ID E4ZUD1_LEPMJ Unreviewed; 570 AA.
AC E4ZUD1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Similar to heat shock protein 70 {ECO:0000313|EMBL:CBX95010.1};
GN ORFNames=LEMA_P114250.1 {ECO:0000313|EMBL:CBX95010.1};
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|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|RuleBase:RU003322}.
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DR EMBL; FP929126; CBX95010.1; -; Genomic_DNA.
DR RefSeq; XP_003838489.1; XM_003838441.1.
DR AlphaFoldDB; E4ZUD1; -.
DR STRING; 985895.E4ZUD1; -.
DR EnsemblFungi; CBX95010; CBX95010; LEMA_P114250.1.
DR GeneID; 13288056; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_3_1; -.
DR InParanoid; E4ZUD1; -.
DR OMA; DQVLMDH; -.
DR OrthoDB; 23943at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0101031; C:protein folding chaperone complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:EnsemblFungi.
DR GO; GO:0002181; P:cytoplasmic translation; IEA:EnsemblFungi.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
DR GO; GO:0006452; P:translational frameshifting; IEA:EnsemblFungi.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF537; RIBOSOME-ASSOCIATED COMPLEX SUBUNIT SSZ1; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
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:CBX95010.1}.
FT REGION 477..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 60926 MW; 0040976884B03C33 CRC64;
MSEQTDPASR VAIGISFGNS YSSIAFTTSD GKAEVIANED GDRQIPSALS YVEGEELHGN
QAKSQMIRNA KNTAAYFRDF LGQDFKSIDP SPCHQSAHPV DNGSDVAFTL RDTESDQENT
ISVGEITTRH LKRLRSSASA YLGKDVNAAV ITVPTNFSDA QKEALKKASK DAGMEVLQFI
NEPTAAVLAY DARPGAKVAD KIIVVADLGG TRSDVAVLAS RGGIYTILAT LHDYEVSGFK
LDQVLMDYFA KEFLKKHKTV GDPREDERAL AKMKLECEAV KKALSIGSSA SFSVESLLGG
VDFTATINRT RYDLLGNKLF SAFTRLVTHA VEKANLDPLD ISEIILAGGN SHTPKVASAV
RSAFPESTRV LSPSTSSTAI NPSELPVRGA AIQASLIQEF ELEDIEQSTH PMVTVTPHLS
TAVGVLCISG DDSHGVFHAV VEAETSLPVR RTATIATPRE GGDVLIKIVE GSRHIKVTKP
EPKSKAEKAE DDSEDSDDDS EEEEEELREK TWKVGQTLAE AAIRGVKKGA KVEVQINIAA
DLSINTIIRE VGGKGGVRGA VQGSKASGSA
//
