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Database: UniProt
Entry: A0A367LRJ0_9HYPO
LinkDB: A0A367LRJ0_9HYPO
Original site: A0A367LRJ0_9HYPO 
ID   A0A367LRJ0_9HYPO        Unreviewed;       389 AA.
AC   A0A367LRJ0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=L249_3215 {ECO:0000313|EMBL:RCI16970.1};
OS   Ophiocordyceps polyrhachis-furcata BCC 54312.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI16970.1, ECO:0000313|Proteomes:UP000253664};
RN   [1] {ECO:0000313|EMBL:RCI16970.1, ECO:0000313|Proteomes:UP000253664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI16970.1,
RC   ECO:0000313|Proteomes:UP000253664};
RX   PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA   Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA   Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT   "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT   pathogenicity and host specificity in insect fungi.";
RL   BMC Genomics 16:881-881(2015).
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:RCI16970.1}.
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DR   EMBL; LKCN02000001; RCI16970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367LRJ0; -.
DR   STRING; 1330021.A0A367LRJ0; -.
DR   Proteomes; UP000253664; 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:SF12; 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:UP000253664}.
FT   DOMAIN          165..304
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          11..45
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   389 AA;  43424 MW;  6DD04599EF1241DD CRC64;
     MALDQYYHNK IEAMKLEILK GQAALRRLEA QRNDYNSRVR LLREELGLLQ QPGSYVGEVV
     KVMSTKKILV KVHPEGKYVV DVSDSVDVSK LTPGKRVTLL SDSYKLEKLL PSSVDPLVSL
     MMVEKVPDST YDMIGGLDQQ IKEIKEVIEL GLKHPELFES LGIAQPKGVL LYGPPGTGKT
     LLARAVAHHT ACKFIRVSGS ELVQKYIGEG SRMVRELFIM AREHAPSIIF MDEIDSIGSS
     RVEGSSGGDS EVQRTMLELL NQLDGFEPTK NIKVIMATNR LDILDPALLR PGRIDRKIEF
     PPPSVEARAD ILRIHSRKMN LTRGINLNKI AEKMSGCSGA ELKGVCTEAG MYALRERRVH
     VTQEDFELAT AKILNKHDDK EVSLGKLWK
//
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