ID E3S4U3_PYRTT Unreviewed; 584 AA.
AC E3S4U3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=PTT_17627 {ECO:0000313|EMBL:EFQ87007.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ87007.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ87007.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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}.
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DR EMBL; GL537205; EFQ87007.1; -; Genomic_DNA.
DR RefSeq; XP_003304898.1; XM_003304850.1.
DR AlphaFoldDB; E3S4U3; -.
DR MEROPS; S53.007; -.
DR EnsemblFungi; EFQ87007; EFQ87007; PTT_17627.
DR KEGG; pte:PTT_17627; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000001067; 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: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:UP000001067};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT DOMAIN 162..583
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 501
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 561
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 563
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 584 AA; 63919 MW; EC31D2608E3D6398 CRC64;
MPVRIGLKQR NLEHGDRFLH DISDPDSPNF GKHWTAQQVA NMFTPHPETS DATLEWLHSS
GIDRTRVKHS HGRNWVEFSA LVSELEDLLQ TTYYSYKHET GGFRIACDEY RLPHQVREHV
DFIMPTIQLD SLKPVAQKLP AIMTEATPKN GSLTNLSKCR SLITINCLRA IYKIPVAKFN
HKGNELGIAE WADYLYLPDL RTFFEKWSSP KIPSDVTPEF ISIDGGKPSN LTVAKASEVV
ESALDFQTAY SIIYPQNTRL YQNGDSVNVD SVGTFNIFLD ALDGSYCTYQ GGNQPYVDPA
YPDPNEGGYT GPLQCGGAPM SNVISVSYGQ IEGALPLFYQ QRQCREWMKL ALQGVSVIFA
SGDSGVANRY NAGYNNTCLN EVDGYVDQDG KKFSPSFPAT CPYITAVGAT DLRNASIYGG
EVAVAQPNGV TSYYSGGGFS SVFPQPSFQS SAVKTYLTSY APKYGDSVFN SSGRAYPDVS
ALGLNLATVY LNRTLGVGGT SASAPLFASI INLLNEERLE AGKKPVGFLN PLMYKNPGMF
NDVTEGGNPG CGTEGFPASK GWDPVTGLGT PDYEKMRKVF MSLP
//