CDA4_ARATH
ID CDA4_ARATH Reviewed; 251 AA.
AC Q9S7S2; Q9ZT31;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable inactive cytidine deaminase 4;
GN Name=CDA4; Synonyms=DESH; OrderedLocusNames=At4g29650; ORFNames=T16L4.160;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Sanchez H., Schuster W.;
RT "Cytidine deaminases in Arabidopsis thaliana: a gene family of eight
RT members are located within a 24 kb region.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Faivre-Nitschke S.E., Grienenberger J.M., Gualberto J.M.;
RT "Cloning and characterisation of a cytidine deaminase gene family from
RT Arabidopsis thaliana.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
CC -!- CAUTION: Lacks part of the deaminase domain and the catalytically
CC essential zinc-binding residues. It is therefore most likely inactive.
CC {ECO:0000305}.
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; AF121877; AAD30448.1; -; Genomic_DNA.
DR EMBL; AF080676; AAC69570.1; -; Genomic_DNA.
DR EMBL; AL079344; CAB45325.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79723.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85655.1; -; Genomic_DNA.
DR EMBL; DQ056663; AAY78810.1; -; mRNA.
DR PIR; T09928; T09928.
DR RefSeq; NP_194694.1; NM_119110.2.
DR AlphaFoldDB; Q9S7S2; -.
DR SMR; Q9S7S2; -.
DR STRING; 3702.AT4G29650.1; -.
DR PaxDb; Q9S7S2; -.
DR PRIDE; Q9S7S2; -.
DR EnsemblPlants; AT4G29650.1; AT4G29650.1; AT4G29650.
DR GeneID; 829086; -.
DR Gramene; AT4G29650.1; AT4G29650.1; AT4G29650.
DR KEGG; ath:AT4G29650; -.
DR Araport; AT4G29650; -.
DR TAIR; locus:2134418; AT4G29650.
DR eggNOG; KOG0833; Eukaryota.
DR HOGENOM; CLU_052424_1_0_1; -.
DR InParanoid; Q9S7S2; -.
DR OMA; CIESAAY; -.
DR OrthoDB; 1400471at2759; -.
DR PhylomeDB; Q9S7S2; -.
DR BioCyc; ARA:AT4G29650-MON; -.
DR PRO; PR:Q9S7S2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S7S2; baseline and differential.
DR Genevisible; Q9S7S2; AT.
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 InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF08211; dCMP_cyt_deam_2; 1.
DR SUPFAM; SSF53927; SSF53927; 2.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..251
FT /note="Probable inactive cytidine deaminase 4"
FT /id="PRO_0000429146"
FT DOMAIN 136..251
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 76
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61..63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 153
FT /note="N -> Y (in Ref. 2; AAC69570)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..198
FT /note="MA -> IV (in Ref. 2; AAC69570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 251 AA; 27226 MW; 553A1A8866056F97 CRC64;
MTQQLKFILT REEAASKGVS RPSDLVKLEE EAMILARAPI SGVQDAVLGL ASSDRIFLGV
NVEFEGLPLH HSISAEQFLV ANLALNFEQE LHACLIPSRF YLESFEEDVP LLLVPQNNRL
AHSDPFSAAE ICSNPEHCSH LKCRALTAAN KSNAQYSKCP SGVALICEGE VYGGWCIESA
AYNLSLGPVQ AALVDFMARG EGKGFEMITG AVLVEMNDAK VSQEATARIL LKTIAPGCNF
SVFRCHKTAE N
