ID   PRS7_SPIOL              Reviewed;         426 AA.
AC   Q41365;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 80.
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;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9207846; DOI=10.1023/a:1005839501822;
RA   Ito N., Tomizawa K., Tanaka K., Matsui M., Kendrick R.E., Sato T.,
RA   Nakagawa H.;
RT   "Characterization of 26S proteasome alpha- and beta-type and ATPase
RT   subunits from spinach and their expression during early stages of seedling
RT   development.";
RL   Plant Mol. Biol. 34:307-316(1997).
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; D86121; BAA13021.1; -; mRNA.
DR   PIR; T09104; T09104.
DR   AlphaFoldDB; Q41365; -.
DR   SMR; Q41365; -.
DR   PRIDE; Q41365; -.
DR   OrthoDB; 571919at2759; -.
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..426
FT                   /note="26S proteasome regulatory subunit 7"
FT                   /id="PRO_0000084717"
FT   BINDING         209..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   426 AA;  47719 MW;  FD971FDE13E98DC2 CRC64;
     MAIEHEDDLK DEKNPRPLDE DDIALLKTYG LGPYSASIKK VEKEIKDMSK KVNDLIGIKE
     SDTGLAAPSQ WDLVSDKQMM QEEQPLQVAR CTKIINPNTE DAKYVINVKQ IAKFVVGLGD
     KVSPTDIEEG MRVGVDRNKY QIQIPLPPKI DPSVTMMTVE EKPDVTYNDV GGCKEQIEKM
     REVVELPMLH PEKFVKLGID PPKGVLCYGP PGTGKTLLAR AVANRTDACF IRVIGSELVQ
     KYVGEGARMV RELFQMARSK KACIVFFDEV DAIGGARFDD GVGGDNEVQR TMLEIVNQLD
     GFDARGNIKV LMATNRPDTL DPALLRPGRL DRKVEFGLPD LEGRTQIFKI HTRTMNCERD
     IRFELLARLC PNSTGADIRS VCTEAGMYAI RARRKTVTEK DFLDAVNKVI KGYQKFSATP
     KYMVYN