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Conserved domains on  [gi|17542438|ref|NP_500844|]
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Beclin homolog [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APG6 pfam04111
Apg6 BARA domain; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 196-370 2.39e-35

Apg6 BARA domain; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway. This entry is the Beta-Alpha repeated, autophagy-specific (BARA) domain.


:

Pssm-ID: 461178  Cd Length: 176  Bit Score: 127.66  E-value: 2.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   196 TNVLDLCFHIWVDGIVGEINGFRLGYLKDAPVEFTEINAALGQIVLLLEILLERIGV--QHHELMPvaMGSHSYIKlrRN 273
Cdd:pfam04111   1 TNVYNDTFHISHDGPFGTINGLRLGRLPNVPVEWSEINAAWGQTALLLATLAKKLGLkfQGYKLVP--MGSFSKIE--KL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   274 GIDMETYALYGQG----TPLSGSSGIDPGIRRFLQLLEFLLKELKDRNKNFKPPYQIHADSLVDNGVKYNavMTLNT-DV 348
Cdd:pfam04111  77 DDDSQELELYGSGdfslGLFFSERKFDKAMVAFLDCLQQLGEFLEKLDPEFELPYKIDKDKGKIGDYSIK--LQFNTsDE 154

                         170       180
                  ....*....|....*....|..
gi 17542438   349 RWTRAMALMLTDLKAACAQCDA 370
Cdd:pfam04111 155 EWTKALKFMLTNLKWLLAWVSS 176
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 63-189 9.32e-28

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


:

Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 105.76  E-value: 9.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438    63 PVCNDCSDALRNEMDAQVATLDDEIKTYQTYINYLKENHPTtSIPDLKAKLQNVSDEEKELEQQLKKLLAEEEQLDLDLQ 142
Cdd:pfam17675   1 PLCEECTDLLLEELDKQLEDAEKERDAYISFLKKLEKETPE-ELEELEKELEKLEKEEEELLQELEELEKEREELDAELE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 17542438   143 TKRRTAEAASEKSGELWKKYRDNLRQVFEDQDELHSLEAERQYAEVQ 189
Cdd:pfam17675  80 ALEEELEALDEEEEEFWREYNALQLQLLEFQDERDSLEAQYEHALNQ 126
 
Name Accession Description Interval E-value
APG6 pfam04111
Apg6 BARA domain; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 196-370 2.39e-35

Apg6 BARA domain; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway. This entry is the Beta-Alpha repeated, autophagy-specific (BARA) domain.


Pssm-ID: 461178  Cd Length: 176  Bit Score: 127.66  E-value: 2.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   196 TNVLDLCFHIWVDGIVGEINGFRLGYLKDAPVEFTEINAALGQIVLLLEILLERIGV--QHHELMPvaMGSHSYIKlrRN 273
Cdd:pfam04111   1 TNVYNDTFHISHDGPFGTINGLRLGRLPNVPVEWSEINAAWGQTALLLATLAKKLGLkfQGYKLVP--MGSFSKIE--KL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   274 GIDMETYALYGQG----TPLSGSSGIDPGIRRFLQLLEFLLKELKDRNKNFKPPYQIHADSLVDNGVKYNavMTLNT-DV 348
Cdd:pfam04111  77 DDDSQELELYGSGdfslGLFFSERKFDKAMVAFLDCLQQLGEFLEKLDPEFELPYKIDKDKGKIGDYSIK--LQFNTsDE 154

                         170       180
                  ....*....|....*....|..
gi 17542438   349 RWTRAMALMLTDLKAACAQCDA 370
Cdd:pfam04111 155 EWTKALKFMLTNLKWLLAWVSS 176
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 63-189 9.32e-28

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 105.76  E-value: 9.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438    63 PVCNDCSDALRNEMDAQVATLDDEIKTYQTYINYLKENHPTtSIPDLKAKLQNVSDEEKELEQQLKKLLAEEEQLDLDLQ 142
Cdd:pfam17675   1 PLCEECTDLLLEELDKQLEDAEKERDAYISFLKKLEKETPE-ELEELEKELEKLEKEEEELLQELEELEKEREELDAELE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 17542438   143 TKRRTAEAASEKSGELWKKYRDNLRQVFEDQDELHSLEAERQYAEVQ 189
Cdd:pfam17675  80 ALEEELEALDEEEEEFWREYNALQLQLLEFQDERDSLEAQYEHALNQ 126
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 73-183 8.46e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 8.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438     73 RNEMDAQVATLDDEIKTYQTYINYLKENhpttsIPDLKAKLQNVSDEEKELEQQLKKLLAE-EEQLDL-DLQTKRRTAEA 150
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKR-----LSELKAKLEALEEELSEIEDPKGEDEEIpEEELSLeDVQAELQRVEE 965

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 17542438    151 ASEKSGELWKKYRDNLRQVFEDQDELHS----LEAER 183
Cdd:TIGR02169  966 EIRALEPVNMLAIQEYEEVLKRLDELKEkrakLEEER 1002
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-192 2.14e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   70 DALRNEM---DAQVATLDDEIKTYQTYINYLKE---NHPTTSIPDLKAKLQNVSDEEKELEQQLKKLLAEEEQLDL---- 139
Cdd:COG4913  298 EELRAELarlEAELERLEARLDALREELDELEAqirGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLplpa 377

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438  140 ---DLQTKRRTAEAASEKSGELWKKYRDNL----RQVFEDQDELHSLEAERqyAEVQHRK 192
Cdd:COG4913  378 saeEFAALRAEAAALLEALEEELEALEEALaeaeAALRDLRRELRELEAEI--ASLERRK 435
 
Name Accession Description Interval E-value
APG6 pfam04111
Apg6 BARA domain; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 196-370 2.39e-35

Apg6 BARA domain; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway. This entry is the Beta-Alpha repeated, autophagy-specific (BARA) domain.


