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Database: UniProt
Entry: M1WEX0_CLAP2
LinkDB: M1WEX0_CLAP2
Original site: M1WEX0_CLAP2 
ID   M1WEX0_CLAP2            Unreviewed;       582 AA.
AC   M1WEX0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE            EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN   ORFNames=CPUR_07062 {ECO:0000313|EMBL:CCE33138.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE33138.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE33138.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE33138.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE33138.1}.
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DR   EMBL; CAGA01000052; CCE33138.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1WEX0; -.
DR   STRING; 1111077.M1WEX0; -.
DR   MEROPS; S53.010; -.
DR   VEuPathDB; FungiDB:CPUR_07062; -.
DR   eggNOG; ENOG502RS6E; Eukaryota.
DR   HOGENOM; CLU_013783_3_0_1; -.
DR   OrthoDB; 1344271at2759; -.
DR   PhylomeDB; M1WEX0; -.
DR   Proteomes; UP000016801; 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; IPR000209; Peptidase_S8/S53_dom.
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:SF15; TRIPEPTIDYL-PEPTIDASE 1; 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:UP000016801};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..582
FT                   /note="tripeptidyl-peptidase II"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004019215"
FT   DOMAIN          191..580
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        269
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        273
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        490
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         533
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
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         558
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         560
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   582 AA;  63297 MW;  5B61DA2507735B4C CRC64;
     MMLLSLFTAA CAFAGLAASA VCLEKAATIP DGWKFLHEAP EPWTPMRISI ALRQPHIHEL
     PSKILSATFL AQEDVESLRQ PALEHVHQVT KWLSDNGITT AQVDQDWVHV TATVGEVDKL
     LNTKLHRYRF GNGKDVLRTT EYSIPDDLTS AIDFVHPVVN FMTPEHQVSF APQLGALQRR
     RHRRSVACSP NTTPDCINKL YGINYTTPDG QSPVRFGIAG FLDQWASYAD LHKNFAQSRP
     DLVEAGYNFS VESINGGENR QDVGTAGIEA NLDIQYGMAV GFPTNVIFYS TAGRGEKLDD
     NGKPVTGELN DNEPYLDLLQ YLAKKPDNEL PHVLSISYAD DEFTMPQPYA IRVCNEIGLL
     AARGVSVLSG SGDGGARGGR NATCHSRDGL NKDMTISTFP ASCPWVTSVG AVNNGEEPPR
     GAEFSGGGFS NLFTRPDWQK KAVEEYVGEL KGHLQGYYNP EMRATPDISV LGTQFNTVLN
     GVDVSVQGTS ASTPVLAAMI ALINDARLRQ GKKALGWLNG RLYSDEVRSV LQDIANGRSL
     SCIFSGGQMP GGWPATKGYD AITGVGVPNN FQKFMDVLVN CA
//
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