SED1_ARTOC
ID SED1_ARTOC Reviewed; 670 AA.
AC C5FHK0;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Tripeptidyl-peptidase SED1;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-A;
DE Flags: Precursor;
GN Name=SED1; ORFNames=MCYG_01559;
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; DS995702; EEQ28740.1; -; Genomic_DNA.
DR RefSeq; XP_002848625.1; XM_002848579.1.
DR AlphaFoldDB; C5FHK0; -.
DR SMR; C5FHK0; -.
DR EnsemblFungi; EEQ28740; EEQ28740; MCYG_01559.
DR GeneID; 9230764; -.
DR eggNOG; ENOG502QZ4I; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR OMA; AWINDAR; -.
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; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..231
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390742"
FT CHAIN 232..670
FT /note="Tripeptidyl-peptidase SED1"
FT /id="PRO_0000390743"
FT DOMAIN 241..669
FT /note="Peptidase S53"
FT ACT_SITE 318
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 322
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 586
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 627
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 670 AA; 73464 MW; 0CA76062EACACE14 CRC64;
MSTMIFMYFI YIVLYASGIA ANLSYHVHEK RSIPVWWQRV SRIDPHAFLP LTIALAQQNL
EHAEDYLLSV SDPSSPQYAQ YWTAEAVAAK FAPSEPTARK VMSWLNQSGI APAGVRRSKS
GGELYMNITA QEAEKLLHTT FYIYKHQLTN KTLAICEKYS VATFVEKYVD FITTTEQFHH
GLRRRSFQDP EPRMPSGKSP GHYVELADDS FPFPYLSFGS SVGLLKNKIL SDSLPSNCDK
LITPDCLRAL YHIPVRNTSH PDNSLGIIEF TWVGYLESDL DKFFNIFQPS MVGNRPKFES
IDGGFIQTLV PSFAFNGEAD LDIEYAMALT HPLNITNYQV GDIWSLGNMN NFLASLDSTY
CSAVDPVYDP IYPDPTPANP PLPSGYNSSD CGTHKPTKVI SISYAYEEGE FSPAYERRQC
LEYLKLGLQG VTVVFASGDH GTATRDGMCG NTVIDSNQIS DHEPSYVPTF PSTCPYVTSV
GGTQVPANGS VLDAEVAFDT IITSSDGNVS SRLTSAGGFS NVFAVPGYQA TATRDYLQRL
QNKYTLPVNL NVTGFGSGRG FPDVAANAAA YATAVNGKLV KVYGTSASAP VFASVIAWIN
DARLNMGKQP VGFVNPVLYA NPQVLNDVAK GSNYDCANLP AYHASSGWDP VTGLGTPNFD
RMLDLFLQLS
