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Database: UniProt
Entry: A0A316BCN4_9BACT
LinkDB: A0A316BCN4_9BACT
Original site: A0A316BCN4_9BACT 
ID   A0A316BCN4_9BACT        Unreviewed;       496 AA.
AC   A0A316BCN4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:PWJ60217.1};
GN   ORFNames=CLV98_101398 {ECO:0000313|EMBL:PWJ60217.1};
OS   Dyadobacter jejuensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=1082580 {ECO:0000313|EMBL:PWJ60217.1, ECO:0000313|Proteomes:UP000245880};
RN   [1] {ECO:0000313|EMBL:PWJ60217.1, ECO:0000313|Proteomes:UP000245880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100346 {ECO:0000313|EMBL:PWJ60217.1,
RC   ECO:0000313|Proteomes:UP000245880};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) 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:PWJ60217.1}.
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DR   EMBL; QGDT01000001; PWJ60217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316BCN4; -.
DR   OrthoDB; 1119199at2; -.
DR   Proteomes; UP000245880; 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:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 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   Carboxypeptidase {ECO:0000313|EMBL:PWJ60217.1};
KW   Hydrolase {ECO:0000313|EMBL:PWJ60217.1};
KW   Protease {ECO:0000313|EMBL:PWJ60217.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245880}.
FT   DOMAIN          32..289
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   496 AA;  56074 MW;  3626D9A063DAB5F6 CRC64;
     MLATFLRLSS TSLLFILLTS ISPSTDLSDS LYKTHHTFKE QGLSQRRFKQ KDILPLLDRR
     RNNPLYTITK VGESFEGRNI QMVRIGTGPK KILLWTQMHG DEPTATMASF DIFNFLERHN
     DGFDAFRKKI LEQTTLYFVP MLNPDGAERY QRRTAQGIDM NRDAAALQTP EGALLKRLVD
     EIKPDFGFNL HDQSPRYSVG RSAEAAAISF LATAYDYPRS INPVRERSMQ LIVAMNRQLQ
     RYIPGKVGRY ADDHEPRGFG DNVQKWGTTL VLIESGGLAG DPEKQYLRRL NFMAILSAID
     KIADNSLTQE NRNDYYEIPE NGRWLYDLVI RHATVKQGTK SFEADLGINR NEVSYANASK
     FFYYSKVEEF GDLHPQFGTQ EIDAKGLTLE KGKLYPKAFK TIGEVSQLNA LNLLKEGYTY
     IRLTADNGGR NLGLYYTTAP LHILRNNKSA PIDSPRLGST ATFLLKKGGV VKYAVVNGFV
     YDLANFKTKA GNGIVE
//
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