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Database: UniProt
Entry: A0A0J9X567_GEOCN
LinkDB: A0A0J9X567_GEOCN
Original site: A0A0J9X567_GEOCN 
ID   A0A0J9X567_GEOCN        Unreviewed;       414 AA.
AC   A0A0J9X567;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Similar to Saccharomyces cerevisiae YOR259C RPT4 One of six ATPases of the 19S regulatory particle of the 26S proteasome involved in degradation of ubiquitinated substrates {ECO:0000313|EMBL:CDO52341.1};
GN   ORFNames=BN980_GECA03s00384g {ECO:0000313|EMBL:CDO52341.1};
OS   Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Geotrichum.
OX   NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO52341.1, ECO:0000313|Proteomes:UP000242525};
RN   [1] {ECO:0000313|EMBL:CDO52341.1, ECO:0000313|Proteomes:UP000242525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO52341.1,
RC   ECO:0000313|Proteomes:UP000242525};
RA   Casaregola S.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; CCBN010000003; CDO52341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J9X567; -.
DR   STRING; 1173061.A0A0J9X567; -.
DR   OrthoDB; 360215at2759; -.
DR   Proteomes; UP000242525; 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   GO; GO:0010604; P:positive regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0051173; P:positive regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProt.
DR   GO; GO:0070682; P:proteasome regulatory particle assembly; IEA:UniProt.
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; 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_2nd.
DR   PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23073:SF155; 26S PROTEASOME REGULATORY SUBUNIT 10B; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 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:CDO52341.1}.
FT   DOMAIN          191..330
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          44..78
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   414 AA;  46467 MW;  877C596366D03228 CRC64;
     MSTSERDPLL DALNAESSSG APEPPVDRER EKALEDFKKK LKDHREWESK LRDLRLGLKD
     LDKEFEKTED DIKALQSLGQ LIGEVLKQLD DERFIVKASN GPRYIVGCRN SIKKENLKQG
     VRVALDMTTL TIMRILPREV DPLVYNMTTF EPGSLTFGGV GGLNEQVREL REVIELPLKN
     PELFHRVGIN PPKGVLLYGP PGTGKTLLAK AVAATIGANF IFSPASAIVD KYIGESARLI
     REMFGYAKEH APCIIFMDEV DAIGGRRFSE GTSADREIQR TLMELLNQMD GFDYLGQTKV
     IMATNRPDTL DPALLRAGRL DRKIEIPLPN EIGRLEIFKI HAANVNKQGE FDYEAVVKMS
     DGFNGADIRN VVTEAGFFAI RDDRDYIVQN DMMKAVRKVA EAKKLEGKLE YEKL
//
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