SED4_ASPFU
ID SED4_ASPFU Reviewed; 594 AA.
AC Q4WQU0;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Tripeptidyl-peptidase sed4;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-D;
DE Flags: Precursor;
GN Name=sed4; Synonyms=sedD; ORFNames=AFUA_4G14000;
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 [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).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION, FUNCTION, SUBCELLULAR
RP 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).
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 5. {ECO:0000269|PubMed:16517617};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:16517617}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16517617}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000005; EAL89394.1; -; Genomic_DNA.
DR RefSeq; XP_751432.1; XM_746339.1.
DR AlphaFoldDB; Q4WQU0; -.
DR SMR; Q4WQU0; -.
DR STRING; 330879.Q4WQU0; -.
DR MEROPS; S53.010; -.
DR EnsemblFungi; EAL89394; EAL89394; AFUA_4G14000.
DR GeneID; 3508961; -.
DR KEGG; afm:AFUA_4G14000; -.
DR VEuPathDB; FungiDB:Afu4g14000; -.
DR eggNOG; ENOG502RXDG; Eukaryota.
DR HOGENOM; CLU_013783_3_3_1; -.
DR InParanoid; Q4WQU0; -.
DR OMA; TTTWAGE; -.
DR OrthoDB; 1294880at2759; -.
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; 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; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..187
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:16517617"
FT /id="PRO_0000390750"
FT CHAIN 188..594
FT /note="Tripeptidyl-peptidase sed4"
FT /id="PRO_0000390751"
FT DOMAIN 197..594
FT /note="Peptidase S53"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 494
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 537
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 BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 594 AA; 63945 MW; 5F46D7B4DEF0784C CRC64;
MLSSTLYAGW LLSLAAPALC VVQEKLSAVP SGWTLIEDAS ESDTITLSIA LARQNLDQLE
SKLTTLATPG NPEYGKWLDQ SDIESLFPTA SDDAVLQWLK AAGITQVSRQ GSLVNFATTV
GTANKLFDTK FSYYRNGASQ KLRTTQYSIP DHLTESIDLI APTVFFGKEQ NSALSSHAVK
LPALPRRAAT NSSCANLITP DCLVEMYNLG DYKPDASSGS RVGFGSFLNE SANYADLAAY
EQLFNIPPQN FSVELINRGV NDQNWATASL GEANLDVELI VAVSHPLPVV EFITGGSPPF
VPNADEPTAA DNQNEPYLQY YEYLLSKPNS HLPQVISNSY GDDEQTVPEY YARRVCNLIG
LMGLRGITVL ESSGDTGIGS ACMSNDGTNK PQFTPTFPGT CPFITAVGGT QSYAPEVAWD
GSSGGFSNYF SRPWYQSFAV DNYLNNHITK DTKKYYSQYT NFKGRGFPDV SAHSLTPYYE
VVLTGKHYKS GGTSAASPVF AGIVGLLNDA RLRAGKSTLG FLNPLLYSIL AEGFTDITAG
SSIGCNGINP QTGKPVPGGG IIPYAHWNAT AGWDPVTGLG VPDFMKLKEL VLSL
