ID   SED2_TRIVH              Reviewed;         596 AA.
AC   D4DBH6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Probable tripeptidyl-peptidase SED2;
DE            EC=3.4.14.10;
DE   AltName: Full=Sedolisin-B;
DE   Flags: Precursor;
GN   Name=SED2; ORFNames=TRV_04476;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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}.
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DR   EMBL; ACYE01000226; EFE40784.1; -; Genomic_DNA.
DR   RefSeq; XP_003021402.1; XM_003021356.1.
DR   AlphaFoldDB; D4DBH6; -.
DR   SMR; D4DBH6; -.
DR   EnsemblFungi; EFE40784; EFE40784; TRV_04476.
DR   GeneID; 9578281; -.
DR   KEGG; tve:TRV_04476; -.
DR   HOGENOM; CLU_013783_3_0_1; -.
DR   Proteomes; UP000008383; 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; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..203
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397831"
FT   CHAIN           204..596
FT                   /note="Probable tripeptidyl-peptidase SED2"
FT                   /id="PRO_0000397832"
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;  64750 MW;  F1065580997B5ED2 CRC64;
     MRLLKFVCLL ASVAAAKPTP GASHKVIEHL DFVPEGWQMV GAADPAAIID FWLAIERENP
     EKLYDTIYDV STPGRAQYGK HLKREELDDL LRPRVETSES IISWLTNGGV NPQHIRDEGD
     WVKFSTNVKT AEKLMNTRFN VFKDNLNSVS KIRTLEYSVP VAISAHVQMI QPTTLFGRQK
     PQNSLILNPL TKDLESMSVE EFAASQCRSL VTTACLRELY GLGDRVTQAR DDNRIGVSGF
     LEEYAQYRDL ELFLSRFEPS AKGFNFSEGL IAGGKNTQGG PGSSTEANLD MQYVVGLSHK
     AKVTYYSTAG RGPLVPDLSQ PSQASNNNEP YLEQLRYLVK LPKNQLPSVL TTSYGETEQS
     LPASYTKATC DLFAQLGTMG VSVIFSSGDT GPGSSCQTND GKNATRFNPI YPASCPFVTS
     IGGTVGTGPE RAVSFSSGGF SDRFPCPQYQ DNAVKGYLKI LGNQWSGLFD PNGRAFPDIA
     AQGSNYAVYD KGRMTGVSGT SASAPAMAAI IAQLNDFRLA KGSPVLGFLN PWIYSKGFSG
     FTDIVDGGSR GCTGYDIYSG LKAKKVPYAS WNATKGWDPV TGFGTPNFQA LTKVLP