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Database: UniProt
Entry: A0A1W2BJV7_9FIRM
LinkDB: A0A1W2BJV7_9FIRM
Original site: A0A1W2BJV7_9FIRM 
ID   A0A1W2BJV7_9FIRM        Unreviewed;       161 AA.
AC   A0A1W2BJV7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=dCMP deaminase {ECO:0000313|EMBL:SMC72972.1};
GN   ORFNames=SAMN02745168_2245 {ECO:0000313|EMBL:SMC72972.1};
OS   Papillibacter cinnamivorans DSM 12816.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Papillibacter.
OX   NCBI_TaxID=1122930 {ECO:0000313|EMBL:SMC72972.1, ECO:0000313|Proteomes:UP000192790};
RN   [1] {ECO:0000313|EMBL:SMC72972.1, ECO:0000313|Proteomes:UP000192790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12816 {ECO:0000313|EMBL:SMC72972.1,
RC   ECO:0000313|Proteomes:UP000192790};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
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};
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DR   EMBL; FWXW01000005; SMC72972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2BJV7; -.
DR   STRING; 1122930.SAMN02745168_2245; -.
DR   OrthoDB; 9788517at2; -.
DR   Proteomes; UP000192790; 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; 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; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006019-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192790};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006019-2}.
FT   DOMAIN          5..161
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   ACT_SITE        81
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-1"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
SQ   SEQUENCE   161 AA;  18001 MW;  6B4DE0AC7F3D8307 CRC64;
     MERIDKENYY LDIAETVLER ATCLRRNYGA IIVLNDEIVS TGYSGAPRGR ANCVDLGYCI
     REQLKVPSGE RYELCRSVHA EANAIISAAR RDMLGATMYL VGRDAKTGEL VQDATSCSMC
     RRLIINAGLK RVVIRNTEDS YTVVNVRDWV FEDDSLLNGL G
//
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