ID A0A3F3Q3T5_9EURO Unreviewed; 486 AA.
AC A0A3F3Q3T5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=26S proteasome subunit P45 {ECO:0000313|EMBL:RDH33745.1};
GN ORFNames=BDQ94DRAFT_142578 {ECO:0000313|EMBL:RDH33745.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH33745.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH33745.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH33745.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) 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; KZ852045; RDH33745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3Q3T5; -.
DR STRING; 1341132.A0A3F3Q3T5; -.
DR OrthoDB; 5477077at2759; -.
DR Proteomes; UP000253729; 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:RDH33745.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT DOMAIN 199..338
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 59..86
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 486 AA; 53735 MW; B7447B2ACEE7D89C CRC64;
MGDVAVETPA NNVTPLTKAA PLDTIPNIDS LEGTGNDGSD EYATLKRLQR HLEYIQLQEE
YIKDEQRSLK RELVRAQEEI KRIQSVPLVI GQFMEAIDQN TGIVQSSTGS NYVVRILSTL
DREKLKPSSS VALHRHSNAL VDILPPEADS SIAMLGENEK PDVTYADVGG LDMQKQEIRE
AVELPLTQFD LYKQIGIDPP RGVLLYGPPG TGKTMLVKAV ANSTTASFIR VNGSEFVQKY
LGEGPRMVRD VFRMARENSP AIIFIDEIDA IATKRFDAQT GADREVQRIL LELLNQMDGF
EQSSNVKVIM ATNRADTLDP ALLRPGRLDR KIEFPSLRDR RERRLIFSTI ASKMSLSPEV
DLDSLIVRNE PLSGAVIAAI MQEAGLRAVR KNRYNIIQSD LEDAYAAQVK TGQEADRYGT
FSNLPAIGTW LTKHIDLNST GKSSMGRASG WISDYARRTG GPLAVLSTSR LFHIRTTTDA
LGIPLG
//
