IED ID | IndEnz0002008388 |
Enzyme Type ID | protease008388 |
Protein Name |
Proteasome subunit alpha type-1-A 20S proteasome alpha subunit F-1 Proteasome 30 kDa subunit Proteasome component 2A AtPSM30 Proteasome subunit alpha type-6 Protein ARSENIC TOLERANCE 5 |
Gene Name | PAF1 ARS5 PRC2A PRS1 PSM30 At5g42790 MJB21.17 |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | MFRNQYDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERRFESFGDSSREDLIKDAILAVRETLQGETLKSSLCTVAILGVDEPFHFLDQEAIQKVIDTFEKVPEEEEGEGEAGEGEAEAAEAAPAERGGGVAGDQDVAPMEM |
Enzyme Length | 278 |
Uniprot Accession Number | P34066 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Negatively regulates thiol biosynthesis and arsenic tolerance. {ECO:0000269|PubMed:19453443}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Compositional bias (1); Cross-link (1); Modified residue (1); Region (1); Sequence conflict (7) |
Keywords | Acetylation;Cytoplasm;Isopeptide bond;Nucleus;Proteasome;Reference proteome;Ubl conjugation |
Interact With | |
Induction | INDUCTION: Slightly induced by heat-shock and high intensity light. {ECO:0000269|PubMed:8264533}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. |
Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000269|PubMed:20516081 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12952558; 16055689; 16377752; 17317660; 17335514; 17825468; 18070919; 18650403; 23616927; 26384244; 27130079; 28627464; |
Motif | |
Gene Encoded By | |
Mass | 30,476 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |