ID A0A164TI78_DAUCS Unreviewed; 297 AA.
AC A0A164TI78;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=cytidine deaminase {ECO:0000256|ARBA:ARBA00012783};
DE EC=3.5.4.5 {ECO:0000256|ARBA:ARBA00012783};
GN ORFNames=DCAR_024687 {ECO:0000313|EMBL:KZM87557.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM87557.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM87557.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM87557.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006334-3};
CC Note=Binds 1 zinc ion. {ECO:0000256|PIRSR:PIRSR006334-3};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:KZM87557.1}.
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DR EMBL; LNRQ01000007; KZM87557.1; -; Genomic_DNA.
DR RefSeq; XP_017215911.1; XM_017360422.1.
DR AlphaFoldDB; A0A164TI78; -.
DR STRING; 79200.A0A164TI78; -.
DR EnsemblPlants; KZM87557; KZM87557; DCAR_024687.
DR GeneID; 108193668; -.
DR Gramene; KZM87557; KZM87557; DCAR_024687.
DR KEGG; dcr:108193668; -.
DR OMA; NYSPCGH; -.
DR OrthoDB; 102874at2759; -.
DR Proteomes; UP000077755; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd01283; cytidine_deaminase; 2.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd.
DR InterPro; IPR006263; Cyt_deam_dimer.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR NCBIfam; TIGR01355; cyt_deam_dimer; 1.
DR PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1.
DR PANTHER; PTHR11644:SF2; CYTIDINE DEAMINASE; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF08211; dCMP_cyt_deam_2; 1.
DR PIRSF; PIRSF006334; Cdd_plus_pseudo; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR006334-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006334-3}.
FT DOMAIN 23..148
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 180..297
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 79
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-1"
FT BINDING 64..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-2"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-3"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-3"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-3"
SQ SEQUENCE 297 AA; 32163 MW; 00B6FC93BAC80FC7 CRC64;
MDDPRFVIEA SEAESMAKKY GVSVPELLPR LVKSAQTLAR PPTSNYHVAA VGLSSDGRIF
IGVNIEFPGV PLHHSIHAEQ FLVTNHALHN SPRLLYIAVS SAPCGHCRQF LQELRQAGEI
QILITSEPQK DVIYKPLLSL LPSPFGPTDL LDQQTPLILE SHDNGLCLMQ NKNLANGVDQ
DCEKLKSLAL EAANHSHAPY THCPSGVALM DVNGNVFKGC YMESAAYNPS LGPVQAALVA
FIASAGASYH DIVAAVLVEK EEAAVRQEDT ARLLLKMVAP DCDFRVFHCC SSLNGCV
//
