(data stored in ACNUC7421 zone)

SWISSPROT: SED2_ASPFU

ID   SED2_ASPFU              Reviewed;         602 AA.
AC   Q70J59; Q4W9W5;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=Tripeptidyl-peptidase sed2;
DE            EC=3.4.14.10;
DE   AltName: Full=Sedolisin-B;
DE   Flags: Precursor;
GN   Name=sed2; Synonyms=sedB; ORFNames=AFUA_4G03490;
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.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION,
RP   FUNCTION, SUBCELLULAR LOCATION, 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       Kinetic parameters:
CC         KM=62.5 uM for Phe-Pro-Ala-pNA (at 20 degrees Celsius)
CC         {ECO:0000269|PubMed:16517617};
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}.
DR   EMBL; AJ578478; CAE17674.1; -; mRNA.
DR   EMBL; AAHF01000016; EAL84498.1; -; Genomic_DNA.
DR   RefSeq; XP_746536.1; XM_741443.1.
DR   SMR; Q70J59; -.
DR   STRING; 746128.CADAFUBP00009676; -.
DR   MEROPS; S53.010; -.
DR   EnsemblFungi; EAL84498; EAL84498; AFUA_4G03490.
DR   GeneID; 3504066; -.
DR   KEGG; afm:AFUA_4G03490; -.
DR   EuPathDB; FungiDB:Afu4g03490; -.
DR   HOGENOM; HOG000171253; -.
DR   InParanoid; Q70J59; -.
DR   KO; K01279; -.
DR   OMA; TTTWAGE; -.
DR   OrthoDB; 1294880at2759; -.
DR   BRENDA; 3.4.14.9; 508.
DR   Proteomes; UP000002530; Chromosome 4.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
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; IMP:AspGD.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
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; 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   1: Evidence at protein level;
DR   PRODOM; Q70J59.
DR   SWISS-2DPAGE; Q70J59.
KW   Calcium; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal; Virulence;
KW   Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..205
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:16517617"
FT                   /id="PRO_0000390744"
FT   CHAIN           206..602
FT                   /note="Tripeptidyl-peptidase sed2"
FT                   /id="PRO_5000071660"
FT   DOMAIN          212..602
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        503
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   METAL           545
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250"
FT   METAL           546
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           580
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           582
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   602 AA;  65839 MW;  096CF20F9AEBF36A CRC64;
     MFSSLLNRGA LLAVVSLLSS SVAAEVFEKL SAVPQGWKYS HTPSDRDPIR LQIALKQHDV
     EGFETALLEM SDPYHPNYGK HFQTHEEMKR MLLPTQEAVE SVRGWLESAG ISDIEEDADW
     IKFRTTVGVA NDLLDADFKW YVNEVGHVER LRTLAYSLPQ SVASHVNMVQ PTTRFGQIKP
     NRATMRGRPV QVDADILSAA VQAGDTSTCD QVITPQCLKD LYNIGDYKAD PNGGSKVAFA
     SFLEEYARYD DLAKFEEKLA PYAIGQNFSV IQYNGGLNDQ NSASDSGEAN LDLQYIVGVS
     SPIPVTEFST GGRGLLIPDL SQPDPNDNSN EPYLEFLQNV LKMDQDKLPQ VISTSYGEDE
     QTIPEKYARS VCNLYAQLGS RGVSVIFSSG DSGVGAACLT NDGTNRTHFP PQFPAACPWV
     TSVGGTTKTQ PEEAVYFSSG GFSDLWERPS WQDSAVKRYL KKLGPRYKGL YNPKGRAFPD
     VAAQAENYAV FDKGVLHQFD GTSCSAPAFS AIVALLNDAR LRAHKPVMGF LNPWLYSKAS
     KGFNDIVKGG SKGCDGRNRF GGTPNGSPVV PYASWNATDG WDPATGLGTP DFGKLLSLAM
     RR
//

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