ID   A0A178AZH4_9PLEO        Unreviewed;       488 AA.
AC   A0A178AZH4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Zn-dependent exopeptidase {ECO:0000313|EMBL:OAL02250.1};
GN   ORFNames=IQ06DRAFT_133045 {ECO:0000313|EMBL:OAL02250.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL02250.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL02250.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL02250.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441710; OAL02250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AZH4; -.
DR   STRING; 765868.A0A178AZH4; -.
DR   InParanoid; A0A178AZH4; -.
DR   OrthoDB; 1893867at2759; -.
DR   Proteomes; UP000077206; 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:UP000077206};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..488
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008082376"
FT   DOMAIN          132..462
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   488 AA;  54332 MW;  15A047F8D5DDFA0E CRC64;
     MKVPTLLGLL PSAVLAADSL SVAFFAKEKT QLYDFISANS EIDYGCRPVV MASGEEHKLH
     AVVSESELKS LKRSLDSSVV RIETLDNLNK RQTATAPIGK GDRFEGGKIA PRGLGTQSAD
     KYAAYESAGI LNADEVYTAM KGLEKEYGLE LFTAPYKTFE GNTLLGGVAN KAEKINKEKQ
     YIYFTSGIHA RERGGPDNLI YFISDLLYAN EHRTGLTYGN KTYTNKDVKK ALGAGIVFIP
     MTNPDGVRHD QANSNLWRKN RNPASSRPNE PLSVGVDLNR NFDFLWNYTE KFVPDVSPAS
     NNASSQAFYG TAPFSEPETK NIAWVHDVFP NIRWYIDVHS AAGTLLYSWG DDLDQSFDPK
     QNLFNTEYDG LRGNVSDQVY SEYICQEDWD NIRLQANRTT AAMNATAGRA YVPQQAVGLY
     PTSGASDDWT FSRWHKDNKV SKTYGFTLEF GYPTNFYPTA EEYVQNIIDT NAGFMEFILT
     ADEIGLKG
//