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Database: UniProt
Entry: A0A433RS34_9BACL
LinkDB: A0A433RS34_9BACL
Original site: A0A433RS34_9BACL 
ID   A0A433RS34_9BACL        Unreviewed;       193 AA.
AC   A0A433RS34;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Competence protein ComE {ECO:0000313|EMBL:RUS54413.1};
GN   ORFNames=QI30_13425 {ECO:0000313|EMBL:RUS54413.1};
OS   Kurthia sp. 3B1D.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1562256 {ECO:0000313|EMBL:RUS54413.1, ECO:0000313|Proteomes:UP000288623};
RN   [1] {ECO:0000313|EMBL:RUS54413.1, ECO:0000313|Proteomes:UP000288623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3B1D {ECO:0000313|EMBL:RUS54413.1,
RC   ECO:0000313|Proteomes:UP000288623};
RA   Lawson J.N., Gonzalez J.E., Rinauldi L., Xuan Z., Firman A., Shaddox L.,
RA   Trudeau A., Shah S., Reiman D.;
RT   "Genome sequence and analysis of novel Kurthia sp.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:RUS54413.1}.
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DR   EMBL; JTFC01000032; RUS54413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433RS34; -.
DR   OrthoDB; 9788517at2; -.
DR   Proteomes; UP000288623; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; 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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000288623};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          5..137
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
SQ   SEQUENCE   193 AA;  21741 MW;  944C6DB3A9DD9867 CRC64;
     MERITWDQFF MAQSHLLALR STCTRLAVGA TIVRDKRIIA GGYNGSISGD DHCIDKGCYV
     VDNHCVRTVH AETNALLQCA KYGTPTNGAD LYVTHFPCLP CTKSIIQSGI KNLYYAKDYK
     NNTYAIELFK QAGVNVVHVP FDERKIDFLS DEKVTLYLSL LNELRDKGAT SEELAPYEQK
     VEQLFGKHIL ETK
//
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