ID Q0U3T1_PHANO Unreviewed; 645 AA.
AC Q0U3T1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 100.
DE RecName: Full=Heat shock 70 kDa protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_13583 {ECO:0000313|EMBL:EAT79030.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT79030.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CH445351; EAT79030.2; -; Genomic_DNA.
DR RefSeq; XP_001803790.1; XM_001803738.1.
DR AlphaFoldDB; Q0U3T1; -.
DR STRING; 321614.Q0U3T1; -.
DR EnsemblFungi; SNOT_13583; SNOT_13583; SNOG_13583.
DR GeneID; 5980710; -.
DR KEGG; pno:SNOG_13583; -.
DR VEuPathDB; FungiDB:JI435_135830; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; Q0U3T1; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT REGION 587..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 545..579
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 607..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 70095 MW; FAEF6DCA7D40A702 CRC64;
MRAPMGSKFV RGYAEGGEEK VKGSVIGIDL GTTNSAVAVM EGKVPRIIEN SEVVGFTKEG
ERLVGIAAKR QAVVNPENTL FATKRLIGRK FTDAEVQRDI QQVPYKIVQH TNGDAWLEAQ
GQKYSPSQVG GFVLGKMKET AESYMGKNVK NAVVTVPAYF NDSQRQATKD AGQIAGLNVL
RVVNEPTAAA LAYGLDKATD AVVAVYDLGG GTFDISILEI QNGVFEVKST NGDTHLGGED
FDITLVRHLV QQFKKEQGID LNSDRMAIQR IREAAEKAKI ELSSSSQTDI NLPFITADAS
GPKHINTKLT RAQLEKMMDP LISRTVDPVR KALKDANLQP KEISEVILVG GMTRMPKVTE
SVKSIFGRDP AKSVNPDEAV AIGAAIQGAV LAGEVTDLLL LDVTPLSLGI ETLGGVFTRL
INRNTTIPTK KSQVFSTAAD FQSAVEIKVY QGERELVRDN KLLGNFQLVG IPPAHRGVPQ
IEVTFDIDAD SIVHVHAKDK STNKDQSITI ASGSGLSDTE IESMVRDSEQ YAEQDKERKN
AIEAANRADS VVNDTEKALK EFEDRLDKAE AEKIKEKITT MREFIATSQT GEGTATAAEI
KEKTDELQNA SLSLFDQMHK ARSESQNSGE QQQQQPGEGE GEKKP
//