Pssm-ID: 461178  Cd Length: 176  Bit Score: 127.66  E-value: 2.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   196 TNVLDLCFHIWVDGIVGEINGFRLGYLKDAPVEFTEINAALGQIVLLLEILLERIGV--QHHELMPvaMGSHSYIKlrRN 273
Cdd:pfam04111   1 TNVYNDTFHISHDGPFGTINGLRLGRLPNVPVEWSEINAAWGQTALLLATLAKKLGLkfQGYKLVP--MGSFSKIE--KL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   274 GIDMETYALYGQG----TPLSGSSGIDPGIRRFLQLLEFLLKELKDRNKNFKPPYQIHADSLVDNGVKYNavMTLNT-DV 348
Cdd:pfam04111  77 DDDSQELELYGSGdfslGLFFSERKFDKAMVAFLDCLQQLGEFLEKLDPEFELPYKIDKDKGKIGDYSIK--LQFNTsDE 154

                         170       180
                  ....*....|....*....|..
gi 17542438   349 RWTRAMALMLTDLKAACAQCDA 370
Cdd:pfam04111 155 EWTKALKFMLTNLKWLLAWVSS 176
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 63-189 9.32e-28

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 105.76  E-value: 9.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438    63 PVCNDCSDALRNEMDAQVATLDDEIKTYQTYINYLKENHPTtSIPDLKAKLQNVSDEEKELEQQLKKLLAEEEQLDLDLQ 142
Cdd:pfam17675   1 PLCEECTDLLLEELDKQLEDAEKERDAYISFLKKLEKETPE-ELEELEKELEKLEKEEEELLQELEELEKEREELDAELE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 17542438   143 TKRRTAEAASEKSGELWKKYRDNLRQVFEDQDELHSLEAERQYAEVQ 189
Cdd:pfam17675  80 ALEEELEALDEEEEEFWREYNALQLQLLEFQDERDSLEAQYEHALNQ 126
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 73-183 8.46e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 8.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438     73 RNEMDAQVATLDDEIKTYQTYINYLKENhpttsIPDLKAKLQNVSDEEKELEQQLKKLLAE-EEQLDL-DLQTKRRTAEA 150
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKR-----LSELKAKLEALEEELSEIEDPKGEDEEIpEEELSLeDVQAELQRVEE 965

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 17542438    151 ASEKSGELWKKYRDNLRQVFEDQDELHS----LEAER 183
Cdd:TIGR02169  966 EIRALEPVNMLAIQEYEEVLKRLDELKEkrakLEEER 1002
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-192 2.14e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   70 DALRNEM---DAQVATLDDEIKTYQTYINYLKE---NHPTTSIPDLKAKLQNVSDEEKELEQQLKKLLAEEEQLDL---- 139
Cdd:COG4913  298 EELRAELarlEAELERLEARLDALREELDELEAqirGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLplpa 377

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438  140 ---DLQTKRRTAEAASEKSGELWKKYRDNL----RQVFEDQDELHSLEAERqyAEVQHRK 192
Cdd:COG4913  378 saeEFAALRAEAAALLEALEEELEALEEALaeaeAALRDLRRELRELEAEI--ASLERRK 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 75-187 5.08e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438     75 EMDAQVATLDDEIKTYQTYINYLKE--NHPTTSIPDLKAKLQNVSDEEKELEQQLKKLLAEEEQLDLDLQTKRRTAEAAS 152
Cdd:TIGR02169  375 EVDKEFAETRDELKDYREKLEKLKReiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 17542438    153 EKSGELWK---KYRDNLRQVFEDQD-----------ELHSLEAERQYAE 187
Cdd:TIGR02169  455 WKLEQLAAdlsKYEQELYDLKEEYDrvekelsklqrELAEAEAQARASE 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 106-195 7.70e-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: 38.50  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438    106 IPDLKAKLQNVSDEEKELEQQLKKLLAEEEQLDLDLQTKRRTAEAASEKSGELWKKYRDNLRQVFEDQDELHSLEAERQY 185
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90
                   ....*....|
gi 17542438    186 AEVQHRKLTD 195
Cdd:TIGR02168  759 LEAEIEELEE 768
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-188 9.57e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.97  E-value: 9.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542438   70 DALRNEMDAQVATLDDEIKTYQTYINYLKE--NHPTTS--IPDLKAKLQNV---SDEEKELEQQLKKLLAEEEQLDL--- 139
Cdd:COG4913  630 EERLEALEAELDALQERREALQRLAEYSWDeiDVASAEreIAELEAELERLdasSDDLAALEEQLEELEAELEELEEeld 709

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 17542438  140 DLQTKRRTAEAASEKSGELWKKYRDNLRQVFEDQDELHSLEAERQYAEV 188
Cdd:COG4913  710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
 
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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