SED3_ASPFU
ID SED3_ASPFU Reviewed; 596 AA.
AC Q70GH4; Q4WXB8;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Tripeptidyl-peptidase sed3;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-C;
DE Flags: Precursor;
GN Name=sed3; Synonyms=sedC; ORFNames=AFUA_3G08930;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, FUNCTION, SUBCELLULAR LOCATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=D141;
RX PubMed=16517617; DOI=10.1128/aem.72.3.1739-1748.2006;
RA Reichard U., Lechenne B., Asif A.R., Streit F., Grouzmann E., Jousson O.,
RA Monod M.;
RT "Sedolisins, a new class of secreted proteases from Aspergillus fumigatus
RT with endoprotease or tripeptidyl-peptidase activity at acidic pHs.";
RL Appl. Environ. Microbiol. 72:1739-1748(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at
CC acidic pHs and is involved in virulence. {ECO:0000269|PubMed:16517617}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is about 6. {ECO:0000269|PubMed:16517617};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:16517617}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16517617}.
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DR EMBL; AJ581835; CAE46473.1; -; mRNA.
DR EMBL; AAHF01000002; EAL92685.2; -; Genomic_DNA.
DR RefSeq; XP_754723.2; XM_749630.2.
DR AlphaFoldDB; Q70GH4; -.
DR SMR; Q70GH4; -.
DR STRING; 746128.CADAFUBP00003935; -.
DR MEROPS; S53.010; -.
DR EnsemblFungi; EAL92685; EAL92685; AFUA_3G08930.
DR GeneID; 3512055; -.
DR KEGG; afm:AFUA_3G08930; -.
DR VEuPathDB; FungiDB:Afu3g08930; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR HOGENOM; CLU_013783_3_0_1; -.
DR InParanoid; Q70GH4; -.
DR OMA; YHEMASG; -.
DR OrthoDB; 1294880at2759; -.
DR BRENDA; 3.4.14.9; 508.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Calcium; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Virulence; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..201
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390747"
FT CHAIN 202..596
FT /note="Tripeptidyl-peptidase sed3"
FT /id="PRO_5000072081"
FT DOMAIN 209..592
FT /note="Peptidase S53"
FT ACT_SITE 285
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 499
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 542
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 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 596 AA; 65276 MW; 8DBD30E4B3FC491B CRC64;
MAPFTFLVGI LSLCICCIVL GAAAEPSYAV VEQLRNVPDG WIKHDAAPAS ELIRFRLAMN
QERAAEFERR VIDMSTPGHS SYGQHMKRDD VREFLRPPEE VSDKVLSWLR SENVPAGSIE
SHGNWVTFTV PVSQAERMLR TRFYAFQHVE TSTTQVRTLA YSVPHDVHRY IQMIQPTTRF
GQPARHERQP LFHGTVATKE ELAANCSTTI TPNCLRELYG IYDTRAEPDP RNRLGVSGFL
DQYARYDDFE NFMRLYATSR TDVNFTVVSI NDGLNLQDSS LSSTEASLDV QYAYSLAYKA
LGTYYTTGGR GPVVPEEGQD TNVSTNEPYL DQLHYLLDLP DEELPAVLST SYGEDEQSVP
ESYSNATCNL FAQLGARGVS IIFSSGDSGV GSTCITNDGT KTTRFLPVFP ASCPFVTAVG
GTHDIQPEKA ISFSSGGFSD HFPRPSYQDS SVQGYLEQLG SRWNGLYNPS GRGFPDVAAQ
ATNFVVIDHG QTLRVGGTSA SAPVFAAIVS RLNAARLEDG LLKLGFLNPW LYSLNQTGFT
DIIDGGSSGC YVGTSNEQLV PNASWNATPG WDPVTGLGTP IYNTLVKLAT SVSSTP
