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Conserved domains on  [gi|157822327|ref|NP_001100728|]
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beclin 1-associated autophagy-related key regulator [Rattus norvegicus]

Protein Classification

Atg14 domain-containing protein( domain architecture ID 12103842)

Atg14 (autophagy related 14) domain-containing protein, similar to Homo sapiens beclin 1-associated autophagy-related key regulator

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATG14 pfam10186
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ...
 43-383 9.14e-49

Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.


:

Pssm-ID: 462986 [Multi-domain]  Cd Length: 347  Bit Score: 171.10  E-value: 9.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327   43 CPLCNTTRRRLTCAKCVqsgdfvyfdgrdRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQ 122
Cdd:pfam10186   1 CPICERSGRPFYCPTCA------------RNRLYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  123 LKQTICKGNEemkknsegllKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGdlveKKTSDLREHYDRLACLRRLHILELT 202
Cdd:pfam10186  69 LKSEVAISNE----------RLNEIKDKLDQLRREIAEKKKKIEKLRSSLK----QRRSDLESASYQLEERRASQLAKLQ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  203 SVIFPMDEVKTSGRDPADVSSetdsAMTSSMVSKLAEARRttylsgrWVCDDH-NGDTSISITGpwISLPNNGDYsayyn 281
Cdd:pfam10186 135 NSIKRIKQKWTALHSKTAESR----SFLCRELAKLYGLRQ-------VVKSKNgSSKEYYTIGG--IPLPDLRDL----- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  282 wveekkttqgpdmeHNNPAYTISAALGYATQLVNIVSHILDINLPKKLCNSEFC-------------------------- 335
Cdd:pfam10186 197 --------------NSAPPEEISTSLSYIAQLLVLVSHYLSIRLPAEITLPHSCypiptifspassylssespfpgltsn 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  336 -----------------GENLSKQR---------------LTRAVRKLNANILYLCSSQHVNLDQLQPLHTLRNLMHLVS 383
Cdd:pfam10186 263 ssspsssskkppshpprPRPLFIEKslpklskedpetyseFLEGVSLLAYNVAWLCRTQGVNSLDLDTLEDLCDIGKNLY 342
 
Name Accession Description Interval E-value
ATG14 pfam10186
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ...
 43-383 9.14e-49

Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.


Pssm-ID: 462986 [Multi-domain]  Cd Length: 347  Bit Score: 171.10  E-value: 9.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327   43 CPLCNTTRRRLTCAKCVqsgdfvyfdgrdRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQ 122
Cdd:pfam10186   1 CPICERSGRPFYCPTCA------------RNRLYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  123 LKQTICKGNEemkknsegllKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGdlveKKTSDLREHYDRLACLRRLHILELT 202
Cdd:pfam10186  69 LKSEVAISNE----------RLNEIKDKLDQLRREIAEKKKKIEKLRSSLK----QRRSDLESASYQLEERRASQLAKLQ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  203 SVIFPMDEVKTSGRDPADVSSetdsAMTSSMVSKLAEARRttylsgrWVCDDH-NGDTSISITGpwISLPNNGDYsayyn 281
Cdd:pfam10186 135 NSIKRIKQKWTALHSKTAESR----SFLCRELAKLYGLRQ-------VVKSKNgSSKEYYTIGG--IPLPDLRDL----- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  282 wveekkttqgpdmeHNNPAYTISAALGYATQLVNIVSHILDINLPKKLCNSEFC-------------------------- 335
Cdd:pfam10186 197 --------------NSAPPEEISTSLSYIAQLLVLVSHYLSIRLPAEITLPHSCypiptifspassylssespfpgltsn 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  336 -----------------GENLSKQR---------------LTRAVRKLNANILYLCSSQHVNLDQLQPLHTLRNLMHLVS 383
Cdd:pfam10186 263 ssspsssskkppshpprPRPLFIEKslpklskedpetyseFLEGVSLLAYNVAWLCRTQGVNSLDLDTLEDLCDIGKNLY 342
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
73-196 2.02e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  73 ERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTIcKGNEEMKKNSEGLLKNKEKN-QKL 151
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK-RKLEEKIRELEERIEELKKEiEEL 278

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 157822327 152 YSRAQRHQEKKEKIQRHnRKLGDLVEKKTSDLREHYDRLACLRRL 196
Cdd:PRK03918 279 EEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEE 322
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-197 5.14e-04

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: 42.74  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327    83 SQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKK 162
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 157822327   163 EKIQRHNRKLGDLVEKKTSDLREHYDRLACLRRLH 197
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRREL 917
 
Name Accession Description Interval E-value
ATG14 pfam10186
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ...
 43-383 9.14e-49

Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.


Pssm-ID: 462986 [Multi-domain]  Cd Length: 347  Bit Score: 171.10  E-value: 9.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327   43 CPLCNTTRRRLTCAKCVqsgdfvyfdgrdRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQ 122
Cdd:pfam10186   1 CPICERSGRPFYCPTCA------------RNRLYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  123 LKQTICKGNEemkknsegllKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGdlveKKTSDLREHYDRLACLRRLHILELT 202
Cdd:pfam10186  69 LKSEVAISNE----------RLNEIKDKLDQLRREIAEKKKKIEKLRSSLK----QRRSDLESASYQLEERRASQLAKLQ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  203 SVIFPMDEVKTSGRDPADVSSetdsAMTSSMVSKLAEARRttylsgrWVCDDH-NGDTSISITGpwISLPNNGDYsayyn 281
Cdd:pfam10186 135 NSIKRIKQKWTALHSKTAESR----SFLCRELAKLYGLRQ-------VVKSKNgSSKEYYTIGG--IPLPDLRDL----- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  282 wveekkttqgpdmeHNNPAYTISAALGYATQLVNIVSHILDINLPKKLCNSEFC-------------------------- 335
Cdd:pfam10186 197 --------------NSAPPEEISTSLSYIAQLLVLVSHYLSIRLPAEITLPHSCypiptifspassylssespfpgltsn 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  336 -----------------GENLSKQR---------------LTRAVRKLNANILYLCSSQHVNLDQLQPLHTLRNLMHLVS 383
Cdd:pfam10186 263 ssspsssskkppshpprPRPLFIEKslpklskedpetyseFLEGVSLLAYNVAWLCRTQGVNSLDLDTLEDLCDIGKNLY 342
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
73-196 2.02e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  73 ERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTIcKGNEEMKKNSEGLLKNKEKN-QKL 151
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK-RKLEEKIRELEERIEELKKEiEEL 278

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 157822327 152 YSRAQRHQEKKEKIQRHnRKLGDLVEKKTSDLREHYDRLACLRRL 196
Cdd:PRK03918 279 EEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRLEEE 322
PTZ00121 PTZ00121
MAEBL; Provisional
 77-185 2.37e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327   77 DKKERLSQLKNKQEEFQK--EVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQT----------ICKGNEEMKKNSEGLLKN 144
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenkikaaeEAKKAEEDKKKAEEAKKA 1683

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 157822327  145 KEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVeKKTSDLRE 185
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEK-KKAEELKK 1723
PTZ00121 PTZ00121
MAEBL; Provisional
 51-190 3.54e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327   51 RRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKmRIEQLKqticKG 130
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK-KADEAK----KK 1323

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327  131 NEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTSDLREHYDRL 190
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-197 5.14e-04

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: 42.74  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822327    83 SQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKK 162
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 157822327   163 EKIQRHNRKLGDLVEKKTSDLREHYDRLACLRRLH 197
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRREL 917
 
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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