M28P2_PYRTR
ID M28P2_PYRTR Reviewed; 483 AA.
AC B2W3C7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Probable zinc metalloprotease PTRG_04977;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN ORFNames=PTRG_04977;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231618; EDU47884.1; -; Genomic_DNA.
DR RefSeq; XP_001935310.1; XM_001935275.1.
DR AlphaFoldDB; B2W3C7; -.
DR SMR; B2W3C7; -.
DR EnsemblFungi; EDU47884; EDU47884; PTRG_04977.
DR GeneID; 6343221; -.
DR eggNOG; ENOG502R701; Eukaryota.
DR HOGENOM; CLU_047420_0_0_1; -.
DR InParanoid; B2W3C7; -.
DR OMA; NNDMIGN; -.
DR OrthoDB; 607736at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
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 InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..483
FT /note="Probable zinc metalloprotease PTRG_04977"
FT /id="PRO_0000411761"
FT DOMAIN 396..483
FT /note="Fibronectin type-III"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 483 AA; 52235 MW; B70A7DBB5682DD81 CRC64;
MLFRSALLSN VLLLPACAHD VLFSRDLPLP IAANAESYTD CANAAWPPSN VGVELVPQPP
DDELRAMVDE MSAENIEATI TKLVSFGTRH TLSTFNSSTR GINAARDWIA SEMRKYAAES
NGTMTVEVQS YVQGVASRIP FPVTISNVLA KATGSEDPSR VYVMTGHYDS RVTDVLNYES
DAPGANDDAS GTAIAMELAR VLAKHQPKST IILGAVSGEE QGLYGSTYLA QTLKNTSTNV
EGMLNCDIVG SSTGDRGQKD PFTIRAFAQG PPPLSAESSA KAAQRLQIGG ENDSPARELA
RFSAEVAANN ATGMKVAIIY RLDRFLRGGD HTGFLQAGYP AIRYTEPNEN FAHQHQDIRT
ENGTVYGDLI EFVDFDFTAR VGKVNLATLW SLAQAPAMPR NVTIDATILD NESRIKWIIS
NSTDVASYEV VWRSTIASLW THMLDVGKVG YVVLPLSKDN VIFGIRAVGK NGYKSPAVYP
FPG
