ID   PRS6B_MANSE             Reviewed;         415 AA.
AC   P46507;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=26S proteasome regulatory subunit 6B;
DE   AltName: Full=ATPase MS73;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Intersegmental muscle;
RX   PubMed=7829521; DOI=10.1074/jbc.270.4.1850;
RA   Dawson S.P., Arnold J.E., Mayer N.J., Reynolds S.E., Billett M.A.,
RA   Gordon C., Colleaux L., Kloetzel P.-M., Tanaka K., Mayer R.J.;
RT   "Developmental changes of the 26 S proteasome in abdominal intersegmental
RT   muscles of Manduca sexta during programmed cell death.";
RL   J. Biol. Chem. 270:1850-1858(1995).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expression of the gene dramatically increases in
CC       the pre-eclosion period.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; Z38135; CAA86294.1; -; mRNA.
DR   AlphaFoldDB; P46507; -.
DR   SMR; P46507; -.
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   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; 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.
FT   CHAIN           1..415
FT                   /note="26S proteasome regulatory subunit 6B"
FT                   /id="PRO_0000084689"
FT   BINDING         203..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   415 AA;  47054 MW;  9A8656016EAD7137 CRC64;
     MEEIGIILPE KDDQVTDAKG LPFAGPQTFD ELESEDLYTK YKKLQRMLEF LEVQEEYIKD
     EQRNLKKEYL HAQEEVKRIQ SVPLVIGQFL EAVDQNTGIV GSTTGSNYYV RILSTIDREL
     LKPSASVALH KHSNALVDVL PPEADSSISM LQADEKPDVQ YSDIGGMDTQ KQEIREAVEL
     PLTHVELYRQ IGIEPPRGVL MYGPPGCGKT MLANAVAHHT TAAFIRVVGS EFVQKYLGEG
     PRMVRDVFRL AKENSPAIIF IDEIDAIATK RFDAQTGADR EVQRILLELL NQMDGFDQTT
     NVKVIMATNR ADTLDPALLR PGRLDRKIEF PLPDRRQKRL IFSTITAKMN LSEEVDLEEF
     VARPDRVSGA DINAICQEAG MNAVRENRYI VLPKDFEKGY KNNIKKDESE YEFYK