ID A0A165KXU1_9APHY Unreviewed; 809 AA.
AC A0A165KXU1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE SubName: Full=Heat shock protein 70 {ECO:0000313|EMBL:KZT63729.1};
GN ORFNames=DAEQUDRAFT_741738 {ECO:0000313|EMBL:KZT63729.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT63729.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT63729.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT63729.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429160; KZT63729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165KXU1; -.
DR STRING; 1314783.A0A165KXU1; -.
DR OrthoDB; 276440at2759; -.
DR Proteomes; UP000076727; 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; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 2.
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:UP000076727};
KW Stress response {ECO:0000313|EMBL:KZT63729.1}.
FT REGION 753..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 89886 MW; 8C0B8449A4E80CEE CRC64;
MAVVGVDFGT LHSKIGVARH RGIDIIVNEV SNRATPSLVS FGPKQRSLGE AAKTLETSNF
RNTVGGLKRL IGRSFSDPEI HEVEKKFHNA TLVDVNGTVG VQIVQLCSGF GVGEDDGRRS
AAKDQHCGST VNYLGEQRQF SVTQLVAMYL GKLRDIAANE LKTGVSDVVI TVPGWFTDIQ
RRAMLDAAQI AGLNPLRLIN DTTAVALGYG ITKSDLPDPE NPRHVVFVDV GHSSTSCAVV
AFSKGRLDVK ATAYDRQAGG RDIDYALVQH FAAEFKEKYK IDVLSSPKAT FRLAAGCDKI
KKVLSANAEA PLNVESIMND VDATSRLTRE DYEQLISGVL ERIPGPIQQA LTDSGLTLEQ
IDTIELIGGC TRIPAVRAKI QSVFEGKVLS TTLNQDEAAA RGATFSCAML SPIFRVRDFS
MHDITPYSIK FHWDRQPEEP DDDTELLVFP KGNSVPSTKA LTFYRKQPFD IEATYADPAA
LPGGINPWIA RFTAKDVGPN EKGDHSTVRV RTRLNLHGVL SFDQTYLEVE VEEEPMQVDG
EAEPQPKKKK IKKLDIPFVW GSTSLDPSIL EKLKEQEAEM HAADKLVLDT EDRKNALEEY
VYDMRGRLDE RYVSYVKTQE KETLLQALQA AEDWLYSEEG EDATKSAYIE RLYALKKLGD
PITNRYKEAE QRSQVISQLR ETINRYMGEA TSPDEKYAHI DEKDKQSIVE KCATIQQWLE
DQIARQSERP KDVDPVLTSA DVLKRKDEII YFSTPILTKP KPRPPKTETP SGTETPKSGT
ETPNTQQQQQ QQEGEAPKEP QGPSEMDVD
//
