SED1_ASPFU
ID SED1_ASPFU Reviewed; 644 AA.
AC Q70DX9; Q4WMD8;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Tripeptidyl-peptidase sed1;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-A;
DE Flags: Precursor;
GN Name=sed1; Synonyms=sedA; ORFNames=AFUA_6G10250;
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, 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 5.5. {ECO:0000269|PubMed:16517617};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16517617}.
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DR EMBL; AJ585109; CAE51075.1; -; mRNA.
DR EMBL; AAHF01000006; EAL88876.1; -; Genomic_DNA.
DR RefSeq; XP_750914.1; XM_745821.1.
DR AlphaFoldDB; Q70DX9; -.
DR SMR; Q70DX9; -.
DR MEROPS; S53.007; -.
DR EnsemblFungi; EAL88876; EAL88876; AFUA_6G10250.
DR GeneID; 3508219; -.
DR KEGG; afm:AFUA_6G10250; -.
DR VEuPathDB; FungiDB:Afu6g10250; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR InParanoid; Q70DX9; -.
DR OMA; ACREYHV; -.
DR OrthoDB; 1294880at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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; IMP:AspGD.
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; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Virulence;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..196
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:16517617"
FT /id="PRO_0000390741"
FT CHAIN 197..644
FT /note="Tripeptidyl-peptidase sed1"
FT /id="PRO_5000072119"
FT DOMAIN 224..643
FT /note="Peptidase S53"
FT ACT_SITE 300
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 561
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 602
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 644 AA; 69963 MW; 1639EDD1A744BC1E CRC64;
MRLSHVLLGT AAAAGVLASP TPNDYVVHER RAVLPRSWTE EKRLDKASIL PMRIGLTQSN
LDRGHDLLME ISDPRSSRYG QHLSVEEVHS LFAPSQETVD RVRAWLESEG IAGDRISQSS
NEQFLQFDAS AAEVERLLGT EYYLYTHQGS GKSHIACREY HVPHSLQRHI DYITPGIKLL
EVEGVKKARS IEKRSFRSPL PPILERLTLP LSELLGNTLL CDVAITPLCI SALYNITRGS
KATKGNELGI FEDLGDVYSQ EDLNLFFSTF AQQIPQGTHP ILKAVDGAQA PTSVTNAGPE
SDLDFQISYP IIWPQNSILF QTDDPNYTAN YNFSGFLNTF LDAIDGSYCS EISPLDPPYP
NPADGGYKGQ LQCGVYQPPK VLSISYGGAE ADLPIAYQRR QCAEWMKLGL QGVSVVVASG
DSGVEGRNGD PTPTECLGTE GKVFAPDFPA TCPYLTTVGG TYLPLGADPR KDEEVAVTSF
PSGGGFSNIY ERADYQQQAV EDYFSRADPG YPFYESVDNS SFAENGGIYN RIGRAYPDVA
AIADNVVIFN KGMPTLIGGT SAAAPVFAAI LTRINEERLA VGKSTVGFVN PVLYAHPEVF
NDITQGSNPG CGMQGFSAAT GWDPVTGLGT PNYPALLDLF MSLP
