SMART: Pfam domain Autophagy_act

The domain within your query sequence starts at position 95 and ends at position 162; the E-value for the Autophagy_act_C domain shown below is 9.1e-19.

VLYSCSYQVPVLYFRASFLDGRPLALEDIWEGVHECYKPRLLQGPWDTITQQEHPILGQP
FFVLHPCK

Autophagy_act_C

PFAM accession number:	PF03987
Interpro abstract (IPR007135):	Proteins in this entry belong to the Atg3 group of proteins and the Atg3 conjugation enzymes. Autophagy is a degradative transport pathway that delivers cytosolic proteins to the lysosome (vacuole) [ (PUBMED:11058089) ] and is induced by starvation [ (PUBMED:9190802) ]. Cytosolic proteins appear inside the vacuole enclosed in autophagic vesicles. Autophagy significantly differs from other transport pathways by using double membrane layered transport intermediates, called autophagosomes [ (PUBMED:11675007) (PUBMED:18472412) ]. The breakdown of vesicular transport intermediates is a unique feature of autophagy [ (PUBMED:11058089) ]. Autophagy can also function in the elimination of invading bacteria and antigens [ (PUBMED:18472412) ]. Atg3 is the E2 enzyme for the LC3 lipidation process [ (PUBMED:18321988) ]. It is essential for autophagocytosis. The super protein complex, the Atg16L complex, consists of multiple Atg12-Atg5 conjugates. Atg16L has an E3-like role in the LC3 lipidation reaction. The activated intermediate, LC3-Atg3 (E2), is recruited to the site where the lipidation takes place [ (PUBMED:18398292) ]. Atg3 catalyses the conjugation of Atg8 and phosphatidylethanolamine (PE). Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region and another with a long alpha-helical structure that protrudes from the core region as far as 30 A [ (PUBMED:17227760) ]. It interacts with atg8 through an intermediate thioester bond between Cys-288 and the C-terminal Gly of atg8. It also interacts with the C-terminal region of the E1-like atg7 enzyme. Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. The cysteine residue within the HPC motif is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex [ (PUBMED:12482611) ].

PFAM accession number:

PF03987

Interpro abstract (IPR007135):

Proteins in this entry belong to the Atg3 group of proteins and the Atg3 conjugation enzymes.

Autophagy is a degradative transport pathway that delivers cytosolic proteins to the lysosome (vacuole) [ (PUBMED:11058089) ] and is induced by starvation [ (PUBMED:9190802) ]. Cytosolic proteins appear inside the vacuole enclosed in autophagic vesicles. Autophagy significantly differs from other transport pathways by using double membrane layered transport intermediates, called autophagosomes [ (PUBMED:11675007) (PUBMED:18472412) ]. The breakdown of vesicular transport intermediates is a unique feature of autophagy [ (PUBMED:11058089) ]. Autophagy can also function in the elimination of invading bacteria and antigens [ (PUBMED:18472412) ].

Atg3 is the E2 enzyme for the LC3 lipidation process [ (PUBMED:18321988) ]. It is essential for autophagocytosis. The super protein complex, the Atg16L complex, consists of multiple Atg12-Atg5 conjugates. Atg16L has an E3-like role in the LC3 lipidation reaction. The activated intermediate, LC3-Atg3 (E2), is recruited to the site where the lipidation takes place [ (PUBMED:18398292) ].

Atg3 catalyses the conjugation of Atg8 and phosphatidylethanolamine (PE). Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region and another with a long alpha-helical structure that protrudes from the core region as far as 30 A [ (PUBMED:17227760) ]. It interacts with atg8 through an intermediate thioester bond between Cys-288 and the C-terminal Gly of atg8. It also interacts with the C-terminal region of the E1-like atg7 enzyme.

Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. The cysteine residue within the HPC motif is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex [ (PUBMED:12482611) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Autophagy_act_C