ID   Q6BNL2_DEBHA            Unreviewed;       801 AA.
AC   Q6BNL2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=DEHA2E20834p {ECO:0000313|EMBL:CAG88481.2};
GN   OrderedLocusNames=DEHA2E20834g {ECO:0000313|EMBL:CAG88481.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88481.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88481.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968 {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CR382137; CAG88481.2; -; Genomic_DNA.
DR   RefSeq; XP_460208.2; XM_460208.1.
DR   AlphaFoldDB; Q6BNL2; -.
DR   STRING; 284592.Q6BNL2; -.
DR   GeneID; 2902074; -.
DR   KEGG; dha:DEHA2E20834g; -.
DR   VEuPathDB; FungiDB:DEHA2E20834g; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_005070_4_0_1; -.
DR   InParanoid; Q6BNL2; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
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:UP000000599}.
FT   DOMAIN          129..274
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          530..704
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          703..792
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          343..457
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   801 AA;  90131 MW;  E50C15896DC2067F CRC64;
     MLRTRLIIQN VRSRAISQAS RNINTVSSLS TRQIHVPAIQ SKSNFGMKNG LQGMKYKHNS
     FGLNHVKFMH SSGIRKLQMS MDKEGQDTRP ALEKYGTDLT QLAKDGKLDP VIGRDEEIRR
     TVQILSRRTK NNPVLIGNAG TGKTAVMEGL AQRILKNEVP DSMKDKQIIT LDLSGIIAGA
     KYRGDFEGKL KQILKEVEEK QGKVILFIDE LHILMGLGKA EGSIDASNLL KPALARGKLS
     LCGATTIEEY RKYVEKDAAL ARRFSAVTVN EPTVQDTISI LRGLKERYEV HHGVRITDGA
     LVTSALYSSR YITDRFLPDK AIDLVDEACS TLRLQHESKP DAIAQLDRQI MTIQIELESL
     RKEDDQLSLD RKTKLEEELN VKSAELKDFT EKWESEKKSI DDVKNAKTDL EQAKFDLEQC
     QREGNYGKAS ELQYATIPKL EEQLKELTDN EKSVEGSTLL HDSVTSDDIA NVISKMTGIP
     LSNLMKGEKD KLLDMEATLK DKVIGQDEAI NAVADAVRLQ RAGLTSDKRP IASFIFLGPT
     GTGKTELTKS LAEFLFHDKS SVIRFDMSEF QEKHTISRLI GSPPGYVGYE ESGELTEAVR
     RKPYSVILFD EFEKAHSDVS KLLLQVLDEG SLTDSHGKHI DFRNTIIVMT SNIGQEILLN
     DKDTSDDGHI SESTKTQVSD MLKHYYPPEF LNRLDDVLIF NRLSKQSLKN ILTIRLKEID
     ERLADRRINL SLSNESKDKL CELGYDPVYG ARPLNRVLQK KVLNPLSKLM IKGQIREGET
     ILVDLKDDEI YVTPNHEEDH P
//