ID G0WE45_NAUDC Unreviewed; 318 AA.
AC G0WE45;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=CMP/dCMP-type deaminase domain-containing protein {ECO:0000259|PROSITE:PS51747};
GN Name=NDAI0G02790 {ECO:0000313|EMBL:CCD26056.2};
GN OrderedLocusNames=NDAI_0G02790 {ECO:0000313|EMBL:CCD26056.2};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26056.2, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD26056.2, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 ---------------------------------------------------------------------------
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; HE580273; CCD26056.2; -; Genomic_DNA.
DR RefSeq; XP_003671299.2; XM_003671251.2.
DR AlphaFoldDB; G0WE45; -.
DR STRING; 1071378.G0WE45; -.
DR GeneID; 11495556; -.
DR KEGG; ndi:NDAI_0G02790; -.
DR eggNOG; KOG3127; Eukaryota.
DR HOGENOM; CLU_047993_0_0_1; -.
DR OMA; PPLRPDW; -.
DR OrthoDB; 178124at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
DR GO; GO:0019239; F:deaminase activity; IEA:UniProt.
DR GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; 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 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:UP000000689};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 168..297
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 318 AA; 36187 MW; CE0846ED0628C1D2 CRC64;
MLVAITGNGK FGAEHVRDIF IKNHEFKSLE EDDFETNDEI LEYATKHYKE NLIMLTNDLY
LITVLEKRPF FVHLTVNSSL ALKRAIISKT SKDLSPEDAL AAIMNEMSLE ESNHEYLELY
EKAHIKFKLV GKDWATVEKR LIKVVKEQIE QLQVKKNPFE NVPPLRPSWD TYFMKLATLA
ATRSNCMKRK VGCVIVRDHR VIATGYNGTP RHLTNCFNGG CDRCNDGGSK NLNTCLCLHA
EENALLEAGR DRVGFNATLY CDTCPCLTCS VKIVQSGITE VVYSQTYRMD EQSYKVLTAA
GINVRQYSFI EEPRLVIV
//
