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Database: UniProt
Entry: C0NGV5_AJECG
LinkDB: C0NGV5_AJECG
Original site: C0NGV5_AJECG 
ID   C0NGV5_AJECG            Unreviewed;       539 AA.
AC   C0NGV5;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Hsp7-like protein {ECO:0000313|EMBL:EEH09040.1};
GN   ORFNames=HCBG_02577 {ECO:0000313|EMBL:EEH09040.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH09040.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; GG663365; EEH09040.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NGV5; -.
DR   STRING; 447093.C0NGV5; -.
DR   VEuPathDB; FungiDB:I7I50_10462; -.
DR   HOGENOM; CLU_005965_0_3_1; -.
DR   InParanoid; C0NGV5; -.
DR   OrthoDB; 23943at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF537; RIBOSOME-ASSOCIATED COMPLEX SUBUNIT SSZ1; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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:UP000001631}.
FT   REGION          436..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..474
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  57944 MW;  5450BA5C40E1E327 CRC64;
     MSEETNGVSP ENAERCAIGL SFGNTNSSIA YTSPEGKAEV IANEEGDPTP CHASAHPQLH
     DSTVAFTIHD TTNAEPSTVT VSEITTRHLR RLRRSASEFL GKDVNAAVFT VPTNFSDAQR
     TALTSAAKDA CIEVLQFIPE PVASLLAYDA RPEAVVKDKL VVVADFGGTR SDVAVIASRG
     GMYTILATAH DYELGGAQLD QVLIDHFSKE FIKKHKVDPR ENARSLAKLK LEAELTKKSL
     SLGTNATLSI ESLASGVDFS STVNRTRYEL LSGKVFANFT RLIEESVKKA DLDILDIDEV
     ILCGGTSHTP KIARLVQSLF PATTTVLAPA TSPTAINPSD LSARGAAIQA SLIEEFEKDD
     IEQSTHPMVT VTPHLEKAIG IQLISATDDA HAIFKPLLNA ETALPARRTA RYAVPKAGGD
     VLVRVCEGIR EIKVTKPDPK RKQPAKEAGG ENDNEDVDSD FDSDDDDEEE EEEIREAVWK
     VSKPIAEFAI RGVKANGKVE VMVGVSEQLA VQIMGREVGG KDGVRVLVDA PKPVENGST
//
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