ID G3JPS1_CORMM Unreviewed; 341 AA.
AC G3JPS1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Clp protease, ATP-binding subunit ClpX {ECO:0000313|EMBL:EGX89172.1};
GN ORFNames=CCM_07424 {ECO:0000313|EMBL:EGX89172.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX89172.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX89172.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX89172.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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DR EMBL; JH126404; EGX89172.1; -; Genomic_DNA.
DR RefSeq; XP_006672628.1; XM_006672565.1.
DR AlphaFoldDB; G3JPS1; -.
DR STRING; 983644.G3JPS1; -.
DR GeneID; 18169435; -.
DR KEGG; cmt:CCM_07424; -.
DR VEuPathDB; FungiDB:CCM_07424; -.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_1_1_1; -.
DR InParanoid; G3JPS1; -.
DR OMA; LMETMFV; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:EGX89172.1};
KW Hydrolase {ECO:0000313|EMBL:EGX89172.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EGX89172.1};
KW Protease {ECO:0000313|EMBL:EGX89172.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT DOMAIN 213..295
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 77..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 37082 MW; 15CEF2D967A4BEDB CRC64;
MTQAGYIGQD VETCVERLLI EASYDIKATE HGIIVLDEFD KLARRETSTG RDVGGEGVQQ
ALLKLVEGTK VTINVKDNRS SRSASPITTN YSAGGSSSSA AQAAPPAAKV DQYTIDTTNI
LFVFCGAFVG LDKSVIQRVA KPTMGFGGEV KGRTTLSGEQ QTLPSELYEH LAHHDSASKF
TPLDLATPAD LQKFGFIPEL IGRLHNICAL SPLSRKDLYR ILTEPRNSLV AQYTALFETY
PSRLYFTEKA LFAIADRASQ SGTGARGLKM EMERVLGEPM FDAPMPYVLI TEGCVNGTEK
AGYWAKDGRF EVDRRMEEEQ LLTANPTAPE LLPQAGQSSS G
//