ID A0A094DGH1_9PEZI Unreviewed; 711 AA.
AC A0A094DGH1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Heat shock protein Hsp88 {ECO:0008006|Google:ProtNLM};
GN ORFNames=V497_04768 {ECO:0000313|EMBL:KFY58585.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY58585.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY58585.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY58585.1}.
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DR EMBL; JPJZ01000947; KFY58585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DGH1; -.
DR STRING; 1420910.A0A094DGH1; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR OrthoDB; 276440at2759; -.
DR Proteomes; UP000029268; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268}.
FT REGION 508..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 79054 MW; 54FCC135C5162B8A CRC64;
MSVVGVDFGS LNTVIAVARN RGVDVITNEV SNRATPSLVG FGPKARYLGE AAKTQEISNL
KNTVGSLKRL AGRALSDPDV AKEQQHISAP LVDINGQVGA EVTYLGKKEQ FTATQLISMF
LGKVKATAAA ELKLPVKEIV MSVPAWFTDV QRRALMDAAE IAGLQLLRLM NDTTAAALGW
GITKLDLPTA DEKPKRVAFV DIGHSDYTCS IVEFRKGELT VKGTAYDRDF GGRDFDKALV
DHFAAEFKEK YKIDIKTNPK AMVRVAAAAE KLKKILSANQ QAPLNIESLM NDVDVQSMLK
REDLEALVEP LLKRAHIPLE EALAQAKLKV EDIDTIEVVG GCTRVPALKE RIQDFFGKQL
SFTINQDEGV ARGCAFSCAI LSPVFRVRDF TIHDIVPYPI EFNWEKSEDI PDEDTSLTVF
NKGNVMPSTK ILTFYRKQNF DLEARYAKPE DLPGAIKPWI GRFSVKNVKA DSKDDFMICK
LKARINLHGI LNVEQGYFVE DVEIEEPIPE DKDEKKDADA MDTDAEPKVP KTRKVKKQVR
KGDLPISAGT ASLDPEAKAT AAEKENNMFM EDKLVGDTDE KKNELETYIY EMRNNIDDKY
AEFASDAEKE KLKAKLELIE DWLYDEGEDT TKAVYIAKYD DIRSLAGPIA QRYFDKLEEE
RQAAQAQLDA ELAAKREAAE AAKKAEKPAE EPASKEEVMT DADTPVVEDV E
//
