ID   A0AAD4LGY7_9AGAM        Unreviewed;       563 AA.
AC   A0AAD4LGY7;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   02-OCT-2024, entry version 3.
DE   SubName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000313|EMBL:KAH8991251.1};
GN   ORFNames=EDB92DRAFT_2053915 {ECO:0000313|EMBL:KAH8991251.1};
OS   Lactarius akahatsu.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Russulaceae; Lactarius.
OX   NCBI_TaxID=416441 {ECO:0000313|EMBL:KAH8991251.1, ECO:0000313|Proteomes:UP001201163};
RN   [1] {ECO:0000313|EMBL:KAH8991251.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=QP {ECO:0000313|EMBL:KAH8991251.1};
RG   DOE Joint Genome Institute;
RA   Lebreton A., Tang N., Kuo A., LaButti K., Drula E., Barry K., Clum A.,
RA   Lipzen A., Mousain D., Ng V., Wang R., Wang X., Dai Y., Henrissat B.,
RA   Grigoriev I.V., Guerin-Laguette A., Yu F., Martin F.M.;
RT   "Comparative genomics reveals a dynamic genome evolution in the
RT   ectomycorrhizal milk-cap (Lactarius) mushrooms.";
RL   Submitted (JAN-2022) 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:KAH8991251.1}.
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DR   EMBL; JAKELL010000027; KAH8991251.1; -; Genomic_DNA.
DR   Proteomes; UP001201163; 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:0008240; F:tripeptidyl-peptidase activity; IEA:TreeGrafter.
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   InterPro; IPR050819; Tripeptidyl-peptidase_I.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 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:UP001201163};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..563
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5042137593"
FT   DOMAIN          223..563
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        297
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        301
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        485
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         527
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         528
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         546
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         548
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   563 AA;  61521 MW;  7FDBB72DC1A7B14C CRC64;
     MHYRWIPVLF LLSAVPLDGL ATSRWEHMRS KHSWKTIPEN WESLGLPPAD TMIDLYIALK
     PYRENALIDA LNEVSDPGHT RYGAHLSREQ VADIVAPHPD TVQLVHSWLE HHRVLPSSIS
     VTHGGSFLTV TRASVSQAND LLGASYQLYT HTKTNETIIR TLGYSLPVAL HGHVQTVAPT
     TFFSSPLTQW QTPHKRSSVA AVGLGKSPPA ELVKMPPSRR ITSVTPAFLR WLYNTFAYVP
     SATDRNVVGI TGFAEQYPNP ADLTSFMRKY RPDGIDATYV VELYNGAGYD PNNPGLEANI
     DLQLSEGMSY PTPHIFYSIK ASENGDVFLA WLDALLSQES VPQTITTSYG DYEKLHPMEY
     ATQICDLFAQ LGARGASVLF SSGDHGIGEG DCKNDDGAVR FTPLFPATCP YVTAVGGTTS
     FVPEVAASLS GGGFSEYFLR PWYQQQAVYS GLYNPSGRGI PDVAAQAMRI PFFYRGREII
     GRGTSCSTPI VAGIISLLND HRLSQGRPPL GFLNPWLYNG GLNGFNDIVS GSNPGCNTDG
     FSAIAGWDPV TGLGTPDLEQ LLH
//