SED3_ARTOC
ID SED3_ARTOC Reviewed; 595 AA.
AC C5FTQ5;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Tripeptidyl-peptidase SED3;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-C;
DE Flags: Precursor;
GN Name=SED3; ORFNames=MCYG_06077;
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; EEQ33258.1; -; Genomic_DNA.
DR RefSeq; XP_002846208.1; XM_002846162.1.
DR AlphaFoldDB; C5FTQ5; -.
DR SMR; C5FTQ5; -.
DR STRING; 63405.XP_002846208.1; -.
DR MEROPS; S53.010; -.
DR EnsemblFungi; EEQ33258; EEQ33258; MCYG_06077.
DR GeneID; 9228377; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR HOGENOM; CLU_013783_3_0_1; -.
DR OMA; TPGHRSY; -.
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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..201
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390748"
FT CHAIN 202..595
FT /note="Tripeptidyl-peptidase SED3"
FT /id="PRO_0000390749"
FT DOMAIN 209..595
FT /note="Peptidase S53"
FT ACT_SITE 285
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 499
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 573
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 575
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 595 AA; 65327 MW; 720BC52270A5FED1 CRC64;
MLLPWQQTII ILFLGVNSLV AALRNTYRTV EELPTIPEGW IQGKPPSPET SIRMNLALFQ
EKAHAFEQMV VDISTPGHSN YGKHLSRRTL KDFLRPRKEV SDSILSWLEE AGVAKKSILN
DGDWIHFAIS VSQAERMLKT RFHYYHDSGD PSVFMIRTLQ YSVPSHLAPD IHMIQPTTKF
GKPKKHGNSI AKLETIQLSS NATTNCNVTI TPQCLRDIYK MGNSLATPDY RNVIGVSGYL
DQYARYNDFY KFIDLYAPDL KGANFSVKYI GKGQNLQNST KNSVEASLDI DYALGLSNAT
TVFYTTSGRG PLVPDLEQPD QEHNSNEPYL DQLHYLLSLP SDELPAILST SYGENEQSVP
EKFSNATCSL FAQLAARGVS VIFSSGDTGV GSSCLTNGRK KVSRFNPTFP ASCPFVTSVG
ATFRINPEMA ISFSSGGFSD RHIRPRFQDD AVLTYLDKLG NQWEGLYDPR GRGIPDVAAQ
GSNFAVYDHG RVGMVSGTSA SAPAFAAIIA NLNSIRLNAN KPVLGYLNPF IYGQGRQGFT
DIVHGGSRGC AGYNSTNGSA PAVPYASWNA TEGWDPVTGV GTPNFEILAK IVRDL
