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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//