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Database: UniProt
Entry: Q6BKQ2_DEBHA
LinkDB: Q6BKQ2_DEBHA
Original site: Q6BKQ2_DEBHA 
ID   Q6BKQ2_DEBHA            Unreviewed;       366 AA.
AC   Q6BKQ2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=DEHA2F20086p {ECO:0000313|EMBL:CAG89607.2};
GN   OrderedLocusNames=DEHA2F20086g {ECO:0000313|EMBL:CAG89607.2};
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:CAG89607.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89607.2, 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004572}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
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DR   EMBL; CR382138; CAG89607.2; -; Genomic_DNA.
DR   RefSeq; XP_461219.2; XM_461219.1.
DR   AlphaFoldDB; Q6BKQ2; -.
DR   STRING; 284592.Q6BKQ2; -.
DR   GeneID; 2904038; -.
DR   KEGG; dha:DEHA2F20086g; -.
DR   VEuPathDB; FungiDB:DEHA2F20086g; -.
DR   eggNOG; KOG0737; Eukaryota.
DR   HOGENOM; CLU_000688_21_14_1; -.
DR   InParanoid; Q6BKQ2; -.
DR   OMA; CRNAAMR; -.
DR   OrthoDB; 102713at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45644; AAA ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G12920)-RELATED-RELATED; 1.
DR   PANTHER; PTHR45644:SF3; FI08533P-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          133..267
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          326..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  41191 MW;  24F392E62513F30E CRC64;
     MNRFKIDLGK FKFDIKFLGD LFLLTGAGLS MYYIMNHLLN ESLGEGSVKN RESKKKGTGV
     LRRMQATNPE LKNVTFNDYE KSLLSCLITP EDISVTFGDI GGLKDIIDEL REAVILPLTE
     PELFAAHSSL VQSPKGVLFY GPPGCGKTML AKAIAKESGA FFLSIRMSTI MDKWYGESNK
     IVDAIFSLAN KLQPCIVFID EIDSFLRDRS SNDHEVSSII KAEFMTLWDG LMSNGRIMVM
     GATNRREDID QAFMRRLPKQ FPIGRPDASQ RRSILNKILK DSKLDEDDFD LEAIVSNTRS
     FSGSDLKELC REAALNSMRE FIRDNYKDGK KLTKDTEPES TPKVRPLRTS DFLKGFSETI
     PSSTVD
//
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