ID   PR6AB_XENLA             Reviewed;         404 AA.
AC   O42586;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=26S proteasome regulatory subunit 6A-B;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT5-B;
DE   AltName: Full=Proteasome 26S subunit ATPase 3-B;
DE   AltName: Full=Tat-binding protein 10;
DE            Short=TBP-10;
GN   Name=psmc3-b; Synonyms=tbp10;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9375782; DOI=10.1016/s0167-4781(97)00109-7;
RA   Nacken W.;
RT   "Members of the AAA-gene family are involved in early embryogenesis of
RT   vertebrates.";
RL   Biochim. Biophys. Acta 1354:1-6(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   -!- SUBUNIT: May form a heterodimer with a related family member.
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; Y10460; CAA71486.1; -; mRNA.
DR   AlphaFoldDB; O42586; -.
DR   SMR; O42586; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..404
FT                   /note="26S proteasome regulatory subunit 6A-B"
FT                   /id="PRO_0000084702"
FT   BINDING         192..199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   404 AA;  45276 MW;  FC988BBBDCEFC2E3 CRC64;
     MSTEEIIQRT RLLDSEIKIM KSEVLRVTHE LQAMRDKIKE NSEKIKVNKT LPYLVSNVIE
     LLDVDPNDQE EDGANIDLDS QRKGKCAVIK TSTRQTYFLP VIGLVDAEKL KPGDLVGVNK
     DSYLILETLP TEYDSRVKAM EVDERPTEQY SDIGGLDKQI QELVEAIVLP MNHKEKFENL
     GIQPPKGVLM YGPPGTGKTL LARACAAQTK ATFLKLAGPQ LVQMFIGDGA KLVRDAFSLA
     KEKAPSIIFI DELDAIGNKR FDSEKAGDRE VQRTMLELLN QLDGFQPTTQ VKVIAATNRV
     DILDPALLRS GRLDRKIEFP MPNEEARARI MQIHSRKMNV SPDVNYEELA RCTDDFNGAQ
     CKAVCVEAGI IALRRGATEL THEDYMEGIL EVQAKKKANL QYYA