IED ID | IndEnz0002012997 |
Enzyme Type ID | protease012997 |
Protein Name |
Tricorn protease-interacting factor F3 EC 3.4.11.- |
Gene Name | trf3 Ta0815 |
Organism | Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
Taxonomic Lineage | cellular organisms Archaea Candidatus Thermoplasmatota Thermoplasmata Thermoplasmatales Thermoplasmataceae Thermoplasma Thermoplasma acidophilum Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
Enzyme Sequence | MEVEKYDLTLDFDIQKRTFNGTETITADAGDIVLDAVGLQINWMKVNGRDTAFTYDGQTVRAPGDSQPQKIEISFAGKVSDSLSGIYYAGRENGMITTHFEATDARRMFPCVDHPAYKAVFAITVVIDKDYDAISNMPPKRIEVSERKVVEFQDTPRMSTYLLYVGIGKFRYEYEKYRDIDLILASLKDIRSKYPLDMARKSVEFYENYFGIPYALPKMHLISVPEFGAGAMENWGAITFREIYMDIAENSAVTVKRNSANVIAHEIAHQWFGDLVTMKWWNDLWLNESFATFMSYKTMDTLFPEWSFWGDFFVSRTSGALRSDSLKNTHPIEVDVRDPDEISQIFDEISYGKGASILRMIEDYAGYEEFRKGISKYLNDHKFGNAEGSDLWTAIEDVSGKPVKRVMEYWIKNPGYPVIKLKRNGRKITMYQTRFLLNGEEEGRWPVPVNIKKKDGVERILLEDEASIEADGLIKINADSAGFYRVLYDDATFSDVMGHYRDLSPLDRIGLVDDLFAFLLSGHIDPETYRQRIRNFFDDEDHNVITAIVGQMEYLRMLTHAFDDDARAFCRSRMQFLTGKQDENLKIALGRVSRLYVMVDESYAEEMSKLFKDFDSAEPEMRSSIATAYALVTGDLKGLLEKFRSVDRDEDRVRIISAFGKLKSNTDLSTVYGMVEKTEIKKQDMISFFSSALETLPGREFIFANLDRIIRLVIRYFTGNRTASRTVEMMIPVIGLDHPDAEDIVRNIGSKNISMGLAKGIEMLAVNRKLVERIRQTAVK |
Enzyme Length | 780 |
Uniprot Accession Number | O93655 |
Absorption | |
Active Site | ACT_SITE 266; /note=Proton acceptor; /evidence=ECO:0000305 |
Activity Regulation | |
Binding Site | BINDING 101; /note=Substrate; /evidence=ECO:0000250 |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.11.- |
Enzyme Function | FUNCTION: Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome), yielding free amino acids. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (31); Binding site (1); Chain (1); Helix (34); Metal binding (3); Region (1); Site (1); Turn (7) |
Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 1Z1W; 1Z5H; 3Q7J; |
Mapped Pubmed ID | 21493078; |
Motif | |
Gene Encoded By | |
Mass | 89,380 |
Kinetics | |
Metal Binding | METAL 265; /note=Zinc; catalytic; METAL 269; /note=Zinc; catalytic; METAL 288; /note=Zinc; catalytic |
Rhea ID | |
Cross Reference Brenda | 3.4.11.7; |