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Database: UniProt
Entry: E4ZR03_LEPMJ
LinkDB: E4ZR03_LEPMJ
Original site: E4ZR03_LEPMJ 
ID   E4ZR03_LEPMJ            Unreviewed;       498 AA.
AC   E4ZR03;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=LEMA_P033420.1 {ECO:0000313|EMBL:CBX93668.1};
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
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DR   EMBL; FP929116; CBX93668.1; -; Genomic_DNA.
DR   RefSeq; XP_003837108.1; XM_003837060.1.
DR   AlphaFoldDB; E4ZR03; -.
DR   STRING; 985895.E4ZR03; -.
DR   EnsemblFungi; CBX93668; CBX93668; LEMA_P033420.1.
DR   GeneID; 13284635; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_024336_1_1_1; -.
DR   InParanoid; E4ZR03; -.
DR   OMA; YVYGLTY; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04816; PA_SaNapH_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF17; AMINOPEPTIDASE Y; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:CBX93668.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   DOMAIN          131..224
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          251..447
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   498 AA;  53053 MW;  72E92F1975B3C435 CRC64;
     MKIQHGITFA CAAHVYAAAF PATTYGDKLR PFVSSQEIQS AIKTEKLMGN LEAFDSIAKA
     NGGNRAFGLP GYAASVDYIL SKTQNTNFKT WVQDFPALFF RVESIKFTVS NTSYHVIGLS
     YSPSTTREGL TAPLVLGASG PEGCNVAAYD NIDVQDKIVL VQRGTCPDGT TLAGRIKPAV
     AAGAAAVILY SDVITPVTGG TLSNPNPEEY RPSGYINLAD GEPLAARLRA GESLEAYFQQ
     TQTVETRITQ NVFSETKDGD PSNVIMLGAH LDSVQAGAGI NDDGSGSTLI LELAKALRKF
     RVKNKVRFAW WGAEENGLLG SKYYTQNLNV TEANNILTYL NFDMVSRGYY GVFDGDGSSF
     NLTGAPGSGA IEKLFVDHLT QNGINVTAAR FTGGSDYQSF MNIGKPVGGL FTGTGVEQDP
     CYHQACDSID NPNPTTLTIN AKAAAHVLSI LATKGTELIP QSPVNASMIT SRGLVGIEPQ
     WTVPVEGDDH SSTCGHEI
//
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