ID A0A0D2SIM9_GOSRA Unreviewed; 312 AA.
AC A0A0D2SIM9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=cytidine deaminase {ECO:0000256|ARBA:ARBA00012783};
DE EC=3.5.4.5 {ECO:0000256|ARBA:ARBA00012783};
GN ORFNames=B456_013G228000 {ECO:0000313|EMBL:KJB83062.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB83062.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB83062.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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 EMBL; CM001752; KJB83062.1; -; Genomic_DNA.
DR RefSeq; XP_012464928.1; XM_012609474.1.
DR AlphaFoldDB; A0A0D2SIM9; -.
DR STRING; 29730.A0A0D2SIM9; -.
DR EnsemblPlants; KJB83062; KJB83062; B456_013G228000.
DR GeneID; 105783815; -.
DR Gramene; KJB83062; KJB83062; B456_013G228000.
DR KEGG; gra:105783815; -.
DR eggNOG; KOG0833; Eukaryota.
DR OMA; HSISPDC; -.
DR OrthoDB; 102874at2759; -.
DR Proteomes; UP000032304; Chromosome 13.
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:UP000032304};
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 191..312
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 312 AA; 33944 MW; 87E4DDF79C70CD6E CRC64;
MDRPRFVIDS AEVEQMAKQS RQTVLHLLPS LVKSAQALAR PPISNYHVGA VGVGSSGRIF
FGVNLEFPGL PLNHSVHAEQ FLITNLSLNA ESCLKFLAVS AAPCGHCRQF LQELRAAPDV
NILITATEKE KENKTINNRN DKDMQFAPLS YFLPHRFGPD DLLEKDVPLL LEPHRNGLSF
CSDTRNGEIN GDGDDSKYAA LEAANASHAP YSGCPSGAAL VDVEGKIYKG SYMESAAYNP
SLPPVQAALV AYVASGGGGG YERIVKAVLV ETADAVIKQE HTAKLLLQCI SPKCEFKVFH
CNKNMLKCEY QV
//
