ID   A0A0P7BMY9_9HYPO        Unreviewed;       454 AA.
AC   A0A0P7BMY9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN   ORFNames=AK830_g4461 {ECO:0000313|EMBL:KPM42079.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM42079.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM42079.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM42079.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KPM42079.1}.
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DR   EMBL; LKCW01000054; KPM42079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7BMY9; -.
DR   STRING; 78410.A0A0P7BMY9; -.
DR   OrthoDB; 1893867at2759; -.
DR   Proteomes; UP000050424; 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:InterPro.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF119; OS02G0119300 PROTEIN; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..454
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006136009"
FT   DOMAIN          83..408
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   454 AA;  49402 MW;  B26C24B7231AEAC2 CRC64;
     MRFPTFVAVL GITSSVNACL LPSEREADRQ FALTGVRPER RSTIPRRQAS TTFPIGTGDR
     FANGCVAPVG LGVKDRNLKS VLSVKEVASA LKGLKKKYKH EVELFEPPFK TFEGRKFHGA
     VVGDNPRVFI MSGIHARERG GPDNVIYFLA DLLAARKAGS GISYGDKNYT AEDVETALSA
     GIIVLPLTNP DGVAYDQTTD TCWRKNRNTE SSSGAEDGSD VGVDLNRNYD FVWDYKKAFN
     LDAGDPPASD DPSSEVFYGT GPASEPETEA VVWTLDQYQN ITWFMDLHSY TGSILYAWGD
     DDAGQEETEQ NFVNPAFDGK RGYVGEDPPD SVYKEFFTAE DLKTEEDVTS VMVKSMLAAG
     NVLYDAYPAV GLYPTSGASN DYAMGRYYGK LACGSSRMFG LTLEFGAEAT ADPSCPFYPD
     AAGYHDNVRQ VGAGFMEMML LAAGPAGDPV YLEC
//