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Database: UniProt
Entry: E5A117_LEPMJ
LinkDB: E5A117_LEPMJ
Original site: E5A117_LEPMJ 
ID   E5A117_LEPMJ            Unreviewed;       454 AA.
AC   E5A117;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Similar to lipolytic protein G-D-S-L family {ECO:0000313|EMBL:CBX97313.1};
GN   ORFNames=LEMA_P104440.1 {ECO:0000313|EMBL:CBX97313.1};
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; FP929131; CBX97313.1; -; Genomic_DNA.
DR   RefSeq; XP_003840792.1; XM_003840744.1.
DR   AlphaFoldDB; E5A117; -.
DR   STRING; 985895.E5A117; -.
DR   EnsemblFungi; CBX97313; CBX97313; LEMA_P104440.1.
DR   GeneID; 13281190; -.
DR   eggNOG; ENOG502QVFK; Eukaryota.
DR   HOGENOM; CLU_029872_0_1_1; -.
DR   InParanoid; E5A117; -.
DR   OMA; RYAMIFE; -.
DR   OrthoDB; 1328767at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   CDD; cd01830; XynE_like; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR43784:SF3; GDSL FAMILY LIPASE; 1.
DR   PANTHER; PTHR43784; GDSL-LIKE LIPASE/ACYLHYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00820)-RELATED; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..454
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003194741"
FT   DOMAIN          235..431
FT                   /note="SGNH hydrolase-type esterase"
FT                   /evidence="ECO:0000259|Pfam:PF13472"
SQ   SEQUENCE   454 AA;  49046 MW;  E65356391560EEAA CRC64;
     MQGRMMIFSR LAVLLLGVVV LVKGEDGDQN AAGRKAIRPN PSKGHWIDAW ATMPQLTEPA
     NLPPAPFNQT GAVFVNSTIR QTLFMTATAK QIRLKFSNVF GGSNLPITAV TVALPINNTA
     GIHQIQPHTL QNVTFFGQSS ISIPNGALAV SDPLNFPIHA QQVITVTLYL ATGQLSNAIT
     SHPGSRTTSY FQFGNAVHAP SINVNDPASQ AAAHWYFLSS IEAWTPRHQT SLVLLGDSIT
     DGRGSTTNAN NRWPDQLLSR LQSSPSTSHI ALSNLAAGGN RILADGLGPS AFSRIDRDIL
     AHPNVAAVLV FIGVNDIGTT DPSPAAQSTL FPALTQAYAQ IVALLHGHAI PVFAATITPF
     SAPANASSIQ PYSHPERERT RQRVNAWIRN SAVFDGVVDF DAVVRDPRVP ERLDARFDVG
     DYLHLSPRGY RELAERFPVE LLIRRGGYEF GGFF
//
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