CDAC1_DANRE
ID CDAC1_DANRE Reviewed; 471 AA.
AC Q5U3U4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=zgc:101622;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the deamination of cytidine and deoxycytidine into
CC uridine and deoxyuridine, respectively. {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 -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; BC085391; AAH85391.1; -; mRNA.
DR RefSeq; NP_001007449.1; NM_001007448.1.
DR AlphaFoldDB; Q5U3U4; -.
DR SMR; Q5U3U4; -.
DR STRING; 7955.ENSDARP00000124195; -.
DR PaxDb; Q5U3U4; -.
DR GeneID; 492807; -.
DR KEGG; dre:492807; -.
DR CTD; 81602; -.
DR ZFIN; ZDB-GENE-041114-163; cdadc1.
DR eggNOG; KOG3127; Eukaryota.
DR InParanoid; Q5U3U4; -.
DR OrthoDB; 1569973at2759; -.
DR PhylomeDB; Q5U3U4; -.
DR PRO; PR:Q5U3U4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 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 Hydrolase; Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..471
FT /note="Cytidine and dCMP deaminase domain-containing
FT protein 1"
FT /id="PRO_0000300495"
FT DOMAIN 57..153
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 312..460
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 COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 395
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 393
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 421
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 424
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 471 AA; 52700 MW; B99E92254FE9F920 CRC64;
MAESNSWRSH RESDGNRSIP NGDDARNVRE TGVQTDAKVQ GQGPRLSKAN LFTLLSLWME
LFPKREACQQ ENDAAGVSGL VVVHECRVLG LHCSSAQLHA GQVAVVKHGP RLKSCELYFS
RKPCSTCLKM LINAGVSRIS YWPGDAELSL LSESLHHGSS SALQEAVLDA TAAERLKSNS
RPHISVLLQP LDCTVLQFLD ETSQNADFLG KIVADNPALD TGDIYRREFW NNSDNFLEKF
FISDEERHKY VLNKMGLENF CMEPNFSNLR QHMRNLIRIL ASVASSVPAL LEDYGFFMRE
PVGMGSPGLP QGVIRHCVIQ ARLLACRTED PKVGVGAVIW AEGKQSQCDG TGQLYLVGCG
YNAYPVGSQY AEYPQMDHKQ EERQNRKYRY ILHAEQNALT FRSAEIKAED NTMMFVTKCP
CDECVPLIGC AGIKQIYTTD LDSNKVKHDI SYLRFNKLNG VQKFIVSVRE K
