ID A0A369HBB4_9HYPO Unreviewed; 926 AA.
AC A0A369HBB4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN ORFNames=CP533_4961 {ECO:0000313|EMBL:RDA94011.1};
OS Ophiocordyceps camponoti-saundersi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA94011.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA94011.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA94011.1,
RC ECO:0000313|Proteomes:UP000253071};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RDA94011.1}.
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DR EMBL; PDHQ01000019; RDA94011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369HBB4; -.
DR STRING; 2039874.A0A369HBB4; -.
DR Proteomes; UP000253071; 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; 1.10.1780.10; Clp, N-terminal domain; 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; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
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:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
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:UP000253071};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..162
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 891..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..518
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 899..926
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 103332 MW; 82E7B0B842555444 CRC64;
MNARMDFTDR AQKAVEDSMA LAEQYAHSQL LPVHLAVALL DPPVDQSKDQ QNGPAQTTVT
LLRQVVERAR GDPQLFDRAL KKMLVRLPSQ DPPPEHISPS PSYHAVLRKA MELQKVQKDT
FIGVDHLITA LAEDSNIQQA LRDSNIPKAK LVQEAVQAIR GTKRVDSKTA DTEQENENLA
KFTIDMTAMA RDKKIDPVIG REEEIRRVVR ILSRRTKNNP VLIGEPGVGK TTVVEGLAQR
IVNRDVPDNL KHCKLLSLDV GALVAGSKYR GEFEERMKGV LKEIEDSKEM IVLFVDEIHL
LMGAGSSGEG GMDAANLLKP MLARGQLHCI GATTLAEYRK YVEKDAAFER RFQQVMVKEP
TIPETISILR GLKERYDRHH RVTILDSALV AAANLAARYL TSRRMPDSAI DLVDEAAAAV
RVARESQPEI IDSLDRKLRQ LMIEIAALEK EHDEASKTRL QQARKDAQNV EEELEPLREK
YQNEIKRGEE IHQAKVKLDD LEKRLEDATN NGEHVKAADL KYGAIPEQEA VIKELEARKV
AADAALNATG ADAGSSMVTD VVTADHINEI VARWTGIPVT RLRTSEKEKL VNMEKVLGKV
VVGQKEAVQS VANAIRLQRS GLSNPNQPPS FLFCGPSGTG KTLLTKALAE FLFDDAKAMI
RFDMSEYQER HALSRMIGAP PGYVGHDSGG QLTEALRRRP FSILLFDEVE KAAKEVLTVL
LQLMDDGRIT DGQGRVVDAK NCIVVMTSNL GAEFLTRPEA REGRVDGPTR ELVMNALRNY
FLPEFLNRIN SVVIFNRLTR REIRKIVDLR LSEIQKRLED NGRKVRIEVS DEAKDYLGSS
GYSPAYGARP LSRLIEKEVL NRLAILILRN SIRDGETARV ELDDGKIVVL SNHTDSEGGE
DEDMMDDEDD AVDELVGDNM DEDIYD
//