ID   A0A1I0NDJ1_9BACT        Unreviewed;       905 AA.
AC   A0A1I0NDJ1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:SEV99470.1};
GN   ORFNames=SAMN05428988_1090 {ECO:0000313|EMBL:SEV99470.1};
OS   Chitinophaga sp. YR573.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEV99470.1, ECO:0000313|Proteomes:UP000198758};
RN   [1] {ECO:0000313|EMBL:SEV99470.1, ECO:0000313|Proteomes:UP000198758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR573 {ECO:0000313|EMBL:SEV99470.1,
RC   ECO:0000313|Proteomes:UP000198758};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOJF01000001; SEV99470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0NDJ1; -.
DR   STRING; 1881040.SAMN05428988_1090; -.
DR   Proteomes; UP000198758; 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; cd06240; M14-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   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SEV99470.1};
KW   Hydrolase {ECO:0000313|EMBL:SEV99470.1};
KW   Protease {ECO:0000313|EMBL:SEV99470.1}.
FT   DOMAIN          33..307
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   905 AA;  100967 MW;  521A1F48A4AFC1C1 CRC64;
     MLALLLSIVT AQAQTIPSPK EHFGFNIGDD YQLATYTQTE AYFKKLATSD RAKLVDIGMT
     EEGRHQYMLI VSSPENMKQL EKYKAISQQL AHATGLTDEQ AKSLAAEGKS VIWIDGGLHA
     TEVVGTHQLI ETMWQLVSRT DPETMEILKN DIILFAHANP DGQELVTNWY MRTADPKKRA
     MNIPRLYEKY VGHDNNRDFY MMNMKESQNI SRQLYVEWIP QIMYNHHQRG PNGSVLAGPP
     YRDPFNHVFD PLIVTSIDAV GAAMNNRLNA EGKPGYTQRA GSQFSTWWNG GLRTAPYFHN
     MIGLLTEIIG GPTPETVPLV PERLIPNGAT PNPVAPQEWH FRQSIDYSVS LNYAVLDYAS
     RYRSELLYNI YRMGKNAIAR GEADHWTFYP RYIDSIQTAY KKDKKDSLLA SGKKDTVKES
     AEEYTLGKED TIAAKYYTAI LKNPAYRDAR AYIIPADQQD FPTAVKFINA LSRAGITIQK
     ATAAFTVAGK TYPAGSYVVK TAQAFRPHVI DMFEPQDHPN DFQYVGGPPV RPYDAAGWTL
     AFQMGVKFDR VLDSVGGPFT QLPYGQIESP PAHTFAISKT GYLLSPAVNN SFIAVNDLLK
     AGAKVYRLPN GDFYIPASSK AQESLTKSVA ELGITVNTAT GSSKEMKAVS PMRIAIWNTY
     GGSIPAGWVS WLMEQYHYDY KTIYSQEIDA GALRKKYDMI IFVTGAIPDT GKPKKSDYWF
     GKLPKPEELT AEFKPWLGRI SADTSIPQLK TFLEAGGQIF TIGTSTNLAY HLKLPVENAL
     VEKNSKGELK PLAGAKYYIP GSLLTADLDT TAAENWGMHA KNDVYFERSP VFKILPGSNI
     KQLMWFSTGT PLHSGWAWGQ KYLKDGVAAF SVSVGAGKLY AFGPEITFRG QSHSTFKLLF
     NQLYK
//