ID   SED2_ARTOC              Reviewed;         596 AA.
AC   C5FBW2;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Tripeptidyl-peptidase SED2;
DE            EC=3.4.14.10;
DE   AltName: Full=Sedolisin-B;
DE   Flags: Precursor;
GN   Name=SED2; ORFNames=MCYG_00184;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at
CC       acidic pHs and is involved in virulence. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC         EC=3.4.14.10;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
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; DS995701; EEQ27296.1; -; Genomic_DNA.
DR   RefSeq; XP_002850080.1; XM_002850034.1.
DR   AlphaFoldDB; C5FBW2; -.
DR   SMR; C5FBW2; -.
DR   STRING; 63405.XP_002850080.1; -.
DR   EnsemblFungi; EEQ27296; EEQ27296; MCYG_00184.
DR   GeneID; 9230210; -.
DR   eggNOG; ENOG502QR6D; Eukaryota.
DR   HOGENOM; CLU_013783_3_0_1; -.
DR   OMA; CDMIGQL; -.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   3: Inferred from homology;
KW   Calcium; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..203
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390745"
FT   CHAIN           204..596
FT                   /note="Tripeptidyl-peptidase SED2"
FT                   /id="PRO_0000390746"
FT   DOMAIN          210..596
FT                   /note="Peptidase S53"
FT   ACT_SITE        286
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        501
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         543
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         544
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         576
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         578
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   596 AA;  64843 MW;  B64DC85AF7340C18 CRC64;
     MLVLKFVCLL ASVAAAKPTS WSSHKVVEHL ESAPEGWRIV GAADPAAVID FWLAIERENP
     EQLYDTIYDV STPGRARYGK HLKREELDDL LRPRVETSEG IISWLTNGGV KPQGIRDEGD
     WIRFSTDVKT AEQLMKTQFH VFKDDVSSVS RIRTLEYSVP ASISSHVQMI QPTTLFGRQK
     PQNSLILSPL TTDLEAMSEE EFSASNCRSL VTTACLRELY GLGDRVTQAR DDNRIGVSGF
     LEEYAQYRDL DLFLSRFEPS AKGFNFSEGL IAGGKNTQGG PGSSTEANLD MQYVVGLSHK
     AKVTYYSTAG RGPLIPDLSQ PDQASNDNEP YLEQLRYLVK LPKNQLPSVL STSYGDTEQS
     LPASYTKATC DLFAQLGTMG VSVIFSSGDT GPGSSCQTND GKNSTRFNPI YPASCPFVTS
     IGGTVGTEPE RAVSFSSGGF SDRFPRPQYQ DNAVKGYLKI LGNQWSGLFN PNGRAFPDIA
     AQGSNYAVYD KGRMTGVSGT SASAPAMAAI IAQLNDFRLA KGSPVLGFLN PWIYSKGFSG
     FTDIVDGGSR GCTGYDIYSG LKAKRVPYAS WNATKGWDPV TGFGTPNFQA LTKVLP