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Conserved domains on  [gi|290560746|ref|NP_004698|]
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ubiquitin-like protein ATG12 isoform 1 [Homo sapiens]

Protein Classification

ubiquitin-like protein ATG12( domain architecture ID 10108002)

ubiquitin-like protein ATG12 is involved in autophagy vesicle formation and is localized at the developing autophagosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_ATG12 cd01612
ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an ...
 54-139 7.55e-55

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: 166.54  E-value: 7.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290560746  54 KIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHY 133
Cdd:cd01612    1 KVVVLFKAVGDAPILKQKKFKVSASQKFASVIDFLRKQLKLKPSESLFLYINQSFAPSPDEEVGDLYDCFGSNGKLVLNY 80


                 ....*.
gi 290560746 134 CKSQAW 139
Cdd:cd01612   81 CKTPAW 86
 
Name Accession Description Interval E-value
Ubl_ATG12 cd01612
ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an ...
 54-139 7.55e-55

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: 166.54  E-value: 7.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290560746  54 KIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHY 133
Cdd:cd01612    1 KVVVLFKAVGDAPILKQKKFKVSASQKFASVIDFLRKQLKLKPSESLFLYINQSFAPSPDEEVGDLYDCFGSNGKLVLNY 80


                 ....*.
gi 290560746 134 CKSQAW 139
Cdd:cd01612   81 CKTPAW 86
APG12 pfam04110
Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of ...
 54-140 2.34e-53

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: 162.97  E-value: 2.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290560746   54 KIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHY 133
Cdd:pfam04110   1 KITIRLRAIGDAPILKKSKFKVNPSQTFASVILFLKKFLKLQASDSLFLYVNNSFAPSPDQIVGNLYECFGTDGKLVLNY 80


                  ....*..
gi 290560746  134 CKSQAWG 140
Cdd:pfam04110  81 CISVAWG 87
 
Name Accession Description Interval E-value
Ubl_ATG12 cd01612
ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an ...
 54-139 7.55e-55

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: 166.54  E-value: 7.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290560746  54 KIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHY 133
Cdd:cd01612    1 KVVVLFKAVGDAPILKQKKFKVSASQKFASVIDFLRKQLKLKPSESLFLYINQSFAPSPDEEVGDLYDCFGSNGKLVLNY 80


                 ....*.
gi 290560746 134 CKSQAW 139
Cdd:cd01612   81 CKTPAW 86
APG12 pfam04110
Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of ...
 54-140 2.34e-53

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: 162.97  E-value: 2.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290560746   54 KIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHY 133
Cdd:pfam04110   1 KITIRLRAIGDAPILKKSKFKVNPSQTFASVILFLKKFLKLQASDSLFLYVNNSFAPSPDQIVGNLYECFGTDGKLVLNY 80


                  ....*..
gi 290560746  134 CKSQAWG 140
Cdd:pfam04110  81 CISVAWG 87
Ubl_Autophagy_like cd01611
ubiquitin-like (Ubl) domain found in autophagy-related ubiquitin-like protein; Autophagy is an ...
 54-135 3.10e-37

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: 122.15  E-value: 3.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290560746  54 KIDILLKAVGDT--PIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQsFAPSPDQEVGTLYECFGS-DGKLV 130
Cdd:cd01611    1 KIPVILEKAGKTkiPILDKKKYLVPRDLTVGQLIDFIRKRLKLVAEEALFIFVNQ-FAPPTSAEMGTLYEEHGDeDGFLY 79


                 ....*
gi 290560746 131 LHYCK 135
Cdd:cd01611   80 LHYSK 84
Ubl_ATG8_like cd16108
ubiquitin-like (Ubl) domain found in autophagy-related 8 (ATG8) and similar proteins; The ATG8 ...
 64-134 6.52e-04

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: 36.40  E-value: 6.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290560746  64 DTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSfAPSPDQEVGTLYECF-GSDGKLVLHYC 134
Cdd:cd16108   14 DLPDIDKKKFLVPSDLTVGQFMYIIRKRIKLSPEKAIFLFVNNT-LPPTSALMSEVYEEYkDEDGFLYVKYS 84
ATG8 pfam02991
Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a ...
 57-140 9.60e-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: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290560746   57 ILLKAVG-DTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFaPSPDQEVGTLYECF-GSDGKLVLHYC 134
Cdd:pfam02991  20 IIEKASGsDLPDIDKKKYLVPADLTVGQFIYIIRKRIQLRPEKAIFLFVNNTL-PPTSATMSALYEEEkDEDGFLYMVYS 98


                  ....*.
gi 290560746  135 KSQAWG 140
Cdd:pfam02991  99 GENTFG 104
 
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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