ID E5AEZ0_LEPMJ Unreviewed; 647 AA.
AC E5AEZ0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Similar to heat shock protein 70 {ECO:0000313|EMBL:CBY01779.1};
GN ORFNames=LEMA_P005660.1 {ECO:0000313|EMBL:CBY01779.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY01779.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929139; CBY01779.1; -; Genomic_DNA.
DR RefSeq; XP_003845258.1; XM_003845210.1.
DR AlphaFoldDB; E5AEZ0; -.
DR SMR; E5AEZ0; -.
DR STRING; 985895.E5AEZ0; -.
DR EnsemblFungi; CBY01779; CBY01779; LEMA_P005660.1.
DR GeneID; 13285714; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; E5AEZ0; -.
DR OMA; KANPIMM; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000002668; Genome.
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:UP000002668};
KW Stress response {ECO:0000313|EMBL:CBY01779.1}.
FT REGION 614..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 507..538
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 647 AA; 70326 MW; D5C6CF0EBCA26A12 CRC64;
MAPAIGIDLG TTYSCVGIFR DDRIEIIAND QGNRTTPSFV AFTDTERLIG DSAKNQVAMN
PVNTVFDAKR LIGRKFADPE VQADMKHFPF KIIDKGGKPV IQVEFKGETK TFTPEEISSM
VLVKMRETAE SYLGGTVNNA VVTVPAYFND SQRQATKDAG LIAGLNVLRI INEPTAAAIA
YGLDKKTEGE RNVLIFDLGG GTFDVSLLTI EEGIFEVKST AGDTHLGGED FDNRLVNHFC
QEFKRKHKKD LTTNARALRR LRTACERAKR TLSSSAQTSI EIDSLYEGID FYTSITRARF
EELCQDLFRS TMEPVERVLR DAKIDKSSVH EIVLVGGSTR IPKVQKMVSD FFNGKEPNKS
INPDEAVAYG AAVQAAILSG DTSSKSTSEI LLLDVAPLSI GIETAGGVMT PLIKRNTTIP
TKKSEVFSTF SDNQPGVLIQ VYEGERARTK DNNLLGKFEL TGIPPAPRGV PQIEVTFDVD
ANGIINVSAL EKGTGKTNKI VITNDKGRLS KEEIERMLAE AEKYKEEDEA EAARIAAKNA
LESYAYSLRN TLSDSKVDEK LDAGDKEKLK AEIDKTVAWL DDNQTASKDE YESQQKELEG
VANPIMMKFY GAGGEGGMPG GMPGGGMPGG APGGAGQDDG PTVEEVD
//
