLRRK 449
Cdd:pfam04108  243 LLEQKNSLIDELLSALQLIAEIQSRLPEYL-AALKEFEERWEEEKeTIEDYLSELEDlrefyegFPSAYGSLLLEVERRR 321
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 387511659   450 LWINFILKDGLNFATSYKLNSHNEEIKRKKWLDNFGHLL 488
Cdd:pfam04108  322 EWAEKMKKILRKLAEELDRLQEEERKRREKFLKEVGDFL 360
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
248-999 3.91e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 3.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   248 LNKKSLDKKALEVKKLDVYLRKHF--QKMQEIIDENANLQKTLN---FEIVELEKKYSPKTSKSTLEETMISKFYDILST 322
Cdd:pfam02463  288 LKLLAKEEEELKSELLKLERRKVDdeEKLKESEKEKKKAEKELKkekEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   323 MKKQQSVLLSKKDDDlsWTNLSSKNEIYNQLIYAKDNQVKTLLTIAQaLFSQYDEITTLKKQLQIENIQKWGRIATIQIN 402
Cdd:pfam02463  368 LEQLEEELLAKKKLE--SERLSSAAKLKEEELELKSEEEKEAQLLLE-LARQLEDLLKEEKKEELEILEEEEESIELKQG 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   403 VSEIKKELLtncnEELSIYKSHQLVFAKLKDFPIVYGLYLIELLRRKLWINFILKDGLNFATSYKLNSHNEEIKRKKWLD 482
Cdd:pfam02463  445 KLTEEKEEL----EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   483 NFGHLLNDFNLELPSE-KEDLKVINCFFGRDisnpATNPAVKLKNQQEETLTSVLEIENFLNKYISSLQDNDLFANSVDI 561
Cdd:pfam02463  521 GGRIISAHGRLGDLGVaVENYKVAISTAVIV----EVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   562 LTKNIEKVKYFQHNALLSENKNPLPTKFHKSLTQPVLPLDQNEIFLNNATGSGIDNNNKVLVNGFRDRISSMSNKMFQSN 641
Cdd:pfam02463  597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   642 VISNVSSNSLFPTVKPEIEREylQLKDEVRILRKENDMKTSKIQSLESQISDNNVEIHAYRETLTSLNKELSRLItEKED 721
Cdd:pfam02463  677 EIQELQEKAESELAKEEILRR--QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE-EEEE 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   722 NTALKRVKDAEFRDHIQKIINQNVILENKLISSSKysERLEIENKKLLSFVLNIKVELTHMREDFFNYFDKAKSQLNLIT 801
Cdd:pfam02463  754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV--EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   802 LKYTNFKNKLPKSLLQQLPNASKNASVIGINQvnffdqsltsQTDSYINSSNNMPLKLLEMivqifkanvCILENIGLLP 881
Cdd:pfam02463  832 EEELEELALELKEEQKLEKLAEEELERLEEEI----------TKEELLQELLLKEEELEEQ---------KLKDELESKE 892
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   882 TIDKTNNiQIIRVRGLRNNTLSDSTAGSISDSTFLIDQNEK----IKSTFFNNVFQEYSNMKNFEQQEVNSIvvnpiLQL 957
Cdd:pfam02463  893 EKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKyeeePEELLLEEADEKEKEENNKEEEEERNK-----RLL 966
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|..
gi 387511659   958 FKNHLLENAVVRRFKDIESLAKRYKKESKFRKSVLETYKKEK 999
Cdd:pfam02463  967 LAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
666-776 6.62e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 6.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   666 LKDEVRILRKENDMKTSKIQSLESQISDNNVEIHAYRETLTSLNKELSRLITEKEDNTALKRVKDAEFRDHIQKIINQNV 745
Cdd:pfam15921  732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEV 811
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 387511659   746 ILENkliSSSKYSE------RLEIENKKL-LSFVLNIK 776
Cdd:pfam15921  812 ALDK---ASLQFAEcqdiiqRQEQESVRLkLQHTLDVK 846
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
658-819 9.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   658 EIEREYLQLKDEVRILRKENDMKTSKIQSLESQISDNNVEIHAYRETLTSLNKELSRLITEKEDNTALKRVKDAEFRDHI 737
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387511659   738 QKIINQNVILENKLISSSKYSERLEIENKKLLSF---VLNIKVELTHMREDFFNyfdkAKSQLNLITLKYTNFKNKLpKS 814
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELkeeLESLEAELEELEAELEE----LESRLEELEEQLETLRSKV-AQ 390

                   ....*
gi 387511659   815 LLQQL 819
Cdd:TIGR02168  391 LELQI 395
 
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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