ID   PRS6B_ASPNG             Reviewed;         423 AA.
AC   P78578;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=26S proteasome regulatory subunit 6B homolog;
GN   Name=tbpA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RA   Deleu C., Jarai G., Buxton F.;
RT   "Cloning and characterization of the tbpA gene of A. niger homologue of the
RT   human TBP-7 gene encoding the subunit 6 of the 26S proteasome.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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; U15601; AAB40510.1; -; Genomic_DNA.
DR   AlphaFoldDB; P78578; -.
DR   SMR; P78578; -.
DR   STRING; 5061.CADANGAP00002173; -.
DR   PRIDE; P78578; -.
DR   VEuPathDB; FungiDB:An02g07190; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1144750; -.
DR   VEuPathDB; FungiDB:ATCC64974_56930; -.
DR   VEuPathDB; FungiDB:M747DRAFT_315407; -.
DR   eggNOG; KOG0727; Eukaryota.
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; 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; IPR035256; PSMC4.
DR   PANTHER; PTHR23073:SF120; PTHR23073:SF120; 1.
DR   Pfam; PF00004; AAA; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome.
FT   CHAIN           1..423
FT                   /note="26S proteasome regulatory subunit 6B homolog"
FT                   /id="PRO_0000084694"
FT   BINDING         207..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  47223 MW;  2127A643349DD1DD CRC64;
     MGDVAVETPA NNVTPLTKAA PLDTIPNIDS LEGTGNDGSD EYATLKRLQR HLEYIQLQEE
     YIKDEQRSLK RELVRAQEEI KRIQSVPLVI GQFMEAIDQN TGIVQSSTGS NYVVRILSTL
     DREKLKPSSS VALHRHSNAL VDILPPEADS SIAMLGENEK PDVTYADVGG LDMQKQEIRE
     AVELPLTQFD LYKQIGIDPP RGVLLYGPPG TGKTMLVKAV ANSTTASFIR VNGSEFVQKY
     LGEGPRMVRD VFRMARENSP AIIFIDEIDA IATKRFDAQT GADREVQRIL LELLNQMDGF
     EQSSNVKVIM ATNRADTLDP ALLRPGRLDR KIEFPSLRDR RERRLIFSTI ASKMSLSPEV
     DLDSLIVRNE PLSGAVIAAI MQEAGLRAVR KNRYNIIPRS DLEDAYAAQV KTGQEADRLE
     FYR