NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|66771003|gb|AAY54813|]
View 

IP05405p [Drosophila melanogaster]

Protein Classification

APG12_C domain-containing protein( domain architecture ID 10513777)

APG12_C domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
APG12 pfam04110
Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of ...
 25-111 3.79e-51

Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. The Apg12 system is one of the ubiquitin-like protein conjugation systems conserved in eukaryotes. It was first discovered in yeast during systematic analyses of the apg mutants defective in autophagy. Covalent attachment of Apg12-Apg5 is essential for autophagy.


:

Pssm-ID: 397985  Cd Length: 87  Bit Score: 156.03  E-value: 3.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66771003    25 KICILLNATGNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPDQIIKNLYECHGTNGKLVLYY 104
Cdd:pfam04110   1 KITIRLRAIGDAPILKKSKFKVNPSQTFASVILFLKKFLKLQASDSLFLYVNNSFAPSPDQIVGNLYECFGTDGKLVLNY 80


                  ....*..
gi 66771003   105 CKNQAWG 111
Cdd:pfam04110  81 CISVAWG 87
 
Name Accession Description Interval E-value
APG12 pfam04110
Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of ...
 25-111 3.79e-51

Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. The Apg12 system is one of the ubiquitin-like protein conjugation systems conserved in eukaryotes. It was first discovered in yeast during systematic analyses of the apg mutants defective in autophagy. Covalent attachment of Apg12-Apg5 is essential for autophagy.


Pssm-ID: 397985  Cd Length: 87  Bit Score: 156.03  E-value: 3.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66771003    25 KICILLNATGNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPDQIIKNLYECHGTNGKLVLYY 104
Cdd:pfam04110   1 KITIRLRAIGDAPILKKSKFKVNPSQTFASVILFLKKFLKLQASDSLFLYVNNSFAPSPDQIVGNLYECFGTDGKLVLNY 80


                  ....*..
gi 66771003   105 CKNQAWG 111
Cdd:pfam04110  81 CISVAWG 87
Ubl_ATG12 cd01612
ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an ...
 25-110 5.59e-47

ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like (Ubl) proteins such as ATG12 protein have a conserved Ubl fold structure and undergo a unique Ubl conjugation, a process essential for autophagosome formation. ATG12 is conjugated to ATG5 by multistep modifications of the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG10. The ATG12-ATG5 conjugate facilitates the lipidation of ATG8 and directs its correct subcellular localization. ATG12 is localized at the developing autophagosome.


Pssm-ID: 340454  Cd Length: 86  Bit Score: 145.35  E-value: 5.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66771003  25 KICILLNATGNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPDQIIKNLYECHGTNGKLVLYY 104
Cdd:cd01612   1 KVVVLFKAVGDAPILKQKKFKVSASQKFASVIDFLRKQLKLKPSESLFLYINQSFAPSPDEEVGDLYDCFGSNGKLVLNY 80


                ....*.
gi 66771003 105 CKNQAW 110
Cdd:cd01612  81 CKTPAW 86
 
Name Accession Description Interval E-value
APG12 pfam04110
Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of ...
 25-111 3.79e-51

Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. The Apg12 system is one of the ubiquitin-like protein conjugation systems conserved in eukaryotes. It was first discovered in yeast during systematic analyses of the apg mutants defective in autophagy. Covalent attachment of Apg12-Apg5 is essential for autophagy.


Pssm-ID: 397985  Cd Length: 87  Bit Score: 156.03  E-value: 3.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66771003    25 KICILLNATGNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPDQIIKNLYECHGTNGKLVLYY 104
Cdd:pfam04110   1 KITIRLRAIGDAPILKKSKFKVNPSQTFASVILFLKKFLKLQASDSLFLYVNNSFAPSPDQIVGNLYECFGTDGKLVLNY 80


                  ....*..
gi 66771003   105 CKNQAWG 111
Cdd:pfam04110  81 CISVAWG 87
Ubl_ATG12 cd01612
ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an ...
 25-110 5.59e-47

ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like (Ubl) proteins such as ATG12 protein have a conserved Ubl fold structure and undergo a unique Ubl conjugation, a process essential for autophagosome formation. ATG12 is conjugated to ATG5 by multistep modifications of the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG10. The ATG12-ATG5 conjugate facilitates the lipidation of ATG8 and directs its correct subcellular localization. ATG12 is localized at the developing autophagosome.


Pssm-ID: 340454  Cd Length: 86  Bit Score: 145.35  E-value: 5.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66771003  25 KICILLNATGNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPDQIIKNLYECHGTNGKLVLYY 104
Cdd:cd01612   1 KVVVLFKAVGDAPILKQKKFKVSASQKFASVIDFLRKQLKLKPSESLFLYINQSFAPSPDEEVGDLYDCFGSNGKLVLNY 80


                ....*.
gi 66771003 105 CKNQAW 110
Cdd:cd01612  81 CKTPAW 86
Ubl_Autophagy_like cd01611
ubiquitin-like (Ubl) domain found in autophagy-related ubiquitin-like protein; Autophagy is an ...
 25-106 6.49e-21

ubiquitin-like (Ubl) domain found in autophagy-related ubiquitin-like protein; Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like proteins, such as Saccharomyces cerevisiae Atg8p, undergo a unique ubiquitin-like (Ubl) conjugation, a process essential for autophagosome formation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. ATG8 family proteins undergo multistep modifications by the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG3. The mammalian ATG8 family is classified into three subfamilies: i) MAP1LC3 (microtubule associated protein 1 light chain 3) which includes MAP1LC3A, MAP1LC3B, MAP1LC3B2, and MAP1LC3C, ii) GABARAP (GABA type A receptor associated protein) which includes GABARAP, GABARAPL1, and GABARAPL3, and iii) GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa).


