ID A0A448YEI1_BRENA Unreviewed; 439 AA.
AC A0A448YEI1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=DEKNAAC100713 {ECO:0000313|EMBL:VEU19353.1};
GN ORFNames=BRENAR_LOCUS90 {ECO:0000313|EMBL:VEU19353.1};
OS Brettanomyces naardenensis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=13370 {ECO:0000313|EMBL:VEU19353.1, ECO:0000313|Proteomes:UP000290900};
RN [1] {ECO:0000313|EMBL:VEU19353.1, ECO:0000313|Proteomes:UP000290900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tiukova I., Dainat J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; CAACVR010000001; VEU19353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448YEI1; -.
DR STRING; 13370.A0A448YEI1; -.
DR InParanoid; A0A448YEI1; -.
DR Proteomes; UP000290900; Unassembled WGS sequence.
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: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 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; 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:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000290900}.
FT DOMAIN 217..356
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 48911 MW; 8EE3F4EF51330BBA CRC64;
MGQDASMPSK GKKKDHDKKK QKPKYEPPVQ SKTFGRKRRK GIDATAKLPA VLPNTRCKLR
LLKLERIKDH LLLEEEFVTN QENLQPTDQR QAEEREKIDD VRGSPMSIGT LEEIIDDDHA
IVSSATGPEY YVSILSFVDK SLLEPGCQVL LHHKTVSVVG VLQDETDPMV NVMKMDKAPT
ESYADVGGLE AQIQEIKESV ELPLTHPELY EEMGIKPPKG VILYGPPGTG KTLLAKAVAN
QTSATFLRIV GSELIQKYLG DGPRMCRQLF KVASENAPAI VFIDEIDAIG TKRYDSSSGG
EREVQRTMLE LLNQLDGFDD RGDVKVIMAT NKIESLDPAL IRPGRIDRKI KFENPDSATK
KKILQIHTSK MNIAPDVNLD EVIGTKDDIS GADIKAICTE AGLLALRERR MQVIAEDFKQ
GKERVMKNKI DTNLEGLYL
//
