ID A0A0F8XT10_9EURO Unreviewed; 592 AA.
AC A0A0F8XT10;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Tripeptidyl peptidase A {ECO:0000313|EMBL:KKK26637.1};
GN ORFNames=ARAM_005845 {ECO:0000313|EMBL:KKK26637.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26637.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK26637.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26637.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01032};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKK26637.1}.
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DR EMBL; JZBS01000299; KKK26637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8XT10; -.
DR STRING; 308745.A0A0F8XT10; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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 PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF34; TRIPEPTIDYL-PEPTIDASE SED4; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..592
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002529518"
FT DOMAIN 195..592
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 492
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 534
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 535
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 570
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 592 AA; 63922 MW; 6202D43D0E0253CF CRC64;
MLPSHLYGGL LCSLAAATEA LVHEKLAAVP NGWSYIQNAA GENSILLSIA LARTNLEQLE
SILLARATPG QAQYGQWMEQ SEIESQFPLV SDESVVNWLK EAGVTQIARQ GGLVNFATDV
NTANKLLNTT FAVYQNGAIA RVRTTQYSIP DEFRDSVDLI SPTVFFGKEQ GEVYLTPLPR
EASNNSSGSS SCTNVITPDC LKGMYNYGDY TPSVSSGSRI GFGSFLNQSA SYSDLAVFEK
LFGIPSQNFT VELFDGGIDD QNPNTASLGE ANLDVQNIVA VSHPLPVHEY ITGGSPPFIP
NVDEPTAADN QNEPYLPYYE HLLSKPNSEL PQVISNSYGD DEQTVPEYYA RRVCNLIGLM
GLRGITILES SGDTGIGAGC LANDGSNKPQ FTPQFPGTCP FITAVGGTQS YGPEIAWNSS
SGGFSNYFPR AWYQEDAVED YLKKHITKDT KEYYSQYTNF NGRGFPDVAT HSFYPPYEVI
YYGKRYGSGG TSAASPVFAG IVGMLNDARL KAGRPTLGFL NPLLYAINYE GFNDITAGSS
VGCDGTNPQS GDKVVGGGII PYAHWNATEG WDPVTGIGIP DFERLKAIVL SL
//
