ID   MEP1_PODAN              Reviewed;         293 AA.
AC   B2AC45; A0A090CKY3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Extracellular metalloprotease PODANS_2_14170;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=Pa_2_14170; ORFNames=PODANS_2_14170;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR   EMBL; CU633447; CAP61020.1; -; Genomic_DNA.
DR   EMBL; FO904937; CDP26407.1; -; Genomic_DNA.
DR   RefSeq; XP_001903248.1; XM_001903213.1.
DR   AlphaFoldDB; B2AC45; -.
DR   SMR; B2AC45; -.
DR   MEROPS; M43.002; -.
DR   EnsemblFungi; CAP61020; CAP61020; PODANS_2_14170.
DR   GeneID; 6187257; -.
DR   KEGG; pan:PODANSg260; -.
DR   VEuPathDB; FungiDB:PODANS_2_14170; -.
DR   eggNOG; ENOG502S6EM; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   OrthoDB; 1569419at2759; -.
DR   Proteomes; UP000001197; Chromosome 2.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04275; ZnMc_pappalysin_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR008754; Peptidase_M43.
DR   Pfam; PF05572; Peptidase_M43; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..293
FT                   /note="Extracellular metalloprotease PODANS_2_14170"
FT                   /id="PRO_0000407204"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        242..269
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  31294 MW;  1AC4CF05108C8586 CRC64;
     MRFSLALAAA GLAQTAFAAP QPSRGFGCGA PEPSEELLQV SQQFAVEEAQ ALAESYRSGN
     LTARDVTAQA ISVKVYIHVV AASTALSGGY LTDTMINNQF SVLQSAFAPY GISFTLAGTD
     KTVNANWADD SKGYEMTMKR ALRKGTYKDL NLYFLQKMGG NLGYCYFPTT ASPGSTAYIR
     DGCTILYSTT PGGSSTNYNL GHTATHEVGH WFGLYHTFQG GCTGAGDSVS DTPAQASASS
     GCPVGRDSCP SQAGVDPIHN YMDYSIDSCY EEFTPGQQTR INSFWTSYRQ NAS