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Database: UniProt
Entry: I6NE27_ERECY
LinkDB: I6NE27_ERECY
Original site: I6NE27_ERECY 
ID   I6NE27_ERECY            Unreviewed;       798 AA.
AC   I6NE27;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Clp R domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=Ecym_5581 {ECO:0000313|EMBL:AET40319.1};
OS   Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS   NRRL Y-17582) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=931890 {ECO:0000313|EMBL:AET40319.1, ECO:0000313|Proteomes:UP000006790};
RN   [1] {ECO:0000313|EMBL:AET40319.1, ECO:0000313|Proteomes:UP000006790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC   {ECO:0000313|Proteomes:UP000006790};
RX   PubMed=22384365;
RA   Wendland J., Walther A.;
RT   "Genome evolution in the Eremothecium clade of the Saccharomyces complex
RT   revealed by comparative genomics.";
RL   G3 (Bethesda) 1:539-548(2011).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP002501; AET40319.1; -; Genomic_DNA.
DR   RefSeq; XP_003647136.1; XM_003647088.1.
DR   AlphaFoldDB; I6NE27; -.
DR   STRING; 931890.I6NE27; -.
DR   GeneID; 11468653; -.
DR   KEGG; erc:Ecym_5581; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_0_1; -.
DR   InParanoid; I6NE27; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000006790; Chromosome 5.
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; 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; 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 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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|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:UP000006790}.
FT   DOMAIN          120..263
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          516..657
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          689..778
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          332..412
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   798 AA;  89619 MW;  B25BCC8F2564B11E CRC64;
     MLRNMAFMRS LQRTCPSFAV RGPLRTLGGI RTVVVPNSFP DVRLSSGNIA VGTRYFSGGM
     NNWVANKNFN LNLSNKDSSQ SALEQFGTNL TRLAKEGKLD PVIGRDQEIS RAIQILSRRT
     KNNPVLIGRA GVGKTSLIDG LAQRIVKGEV PSSLANKELV VLDLGSLVAG AKYRGEFEER
     LKNVLDEIDK ANGQVIVFID EVHMLLGLGK TDGSMDASNI LKPRLAKGMR CISATTFDEF
     KIIEKDPALT RRFQPIVLNE PSVPDTISIL RGLKERYEVH HGVRITDSAI VSAAVLSNRY
     INDRFLPDKA IDLVDEACAV LRLQHESKPD SIQEIDRAIM TIEIELESLK KETDPVSTAK
     KESLTEELNS KRQELSRLTK IWETEKGEIE SVKSVKAELE KAKIELEISQ REGDYGKASE
     LRYAKIPELE RRITNNEQKG NKNNLLHDAV TSEDISKVIS RMTGIPMETV FQGDKDRLLF
     MEDSLRKRVV GQNEAISAIS DAVRLQRAGL TNDKRPIASF MFLGPTGTGK TELTKALAQF
     LFDNESYVVR FDMSEFQEKH TVSRLIGAPP GYVMSESGGQ LTEAVRRKPY AVVLFDEFEK
     AHPDICKVLL QVLDEGKLTD SQGHHVDFRN TIIVMTSNIG QDILLNDQEL GTDGKVSDST
     KTRVLDAVKR SYPPEFINRI DDLLVFNRLS KDVLRSIVDI RLKEIQERLA DKRMSLKLTA
     DAKEWLTERG YDPAYGARPL NRLIHKQVLN PMAMYLLKGQ LRNEETIEVV VENEKLVVKP
     NHEENEDQKK VEITTVNE
//
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