M28P3_PHANO
ID M28P3_PHANO Reviewed; 496 AA.
AC Q0UNS4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Probable zinc metalloprotease SNOG_06590;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN ORFNames=SNOG_06590;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445333; EAT86421.2; -; Genomic_DNA.
DR RefSeq; XP_001796957.1; XM_001796905.1.
DR AlphaFoldDB; Q0UNS4; -.
DR SMR; Q0UNS4; -.
DR EnsemblFungi; SNOT_06590; SNOT_06590; SNOG_06590.
DR GeneID; 5973836; -.
DR KEGG; pno:SNOG_06590; -.
DR eggNOG; ENOG502R701; Eukaryota.
DR HOGENOM; CLU_047420_0_0_1; -.
DR InParanoid; Q0UNS4; -.
DR OrthoDB; 607736at2759; -.
DR Proteomes; UP000001055; 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; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..496
FT /note="Probable zinc metalloprotease SNOG_06590"
FT /id="PRO_0000411766"
FT DOMAIN 402..496
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
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 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 54820 MW; 3309D3F80B640BD7 CRC64;
MRSSMFFAVC AAAALQTALS SPIHPRHAHQ SFPNTEQWPI ATVGKALKQQ LPDEELQGIL
SQVSQDNIEA TIRKLASFGT RHTLSSQTDP ARGIGAARTW LTEQFQEAAD ASEGRMTVDW
NSFVKYPGDN ERIIFPVNIT NIVTTLKGSE DPDRLYVTGG HYDSRNSNPI DYQGDAPGAV
DVSNSCYTNW VWEDASGVAV SLELARIFAK YQPKTTIVFT AFAGEEQGLL GAENLAQTYK
NNSVNVAGMI NLDMVGNSKA EDGTSDPYNI RLFCQGTPLT ENSTTTTSRL SIGGDNDSPA
RNLGRHIYEV ASNAFTEMTV RLIYRLDRYS RGGDHRPFLE AGYTGVRFVQ PNEDYTQQHQ
NVTVRNGKQY GDLVEWLDFE YNTRAAKVVA STMWSLANAP GEPMNVGINT TTSDNFSQFK
WTAPKGLPVE GYEIVYRETL EPHWTSVIEV GDVNWYNLTS ATIHKDNVIF GVRSVGKGGY
RSPAVLPFPF GCTRNC
