ID   K2S0E3_MACPH            Unreviewed;       641 AA.
AC   K2S0E3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JUL-2024, entry version 40.
DE   RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE            EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN   ORFNames=MPH_12775 {ECO:0000313|EMBL:EKG10175.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG10175.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG10175.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG10175.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
CC   -!- FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at
CC       acidic pHs and is involved in virulence.
CC       {ECO:0000256|ARBA:ARBA00002451}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC         EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
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:EKG10175.1}.
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DR   EMBL; AHHD01000526; EKG10175.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2S0E3; -.
DR   STRING; 1126212.K2S0E3; -.
DR   MEROPS; S53.007; -.
DR   VEuPathDB; FungiDB:MPH_12775; -.
DR   eggNOG; ENOG502QTN1; Eukaryota.
DR   HOGENOM; CLU_013783_4_0_1; -.
DR   InParanoid; K2S0E3; -.
DR   OrthoDB; 1405251at2759; -.
DR   Proteomes; UP000007129; 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; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
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:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 1.
DR   Pfam; PF00082; Peptidase_S8; 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}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..641
FT                   /note="tripeptidyl-peptidase II"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003867203"
FT   DOMAIN          214..640
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        293
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        297
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        558
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         599
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         600
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         618
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         620
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   641 AA;  70247 MW;  2082D4A511680189 CRC64;
     MRASFFLGIA ACCRLIAAAP SSPGHFVVHE KRNSHPHEWT KRDRAHGDQI LPIRIGLQQR
     NLHLADEYLQ DVSDPASPNF GKHWSAEKVA KTFAPSREAT NSVTKWLQES GIDTSRITYS
     AGRNWVQFNG TVDEAERLFN TQYHFFEHKE TGGYRIACDE YHLPQHIQQH VDFAMPTIQL
     DGLRPVANLN IAHAAALTPL NLTGLTGTQN CDRLITIDCL RALYKFSFLN SSIAGNEMGI
     GEWADYLYNP DLVPFFEHWT SPKIPSDTVP EFISIDGGKP SNITQAEAGT VIESALDFQT
     AYSIIWPQKL RLYQVGDGVN VDSVGTFNIF LDALDASYCT YEGGDAPYVD PAYPDPNLGG
     YTGPLQCGGA PISNVYSFSY NQIEAALPEF YQRRQCNEWM KLGLQGVSVL FASGDSGVAN
     RYNAGYENSC LNADELYVDV NGTRFSPAFP CNCPYVTVVG ATQLLDGTIE GGERAVSDPD
     KTNPKEDYYS GGGFSNIFSL PSYQKDAVNG YLQNYPPPYD SKTYNNSGTS RAYPDVAALG
     LNITTVYLNR TYGVGGTSAS TPIVASLVNL LNEERYQAGK GPVGFLNPIF YAHPEAFNDV
     TVGANPGCGT DGFAAQPGWD PVTGLGTPDY QKLKKIFLDL P
//