ID   A0A1X7S4G9_ZYMTR        Unreviewed;       649 AA.
AC   A0A1X7S4G9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Heat shock 70 kDa protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ZT3D7_G9751 {ECO:0000313|EMBL:SMQ54596.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ54596.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ54596.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; LT853701; SMQ54596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7S4G9; -.
DR   STRING; 1276538.A0A1X7S4G9; -.
DR   Proteomes; UP000215127; Chromosome 10.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10233; HSPA1-2_6-8-like_NBD; 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; PTHR19375:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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:UP000215127}.
FT   REGION          613..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          507..538
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   649 AA;  70530 MW;  BFCD9A63130B9665 CRC64;
     MAPAIGIDLG TTYSCVGIYR DDRIEIIAND QGNRTTPSFV AFTDTERLIG DSAKNQVAMN
     PVNTVFDAKR LIGRKFDDAE VQADMKHFPF KVINKGGKPV VQVEFKGEEK QFTPEEISSM
     VLTKMRETAE AYLGGTVNNA VVTVPAYFND SQRQATKDAG LIAGLNVLRI INEPTAAAIA
     YGLDKKTEGE RNVLIFDLGG GTFDVSLLTI EEGIFEVKST AGDTHLGGED FDNRLVNHFV
     NEFKRKNKKD LTSNARALRR LRTACERAKR TLSSSAQTSI EIDSLYEGVD FYTSITRARF
     EELCQDLFRS TMEPVERTLR DAKIDKSSVH EIVLVGGSTR IPKVQKMVSD FFNGKEPNRS
     INPDEAVAYG AAVQAAILSG DTSSKSTNEI LLLDVAPLSL GIETAGGVMT PLIKRNTTIP
     TKKSETFSTF SDNQPGVLIQ VFEGERARTK DNNLMGKFEL TGIPPAPRGV PQIEVTFDLD
     ANGIMNVSAL EKGTGKTNKI VITNDKGRLS KEEIERMLAE AEKYKDEDEA ESARIQAKNG
     LESYAYSLKN TLSDSKVDEK LEAGDKETLK AKIDETVTWL DDNQTATKDE YESTQKDLES
     VANPIMMKFY GGAEGGMPGG MPGGGMPGGA PGGAPGAGGD DGPTVEEVD
//