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Database: UniProt
Entry: A0A3E0U4I3_9GAMM
LinkDB: A0A3E0U4I3_9GAMM
Original site: A0A3E0U4I3_9GAMM 
ID   A0A3E0U4I3_9GAMM        Unreviewed;       857 AA.
AC   A0A3E0U4I3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN   ORFNames=DXX94_10500 {ECO:0000313|EMBL:REL31105.1};
OS   Thalassotalea euphylliae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1655234 {ECO:0000313|EMBL:REL31105.1, ECO:0000313|Proteomes:UP000256899};
RN   [1] {ECO:0000313|Proteomes:UP000256899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3 {ECO:0000313|Proteomes:UP000256899};
RA   Summers S., Rice S.A., Freckelton M.L., Nedved B.T., Hadfield M.G.;
RT   "Thalassotalea euphylliae genome.";
RL   Submitted (AUG-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:REL31105.1}.
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DR   EMBL; QUOT01000001; REL31105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E0U4I3; -.
DR   Proteomes; UP000256899; 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; IPR029062; Class_I_gatase-like.
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; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000256899};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..857
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017726498"
FT   DOMAIN          60..338
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   857 AA;  96669 MW;  5A77F1B94AEE0F20 CRC64;
     MFFQQILNRC LTVSTGFLLS LFTLTANAAE LSYYLSSTDN YAAQISKPSQ VLGFGVGERH
     LRHDQLLDYM SQLAGQSERI KLTEFGRTYQ QRKQVLLTIS SPENLAKLDS TLTNRQNNKV
     SDDDPLVVWL GYSVHGDEIS GAHASMLVAY HLAASQSDEV KQWLDDMVIV IEPSVNPDGM
     DRFANWVTTF RSHSANSDPN HIEHNQSWPT GRTNHYWFDL NRDWLLLSQV ESVNRLKMYH
     QYQPNVLGDF HEMGANSSYF FQPGIPTRTN PLTPAKNVEL TQKLAEFHAK ALDEEQRLYY
     TQESFDDFYY GKGSTYPDVN GAVGILFEQA SSRGMQQDTV NGLLTFEYGI KNQLLTSFST
     LRGAWQQRGA LAEYRETFYE SGLKAAKKEK YAGYLFTESD DNTRLNLFLS KLAQHQIEVF
     PLSEDFRLNN RVFSAEHSYF VPLAQRQYRL IQALFTKQTE FADNTFYDVS GWTLPLAMNI
     DVSQVARTWG LKLLNKAWQQ KAKQTSELEG AAYAYAIEWQ DYLAPKLLNK LLAKGLQVKV
     ATKSFSNLDA ETEQTFASGT LLIAAGIQQQ GDWFNILKAE SDALALPVFP INTGLTINGI
     DLGSQSFKLI EPAKVLLIGG YGVSQYEAGE IRYYLDQELE IPVSIVDKQR LSKLNFDDYS
     HIVMVDGHYD DLSKSVTKRL SNWLHRGGVV FAQKRAAKWL ADKELLQASF ATKEQLDQLF
     DTDNLSYQDK QGLTARKRIA GTIFNAEIDT SHPLAFGFKS NNLPVFKNSS LIMNKPKVPF
     STVAKFGQSP LLSGYADENL VNRLAHNASL VAHNVGRGRV VATTENYTFR GYWQGTAKIL
     ANTLFFATAF DVAAKSK
//
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