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Database: UniProt
Entry: E9E565_METAQ
LinkDB: E9E565_METAQ
Original site: E9E565_METAQ 
ID   E9E565_METAQ            Unreviewed;       926 AA.
AC   E9E565;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Heat shock protein 101 {ECO:0000313|EMBL:EFY88940.1};
GN   ORFNames=MAC_05034 {ECO:0000313|EMBL:EFY88940.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY88940.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY88940.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; GL698505; EFY88940.1; -; Genomic_DNA.
DR   RefSeq; XP_007811374.1; XM_007813183.1.
DR   AlphaFoldDB; E9E565; -.
DR   STRING; 655827.E9E565; -.
DR   GeneID; 19249345; -.
DR   KEGG; maw:MAC_05034; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_2_1; -.
DR   InParanoid; E9E565; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000002499; 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; 2.
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:UP000002499};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:EFY88940.1}.
FT   DOMAIN          2..162
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          431..518
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   926 AA;  103137 MW;  04ACDBB9E830CD9D CRC64;
     MTSRMDFTDR AQKAVEDAMG LAEQYGHSQL LPVHLAVSLL EPPVDLSKDQ QNAPQNSTIT
     LFRQVIEKAH GDPQLFDRAL KKTLVRLPSQ DPPPEQVSLA PSFHAVLRKA MELQKVQKDT
     YIGVDHLITA LADDSSMQAP LKEASIPKPK LVQDAVQAIR GTKRVDSKTA DTEQENENLA
     KFTIDMTAMA RDKKIDPVIG REEEIRRVVR ILSRRTKNNP VLIGEPGVGK TTVVEGLAQR
     IVNRDVPDNL KHCKLLSLDV GALVAGSKFR GEFEERMKGV LKEIEDSKDM IVLFVDEIHL
     LMGAGSSGEG GMDAANLLKP MLARGQLHCI GATTLAEYRK YVEKDAAFER RFQQVMVKEP
     TIPETISILR GLKERYDRHH RVTILDSALV AAANLAARYL TSRRMPDSAI DLVDEAAAAV
     RVARESQPEI IDSLERKLRQ LMIEIAALEK EKDEASQIRL QQAKKDAKNV EEELEPLREK
     YQNEIKRGEE IHQAKLKLDE LEKRLEDAMN MGDNAKAADI KYGAIPEQQT TIKELEARKV
     AADAALNAAG GEAATAMVTD IVTADHINEI VARWTGIPVT RLRTSEKEKL INMEKVLGKV
     VVGQREAVNS VANAIRLQRS GLANPNQPPS FLFCGPSGTG KTLLTKALAE FLFDDPKSMI
     RFDMSEYQER HALSRMIGAP PGYVGHDAGG QLTEALRRKP FSILLFDEVE KAAKEILTVL
     LQLMDDGRIT DGQGRVVDAK NCIVVMTSNL GAEYLTRPGA KEGKIDGSTR ELVMSALRNY
     FLPEFLNRIN SVVIFNRLTR KEIRKIVDLR INEIQKRLED NGRKVKIDVS DEAKDHLGNA
     GYSPAYGARP LARLIEKEVL NKLAILILRN NIRDGETARV ELIDDKITVL SNHPDSEMSD
     DEDMMEDEGD AVDEIIGDDM DEDIYD
//
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