ID   A0A1Y2M789_EPING        Unreviewed;       451 AA.
AC   A0A1Y2M789;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN   ORFNames=B5807_03540 {ECO:0000313|EMBL:OSS51984.1};
OS   Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX   NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS51984.1, ECO:0000313|Proteomes:UP000193240};
RN   [1] {ECO:0000313|EMBL:OSS51984.1, ECO:0000313|Proteomes:UP000193240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS51984.1,
RC   ECO:0000313|Proteomes:UP000193240};
RA   Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT   "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT   strain isolated from New Zealand.";
RL   Genome Announc. 0:0-0(2017).
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; KZ107840; OSS51984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2M789; -.
DR   STRING; 105696.A0A1Y2M789; -.
DR   InParanoid; A0A1Y2M789; -.
DR   OMA; MYKVNSE; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000193240; 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   CDD; cd03860; M14_CP_A-B_like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
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   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193240};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..451
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013322500"
FT   DOMAIN          127..436
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   451 AA;  50155 MW;  F6D5B211B4F8CE72 CRC64;
     MVLANLLLLV SLVASSPFEA GQASASRNAG VSYDGYRIYS ITPASSSEAR DLTSRFSRYH
     THPIRDALSV AIPPDEVATF ESLGLNTRLV NADLGAHIRA IDSKPSLYNR ALHKRGELPD
     LSWFDTYHPY ADHLDYWDDL TRAFPKNTEK LELGKSYENR TIYAYHMFGD KKKGGYGPRT
     KDVPQKPAIL WHATVHAREW ISTMVIEYLA HQLISGYKSN DTDATAFLDH YDFYLVPFHN
     PDGFVHTQTT DRLWRKNRQP RPSLNTTCLG TDGNRNWIFE WDAEPPEGGS TPDPCGQTYR
     GLAPGDTPEN AALDALSAAL AETPGGIRSF IDFHSYGQLV LTPWGYSCDP LPETIGRMVE
     VANATARAIE AASERNSTYQ AGPGCEILYF STGNSRDHHH AVHGAHHSWT LELSPVDAAG
     GGFVLDPAQI WPVVREQWAG QKAALREVWD E
//