SED3_TRIVH
ID SED3_TRIVH Reviewed; 593 AA.
AC D4D7N6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Probable tripeptidyl-peptidase SED3;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-C;
DE Flags: Precursor;
GN Name=SED3; ORFNames=TRV_03120;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE42120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EFE42120.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; ACYE01000161; EFE42120.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003022738.1; XM_003022692.1.
DR AlphaFoldDB; D4D7N6; -.
DR SMR; D4D7N6; -.
DR EnsemblFungi; EFE42120; EFE42120; TRV_03120.
DR GeneID; 9581428; -.
DR KEGG; tve:TRV_03120; -.
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; 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; Secreted;
KW Serine protease; Signal; Virulence; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397833"
FT CHAIN 199..593
FT /note="Probable tripeptidyl-peptidase SED3"
FT /id="PRO_0000397834"
FT DOMAIN 206..592
FT /note="Peptidase S53"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 286
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 496
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
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 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 593 AA; 65390 MW; DF1AD6C09588AD9B CRC64;
MLLRWHSVIP LFLTMTVALP NTYRTVVEDL PAIPEGWVQG NPPSPETSVR MNLAVGQRNT
RTFEQIVLDI STPGHRNYGK HLSRRDLKGL LRPRRETSNL ILSWLEESGV PKRSIVDDGD
WIHFVISISQ AERMLQTRFY YFHDVQDPGI SMIRTLKYSV PSRLARHVYM IQPTTKFGKP
KKHANSVASL QVIYSSTNAT ENCNATITPR CLRELYKMGD YVAKPDCRNV IGISGYLDQY
ARYSDFYKFL ELYAPEMKGA NFSVAHIGNG QNLQNSTRNS IEASLDIEYA LGLSNASAVF
YTTSGRGPLV PDLDQPEQEH NSNEPYLDQL HYLLSLPQEA LPAVLSTSYG ENEQSVPERF
SHATCNLFAQ LGARGVSVIF SSGDSGVGSS CLTNGKKKIT RFNPTFPASC PFVTSVGATF
KINPERAIGF SSGGFSDRHS RPVYQNDAVQ HYLDKLGDQW KGLYNPKGRG IPDVSAQGAN
FAIYDHGKVI TVSGTSASAP AFAAIIANLN AIRLRANKPV LGYLNPFIYG KGREGFTDIV
HGGSKGCVGY SSTNGSTPAV PYASWNATEG WDPVTGVGTP NFRILAKIVQ HME
