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Database: UniProt
Entry: A0A367LML2_9HYPO
LinkDB: A0A367LML2_9HYPO
Original site: A0A367LML2_9HYPO 
ID   A0A367LML2_9HYPO        Unreviewed;       788 AA.
AC   A0A367LML2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L249_3454 {ECO:0000313|EMBL:RCI15492.1};
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:RCI15492.1, ECO:0000313|Proteomes:UP000253664};
RN   [1] {ECO:0000313|EMBL:RCI15492.1, ECO:0000313|Proteomes:UP000253664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI15492.1,
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 ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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:RCI15492.1}.
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DR   EMBL; LKCN02000002; RCI15492.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367LML2; -.
DR   STRING; 1330021.A0A367LML2; -.
DR   Proteomes; UP000253664; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF176; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253664}.
FT   DOMAIN          112..257
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          513..653
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          691..782
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          325..405
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   788 AA;  87106 MW;  F684230927AEFE17 CRC64;
     MQARKQLITS AQRLVGASTR SARPLARLGT GQIARGTLLR LTPTISVRNY ASGRPHPPGG
     THRMNLGGEA EKPALEQYGI DLTARARDGK LDPVIGRDSE IQRTIQILSR RTKNNPVLIG
     NAGTGKTAIL EGLASRIIRG DVPESIKNKR VISLDLGSLI AGAKFRGDFE ERLKKVLDEV
     QKAEGEVILF IDELHTLLGL GKAEGSIDAS NLLKPALARG ELQCCGATTL NEYRQIEKDV
     ALARRFQPIV VSEPTVEDTI SILRGIKDKY EVHHGVRITD GALVAAATLS NRYITDRFLP
     DKAIDLMDEA ASHLKLQHES KPEEIMRLDH KIMTIQIELE SLRKEKDVAS KERREKLEKD
     LKKFYDDISH LNARWDKEKA EYGAVKKIQE ELDKAKFELE QAQRDGNFGR ASELRFGVIP
     DLEEKLPKED GSARQDGEEP SLVHDAVDSD DIAAVVSRIT GIPVSKLTSG HIEKLVHMED
     SLRDKVKGQD DAIKAVSDAV RLQRAGLSGD NRPLASFFFL GPTGVGKTEL CKKLAGFLFS
     TESAVVRFDM SEFQEKHTVS RLIGAPSGYV GYDDAGQLTE AVRRKPYAVL LFDEFEKAHR
     DISALLLQVL DEGYLTDAQG HRVDFKNTII VLTSNLGADI LVGQNALHPY KENAKGEMDA
     SVRDAVMDVV GRAYPPEFLN RIDSFIIFKR LSRDAIRSIV DIRLSDLQAR LEERRIKLSV
     PAKARDWLGD RGYDPKYGAR PLNRLITNEI SNGLADGIIR GSLKMGQTAE VAVREDQKGL
     VVAAAEAS
//
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