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Database: UniProt
Entry: A0A1Y3WKH7_9FIRM
LinkDB: A0A1Y3WKH7_9FIRM
Original site: A0A1Y3WKH7_9FIRM 
ID   A0A1Y3WKH7_9FIRM        Unreviewed;       165 AA.
AC   A0A1Y3WKH7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Cytidine deaminase {ECO:0000313|EMBL:OUN71707.1};
GN   ORFNames=B5G11_01935 {ECO:0000313|EMBL:OUN71707.1};
OS   Drancourtella sp. An57.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Drancourtella.
OX   NCBI_TaxID=1965647 {ECO:0000313|EMBL:OUN71707.1, ECO:0000313|Proteomes:UP000196207};
RN   [1] {ECO:0000313|Proteomes:UP000196207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An57 {ECO:0000313|Proteomes:UP000196207};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|PIRSR:PIRSR006019-2};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000256|ARBA:ARBA00006576}.
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:OUN71707.1}.
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DR   EMBL; NFHY01000002; OUN71707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3WKH7; -.
DR   Proteomes; UP000196207; Unassembled WGS sequence.
DR   GO; GO:0004132; F:dCMP deaminase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:InterPro.
DR   CDD; cd01286; deoxycytidylate_deaminase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR016473; dCMP_deaminase.
DR   InterPro; IPR015517; dCMP_deaminase-rel.
DR   InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR   PANTHER; PTHR11086:SF18; CYTIDINE AND DCMP DEAMINASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR11086; DEOXYCYTIDYLATE DEAMINASE-RELATED; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   PIRSF; PIRSF006019; dCMP_deaminase; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR006019-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196207};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006019-2}.
FT   DOMAIN          11..151
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   ACT_SITE        87
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-1"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
SQ   SEQUENCE   165 AA;  18268 MW;  D9F3E1096C88FC7D CRC64;
     MVKPEKGKRI SKIDTYLNCA ETFAYRSTCL KRKYGAVIVK DDVVVSTGYN GSPRGFENCC
     DKGTCPRMEK NMHQGEGYGV CRAIHAEANA LLNCSRLQTI GADLYLTGVN PEDNSIHKAN
     PCPMCARSII QAGIRNVIMR TGEGPEQYTI VPAKELKWYL DDSNV
//
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