SED3_ARTBC
ID SED3_ARTBC Reviewed; 593 AA.
AC D4AK75; D4AK76;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 49.
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=ARB_04677/ARB_04678;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
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=EFE37148.1; Type=Frameshift; Note=The predicted genes ARB_04677 and ARB_04678 have been merged.; Evidence={ECO:0000305};
CC Sequence=EFE37149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EFE37149.1; Type=Frameshift; Note=The predicted genes ARB_04677 and ARB_04678 have been merged.; Evidence={ECO:0000305};
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DR EMBL; ABSU01000001; EFE37148.1; ALT_FRAME; Genomic_DNA.
DR EMBL; ABSU01000001; EFE37149.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003017793.1; XM_003017747.1.
DR RefSeq; XP_003017794.1; XM_003017748.1.
DR AlphaFoldDB; D4AK75; -.
DR SMR; D4AK75; -.
DR EnsemblFungi; EFE37148; EFE37148; ARB_04677.
DR EnsemblFungi; EFE37149; EFE37149; ARB_04678.
DR GeneID; 9522640; -.
DR GeneID; 9522641; -.
DR KEGG; abe:ARB_04677; -.
DR KEGG; abe:ARB_04678; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR HOGENOM; CLU_1730971_0_0_1; -.
DR Proteomes; UP000008866; 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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000406412"
FT CHAIN 199..593
FT /note="Probable tripeptidyl-peptidase SED3"
FT /id="PRO_0000406413"
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 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; 65507 MW; 225DE526838E5FE8 CRC64;
MLLRWHSVIP LFLAMTVAFP NTYRTVVEDL PAIPEGWVQG NPPSPETSVR MNLAVGQQNT
RTFEQIVLDI STPGHRNYGK HLSRRDLKGL LRPRRETSNL ILSWLEKSGV PKRSIVDDGD
WIHFVISISQ AERMLQTRFY HFHDVQDPGI SMIRTLKYSV PSRLARHVYM IQPTTKFGKP
KKHANSIANL QAIYLSTNAT ENCNATITPR CLRELYKMGD YVAKPDCRNV IGVSGYLDQY
ARYSDFYKFL ELYAPEMKGA NFSVAHIGNG QNLQNSTRNS IEASLDIEYA LGLSNASAVF
YTTSGRGPLV PDLDQPEQEH NSNEPYLDQL HYLLSLPQEA LPAVLSTSYG ENEQSVPERF
SHATCNLFAQ LGARGVSVIF SSGDSGVGSS CLTNDKKKIT RFNPTFPASC PFVTSVGATF
KINPERATGF SSGGFSDRHS RPGYQNDAVQ HYLDKLGDRW KGLYNPKGRG IPDVSAQGAN
FAIYDHGKVI IVSGTSASAP AFAAIIANLN AIRLRANKPV LGYLNPFIYG KGREGFTDIV
HGGSKGCVGY SSTNRSTPAV PYASWNATEG WDPVTGVGTP NFRILAKIVQ HME
