(data stored in ACNUC8465 zone)

SWISSPROT: Q6FJ65_CANGA

ID   Q6FJ65_CANGA            Unreviewed;       787 AA.
AC   Q6FJ65;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 100.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62705.1};
GN   Name=HSP78 {ECO:0000313|CGD:CAL0136887};
GN   OrderedLocusNames=CAGL0M08822g {ECO:0000313|CGD:CAL0136887,
GN   ECO:0000313|EMBL:CAG62705.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62705.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   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|RuleBase:RU004432}.
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DR   EMBL; CR380959; CAG62705.1; -; Genomic_DNA.
DR   RefSeq; XP_449729.1; XM_449729.1.
DR   ProteinModelPortal; Q6FJ65; -.
DR   STRING; 284593.XP_449729.1; -.
DR   EnsemblFungi; CAG62705; CAG62705; CAGL0M08822g.
DR   KEGG; cgr:CAGL0M08822g; -.
DR   CGD; CAL0136887; HSP78.
DR   EuPathDB; FungiDB:CAGL0M08822g; -.
DR   eggNOG; KOG1051; Eukaryota.
DR   eggNOG; COG0542; LUCA.
DR   HOGENOM; HOG000218211; -.
DR   InParanoid; Q6FJ65; -.
DR   OMA; HHKVRIK; -.
DR   OrthoDB; EOG092C0JLO; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:EnsemblFungi.
DR   GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR   GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR   GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR   GO; GO:0043335; P:protein unfolding; IEA:EnsemblFungi.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 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; SSF52540; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJ65.
DR   SWISS-2DPAGE; Q6FJ65.
KW   ATP-binding {ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN      112    255       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      509    650       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      682    771       ClpB_D2-small. {ECO:0000259|SMART:
FT                                SM01086}.
FT   COILED      350    404       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   787 AA;  88895 MW;  553CA6F174EAECFC CRC64;
     MLSRVCRSSL RNSVARVSRY AGPRALALSM VVSGRQVSGS WQTCAYGVRY IHSSRPRYVQ
     MRMNPNQGEP EKPPLEQFGT NLTKLARDGK LDPVIGRDEE ISRAIQILSR RTKNNPVLIG
     RAGVGKTALI DGLAQRIVAG EVPESLKDKE LVALDLGALI AGAKYRGEFE ERLKKVLEDI
     DKADGKVIVF IDEVHMLLGL GKTDGSMDAS NILKPKLARG LRCISATTID EFKIIEKDPA
     LTRRFQPILL NEPSVQDTIS ILRGLKERYE VHHGVRITDT ALVSAAVLSN RYINDRFLPD
     KAIDLVDEAC AVLRLQHESK PDEIQRLDRA IMKIQIELES LKKETDPVSI ERKEDLEKEL
     ERKNEELQRL TKIWEEEKAE IESIKNSKAD LEKARIELDR CQREGDYAKA SELRYAKIPA
     LEEKVKLSET KDSNKENLLH DAVTSDDISK VIAKMTGIPM ETVLKGDKDR LLYMENSLRE
     RVVGQDEAIE AVSDAVRLQR AGLTSEKRPI ASFMFLGPTG TGKTELTKAL AEFLFDDESN
     VIRFDMSEFQ EKHTVSKLIG APPGYVLSES GGQLTEAVRR KPYAVVLFDE FEKAHPDVCK
     ILLQVLDEGK LTDSLGHHVD FRNTIIVMTS NIGQDILLSD TKLDDEGKID PSTRNEVIEA
     MKRSYPPEFI NRIDDILVFN RLSKKVLRSI VDIRAKEIQE RLNDKRMTIE ISDTAKEWLT
     EHGYDQLYGA RPLNRLIHRR ILNPMATYLL KGQIRNGETV QVDVENKELV VKSNHAEGEI
     VDEEPEK
//

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