ID D4DEZ2_TRIVH Unreviewed; 693 AA.
AC D4DEZ2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 13-SEP-2023, entry version 52.
DE RecName: Full=Hsp88-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRV_05733 {ECO:0000313|EMBL:EFE39576.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39576.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE39576.1}.
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DR EMBL; ACYE01000317; EFE39576.1; -; Genomic_DNA.
DR RefSeq; XP_003020194.1; XM_003020148.1.
DR AlphaFoldDB; D4DEZ2; -.
DR GeneID; 9583971; -.
DR KEGG; tve:TRV_05733; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR OrthoDB; 276440at2759; -.
DR Proteomes; UP000008383; 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 CDD; cd10228; HSPA4_like_NDB; 1.
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; PTHR45639:SF4; HSC70CB, ISOFORM G; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-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; PS01036; HSP70_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT REGION 507..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 76953 MW; 13D9608AAFA6DAE8 CRC64;
MSVVGIDFGA LSTKIGVARN KGIDIVTNEV SNRSTPSLVG FGPKSRYIGE PAKTQEISNL
KNTVGSLKLL VGRQFSDPDV QLEQEFCSAK LVDVNGEAGA EVSYMGKKEQ FSATQLVAMY
LTKIKSTASA ELKLPVSDVV VSVPPWFTDA QRRALIDASA IAGLNMLRLI NDTTAIALGY
GITKLDLPAE GETPRRVAFV DIGHCNYSCA IVEFKKGELN VKGTAWDRHF GGRALDKALV
DHLAKEFKEK FKIDIKTNPK AMTRTFAAAE KLKKILSANA QAPISIESIM NDVDVRAMVK
REELEEMIRP LLDRITVPLE QALAEAGLKP EEIDSIEMVG GCTRVPSIKE AISKFFGKQL
SFTLNQDEAV ARGCAFSCAI LSPVFRVRDF SVHDVINYPI EFTWEQSPDI PDEATSLTVF
NKGNIMPSTK ILTFYRKQPF DLEARYSKPD MLPGKTNPWI GRFSVKGVTA DANSDFMICK
LKARLNLHGI LNIESGYYVE DVEVEEPIPE EKKEGETMDT DDANGEAEAK PKMRKVKKQL
RKGDLPVVVG STSLDPAARE KLAERENAMF MEDKLVADTE DKKNELESFI YELRDKIDGV
YAEHASEEEK EKLRAKLTST EDWLYEEGED TTKAVYMSKM DDIRFLSGPI VQRYLDKLEA
ERQAAAPKKH VEIKGDTVDN ADANGDSKME EVE
//
