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Database: UniProt
Entry: E5A0A6_LEPMJ
LinkDB: E5A0A6_LEPMJ
Original site: E5A0A6_LEPMJ 
ID   E5A0A6_LEPMJ            Unreviewed;       347 AA.
AC   E5A0A6;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   28-JUN-2023, entry version 44.
DE   SubName: Full=Similar to zinc metalloproteinase {ECO:0000313|EMBL:CBX96966.1};
GN   ORFNames=LEMA_P100970.1 {ECO:0000313|EMBL:CBX96966.1};
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; FP929130; CBX96966.1; -; Genomic_DNA.
DR   RefSeq; XP_003840445.1; XM_003840397.1.
DR   AlphaFoldDB; E5A0A6; -.
DR   STRING; 985895.E5A0A6; -.
DR   MEROPS; M80.A04; -.
DR   EnsemblFungi; CBX96966; CBX96966; LEMA_P100970.1.
DR   GeneID; 13283578; -.
DR   eggNOG; KOG4842; Eukaryota.
DR   HOGENOM; CLU_056790_0_0_1; -.
DR   InParanoid; E5A0A6; -.
DR   OMA; GMQKHPF; -.
DR   OrthoDB; 1469126at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0070628; F:proteasome binding; IEA:EnsemblFungi.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:EnsemblFungi.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR013536; WLM_dom.
DR   PANTHER; PTHR47795:SF1; DNA-DEPENDENT METALLOPROTEASE WSS1 HOMOLOG 2; 1.
DR   PANTHER; PTHR47795; UBIQUITIN AND WLM DOMAIN-CONTAINING METALLOPROTEASE SPCC1442.07C; 1.
DR   Pfam; PF08325; WLM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51397; WLM; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT   DOMAIN          128..331
FT                   /note="WLM"
FT                   /evidence="ECO:0000259|PROSITE:PS51397"
FT   REGION          297..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  38303 MW;  BA68C63685C7BC7E CRC64;
     MADTDSLSAP TASSDELQLT LTHHGKPVTL SFPRYATISD LSDRVAAELS IPPSNQKFLL
     ASKHGLQKPP FKDPTLALST IASKKITLMG STTAEISSLN ATITAASAAR RQGPIKTATP
     ARHRDYKKIQ EEAQYTFHTL RPLPYLPNPD RSLRFLERLR DEEGIKAAMR THKFSVPLLT
     EMDPAMHTTQ ESRTLGLNRN RGEVIELRLR TDAYDGYRDY KTIRNTLCHE LAHNVWGPHD
     RNFWELCKQI EREVARDDWK SGGRSVADVQ YYEPGGEDEV HDHGGWTGGE FTLGGTSSGS
     GSTVGVAGNN VTMDGLSRRE VLAKAAEERM KRTKRAEEET GGSGGAS
//
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