PRS6A_ENCCU
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 03-AUG-2022, entry version 115.
DE RecName: Full=26S proteasome regulatory subunit 6A;
GN Name=RPT5; OrderedLocusNames=ECU10_1420;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC 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., Weissenbach J.,
RA 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 cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT 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 and for
CC the removal of misfolded proteins. The proteasome is a multicatalytic
CC proteinase complex that is characterized by its ability to cleave
CC peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC at neutral or slightly basic pH (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AL590449; CAD25861.1; -; Genomic_DNA.
DR RefSeq; NP_586257.1; NM_001042090.1.
DR AlphaFoldDB; Q8SR13; -.
DR SMR; Q8SR13; -.
DR STRING; 284813.Q8SR13; -.
DR GeneID; 859907; -.
DR KEGG; ecu:ECU10_1420; -.
DR VEuPathDB; MicrosporidiaDB:ECU10_1420; -.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; Q8SR13; -.
DR OMA; HEKAAMG; -.
DR OrthoDB; 571919at2759; -.
DR Proteomes; UP000000819; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR035254; PSMC3.
DR PANTHER; PTHR23073:SF90; PTHR23073:SF90; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1..401
FT /note="26S proteasome regulatory subunit 6A"
FT /id="PRO_0000382905"
FT BINDING 189..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
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