ID   A0A316YFY5_9BASI        Unreviewed;       414 AA.
AC   A0A316YFY5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative RPT3-26S proteasome regulatory subunit {ECO:0000313|EMBL:PWN87754.1};
GN   ORFNames=FA10DRAFT_269054 {ECO:0000313|EMBL:PWN87754.1};
OS   Acaromyces ingoldii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX   NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN87754.1, ECO:0000313|Proteomes:UP000245768};
RN   [1] {ECO:0000313|EMBL:PWN87754.1, ECO:0000313|Proteomes:UP000245768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN87754.1,
RC   ECO:0000313|Proteomes:UP000245768};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ819639; PWN87754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316YFY5; -.
DR   STRING; 215250.A0A316YFY5; -.
DR   InParanoid; A0A316YFY5; -.
DR   OrthoDB; 5477077at2759; -.
DR   Proteomes; UP000245768; Unassembled WGS sequence.
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   CDD; cd19502; RecA-like_PAN_like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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_2nd.
DR   PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23073:SF8; 26S PROTEASOME REGULATORY SUBUNIT 6B; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:PWN87754.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT   DOMAIN          193..332
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          53..80
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   414 AA;  46733 MW;  0B266192E9BEAECA CRC64;
     MEELGIQMKR EEPTFEDAVA EKTAIHQEMQ QEEDTFLRFK KLQQHLEFLS TMEDYVKDEQ
     RNLKRELVRA QEEVKRIQSV PLVIGQFLEP IDQHTGIVGS TTGSNYVVRI LSTIDRELLK
     PNSSVALHRH SNSLVDVLPP EADSSISMLG QDEKPTETYG DIGGMDIQKQ EIREAVELPL
     VQGDLYKQIG IDPPRGVLLY GPPGTGKTML VKAVANATTA SFIRVVGSEF VQKYLGEGPR
     MVRDVFRLAR ENAPAIIFID EIDAIATKRF DAQTGADREV QRILLELLNQ MDGFDQGSNV
     KVIMATNRAD TLDPALLRPG RLDRKIEFPL PSRREKRLIF QTITSKMNLS PDVDLEDYVS
     RPDKLSSAEI ASICQAAGLK AVRSTRYVII PADFEDAWKQ VVKRSDDSKM EFYQ
//