TAD3_ARATH
ID TAD3_ARATH Reviewed; 400 AA.
AC F4KH86; Q0WRI1; Q5XF54; Q9FIR8;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=tRNA-specific adenosine deaminase TAD3 {ECO:0000303|PubMed:25315605};
DE Short=AtTAD3 {ECO:0000303|PubMed:25315605};
DE EC=3.5.4.33 {ECO:0000269|PubMed:25315605};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2820 {ECO:0000305};
DE AltName: Full=tRNA-specific adenosine-34 deaminase TAD3 {ECO:0000305};
GN Name=TAD3 {ECO:0000303|PubMed:25315605}; Synonyms=EMB2820 {ECO:0000305};
GN OrderedLocusNames=At5g24670 {ECO:0000312|Araport:AT5G24670};
GN ORFNames=MXC17.5 {ECO:0000312|EMBL:BAB09649.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TAD2, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=25315605; DOI=10.1104/pp.114.250498;
RA Zhou W., Karcher D., Bock R.;
RT "Identification of enzymes for adenosine-to-inosine editing and discovery
RT of cytidine-to-uridine editing in nucleus-encoded transfer RNAs of
RT Arabidopsis.";
RL Plant Physiol. 166:1985-1997(2014).
CC -!- FUNCTION: Involved in RNA editing. Catalyzes the specific deamination
CC of adenosine-34 in several cytosolic tRNA species. Generates inosine at
CC the wobble position of the anticodon loop.
CC {ECO:0000269|PubMed:25315605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC Evidence={ECO:0000269|PubMed:25315605};
CC -!- SUBUNIT: Interacts with TAD2. {ECO:0000269|PubMed:25315605}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25315605}. Cytoplasm
CC {ECO:0000269|PubMed:25315605}. Note=Localizes predominantly to the
CC nucleus. {ECO:0000269|PubMed:25315605}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to embryo development
CC arrest at the globular stage. {ECO:0000269|PubMed:25315605}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT3 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09649.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF00268.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB016881; BAB09649.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93347.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69030.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69032.1; -; Genomic_DNA.
DR EMBL; BT015762; AAU90052.1; -; mRNA.
DR EMBL; BT020197; AAV59263.1; -; mRNA.
DR EMBL; AK228326; BAF00268.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001318639.1; NM_001343891.1.
DR RefSeq; NP_001330739.1; NM_001343893.1.
DR RefSeq; NP_197855.3; NM_122376.4.
DR AlphaFoldDB; F4KH86; -.
DR SMR; F4KH86; -.
DR STRING; 3702.AT5G24670.2; -.
DR iPTMnet; F4KH86; -.
DR PRIDE; F4KH86; -.
DR EnsemblPlants; AT5G24670.1; AT5G24670.1; AT5G24670.
DR EnsemblPlants; AT5G24670.3; AT5G24670.3; AT5G24670.
DR EnsemblPlants; AT5G24670.4; AT5G24670.4; AT5G24670.
DR GeneID; 832539; -.
DR Gramene; AT5G24670.1; AT5G24670.1; AT5G24670.
DR Gramene; AT5G24670.3; AT5G24670.3; AT5G24670.
DR Gramene; AT5G24670.4; AT5G24670.4; AT5G24670.
DR KEGG; ath:AT5G24670; -.
DR Araport; AT5G24670; -.
DR OMA; FMRHTIN; -.
DR PRO; PR:F4KH86; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KH86; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IMP:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IMP:UniProtKB.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..400
FT /note="tRNA-specific adenosine deaminase TAD3"
FT /id="PRO_0000443860"
FT DOMAIN 250..385
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 273..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT CONFLICT 138
FT /note="I -> M (in Ref. 3; AAU90052/AAV59263)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 45098 MW; 6FB66D161D8ED701 CRC64;
MDSDAWEIIH IPEKPSLSPD HQPTVKVYAS LIKPRFANTI VRHLCKIAPL EDLRHVKRVK
KKILPDCGET QLTVILCLAP EHNDQLSDMP PDVQRLVDPY ELSPFITQVC KYAAVSKEEW
EEQSKIWPTS FHPPTYNIDG IGGFSEEETQ SICKFMRVVI DMAVSGHTPL VNAAVIVDPS
VRRIIASETD QVYASSAPRD MTSAETRPFE ETGEICLNDT LEKQNGSLSA LSCLNPWQWS
LQPHDTENCS QWHPLRHASM VAIESSSARD RNLFPNPSKI FDQDHVPPSN TDSPAKKQKT
SSQSPDVQND SREETVRDPS MERPYLCTGY DIFLLLEPCT MCAMALVHQR IKRIFYAFPN
TTAGGLGSVH RLQGEKSLNH HYAVFRVLLP DDALRQMTTV
