UniProt functional annotation for Q60177



	UniProt functional annotation for Q60177

UniProt code: Q60177.

Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii).

Taxonomy: Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus.

Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin- like activity. {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:10692374}.

Activity regulation: The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close- gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity. {ECO:0000255|HAMAP-Rule:MF_00289}.

Subunit: The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN. {ECO:0000255|HAMAP-Rule:MF_00289, ECO:0000269|PubMed:10692374, ECO:0000269|PubMed:19481527}.

Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.

Similarity: Belongs to the peptidase T1A family. {ECO:0000255|HAMAP- Rule:MF_00289}.

Annotations taken from UniProtKB at the EBI.


Organism:		Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
Taxonomy:		Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus.



Function:		Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin- like activity. {ECO:0000255\|HAMAP-Rule:MF_00289, ECO:0000269\|PubMed:10692374}.


Activity regulation:		The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close- gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity. {ECO:0000255\|HAMAP-Rule:MF_00289}.
Subunit:		The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN. {ECO:0000255\|HAMAP-Rule:MF_00289, ECO:0000269\|PubMed:10692374, ECO:0000269\|PubMed:19481527}.
Subcellular location:		Cytoplasm {ECO:0000255\|HAMAP-Rule:MF_00289}.
Similarity:		Belongs to the peptidase T1A family. {ECO:0000255\|HAMAP- Rule:MF_00289}.