ID   PRS6A_ENCCU             Reviewed;         401 AA.
AC   Q8SR13;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   01-MAY-2013, entry version 72.
DE   RecName: Full=26S protease regulatory subunit 6A;
GN   Name=RPT5; OrderedLocusNames=ECU10_1420;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Microsporidia; Unikaryonidae; Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M.,
RA   Weissenbach J., Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon
RT   cuniculi (microsporidia): a reference map for proteins expressed in
RT   late sporogonial stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which
CC       degrades poly-ubiquitinated proteins in the cytoplasm and in the
CC       nucleus. It is essential for the regulated turnover of proteins
CC       and for the removal of misfolded proteins. The proteasome is a
CC       multicatalytic proteinase complex that is characterized by its
CC       ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu
CC       adjacent to the leaving group at neutral or slightly basic pH (By
CC       similarity).
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC       two 19S regulatory subunits. The 20S proteasome core is composed
CC       of 28 subunits that are arranged in four stacked rings, resulting
CC       in a barrel-shaped structure. The two end rings are each formed by
CC       seven alpha subunits, and the two central rings are each formed by
CC       seven beta subunits. The catalytic chamber with the active sites
CC       is on the inside of the barrel (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR   EMBL; AL590449; CAD25861.1; -; Genomic_DNA.
DR   RefSeq; NP_586257.1; NM_001042090.1.
DR   HSSP; Q01853; 1YPW.
DR   ProteinModelPortal; Q8SR13; -.
DR   STRING; 6035.ECU10_1420; -.
DR   GeneID; 859907; -.
DR   KEGG; ecu:ECU10_1420; -.
DR   eggNOG; COG1222; -.
DR   HOGENOM; HOG000225143; -.
DR   KO; K03065; -.
DR   OMA; GALMYGP; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   InterPro; IPR005937; 26S_Psome_P45.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding;
KW   Nucleus; Proteasome; Reference proteome.
FT   CHAIN         1    401       26S protease regulatory subunit 6A.
FT                                /FTId=PRO_0000382905.
FT   NP_BIND     189    196       ATP (Potential).
SQ   SEQUENCE   401 AA;  44870 MW;  7A9ED4721D9775BC CRC64;
     MSLEELEAMD QSNPGEFLER VREKIRMLNS ETRILQSRVN TIKHDISTKN ASIAENMERI
     RLNKQLPYLV GNVVEVLDEH SGVVNASTRM SSYLPITGLI PNSELRPGDL VALHKDTNIV
     FEKLPPDYDM KVGGMVLKSD AKPDETYEDI GGLERQIEEL NEAIVLSLTH PERFEKLNIK
     PPKGVLMYGP PGTGKTLMAR ACASKTNATF LKLAGPQLVQ MYIGDGARLV RDAFALAKER
     KPTIIFIDEI DAIGAKRSDS DQTGDREVQR TMLELLNQLD GFSSSEEVKI IAATNRVDIL
     DPALLRSGRL DRKIEFPLPN TLGRKRILQI HARKMSVRDD VNFDELARST EGFNGAQCKA
     VCVEAGMAAL RKEKTEISQN DFMDGIQEVL SRKKSKLLYF T
//