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Database: UniProt
Entry: A0A409XCQ9_PSICY
LinkDB: A0A409XCQ9_PSICY
Original site: A0A409XCQ9_PSICY 
ID   A0A409XCQ9_PSICY        Unreviewed;       390 AA.
AC   A0A409XCQ9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=CVT25_009925 {ECO:0000313|EMBL:PPQ88545.1};
OS   Psilocybe cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX   NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ88545.1, ECO:0000313|Proteomes:UP000283269};
RN   [1] {ECO:0000313|EMBL:PPQ88545.1, ECO:0000313|Proteomes:UP000283269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2631 {ECO:0000313|EMBL:PPQ88545.1,
RC   ECO:0000313|Proteomes:UP000283269};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:PPQ88545.1}.
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DR   EMBL; NHYD01002059; PPQ88545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409XCQ9; -.
DR   STRING; 93625.A0A409XCQ9; -.
DR   InParanoid; A0A409XCQ9; -.
DR   OrthoDB; 5477077at2759; -.
DR   Proteomes; UP000283269; 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; 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:SF166; 26S PROTEASOME REGULATORY SUBUNIT 8; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283269}.
FT   DOMAIN          175..315
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          21..55
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   390 AA;  43331 MW;  88D07258EDE852AB CRC64;
     MATATLTIAP GGIKSYYQAK IESAELLINQ KTQNLRRLEA QRNALNARVR LLREELQLLH
     EPGSYVGEVV KVMGKTKVLV KVQPEGKYIV DIDSEIDVNT LKPTLRVALR SDSYTLHKIL
     PNKVDPLVSL MMVEKVPDST YEMVGGLDKQ IKEIKEVIEL PVKHPELFEA LGIAQPKGVL
     LYGPPGTGKT LLARAVAHHT DCKFIRVSGS ELVQKYIGEG SRMVRELFVM AREHAPSIIF
     MDEIDSIGSS RGDSGSGSSD SEVQRTMLEL LNQLDGFEPT KNIKVIMATN RIDILDSALL
     RPGRIDRKIE FPPPGPEARM SLQRGINLRS LAEKMGQCSG AEVRGICTEA GMYALRERRQ
     HVTQEDFEFA VAKVLKKNQD SNTSVNKLFS
//
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