ID   A0A2S6CF95_9PEZI        Unreviewed;       545 AA.
AC   A0A2S6CF95;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|Pfam:PF00246};
GN   ORFNames=CBER1_11402 {ECO:0000313|EMBL:PPJ58410.1};
OS   Cercospora berteroae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ58410.1, ECO:0000313|Proteomes:UP000237631};
RN   [1] {ECO:0000313|Proteomes:UP000237631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA   de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA   Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA   Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT   "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT   mechanisms and extends production to the genus Colletotrichum.";
RL   bioRxiv 0:0-0(2017).
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:PPJ58410.1}.
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DR   EMBL; PNEN01000459; PPJ58410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6CF95; -.
DR   OrthoDB; 2665904at2759; -.
DR   Proteomes; UP000237631; 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   Pfam; PF00246; Peptidase_M14; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000237631};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..545
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015447560"
FT   DOMAIN          106..201
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
SQ   SEQUENCE   545 AA;  60925 MW;  0FE59888C2D3C35B CRC64;
     MMYSRHALQR FALAVLTPHL LHAQAQSTYG NNSLRVTKDS DIVASAFPEV EGVELIAPAF
     TSPESLPAGW DNGTSGPTDL YELDYFIRSI ADRNDWITYK SSDFLSEEGR AIPYLFLSSS
     PGYTGNNTKL KVYIQAAIHG NEPAADQGAL AFLGKLDANQ TYAASLLEKL DILILPRYNV
     DGVSYFQREL AVNLDPNRDH IKLDRKQTRE IKQVFSNYNP HLAIDLHEFN APTVYGGDYQ
     HGNDALIAGG IHLNIHSSIR NYLSDVLIPT IGERLESYGL RWGPYVTGSS NTTSGSEIVW
     DGPATQPRSG RNAMGLTQTI AFLFEMRGIR LADQHFQRRV ATALIKLETI LEYARDNTEQ
     VRSIVEDARA DFISSNEDIV ITDVPRGNLT QQPFNFVDRR NGSIIELTVD FYETRPAVAN
     LTRSRPEAYL IPRSWYDIAE RLRILGLEVQ TLDYEYRGTV EALNVTSSTL DDSIYEGHVL
     NTVTTEPLTK EVHLPPGSFL VSTRQQNAAL AFIALEPETI DSYVTFNFIA LAAGDEYPIY
     RILAE
//