M28P3_LEPMJ
ID M28P3_LEPMJ Reviewed; 502 AA.
AC E5R501;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Probable zinc metalloprotease Lema_P049800;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN ORFNames=Lema_P049800;
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 Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
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; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; FP929083; CBX92274.1; -; Genomic_DNA.
DR RefSeq; XP_003835639.1; XM_003835591.1.
DR AlphaFoldDB; E5R501; -.
DR SMR; E5R501; -.
DR EnsemblFungi; CBX92274; CBX92274; LEMA_P049800.1.
DR GeneID; 13288704; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_047420_0_0_1; -.
DR InParanoid; E5R501; -.
DR OMA; FEYNTRA; -.
DR OrthoDB; 607736at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; cd00063; FN3; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..502
FT /note="Probable zinc metalloprotease Lema_P049800"
FT /id="PRO_0000411765"
FT DOMAIN 408..502
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 502 AA; 55164 MW; 75FC32F447491D33 CRC64;
MSYVYTSLLL LAEVCEPKML PTFCTFALCA VPPLRSATAS PIHTHYPHAF PDTAQWPLAR
VGKALEQQLP GEDLQAIISE ISQANIEATI RKLASFGTRH TLSSQTDPER GIGAARTWLT
AKFQEAADAS EGRMTVDWNS FIKYPGDNER IIFPVNITTV VATLKGSEDP ERLYVTGGHY
DSRNSNPIDY QGDAPGAVDD ASGVAVSLEL ARIFARYRPK ASIAFTAFAG EEQGLLGAEH
LAQTYKNNSA NVAGMINLDM VGNSKAEDGT SDPNNIRLFC QGTPLTEDDT SAISRVSIGG
ENDSPARNLG RHIYEVASNA FTEMTVRLVY RLDRYSRGGD HRPFLEAGYT GVRFVQPNED
YTQQHQNVTV RAGKQYGDLV EWLDFEYNTR AAKVVASTMW SLANAPDIPR NVGSNVTTSD
NFSQFKWEAP VGLPPEGYEI VYRETIEPHW TSVIEVGNVQ WYNLTSATIH KDNVIFGVRS
VGAGGYRSPA VLPFPFGCTR NC
