CDAC1_PONAB
ID CDAC1_PONAB Reviewed; 515 AA.
AC Q5RAX4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, 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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
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. 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; CR858887; CAH91086.1; -; mRNA.
DR RefSeq; NP_001125631.1; NM_001132159.1.
DR AlphaFoldDB; Q5RAX4; -.
DR SMR; Q5RAX4; -.
DR STRING; 9601.ENSPPYP00000006113; -.
DR GeneID; 100172549; -.
DR KEGG; pon:100172549; -.
DR CTD; 81602; -.
DR eggNOG; KOG3127; Eukaryota.
DR InParanoid; Q5RAX4; -.
DR OrthoDB; 1569973at2759; -.
DR Proteomes; UP000001595; Unplaced.
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:0008270; F:zinc ion binding; IEA:InterPro.
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_0000300494"
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 494..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 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; 58557 MW; C257A4D7CDC34815 CRC64;
MKEAGQMQNL ESARAGRSVS TQTGSMTGQI PRLSKVNLFT LLSLWMELFP AVEAQRQKSQ
KNEEGKHGPL GDNEEMTRVS TDKRQVKRTG LVVVKNMKIV GLHCSSEDLH AGQIALIKHG
SRLKNCDLYF SRKPCSACLK MIVNAGVNRI SYWPADPEIS LLTEASSSED AKLDAKAVER
LKSNSRAHVC VLLQPLVCYM VQFVEETSYK CDFIQKITKT LPDANTDFYY ERKQERIKEY
EMLFLVSNEE MHKQILMTIG LENLCENPYF SNLRQNMKDL ILLLATVASS VPNFKHFGFY
RSNPEQINEI HNQSLPQEIA RHCMVQARLL AYRTEDHKTG VGAVIWAEGK SRSCDGTGAM
YFVGCGYNAF PVGSEYADFP HMDDKQKDRE IRKFRYIIHA ERNALTFRCQ EIKPEERSMI
FVTKCPCDEC VPLIKGAGIK QIYAGDVDVG KKKADISYMR FGELEGVSKF TWQLNPSGAY
GLEQNEPERR ENGVLRPVPQ KEEQHQDKKL CLGIH
