ID   PRS8_ENCCU              Reviewed;         392 AA.
AC   Q8SQK0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=26S proteasome regulatory subunit 8 homolog;
GN   Name=RPT6; OrderedLocusNames=ECU09_1840;
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   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [3]
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; AL590451; CAD27157.2; -; Genomic_DNA.
DR   RefSeq; XP_955738.1; XM_950645.1.
DR   AlphaFoldDB; Q8SQK0; -.
DR   SMR; Q8SQK0; -.
DR   STRING; 284813.Q8SQK0; -.
DR   GeneID; 860525; -.
DR   KEGG; ecu:ECU09_1840; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_1840; -.
DR   HOGENOM; CLU_000688_2_0_1; -.
DR   InParanoid; Q8SQK0; -.
DR   OrthoDB; 571919at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
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; IPR035261; PSMC5.
DR   PANTHER; PTHR23073:SF102; PTHR23073:SF102; 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..392
FT                   /note="26S proteasome regulatory subunit 8 homolog"
FT                   /id="PRO_0000382906"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   392 AA;  44160 MW;  52733ACA374FA0F4 CRC64;
     MAEGFCKNFY SNKLDHLEVQ IAKKTKILRV LEQKRAELNR RVRFLREEIS IVQEPSSNVG
     VVVEKMGKMQ VLVKTNPDGK YLVKVEPGVN YDELKAGVRV ALRSDSYDVH RILPTKVDPL
     VSLMMVEKVP DSTYQMIGGL DEQIKEIREV IELPIKHPEL FENLGIAQPK GVLLYGPPGT
     GKTLLARAVA HHTQCKFIRV SGSELVQKYI GEGSRLVREL FIMAREHAPS IIFMDEIDSI
     GSTRGDSNKG SDSEVQRTML ELLNQLDGFE SHNNIKVIMA TNRIDILDPA LLRTGRIDRK
     IEFPPPNESA RLEILKIHSR KMNLTKGIDL ETIASKMVGC SGAEVKAVCT EAGMYALRER
     RVHVTQEDFE MAVHKVLKKT GDLNSDLRKL LK