SED4_TRIVH
ID SED4_TRIVH Reviewed; 600 AA.
AC D4D9U2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Probable tripeptidyl-peptidase SED4;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-D;
DE Flags: Precursor;
GN Name=SED4; ORFNames=TRV_03885;
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=EFE41373.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; ACYE01000199; EFE41373.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_003021991.1; XM_003021945.1.
DR AlphaFoldDB; D4D9U2; -.
DR SMR; D4D9U2; -.
DR EnsemblFungi; EFE41373; EFE41373; TRV_03885.
DR GeneID; 9578875; -.
DR KEGG; tve:TRV_03885; -.
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; 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; Secreted;
KW 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_0000397837"
FT CHAIN 203..600
FT /note="Probable tripeptidyl-peptidase SED4"
FT /id="PRO_0000397838"
FT DOMAIN 212..600
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 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 600 AA; 65320 MW; FF1E6358DE7C859A CRC64;
MVSFTLRAIG ACLIGLPALI TAAPTSHVSN GFHVVEQLNG VPQGWVQEGS PAPSTQMKFK
LALVQGKTAE FEQRVMDISN PKHADYGKFM SREELDAFLQ PSSQVKDSVF NWLASEGISK
RSVKSNTDWL TFTTSIATAE KLFNTRFYTF KNTADGSQII RTLKYSVAAS AAPYVQMVQP
TTKFSAPRPE LSSVFTSDLE MTSSANVDCN VTITPDCIRE LYKMGNTFAT KDPRNRLGIS
GYLEQYARLD DFSTFIDMFV PSLKGTTFDF KSIDGAKNEQ NSSLDSVEAS LDVDYAIGLS
GALSTYYGTA GRGKLIPDLD QPNITENNNE PYIEQLFYLL DLPDSELPAV LSTSYGENEQ
SVPPTYSSVV CSLFGRLGAR GVSVIFSSGD TGVGSACQSN DGKNTTKFNP IFPAACPFVT
SVGGTRQINP EVAIHFSSGG FSERFARPWY QELDVRYYLG HELEKGKWDG LYNPHGRGFP
DVAAQSYKFA TRDHGKTIGV SGTSASAPLF AGVVSILNSI RLAHNKPRMG FLNPWLYTIG
RSGFTDIVHG GSDGCTGTDM YSHLPTPYVP GASWNATKGW DPVTGLGTPN FEKLSKLVLI
