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Database: UniProt
Entry: A0A059J7I5_TRIIM
LinkDB: A0A059J7I5_TRIIM
Original site: A0A059J7I5_TRIIM 
ID   A0A059J7I5_TRIIM        Unreviewed;       490 AA.
AC   A0A059J7I5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE            EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN   ORFNames=H109_04638 {ECO:0000313|EMBL:KDB23457.1};
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB23457.1, ECO:0000313|Proteomes:UP000024533};
RN   [1] {ECO:0000313|EMBL:KDB23457.1, ECO:0000313|Proteomes:UP000024533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816 {ECO:0000313|EMBL:KDB23457.1,
RC   ECO:0000313|Proteomes:UP000024533};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA   Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA   Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA   Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Trichophyton interdigitale MR816.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDB23457.1}.
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DR   EMBL; AOKY01000305; KDB23457.1; -; Genomic_DNA.
DR   EMBL; AOKY01000305; KDB23458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059J7I5; -.
DR   Proteomes; UP000024533; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 3.30.420.40; -; 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; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024533}.
SQ   SEQUENCE   490 AA;  52961 MW;  5F8543A4A0B7040C CRC64;
     MVLMKMKEVA ETKLGKSVSK AVITVPAYFN DNQRQATKDA GAIAGLNVLR IINEPTAAAI
     AYGLGSGKSE KERNVLIYDL GGGTFDVSLL NIQGGVFTVK ATAGDTHLGG QDFDTNLLDH
     FKKEFTRKTK KDLSGDSRAL RRLRTACERA KRTLSSATQT TVEIDSLFDG EDFNAQITRA
     RFEDLNAKIF AATLEPVQQV LKDAGIDKSK VDEIVLVGGS TRIPRVQKLL SDAFDGKKLE
     KGINPDEAVA YGAAVQAGIL SGKATSADTS DLLLLDVVPL SLGVAMEGNI FAPVVPRGQT
     VPTIKKRTFT TVVDNQQTVQ FPVYQGERTN CEDNTSLGEF TLSPIPPMKA GDAALEVVFE
     VDVNGILKVT ATEKSSGRSS NITISNAVGK LSSAEIEAMI NDAAKFKSSD EAFSQRFEAR
     QQLESYISRV EEIITDPGMS LKIKRGNKDK IESALSDAMA QLEVEDSSPE DLKKKELALK
     RLITKAMSTR
//
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