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
//