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Database: UniProt
Entry: C5MGG4_CANTT
LinkDB: C5MGG4_CANTT
Original site: C5MGG4_CANTT 
ID   C5MGG4_CANTT            Unreviewed;       636 AA.
AC   C5MGG4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Heat shock protein SSC1, mitochondrial {ECO:0000313|EMBL:EER31427.1};
GN   ORFNames=CTRG_05157 {ECO:0000313|EMBL:EER31427.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER31427.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER31427.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; GG692401; EER31427.1; -; Genomic_DNA.
DR   RefSeq; XP_002550859.1; XM_002550813.1.
DR   AlphaFoldDB; C5MGG4; -.
DR   STRING; 294747.C5MGG4; -.
DR   EnsemblFungi; CTRG_05157-t43_1; CTRG_05157-t43_1-p1; CTRG_05157.
DR   GeneID; 8299313; -.
DR   KEGG; ctp:CTRG_05157; -.
DR   VEuPathDB; FungiDB:CTRG_05157; -.
DR   eggNOG; KOG0102; Eukaryota.
DR   HOGENOM; CLU_005965_2_1_1; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:EnsemblFungi.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR   GO; GO:0106034; P:protein maturation by [2Fe-2S] cluster transfer; IEA:EnsemblFungi.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   Stress response {ECO:0000313|EMBL:EER31427.1}.
SQ   SEQUENCE   636 AA;  70399 MW;  10D2F30E5A3E40FE CRC64;
     MLRTNINKLL FRRFKHTVLG IDLGTTNSAV AVMGSDKEPH ILENEEGKRT TPSIVAFDKN
     GKPLVGLPAK RQAVVNPENT FFATKRLIGR KFDDQEVQRD LNNVPYKIIP NTHGEATLST
     TTGNTMTPSE IGGLILQKLQ KDAEIQLKED KIDKAVVTVP AYFNDSQRQA TKNSGKSIGL
     EILRVINEPT AAALAYGCDK TRKDGIIAVF DLGGGTFDIS ILEIDNGVFE VRATNGNTHL
     GGEDFDIQIM NHILNSFKQE TGIDLSGDRF AVQRIREAAE KAKIELDHSD EVEINLPFIT
     AEKHIKQKLT AKEFDDMVMP IIQKTIDPVK RCVRDAELKF KDIDEVLLVG GMTRMPKIRK
     IVEEMFGKKP STAVNPDEAV ALGAAIQGAV LSGEVKNVVL LDVTPLSLGI ETYGGIFTPL
     IPRNSAVPIK KEQMFSTAVD GQTGVEIGVY QGERPLVRDN KHIGQFRLAN IPQGPKGSPQ
     IAVSFEIDAD GIINVNATDK TNYPEDSPHY GKPNSVSIQV TEVGLTDSEI EKMIQESSEN
     KKADEERRRY YEHASRAEIL CTDADNAITQ YGKFMEESEK ESVRQHIVVV KTMIDDIRSG
     KTLHSPKELN KKVNEMQNQC MEVIKNVAAR QQASKK
//
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