ID   PSMA_METJA     STANDARD;      PRT;   261 AA.
AC   Q60177;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   28-FEB-2003 (Rel. 41, Last annotation update)
DE   Proteasome alpha subunit (EC 3.4.25.1) (Multicatalytic endopeptidase
DE   complex alpha subunit) (20S proteasome alpha subunit).
GN   PSMA OR MJ0591.
OS   Methanococcus jannaschii.
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=2190;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=JAL-1 / DSM 2661 / ATCC 43067;
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;
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 at 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: Cytoplasmic.
CC   -!- SIMILARITY: Belongs to peptidase family T1A.
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DR   EMBL; U67507; AAB98581.1; -.
DR   PIR; G64373; G64373.
DR   HSSP; P25156; 1PMA.
DR   MEROPS; T01.UNW; -.
DR   TIGR; MJ0591; -.
DR   HAMAP; MF_00289; -; 1.
DR   InterPro; IPR000426; Proteasome_A.
DR   InterPro; IPR001353; Protsme_protease.
DR   Pfam; PF00227; proteasome; 1.
DR   PROSITE; PS00388; PROTEASOME_A; 1.
KW   Proteasome; Hydrolase; Protease; Complete proteome.
SQ   SEQUENCE   261 AA;  29320 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
//