ID A0A3F3PYL2_9EURO Unreviewed; 393 AA.
AC A0A3F3PYL2;
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=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:RDH31999.1};
GN ORFNames=BDQ94DRAFT_146191 {ECO:0000313|EMBL:RDH31999.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH31999.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH31999.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH31999.1,
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; KZ852052; RDH31999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PYL2; -.
DR SMR; A0A3F3PYL2; -.
DR STRING; 1341132.A0A3F3PYL2; -.
DR OrthoDB; 360215at2759; -.
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 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 Hydrolase {ECO:0000313|EMBL:RDH31999.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT DOMAIN 170..309
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 9..57
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 393 AA; 44194 MW; BCD312A506379756 CRC64;
MNGASDPERE QALEDYKRSL LELREWEAKL KSLRMGIKDL QREFDISEEN IKALQSVGQI
IGEVLKQLDE ERFIVKASSG PRYVVGCRSK VDKAKLKQGT RVALDMTTLT IMRMLPREVD
PLVYNMSLED PGQINFAGIG GLNEQIRELR EVIELPLKNP ELFQRVGIKP PKGVLLYGPP
GTGKTLLARA VASSMETNFL KVVSSAIVDK YIGESARLIR EMFGYAKEHE PCIIFMDEID
AIGGRRFSEG TSADREIQRT LMELLNQLDG FDYLGKTKII MATNRPDTLD PALLRAGRLD
RKIEIPLPNE VGRLEILKIH SSTVQLDGEI DFESVVKMSD GLNGADLRNV VTEAGLFAIK
DYRDAINQDD FNRAVRKVAE AKKLEGKLEY QKL
//
