ID E4ZLZ8_LEPMJ Unreviewed; 289 AA.
AC E4ZLZ8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Similar to haloacid dehalogenase-like hydrolase domain-containing protein 1A {ECO:0000313|EMBL:CBX92347.1};
GN ORFNames=LEMA_P050530.1 {ECO:0000313|EMBL:CBX92347.1};
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).
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DR EMBL; FP929094; CBX92347.1; -; Genomic_DNA.
DR RefSeq; XP_003835712.1; XM_003835664.1.
DR AlphaFoldDB; E4ZLZ8; -.
DR STRING; 985895.E4ZLZ8; -.
DR EnsemblFungi; CBX92347; CBX92347; LEMA_P050530.1.
DR GeneID; 13287075; -.
DR eggNOG; KOG2914; Eukaryota.
DR HOGENOM; CLU_045011_13_0_1; -.
DR InParanoid; E4ZLZ8; -.
DR OMA; FTHEQNE; -.
DR OrthoDB; 21003at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:EnsemblFungi.
DR GO; GO:1990738; F:pseudouridine 5'-phosphatase activity; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR18901; 2-DEOXYGLUCOSE-6-PHOSPHATE PHOSPHATASE 2; 1.
DR PANTHER; PTHR18901:SF38; PSEUDOURIDINE-5'-PHOSPHATASE; 1.
DR Pfam; PF13419; HAD_2; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CBX92347.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT REGION 231..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 32199 MW; 61501AAF413C4C80 CRC64;
MAPTTTRPPR IRAALFDMDG LLIDSEDLYT IVTNTILQRY GRPALPWSIK AQLQGRPGPQ
ASQIFHNWAQ LPISHEKFME EQKALQTELF PTTKPLDGVM DLLAGLKKRN VHMALATSSH
AGNFKLKSSH LGDLFHYFAP EHQVLGDDPR IPPGRGKPAP DIYLLALSTL NETLEAQGQP
PIQPEECLVF EDSIPGVESG RRAGMQVVWC PHPELLAEFK GREPEVLAGL TGEHKEDEEE
QLRKTETEAA QGRRRVGMPG KINDGWARLL HSLVDFPYES YGMVDNANA
//