ID   A0A0D6TEE0_9RHOB        Unreviewed;       510 AA.
AC   A0A0D6TEE0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=CMP/dCMP-type deaminase domain-containing protein {ECO:0000259|PROSITE:PS51747};
GN   ORFNames=SY26_07620 {ECO:0000313|EMBL:KIX18177.1};
OS   Paracoccus sp. 228.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX18177.1, ECO:0000313|Proteomes:UP000032743};
RN   [1] {ECO:0000313|EMBL:KIX18177.1, ECO:0000313|Proteomes:UP000032743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=361 {ECO:0000313|EMBL:KIX18177.1,
RC   ECO:0000313|Proteomes:UP000032743};
RA   Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA   Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT   "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT   Genomic and a Proteomic Perspective.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KIX18177.1}.
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DR   EMBL; JYGY01000002; KIX18177.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D6TEE0; -.
DR   STRING; 1192054.SY26_07620; -.
DR   PATRIC; fig|1603292.4.peg.1582; -.
DR   Proteomes; UP000032743; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; NF041025; antiphage_deaminase; 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:UP000032743};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          239..427
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
SQ   SEQUENCE   510 AA;  56900 MW;  D4AA0F9EEA32D3A3 CRC64;
     MHPLPDEELA YKPELIFGLV GPIGCNIDAA QDALDTHLTR FGYQTKLVHI TKAVGEVIPQ
     AAEVSQGRYE QKITELNNIV SLSGEKDFLA KIAVLFIGRH RLERNKETGL DPSLIADTPA
     NGTAFVIRQL KRSQEIELLR KVYGEKFIQV SVSADEAEQL TAVQGIIGKE DPYLPQDERE
     RKARSLIHKD KNEAQETFGQ RMLDTYHSGD VFVGGSATKI HSQVGRFIDA FFGSNYISPT
     KDEFGAYLAK AASLRTLDLS RQVGAAIVSS DGDVITLGCN EVPKANGGNY WGEDENPQRD
     IERRFESNKL ETNRIIHDFI HALSKHSMVQ CDPEKILGTS ELSQLLKASP ISDLTEFGRM
     THAEMSALMD AARIGRSVKG ATIYVTTFPC HNCAKHIIAS GIKRIVYIEP YAKSKAIELN
     GDALTTYTKS SDRVILEHFH GISPARYREI FDKPRKRRDE NNNIKPWHFD KPKPMVNQLI
     STHIMIEPGA LKEFKLTLNK VSDGLSASRT
//