ID M28P2_PYRTT Reviewed; 483 AA.
AC E3RJ99;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Probable zinc metalloprotease PTT_08196;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN ORFNames=PTT_08196;
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1;
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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}.
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; GL533450; EFQ94200.1; -; Genomic_DNA.
DR RefSeq; XP_003297704.1; XM_003297656.1.
DR AlphaFoldDB; E3RJ99; -.
DR SMR; E3RJ99; -.
DR EnsemblFungi; EFQ94200; EFQ94200; PTT_08196.
DR KEGG; pte:PTT_08196; -.
DR eggNOG; ENOG502R701; Eukaryota.
DR HOGENOM; CLU_047420_0_0_1; -.
DR OrthoDB; 1767742at2759; -.
DR Proteomes; UP000001067; 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 CDD; cd05642; M28_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 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 PTT_08196"
FT /id="PRO_0000411762"
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; 52168 MW; 88C9B7C36958BDAC CRC64;
MLFRSVILSN ALLLPACAHD ILSNLDLSLP IAANAESYTD CANAAWPPSN VGVELVPQPP
DDQLRAMVDE VSAENIEATI TKLVSFGTRH TLSTFNSSTR GINAARDWIA SEMRKYAAES
NGTMTVEVQS YVQSVASRIP FPVTISNVLA KATGSEDPNR VYVMTGHYDS RVTDVLNYES
DAPGANDDAS GTAIAMELAR VLAKHQPKST IILGAVAGEE QGLYGSTYLA QTLKNTSTNV
EGMLNCDIVG SSTGDRGQKD PFTIRAFAQG PPPISAESSA RAAQRLQIGG ENDSPARELA
RFSAEVAANN ATGMNVAIIY RLDRFLRGGD HTGFLQAGYP AIRYTEPNEN FAHQHQDIRT
ENGTVYGDLI EFVDFDFTAR VGKVNLATLW SLAQAPAMPR NVTIDATILD NNSRIKWIVS
NKTDVASYEV VWRSTIASLW THMLDVGKVG YVVLPLSKDN VIFGIRAVGT NGFKSPAVYP
FPA
//
