ID A0A0F8WQN4_9EURO Unreviewed; 672 AA.
AC A0A0F8WQN4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Putative protease S8 tripeptidyl peptidase I {ECO:0000313|EMBL:KKK13562.1};
GN ORFNames=ARAM_001731 {ECO:0000313|EMBL:KKK13562.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK13562.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK13562.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK13562.1,
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:KKK13562.1}.
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DR EMBL; JZBS01003790; KKK13562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8WQN4; -.
DR STRING; 308745.A0A0F8WQN4; -.
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; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 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.
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};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW ECO:0000313|EMBL:KKK13562.1};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..672
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002529321"
FT DOMAIN 233..670
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 588
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 629
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 630
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 672 AA; 74218 MW; 4B6576CFF024567E CRC64;
MIVLRAAVLS ALVVLSVAAP AHTPAKHVLH EKRSRPSADW LRGERIESSA ILPMRIGLSQ
SDLHKGPGYL REVADPRSEK YGQYFSMDEV HDLFAPIQEH VDAIKDWLYE SGIDKSRVVH
SENKGWLAFD ATVEEAEQLF LTTYYEHEHM QSDRVRVGCD EYHLPEHIAP HVDYITPGVK
MTQAVKRTVK KAKRNSQSRA SRTSMKTALK YDVPENWSAP KGVPSDLAHC GFNMTPPCIR
ALYDIPMLTH KPNPNNALGL FEQGDYFAKS DLDLYWNNIY DEVPQGTYPT PQLIDGANYS
VPAYSSWNSG ESNIDIEMTL SLIYPQEVVL YQVDDQLYEP AEVATTNLFN TFLDALDGSY
CTYSGYGETG DDPSIDPVYP DNRAGGYTGE LQCGVYKPTN VISASYGQAE ADLPMKYVER
QCNEFLKLAM QGVTILFASG DYGVASFHGD GPNENGCLGP NANVFNPQYP SGCPWVTSVG
GAMIYNDQSV ADPESVMQVN LGGTAVNFSS AGGFSNYFTR PWYQESAVEE YFRIGDPEYP
YYSGLNVDVN TTTGLYNRIG RAFPDVAANG AYFPSFLDGA LYHFFGSSLA APLWASVITL
INEDRLAAGK STVGFLNPVL YAHPYVLNDI TNGTNLGCGT EGFSAVKGWD PATGLGTPNF
RKLKELFMHH IP
//
