ID   Y3666_SORMK             Reviewed;         452 AA.
AC   P0CI30; D1Z8W6; F7VVU3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Peptidase M20 domain-containing protein SMAC_03666.2;
DE   Flags: Precursor;
GN   ORFNames=SMAC_03666.2;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(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 M20A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCC09634.1; Type=Erroneous gene model prediction; Note=The predicted gene SMAC_03666 has been split into 2 genes: SMAC_03666.1 and SMAC_03666.2.; Evidence={ECO:0000305};
CC       Sequence=CCC09634.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CABT02000009; CCC09634.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P0CI30; -.
DR   SMR; P0CI30; -.
DR   STRING; 771870.P0CI30; -.
DR   PRIDE; P0CI30; -.
DR   EnsemblFungi; CCC09634; CCC09634; SMAC_03666.
DR   eggNOG; KOG1468; Eukaryota.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_339236_0_0_1; -.
DR   InParanoid; P0CI30; -.
DR   OrthoDB; 1410886at2759; -.
DR   Proteomes; UP000001881; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR001160; Peptidase_M20C.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PRINTS; PR00934; XHISDIPTASE.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..452
FT                   /note="Peptidase M20 domain-containing protein
FT                   SMAC_03666.2"
FT                   /id="PRO_0000401970"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  48342 MW;  8423FEBFA53450CD CRC64;
     MKATSNLLLL WGTSLLSPSS AFVIDNHHYQ HPLVVDDSSS SSISPLKIFT SSGPSANKED
     APSYRKNLLS LHKSLIEIPS ISRTEQEVGK FLLDYLRNNL GYIAKAQFLE GSSSDPFSQY
     DDDDHSQGRF NVLAWPSSHN LSSPRVLVTS HIDVVPPFIP YHISTSSESD EEITSDAFIS
     GRGSVDAKAS VAAQIVAVEE LIRAKEVDPA DLMLLFVVGE EISGDGMKTF SVVYNDAEKS
     KKEELPRFKA AIYGEPTENK LSCGHKGHTG GVLKATGIAG HSGYPWLFKS ATEILVKALA
     KIIDADLGSS ERYGNTTVNI GTIAGGVAAN VIPKEASAKL AIRVAAGNQA TGADIVRSAV
     DKILKEVDEE AFTMEWAGGY GPVECDCDVD GFETMVASYG TDVPNFEGDH VSYLYGPGSI
     LVAHGDDEGL KVGDLETAVE GYKTLIKHAL GA