ID A0A133U8M8_9EURY Unreviewed; 171 AA.
AC A0A133U8M8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=CMP/dCMP-type deaminase domain-containing protein {ECO:0000259|PROSITE:PS51747};
GN ORFNames=AKJ61_00425 {ECO:0000313|EMBL:KXA90540.1};
OS candidate division MSBL1 archaeon SCGC-AAA259B11.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698260 {ECO:0000313|EMBL:KXA90540.1, ECO:0000313|Proteomes:UP000070184};
RN [1] {ECO:0000313|EMBL:KXA90540.1, ECO:0000313|Proteomes:UP000070184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA259B11 {ECO:0000313|EMBL:KXA90540.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
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:KXA90540.1}.
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DR EMBL; LHXK01000003; KXA90540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133U8M8; -.
DR PATRIC; fig|1698260.3.peg.335; -.
DR Proteomes; UP000070184; 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; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR016473; dCMP_deaminase.
DR InterPro; IPR015517; dCMP_deaminase-rel.
DR InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
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 Reference proteome {ECO:0000313|Proteomes:UP000070184};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..156
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 171 AA; 19119 MW; E09AB6670B687183 CRC64;
MKGEERPSKD EYYLGIAEAV CKRSPCIRRQ FGAIIVKEDV IVSTGYNGPP RGVINCTEAG
CLKDELDMPH YRQYQFCTAV HAEENAVINA ARHGATVMGG TLYLYGQEYE TGETFEGKPC
DRCKRTLINA GIEEVITKNA EGTVIKKDVS DWVSQDTKKY LNKLEEAKKS K
//
