GenomeNet

Database: UniProt
Entry: SED3_ARTBC
LinkDB: SED3_ARTBC
Original site: 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   16-JAN-2019, entry version 39.
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)
OS   (Trichophyton 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.,
RA   Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W.,
RA   Kniemeyer O., Schroeckh V., Hertweck C., Hube B., White T.C.,
RA   Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F.,
RA   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
CC       at 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; Positions=109; 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; Positions=109; Note=The predicted genes ARB_04677 and ARB_04678 have been merged.; Evidence={ECO:0000305};
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   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   KO; K01279; -.
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:0009405; P:pathogenesis; 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; 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; Complete proteome; Glycoprotein; Hydrolase; Metal-binding;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   PROPEP       19    198       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000406412.
FT   CHAIN       199    593       Probable tripeptidyl-peptidase SED3.
FT                                /FTId=PRO_0000406413.
FT   DOMAIN      206    592       Peptidase S53.
FT   ACT_SITE    282    282       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    286    286       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    496    496       Charge relay system. {ECO:0000250}.
FT   METAL       538    538       Calcium. {ECO:0000250}.
FT   METAL       539    539       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       570    570       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       572    572       Calcium. {ECO:0000250}.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    261    261       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    275    275       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    295    295       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    554    554       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    566    566       N-linked (GlcNAc...) asparagine.
FT                                {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
//
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