CDAC1_MACFA
ID CDAC1_MACFA Reviewed; 515 AA.
AC Q4R683;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cytidine and dCMP deaminase domain-containing protein 1;
DE EC=3.5.4.5 {ECO:0000250|UniProtKB:Q9BWV3};
DE AltName: Full=Cytidine deaminase {ECO:0000305};
GN Name=CDADC1; ORFNames=QtsA-18829;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the deamination of cytidine and deoxycytidine into
CC uridine and deoxyuridine, respectively. May play an important role in
CC testicular development and spermatogenesis.
CC {ECO:0000250|UniProtKB:Q9BWV3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+);
CC Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC Evidence={ECO:0000250|UniProtKB:Q9BWV3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine + H(+) + H2O = NH4(+) + uridine;
CC Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC Evidence={ECO:0000250|UniProtKB:Q9BWV3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9GZX7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BWV3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BWV3}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AB169306; BAE01392.1; -; mRNA.
DR RefSeq; NP_001272023.1; NM_001285094.1.
DR AlphaFoldDB; Q4R683; -.
DR SMR; Q4R683; -.
DR STRING; 9541.XP_005585900.1; -.
DR Ensembl; ENSMFAT00000070562; ENSMFAP00000020007; ENSMFAG00000032976.
DR GeneID; 101866199; -.
DR CTD; 81602; -.
DR VEuPathDB; HostDB:ENSMFAG00000032976; -.
DR eggNOG; KOG3127; Eukaryota.
DR GeneTree; ENSGT00940000153676; -.
DR OMA; ACRQERI; -.
DR OrthoDB; 1569973at2759; -.
DR Proteomes; UP000233100; Chromosome 17.
DR Bgee; ENSMFAG00000032976; Expressed in bone marrow and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0061676; F:importin-alpha family protein binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0070383; P:DNA cytosine deamination; IEA:Ensembl.
DR CDD; cd01286; deoxycytidylate_deaminase; 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; PTHR11086; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 2.
DR SUPFAM; SSF53927; SSF53927; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..515
FT /note="Cytidine and dCMP deaminase domain-containing
FT protein 1"
FT /id="PRO_0000300492"
FT DOMAIN 71..169
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 318..483
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 272..284
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BWV3"
FT MOTIF 489..511
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BWV3"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
SQ SEQUENCE 515 AA; 58548 MW; BD52B9EF49A9F092 CRC64;
MKEAGQMQNL ESARAGRSVS TQTGSMTGQI PRLSKVNLFT LLSLWMELFP AVEAQRQKSQ
KNEEGKHGPL GDNEEMTRVS TDKRQVKRTG LVVVKNMKIV GLHCSSEDLH AGQIALIKHG
SRLKNCDLYF SRKPCSACLK MIVNAGVNRI SYWPADPEIS LLTEASSSED AKLDAKAVER
LKSNSRAHVC VLLQPLVCYM VQFVEETSYK CDFIQKITKT LPDANTDFYY ECKQERIKEY
EMLFLVSNEE MHKQILMTIG LENLCENPYF SNLRQNMKDL ILLLATVASS VPNFKHFGFY
CSNPEQINEI HNQSLPQEIA RHCMVQARLL AYRTEDHKTG VGAVIWAEGK SRSCDGTGAM
YFVGCGYNAF PVGSEYADFP HMDDKQKDRE IRKFRYIIHA EQNALTFRCQ EIKPEERSMI
FVTKCPCDEC VPLIKGAGIK QIYAGDVDVG KKKADISYMR FGELEGVSKF TWQLNPSEAY
GLEQNEPERR ENGVLRPVPQ KEEQHQDKKL RLGIH
