TAD2_ARATH
ID TAD2_ARATH Reviewed; 182 AA.
AC Q6IDB6; Q9LNH1;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=tRNA-specific adenosine deaminase TAD2 {ECO:0000303|PubMed:25315605};
DE Short=AtTAD2 {ECO:0000303|PubMed:25315605};
DE EC=3.5.4.33 {ECO:0000269|PubMed:25315605};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2191 {ECO:0000305};
DE AltName: Full=tRNA-specific adenosine-34 deaminase TAD2 {ECO:0000305};
GN Name=TAD2 {ECO:0000303|PubMed:25315605}; Synonyms=EMB2191 {ECO:0000305};
GN OrderedLocusNames=At1g48175 {ECO:0000312|Araport:AT1G48175};
GN ORFNames=F21D18.9 {ECO:0000312|EMBL:AAF79540.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TAD3, 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 TAD3. {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. ADAT2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79540.1; Type=Erroneous gene model prediction; Evidence={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; AC023673; AAF79540.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32259.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59127.1; -; Genomic_DNA.
DR EMBL; BT014757; AAT41740.1; -; mRNA.
DR EMBL; BT014997; AAT70448.1; -; mRNA.
DR RefSeq; NP_001321516.1; NM_001333303.1.
DR RefSeq; NP_564523.3; NM_103714.4.
DR AlphaFoldDB; Q6IDB6; -.
DR SMR; Q6IDB6; -.
DR STRING; 3702.AT1G48175.1; -.
DR PaxDb; Q6IDB6; -.
DR PRIDE; Q6IDB6; -.
DR ProteomicsDB; 245279; -.
DR EnsemblPlants; AT1G48175.1; AT1G48175.1; AT1G48175.
DR EnsemblPlants; AT1G48175.4; AT1G48175.4; AT1G48175.
DR GeneID; 841237; -.
DR Gramene; AT1G48175.1; AT1G48175.1; AT1G48175.
DR Gramene; AT1G48175.4; AT1G48175.4; AT1G48175.
DR KEGG; ath:AT1G48175; -.
DR Araport; AT1G48175; -.
DR TAIR; locus:505006173; AT1G48175.
DR eggNOG; KOG1018; Eukaryota.
DR HOGENOM; CLU_025810_8_2_1; -.
DR InParanoid; Q6IDB6; -.
DR OMA; MENEKAP; -.
DR OrthoDB; 1616309at2759; -.
DR PhylomeDB; Q6IDB6; -.
DR PRO; PR:Q6IDB6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6IDB6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IMP:UniProtKB.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IMP:UniProtKB.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IBA:GO_Central.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
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.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..182
FT /note="tRNA-specific adenosine deaminase TAD2"
FT /id="PRO_0000443859"
FT DOMAIN 7..135
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 60
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
SQ SEQUENCE 182 AA; 20107 MW; E8B97E09AC156050 CRC64;
MEEDHCEDSH NYMGFALHQA KLALEALEVP VGCVFLEDGK VIASGRNRTN ETRNATRHAE
MEAIDQLVGQ WQKDGLSPSQ VAEKFSKCVL YVTCEPCIMC ASALSFLGIK EVYYGCPNDK
FGGCGSILSL HLGSEEAQRG KGYKCRGGIM AEEAVSLFKC FYEQGNPNAP KPHRPVVQRE
RT
