ID A0A251V3C6_HELAN Unreviewed; 366 AA.
AC A0A251V3C6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE SubName: Full=Putative cytidine/deoxycytidylate deaminase family protein {ECO:0000313|EMBL:OTG30105.1};
GN ORFNames=HannXRQ_Chr03g0060791 {ECO:0000313|EMBL:OTG30105.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG30105.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM007892; OTG30105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251V3C6; -.
DR STRING; 4232.A0A251V3C6; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr03g0087351; CDS:HanXRQr2_Chr03g0087351.1; HanXRQr2_Chr03g0087351.
DR Gramene; mRNA:HanXRQr2_Chr03g0087351; CDS:HanXRQr2_Chr03g0087351.1; HanXRQr2_Chr03g0087351.
DR InParanoid; A0A251V3C6; -.
DR OMA; HSISPDC; -.
DR OrthoDB; 102874at2759; -.
DR Proteomes; UP000215914; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
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; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd.
DR InterPro; IPR016193; Cytidine_deaminase-like.
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; 2.
DR PIRSF; PIRSF006334; Cdd_plus_pseudo; 2.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 2.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006334-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW Zinc {ECO:0000256|PIRSR:PIRSR006334-3}.
FT DOMAIN 25..151
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 241..366
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 81
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-1"
FT BINDING 66..68
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-2"
FT BINDING 79
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"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-3"
SQ SEQUENCE 366 AA; 39384 MW; 47A3D100C58D62A6 CRC64;
MNLPPKTYII EAEEAKSMAK SKNLTLPQLL PSLIKSAQNL ANPPISNFAV GVVGLTSDGR
IFFGGNIEFP GLPLHHTIHG EQFFITNLAA HAAGAKLLYL AVSAAPCGHC RQFFQELRGI
SDTQIVITDQ PQENPDYKPF SSILPHPFGP FDLLDENTPL ILEKHNNQLT LKDGNFIIQD
EKMCDLPNGF SDLNAKNEEF FKTEASAAAR GSHAPPKDGN FINQDENTFD LSNGFCKLIA
KNKEFLKSEA LAAARGSHAP YSGCPSGVAL MDCEGKVYKG SYMESAAYNP SMMPVQAALV
AYMVAGGGGY EKIVAAVVVE KEGVVVRQED TARLVLKHLS PKCGACVGPT VFLSKGGIIR
KEGGCV
//
