ID A0A0G4B1Q3_9BACT Unreviewed; 306 AA. AC A0A0G4B1Q3; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 27-MAR-2024, entry version 16. DE SubName: Full=Zinc-binding CMP/dCMP deaminase, dCMP deaminase {ECO:0000313|EMBL:AKM81759.1}; DE EC=3.5.4.12 {ECO:0000313|EMBL:AKM81759.1}; GN ORFNames=US01_C0001G0836 {ECO:0000313|EMBL:AKM81759.1}; OS candidate division TM6 bacterium GW2011_GWF2_28_16. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619077 {ECO:0000313|EMBL:AKM81759.1, ECO:0000313|Proteomes:UP000035666}; RN [1] {ECO:0000313|EMBL:AKM81759.1, ECO:0000313|Proteomes:UP000035666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large RT radiation of phyla."; RL Nature 0:0-0(2015). CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000256|ARBA:ARBA00006576}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP011212; AKM81759.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0G4B1Q3; -. DR KEGG; tmg:US01_C0001G0836; -. DR Proteomes; UP000035666; Chromosome. DR GO; GO:0004132; F:dCMP deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. 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; IPR015517; dCMP_deaminase-rel. 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 Hydrolase {ECO:0000313|EMBL:AKM81759.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 139..268 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000259|PROSITE:PS51747" SQ SEQUENCE 306 AA; 35008 MW; 0F4A2D30F08E1F27 CRC64; MKQILIAYVP VLHRGYQEFF EKYRGAELWL LDREELLSFE ELEYLKKDIR VLDLSLTEQA INSWHIFNIV KSIKIKNLEQ LDYSNSFVFT SDDIGQFIAQ EFFAKAANKT FEPIFLRWDR NLMSKQNDAP KDIVISKADF EQKMMIKAFM QAGKSSDWWR HVGGLIMKNG QVIFAGSNKH LPNNDEQYKN SDPRISFTSG VGIDFSSSIH AEADLIALAA KQGIALDGAE MFVTTFPCPV CAKQIAVAGI KKVYYAKGYA LLDGLEIFKS FGIEVILVKF SEKEFVEIEK LENQASMVEN CYMLKK //