Pssm-ID: 340453  Cd Length: 84  Bit Score: 79.40  E-value: 6.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66771003  25 KICILLNATG--NVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQtFAPAPDQIIKNLYECHGT-NGKLV 101
Cdd:cd01611   1 KIPVILEKAGktKIPILDKKKYLVPRDLTVGQLIDFIRKRLKLVAEEALFIFVNQ-FAPPTSAEMGTLYEEHGDeDGFLY 79


                ....*
gi 66771003 102 LYYCK 106
Cdd:cd01611  80 LHYSK 84
Ubl_ATG8_like cd16108
ubiquitin-like (Ubl) domain found in autophagy-related 8 (ATG8) and similar proteins; The ATG8 ...
 35-94 2.16e-05

ubiquitin-like (Ubl) domain found in autophagy-related 8 (ATG8) and similar proteins; The ATG8 family of proteins constitute a single member in Saccharomyces cerevisiae, Atg8p, and multiple homologs in higher eukaryotes, they are multifunctional ubiquitin-like (Ubl) key regulators of autophagy. The ATG8 system is a Ubl conjugation system that is essential for autophagosome formation. In the ATG8 system, a cysteine protease (ATG4) cleaves a C-terminal arginine from ATG8, and then the exposed C-terminal glycine is conjugated to phosphatidylethanolamine (PE) by ATG7, an E1-like enzyme, and ATG3, an E2-like enzyme. The mammalian ATG8 family is classified into three subfamilies: i) MAP1LC3 (microtubule associated protein 1 light chain 3) which includes MAP1LC3A, MAP1LC3B, MAP1LC3B2, and MAP1LC3C, ii) GABARAP (GABA type A receptor associated protein) which includes GABARAP, GABARAPL1, and GABARAPL3, and iii) GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa).


Pssm-ID: 340525  Cd Length: 85  Bit Score: 39.48  E-value: 2.16e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66771003  35 NVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTfAPAPDQIIKNLYECH 94
Cdd:cd16108  14 DLPDIDKKKFLVPSDLTVGQFMYIIRKRIKLSPEKAIFLFVNNT-LPPTSALMSEVYEEY 72
Ubl_ATG8 cd16128
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae Atg8p and related proteins; ...
 34-94 7.84e-05

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae Atg8p and related proteins; sub-family of the autophagy-related 8 (ATG8) family; The ATG8 family of proteins constitutes a single member in Saccharomyces cerevisiae, Atg8p, and multiple homologs in higher eukaryotes. These proteins are multifunctional ubiquitin-like (Ubl) key regulators of autophagy. ATG8 is characterized by a C-terminal ubiquitin-like (Ubl) domain with a short N-terminal extension. The covalent attachment of ATG8 to phosphatidylethanolamine (PtdEth) at the autophagosomal membrane places it at a crucial juncture during autophagosome formation. ATG Ubl proteins such as Saccharomyces cerevisiae Atg8p undergo a unique Ubl conjugation, a process essential for autophagosome formation.


Pssm-ID: 340545  Cd Length: 103  Bit Score: 38.60  E-value: 7.84e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66771003  34 GNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPdQIIKNLYECH 94
Cdd:cd16128  29 SDIPDIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVNNVLPPTA-ALMSAIYEEH 88
ATG8 pfam02991
Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a ...
 36-94 4.08e-04

Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a subunit of microtubule associated proteins 1A and 1B and that its expression may regulate microtubule binding activity. Autophagy is generally known as a process involved in the degradation of bulk cytoplasmic components that are non-specifically sequestered into an autophagosome, where they are sequestered into double-membrane vesicles and delivered to the degradative organelle, the lysosome/vacuole, for breakdown and eventual recycling of the resulting macromolecules. The yeast proteins are involved in the autophagosome, and Atg8 binds Atg19, via its N-terminus and the C-terminus of Atg19.


Pssm-ID: 281049  Cd Length: 104  Bit Score: 36.56  E-value: 4.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 66771003    36 VPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFaPAPDQIIKNLYECH 94
Cdd:pfam02991  29 LPDIDKKKYLVPADLTVGQFIYIIRKRIQLRPEKAIFLFVNNTL-PPTSATMSALYEEE 86
NR_LBD_SHP cd07349
The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ...
 28-84 2.09e-03

The ligand binding domain of DAX1 protein, a nuclear receptor lacking DNA binding domain; The ligand binding domain of the Small Heterodimer Partner (SHP): SHP is a member of the nuclear receptor superfamily. SHP has a ligand binding domain, but lacks the DNA binding domain, typical to almost all of the nuclear receptors. It functions as a transcriptional coregulator by directly interacting with other nuclear receptors through its AF-2 motif. The closest relative of SHP is DAX1 and they can form heterodimer. SHP is an orphan receptor, lacking an identified ligand.


Pssm-ID: 132763  Cd Length: 222  Bit Score: 35.95  E-value: 2.09e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66771003  28 ILLNATGNVPIIKKRTWTVDPNKTVGWIQTFIHKFLKLDASEQIFLYVNQTFAPAPD 84
Cdd:cd07349  90 ILLEGQSSSGGSGQPDRPQPSLAAVQWLQCCLNKFWSLDLSPKEYAYLKGTILFNPD 146
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH