ID D5GJ50_TUBMM Unreviewed; 600 AA.
AC D5GJ50;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN ORFNames=GSTUM_00008839001 {ECO:0000313|EMBL:CAZ84543.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ84543.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ84543.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ84543.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; FN430329; CAZ84543.1; -; Genomic_DNA.
DR RefSeq; XP_002840352.1; XM_002840306.1.
DR AlphaFoldDB; D5GJ50; -.
DR STRING; 656061.D5GJ50; -.
DR EnsemblFungi; CAZ84543; CAZ84543; GSTUM_00008839001.
DR GeneID; 9181884; -.
DR KEGG; tml:GSTUM_00008839001; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR InParanoid; D5GJ50; -.
DR OMA; HQTTVQF; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF467; RIBOSOME-ASSOCIATED MOLECULAR CHAPERONE SSB1-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911}.
SQ SEQUENCE 600 AA; 65297 MW; 202E2E28DFC94955 CRC64;
MEGKYEGAIG IDLGTTYSCV AIYEGNGVEI IANEQGNRVT PSFVAFSEKE RLIGDAAKNQ
AALNPRNTVF DAKRLIGRRF DEPSVKKDIQ SWPFKVVDRE GNPYIEVEYL GETKQFSPQE
ISSMVLTKMK EIAEAKLGQA VEKAVITVPA YFNDNQRQAT KDAGAISGMN VLRIINEPTA
AAIAYGLGAG KSDKERHVLI FDLGGGTFDV SLLHIQGGVF TDFDTALLDH FKAEFKRKTQ
LDISDDPRAL RRLRSACERA KRTLSSVTQT TVEIDSLSGG QDFNTSITRA RFEDINASLF
KSTIAPVEQV LKDSGLAKSA VDEVVLVGGS TRIPKIQKLL SDLFNGKKLE KGINPDEAVA
YGAAVQAGIL SGKATSDETA DLLLLDVVPL SLGVAMEGNI FAPVVPRGQT VPTIKKRTFT
TVADNQTTVQ FPVFQGERVN CEDNTSLGEF TLAPIPPMKA GDAVLEVIFE VDVNGILKVT
AIEKSTGRSA NITISNSVGK LSSTEIEKMV QDAEKFKSTD DAYSKKFEAR QQLESYISRV
EEIVSDPTMS LKLKRGAREK IESSLSDAMA QLEVEDASAD DLKKKELALK RTVTKAMSTR
//
