ID V6Q4B9_9ENTE Unreviewed; 166 AA.
AC V6Q4B9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ComE operon protein 2 {ECO:0000313|EMBL:EST89577.1};
GN ORFNames=T233_01332 {ECO:0000313|EMBL:EST89577.1};
OS Vagococcus lutrae LBD1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1408226 {ECO:0000313|EMBL:EST89577.1, ECO:0000313|Proteomes:UP000018126};
RN [1] {ECO:0000313|EMBL:EST89577.1, ECO:0000313|Proteomes:UP000018126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LBD1 {ECO:0000313|EMBL:EST89577.1,
RC ECO:0000313|Proteomes:UP000018126};
RX PubMed=24371201;
RA Lebreton F., Valentino M.D., Duncan L.B., Zeng Q., Manson McGuire A.,
RA Earl A.M., Gilmore M.S.;
RT "High-Quality Draft Genome Sequence of Vagococcus lutrae Strain LBD1,
RT Isolated from the Largemouth Bass Micropterus salmoides.";
RL Genome Announc. 1:e01087-13(2013).
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:EST89577.1}.
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DR EMBL; AYSH01000017; EST89577.1; -; Genomic_DNA.
DR AlphaFoldDB; V6Q4B9; -.
DR STRING; 1408226.T233_01332; -.
DR PATRIC; fig|1408226.3.peg.1304; -.
DR eggNOG; COG2131; Bacteria.
DR Proteomes; UP000018126; 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; IPR013404; Competence_ComEB.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR016473; dCMP_deaminase.
DR InterPro; IPR015517; dCMP_deaminase-rel.
DR InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR NCBIfam; TIGR02571; ComEB; 1.
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:UP000018126};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006019-2}.
FT DOMAIN 7..139
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 74
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-1"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 100
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"
SQ SEQUENCE 166 AA; 18647 MW; E5010C64BED037A4 CRC64;
MTIERIPWDQ YFMAQSVLLS LRSTCQRLSV GATIVRDKRM IAGGYNGSVS GDVHCIDEGC
YVVDGHCVRT IHAEMNAILQ CAKFGIPTDG AEIYVTHFPC LQCTKMILQA GIKKIHYLTD
YRNDDYAIQL LEKTGVIVEQ VTLDQEYFTE LQAIYGGNNQ KETNAE
//
