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 03-AUG-2022, entry version 100.
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;
OC Aspergillus subgen. Fumigati.
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}.
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DR EMBL; AJ578478; CAE17674.1; -; mRNA.
DR EMBL; AAHF01000016; EAL84498.1; -; Genomic_DNA.
DR RefSeq; XP_746536.1; XM_741443.1.
DR AlphaFoldDB; Q70J59; -.
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 VEuPathDB; FungiDB:Afu4g03490; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR HOGENOM; CLU_013783_3_0_1; -.
DR InParanoid; Q70J59; -.
DR OMA; HDEMKRM; -.
DR OrthoDB; 1294880at2759; -.
DR BRENDA; 3.4.14.9; 508.
DR Proteomes; UP000002530; Chromosome 4.
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: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;
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 BINDING 545
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 582
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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
