ID   A0A5N5NS49_9PEZI        Unreviewed;       532 AA.
AC   A0A5N5NS49;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   05-FEB-2025, entry version 13.
DE   SubName: Full=Metalloprotease {ECO:0000313|EMBL:KAB5569917.1};
GN   ORFNames=GE09DRAFT_1101068 {ECO:0000313|EMBL:KAB5569917.1};
OS   Coniochaeta sp. 2T2.1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5569917.1, ECO:0000313|Proteomes:UP000325492};
RN   [1] {ECO:0000313|EMBL:KAB5569917.1, ECO:0000313|Proteomes:UP000325492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5569917.1,
RC   ECO:0000313|Proteomes:UP000325492};
RX   PubMed=31572496;
RA   Mondo S.J., Jimenez D.J., Hector R.E., Lipzen A., Yan M., LaButti K.,
RA   Barry K., van Elsas J.D., Grigoriev I.V., Nichols N.N.;
RT   "Genome expansion by allopolyploidization in the fungal strain Coniochaeta
RT   2T2.1 and its exceptional lignocellulolytic machinery.";
RL   Biotechnol. Biofuels 12:229-229(2019).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000256|ARBA:ARBA00003174}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family.
CC       {ECO:0000256|ARBA:ARBA00008721}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAB5569917.1}.
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DR   EMBL; VSMA01000007; KAB5569917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5NS49; -.
DR   OrthoDB; 291007at2759; -.
DR   Proteomes; UP000325492; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR   GO; GO:0098636; C:protein complex involved in cell adhesion; IEA:TreeGrafter.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046871; F:N-acetylgalactosamine binding; IEA:TreeGrafter.
DR   GO; GO:0070492; F:oligosaccharide binding; IEA:TreeGrafter.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:TreeGrafter.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04327; ZnMc_MMP_like_3; 1.
DR   Gene3D; 2.60.40.2080; -; 3.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR052487; Galactose-binding_lectin.
DR   InterPro; IPR037221; H-type_lectin_dom_sf.
DR   InterPro; IPR019019; H-type_lectin_domain.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR008754; Peptidase_M43.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR46938:SF1; DISCOIDIN-1 SUBUNIT A-RELATED; 1.
DR   PANTHER; PTHR46938; DISCOIDIN-1 SUBUNIT A-RELATED-RELATED; 1.
DR   Pfam; PF09458; H_lectin; 3.
DR   Pfam; PF05572; Peptidase_M43; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF141086; Agglutinin HPA-like; 3.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KAB5569917.1};
KW   Metalloprotease {ECO:0000313|EMBL:KAB5569917.1};
KW   Protease {ECO:0000313|EMBL:KAB5569917.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325492}.
FT   DOMAIN          42..190
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
SQ   SEQUENCE   532 AA;  60172 MW;  E2A8A8C6CA2341B8 CRC64;
     MGELVDDYPK TCVTDALISP EDLSESNIVG TPNGPSRLAL RKDAFWPNGK KLKVRFLNGT
     PFLQDKVKYY AQTWEKYANI DFQFVPSGDA EIRISFKWNG DGGSWSYLGT DNLHIAKDKP
     TMNYGWFDEN TRDEEFSRTV THEFGHALGC IHEHQSPAGS IRWNEARVIA DSKKSNGWDE
     AQTRQQIINK YQAAQTTNSE FDRNSIMCYF FPAEWTTDGQ GTPTNRVLSD KDKEFIGKMY
     PFQTRNSGKF RIQETREWYP PVALNSRVIQ FSPAYLEAPK LVLGLNEVDM DCKANIRIKV
     HTDAIEKRSG QDFKLNIDSW SDSSLYGGGA TWLEFAASEN DFQVGEFDTL TQRTIDQVPQ
     ADAQGVRRDV KTFTFPPGTY SQPPNVVVWL KALDLAKGAN WRVRALARNV TADKFELSIE
     SWSDTRLFSA AASWVAYPKG KEGVYSGVVN SLDYRTWYPP SQDNGGKVRF PKAYDKEPKV
     FAAINYLDMD SARNLRVKGF VDTVDNGGFA WHANTWGDSV LYSGGLNWIS FG
//