ID   E3RUJ2_PYRTT            Unreviewed;       417 AA.
AC   E3RUJ2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00133};
GN   ORFNames=PTT_12758 {ECO:0000313|EMBL:EFQ90610.1};
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:EFQ90610.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ90610.1,
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: Extracellular metalloprotease that contributes to
CC       pathogenicity. {ECO:0000256|ARBA:ARBA00003091}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; GL535137; EFQ90610.1; -; Genomic_DNA.
DR   RefSeq; XP_003301297.1; XM_003301249.1.
DR   AlphaFoldDB; E3RUJ2; -.
DR   MEROPS; M14.014; -.
DR   EnsemblFungi; EFQ90610; EFQ90610; PTT_12758.
DR   KEGG; pte:PTT_12758; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_1_1_1; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03860; M14_CP_A-B_like; 1.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..417
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003181506"
FT   DOMAIN          307..317
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   417 AA;  45313 MW;  F7EE05908B265C56 CRC64;
     MKFLGVTLAS LGLVSAATVA KKVSYDDWKV YRVNVGPDAA KLENVMSKLQ LELWKGKPAT
     SDVVDLMVPP TAIQDFEAST ADFETKVMHT NLGLSIANET TFSTYAAGAA PSATWFNSYH
     SIADHMQWIS DLAAAYPKNA EVISAGKSVE GRDIKGIHIW GSGGKGSKRG VVWHGTVHAR
     EWITTMVVEY AAYQLLTSTD STTANFKNNY DFYIFPIVNP DGFAYTQTTD RMWRKNRQTT
     PSASCIGRDI NRNWPSHWDQ RGGASTSPCA EDYKGPSAGD GVETKALKAQ LDSIAAGKGV
     MLYMDIHSYS QLWLYPYGYT CSGTVPNSAK YASLTKGAIA AVKAVHGTTF TGGPICSTIY
     QVSGDSVDYA FEVAKANFSM TVELRDTGTY GFILPAAQIV PSAEEMWAGL RYMVANM
//