ID   PRS6A_SCHPO             Reviewed;         438 AA.
AC   O14126;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=26S proteasome regulatory subunit 6A;
GN   Name=tbp1; Synonyms=pam2; ORFNames=SPAC3A11.12c, SPAC3H5.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 38364 / 968;
RA   Kitamura K., Tsujimoto K., Yamashita I., Shimoda C.;
RT   "Switch from mitotic to meiotic cell cycle is disturbed by strong
RT   activation of Ras-MAP kinase cascade in the fission yeast 26S proteasome-
RT   related mutants.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; AB012136; BAA88693.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB16588.1; -; Genomic_DNA.
DR   PIR; T11634; T11634.
DR   RefSeq; XP_001713083.1; XM_001713031.2.
DR   AlphaFoldDB; O14126; -.
DR   SMR; O14126; -.
DR   BioGRID; 280538; 19.
DR   STRING; 4896.SPAC3A11.12c.1; -.
DR   iPTMnet; O14126; -.
DR   MaxQB; O14126; -.
DR   PaxDb; O14126; -.
DR   PRIDE; O14126; -.
DR   EnsemblFungi; SPAC3A11.12c.1; SPAC3A11.12c.1:pep; SPAC3A11.12c.
DR   PomBase; SPAC3A11.12c; -.
DR   VEuPathDB; FungiDB:SPAC3A11.12c; -.
DR   eggNOG; KOG0652; Eukaryota.
DR   HOGENOM; CLU_000688_2_4_1; -.
DR   InParanoid; O14126; -.
DR   OMA; HEKAAMG; -.
DR   PhylomeDB; O14126; -.
DR   Reactome; R-SPO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR   Reactome; R-SPO-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-SPO-5689603; UCH proteinases.
DR   Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR   Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-SPO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-SPO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   Reactome; R-SPO-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-SPO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:O14126; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IC:PomBase.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR   GO; GO:0036402; F:proteasome-activating activity; ISM:PomBase.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:UniProt.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..438
FT                   /note="26S proteasome regulatory subunit 6A"
FT                   /id="PRO_0000084707"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         226..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   438 AA;  48836 MW;  B3C7863519FB7676 CRC64;
     MSTLEELDAL DQSQQGGSSN NEGLDGIEQE ILAAGIDELN SRTRLLENDI KVMKSEFQRL
     THEKSTMLEK IKENQEKISN NKMLPYLVGN VVEILDMQPD EVDVQESANQ NSEATRVGKS
     AVIKTSTRQT IFLPLIGLVE PEELHPGDLI GVNKDSYLII DKLPSEYDSR VKAMEVDEKP
     TERYSDIGGL SKQIEELFEA IVLPMQQADK FRKLGVKPPK GCLMFGPPGT GKTLLARACA
     AQSNATFLKL AAPQLVQMFI GDGAKLVRDA FALAKEKSPA IIFIDELDAI GTKRFDSEKA
     GDREVQRTML ELLNQLDGFS SDDRVKVIAA TNRVDTLDPA LLRSGRLDRK LEFPLPNEEA
     RVGILRIHSR KMAIDDDINW EELARSTDEY NGAMLKSVCV EAGMIALRQG DTKINHEHFM
     DGILEVQMRK SKTLQYFA