ID   PRS7_PRUPE              Reviewed;         425 AA.
AC   O64982;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=26S proteasome regulatory subunit 7;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT1;
DE   AltName: Full=26S proteasome subunit 7;
DE   AltName: Full=Regulatory particle triple-A ATPase subunit 1;
GN   Name=RPT1; Synonyms=PS7;
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fruit;
RA   Bassett C.L., Artlip T.S., Nickerson M.L., Wilson C.W., Hixson C.V.;
RT   "Cloning of a 26S proteasome subunit 7 homologue from peach.";
RL   (er) Plant Gene Register PGR98-082(1998).
CC   -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC       complex confers ATP dependency and substrate specificity to the 26S
CC       complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; AF041258; AAC18523.1; -; mRNA.
DR   RefSeq; XP_007215431.1; XM_007215369.1.
DR   AlphaFoldDB; O64982; -.
DR   SMR; O64982; -.
DR   STRING; 3760.EMJ16630; -.
DR   EnsemblPlants; ONI15199; ONI15199; PRUPE_3G030100.
DR   GeneID; 18783658; -.
DR   Gramene; ONI15199; ONI15199; PRUPE_3G030100.
DR   KEGG; pper:18783658; -.
DR   eggNOG; KOG0729; Eukaryota.
DR   HOGENOM; CLU_000688_6_1_1; -.
DR   OMA; INGYKKF; -.
DR   OrthoDB; 571919at2759; -.
DR   PhylomeDB; O64982; -.
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: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   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome.
FT   CHAIN           1..425
FT                   /note="26S proteasome regulatory subunit 7"
FT                   /id="PRO_0000084716"
FT   BINDING         208..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   425 AA;  47558 MW;  28E5DDCCB1945EF9 CRC64;
     MAPEPEDIKD EKNPRPLDED DIALLKTYGL GPYSTHIKKA EKEVKDLAKK VNDLCGIKES
     DTGLAAPSQW DLVSDKQMMQ EEQPLQVARC TKIINPNSED AKYVINVKQI AKFVVGLGDK
     VSPTDIEEGM RVGVDRNKYQ IQIPLPPKID PSVTMMTVEE KPDVTYNDVG GCKEQIEKMR
     EVVELPMLHP EKFVKLGIDP PKGVLCYGPP GTGKTLLARA VANRTDACFI RVIGSELVQK
     YVGEGARMVR ELFQMARSKK ACIVFFDEVD AIGGARFDDG VGGDNEVQRT MLEIVNQLDG
     FDARGNIKVL MATNRPDTLD PALLRPGRLD RKVEFGLPDL ESRTQIFKIH TRTMNCERDI
     RFELLARLCP NSTGADIRSV CTEAGMYAIR ARRKTVTEKD FLDAVNKVIK GYQKFSATPK
     YMVYN