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Database: UniProt
Entry: A0A1U8JMF9_GOSHI
LinkDB: A0A1U8JMF9_GOSHI
Original site: A0A1U8JMF9_GOSHI 
ID   A0A1U8JMF9_GOSHI        Unreviewed;       304 AA.
AC   A0A1U8JMF9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=cytidine deaminase {ECO:0000256|ARBA:ARBA00012783};
DE            EC=3.5.4.5 {ECO:0000256|ARBA:ARBA00012783};
GN   Name=LOC107907145 {ECO:0000313|RefSeq:XP_016689883.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016689883.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016689883.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016689883.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_016689883.1; XM_016834394.1.
DR   AlphaFoldDB; A0A1U8JMF9; -.
DR   STRING; 3635.A0A1U8JMF9; -.
DR   PaxDb; 3635-A0A1U8JMF9; -.
DR   GeneID; 107907145; -.
DR   KEGG; ghi:107907145; -.
DR   OMA; NYSPCGH; -.
DR   OrthoDB; 102874at2759; -.
DR   Proteomes; UP000189702; Chromosome 19.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0009972; P:cytidine deamination; IBA:GO_Central.
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:UP000189702};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006334-3}.
FT   DOMAIN          23..160
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   DOMAIN          190..304
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   304 AA;  32975 MW;  77E4C900A6D2DF73 CRC64;
     MDRPRFVIES AEAEQMAKQS GQTVLQLLPS LVKSAQTLAR PPISNYHVGA VGMGPSGRIF
     FGVNLEFPGL PLNQSVHAEQ FLITNLSLNA EPRLRYLAVS AAPCGHCRQF LQELRGASDV
     KILITSSEDE KENKINNNCN DKDQEFTPLS HFLPHRFGPD DLLEKDVPLL LEPHRNGLSF
     CNDLCNGKIN GVDDLKHAAV DAANMSHAPY SGCPSGMALL DVEGKIYKGS YMESAAYNPS
     LPPAQAALVA YVAGGGGGGY ERIVGAVLVE KADAVIKQEH TSRLLLQCIS PKCEFKVFHC
     TKTC
//
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