ID A0A1T4M2Q3_9FUSO Unreviewed; 162 AA.
AC A0A1T4M2Q3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=dCMP deaminase {ECO:0000313|EMBL:SJZ61243.1};
GN ORFNames=SAMN02745174_01079 {ECO:0000313|EMBL:SJZ61243.1};
OS Cetobacterium ceti.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Cetobacterium.
OX NCBI_TaxID=180163 {ECO:0000313|EMBL:SJZ61243.1, ECO:0000313|Proteomes:UP000191153};
RN [1] {ECO:0000313|EMBL:SJZ61243.1, ECO:0000313|Proteomes:UP000191153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700028 {ECO:0000313|EMBL:SJZ61243.1,
RC ECO:0000313|Proteomes:UP000191153};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUWX01000007; SJZ61243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4M2Q3; -.
DR STRING; 180163.SAMN02745174_01079; -.
DR OrthoDB; 9788517at2; -.
DR Proteomes; UP000191153; 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:UP000191153};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006019-2}.
FT DOMAIN 9..145
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 80
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-1"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
SQ SEQUENCE 162 AA; 18171 MW; 3F845D916482FA3B CRC64;
MGKRNDYIDW DEYFMGVAIL SSKRSKDPGT QVGACIVTPD KRIVGVGYNG FPMGCSDDDF
PWDREGDFLD TKYPFVCHAE MNAILNSIKS LKGCTIYVDL FPCNECAKSI IQSGIREIVY
LSDKYSGTPS DIASKKMLDA AGVNYRKLKS EIDHLVLDFR KN
//
