ID A0A2I1K7A6_9LACT Unreviewed; 170 AA.
AC A0A2I1K7A6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=ComE operon protein 2 {ECO:0000313|EMBL:PKY91435.1};
GN ORFNames=CYJ27_05050 {ECO:0000313|EMBL:PKY91435.1};
OS Aerococcus christensenii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=87541 {ECO:0000313|EMBL:PKY91435.1, ECO:0000313|Proteomes:UP000234775};
RN [1] {ECO:0000313|EMBL:PKY91435.1, ECO:0000313|Proteomes:UP000234775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0844 {ECO:0000313|EMBL:PKY91435.1,
RC ECO:0000313|Proteomes:UP000234775};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-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 -!- 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:PKY91435.1}.
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DR EMBL; PKGZ01000003; PKY91435.1; -; Genomic_DNA.
DR RefSeq; WP_060937297.1; NZ_PKGZ01000003.1.
DR AlphaFoldDB; A0A2I1K7A6; -.
DR OrthoDB; 9788517at2; -.
DR Proteomes; UP000234775; 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; 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; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006019-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000234775};
KW Zinc {ECO:0000256|PIRSR:PIRSR006019-2}.
FT DOMAIN 5..132
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 72
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-1"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006019-2"
SQ SEQUENCE 170 AA; 19301 MW; 0E338D87A59A83CE CRC64;
MVRIPWDQYF LSQALVLSMR STCHRLMVGA VIVRENRIIA GGYNGSVSGE THCIDKGCYL
EDGHCVRTIH SEMNAIIQCA KFGVSTENAD IYVTHFPCLQ CTKQIIQAGI KKVTYLYDYH
NHPYAIELLA KAHVEVVKRE LGATFFDQLT EQNQENLEKQ KISADFSKDE
//
