ID A0A229X8X3_9EURO Unreviewed; 421 AA.
AC A0A229X8X3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=CDV55_104647 {ECO:0000313|EMBL:RHZ63107.1}, CFD26_104975
GN {ECO:0000313|EMBL:RLL99818.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL99818.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL99818.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ63107.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLL99818.1}.
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; NKHV02000084; RHZ63107.1; -; Genomic_DNA.
DR EMBL; NIDN02000024; RLL99818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229X8X3; -.
DR STRING; 1245748.A0A229X8X3; -.
DR OrthoDB; 5477077at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289}.
FT DOMAIN 198..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 58..85
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 421 AA; 47077 MW; CA3F13FA1B4FAAA4 CRC64;
MGDVAVESSL TNVTPSKSAP FDTIPNIDSL EGTDTDGGDE YATLKRLQRH LEYIQLQEEY
IKDEQRSLKR ELVRAQEEIK RIQSVPLVIG QFMEAIDQNT GIVQSSTGSN YVVRILSTLD
REKLKPSSSV ALHRHSNALV DILPPEADSS IAMLGENEKP DVTYADVGGL DMQKQEIREA
VELPLTHFDL YKQIGIDPPR GVLLYGPPGT GKTMLVKAVA NSTTASFIRV NGSEFVQKYL
GEGPRMVRDV FRMARENSPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFE
QTSNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPSLRDRR ERRLIFTTIA SKMSLSPEVD
LDSLIVRNEP LSGAVIAAIM QEAGLRAVRK NRYNIIQSDL EDAYAAQVKT GQEADRLEFY
R
//
