ID PSMA_METJA Reviewed; 261 AA. AC Q60177; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 06-MAR-2007, entry version 47. DE Proteasome alpha subunit (EC 3.4.25.1) (Multicatalytic endopeptidase DE complex alpha subunit) (20S proteasome alpha subunit). GN Name=psmA; OrderedLocusNames=MJ0591; OS Methanococcus jannaschii. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=2190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX MEDLINE=96337999; PubMed=8688087; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX MEDLINE=20158885; PubMed=10692374; RX DOI=10.1128/JB.182.6.1680-1692.2000; RA Wilson H.L., Ou M.S., Aldrich H.C., Maupin-Furlow J.; RT "Biochemical and physical properties of the Methanococcus jannaschii RT 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the RT eucaryal 26S proteasome."; RL J. Bacteriol. 182:1680-1692(2000). CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex CC which is characterized by its ability to cleave peptides with Arg, CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or CC slightly basic pH. CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. CC -!- SUBUNIT: Composed of two subunits, alpha and beta. The complex is CC formed of four rings. The two outer rings are each composed of CC seven alpha subunits. The two inner rings are each composed of CC seven beta subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the peptidase T1A family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L77117; AAB98581.1; -; Genomic_DNA. DR PIR; G64373; G64373. DR HSSP; O29760; 1J2Q. DR GenomeReviews; L77117_GR; MJ0591. DR KEGG; mja:MJ0591; -. DR TIGR; MJ0591; -. DR BioCyc; MJAN243232:MJ0591-MONOMER; -. DR GO; GO:0004298; F:threonine endopeptidase activity; IEA:HAMAP. DR HAMAP; MF_00289; -; 1. DR InterPro; IPR001353; Proteasome_A_B. DR InterPro; IPR000426; Proteasome_alpha. DR Pfam; PF00227; Proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Complete proteome; Hydrolase; Protease; Proteasome; KW Threonine protease. FT CHAIN 1 261 Proteasome alpha subunit. FT /FTId=PRO_0000124174. SQ SEQUENCE 261 AA; 29321 MW; 93FC7DF277E01AD8 CRC64; MQMVPPSAYD RAITVFSPEG RLYQVEYARE AVRRGTTAIG IACKDGVVLA VDRRITSKLV KIRSIEKIFQ IDDHVAAATS GLVADARVLI DRARLEAQIY RLTYGEEISI EMLAKKICDI KQAYTQHGGV RPFGVSLLIA GIDKNEARLF ETDPSGALIE YKATAIGSGR PVVMELLEKE YRDDITLDEG LELAITALTK ANEDIKPENV DVCIITVKDA QFKKIPVEEI KKLIEKVKKK LNEENKKEEE NREETKEKQE E //