ID   SED4_ARTOC              Reviewed;         601 AA.
AC   C5FRX4;
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 SED4;
DE            EC=3.4.14.10;
DE   AltName: Full=Sedolisin-D;
DE   Flags: Precursor;
GN   Name=SED4; ORFNames=MCYG_05446;
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}.
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DR   EMBL; DS995705; EEQ32627.1; -; Genomic_DNA.
DR   RefSeq; XP_002845577.1; XM_002845531.1.
DR   AlphaFoldDB; C5FRX4; -.
DR   SMR; C5FRX4; -.
DR   STRING; 63405.XP_002845577.1; -.
DR   EnsemblFungi; EEQ32627; EEQ32627; MCYG_05446.
DR   GeneID; 9224263; -.
DR   eggNOG; ENOG502QR6D; Eukaryota.
DR   HOGENOM; CLU_013783_3_0_1; -.
DR   OMA; WETGWGT; -.
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; 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; 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..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..202
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390752"
FT   CHAIN           203..601
FT                   /note="Tripeptidyl-peptidase SED4"
FT                   /id="PRO_0000390753"
FT   DOMAIN          212..601
FT                   /note="Peptidase S53"
FT   ACT_SITE        288
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        292
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        504
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         546
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         547
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         579
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         581
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        575
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   601 AA;  65913 MW;  095BD68081FBE309 CRC64;
     MVSFTLRAIG ACLVSLPALV TAAPTSHISG DFQVLEQLHE VPQGWVQTGS PAPSSQLKFK
     LALQQDKAAA FEQHVMDISN PKHENYGKHM TQEEVDAFLQ PPAHMTDSVF NWLASEGIPK
     HSIKADTDWL TFTTTVQKAE KLLNTRFYNF KNTIDNTQVI RTLQYSVAET VAPYVHMIQP
     TTKFSAPRPE LSSVFTSDLE ITSSADVDCN VTITPDCIRD LYKMGNTFAK KDPRNRLGIS
     GYLEQYARLD DFSTFIDMFV PSLKGTTFDF KSINGGKNEQ NSSLDSVEAS LDVDYAIGLS
     GALSTYYGTA GRGMLIPDLD QPNITNNNNE PYLEQLHYLL GLPDSELPAV LSTSYGENEQ
     SVPKKYTDSA CHLFARLGAR GVSVIFSSGD TGVGSACQSN DGKKITKFNP IFPAACPFVT
     SVGGTHQINP EVAIHFSSGG FSERFSRPWY QELDVNHYLQ HELEHGKWDG MYNPSGRGFP
     DVSAQSYKFA TRDHGRTIGV SGTSASAPLF AGVVSILNSI RLAHHKPRLG FLNPWLYTIG
     RSGFTDIVHG GSDGCTGTDQ YSHLPTPYVP GASWNATRGW DPVTGLGTPN FETLSKLVLQ
     Y