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Database: UniProt
Entry: U6KUM9_EIMTE
LinkDB: U6KUM9_EIMTE
Original site: U6KUM9_EIMTE 
ID   U6KUM9_EIMTE            Unreviewed;       926 AA.
AC   U6KUM9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Heat shock protein, putative {ECO:0000313|EMBL:CDJ39210.1};
GN   ORFNames=ETH_00021420 {ECO:0000313|EMBL:CDJ39210.1};
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ39210.1};
RN   [1] {ECO:0000313|EMBL:CDJ39210.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ39210.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDJ39210.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ39210.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; HG674237; CDJ39210.1; -; Genomic_DNA.
DR   RefSeq; XP_013229965.1; XM_013374511.1.
DR   AlphaFoldDB; U6KUM9; -.
DR   EnsemblProtists; CDJ39210; CDJ39210; ETH_00021420.
DR   GeneID; 25253399; -.
DR   VEuPathDB; ToxoDB:ETH2_1263400; -.
DR   VEuPathDB; ToxoDB:ETH_00021420; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 35211at2759; -.
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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000313|EMBL:CDJ39210.1}.
FT   DOMAIN          3..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          881..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          412..526
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        897..915
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   926 AA;  104113 MW;  F56BA8B1FCC00407 CRC64;
     MDPAQWTGLV RKVYAAAQEI CRERGAPQID PVHLLSALLQ DPQQLPTQAL RKVGTDLTLL
     HEQVDLEISK FPAQNPPPQY IGPNHACTAV FRQAKTIQTE MKDTHLAVDH LLLAVCENRT
     IKHVLQQAGC DYKKIKEVCM KLRAGARVTG DAADQNFDAL TKYGIDFTDL AEQGKLDPVI
     GRDEEIRRVI RILCRRTKNN PVELYEFFPG VGKSAIVEGL ARRVVEGDVP SSLRCRVISL
     DLGALISGAK YRGEFEERLK AVLMEVKNAE GSVILFIDEI HMVMGAGKTD GAMDAANLLK
     PMLARGELRC IGATTLDEYR KHVEKDAAFE RRFQQVHVHE PSVSATISIL RGLKDRYAAH
     HGVRILDSAL VEAAQLADRY ITSRFLPDKA IDLMDEACAI ARVQVDSKPE IMDRLERLIF
     QLEVEATALA KESDAASQER LNEVRQEIAK HRETLKPLQL QYTREKETLD ELRQLALKED
     ELKAKIEKAE RLGQMDLVAE LRYDALPGLQ KRLTELRKEQ ETYEKTHKPL LTEVVGPEQI
     ADVVHRWTNI PVQKLTQTEK ERLLQLKEKL SRRVVGQIAA VTAVSESILR SAAGLARRNK
     PIGSFLFLGP TGVGKTELCK AVAEELFDTK ERIVRLDMSE YMESHSVARL IGAPPGYVGH
     EEGGQLTEAV RRNPYSVVLL DEVEKAHHQV WNVLLQVLDE GRLTDSQGRT VDFSNCLLIL
     TSNIGAHHLL AAAENSVAGP EKAEEAFAEA FTKVMKEVRH IFRPELLNRL DDIVAFKALS
     DTDLKEVMRL QVDEVRQRLR EKRIDLQLTD RALEHALEEA FDPAFGARPL KRYLEKHIVS
     DLSVMLLNGD LGPDHEAIAD WSTTEKKWKW RVTRLHGVEG QAQNEMDADP SVEAGLPRSI
     SESSRTSSYT GRSEAMHAAN TKRFRY
//
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