TADA_ARATH
ID TADA_ARATH Reviewed; 1307 AA.
AC Q9S7I0; Q8GY37;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=tRNA(adenine(34)) deaminase, chloroplastic;
DE Short=TADA;
DE EC=3.5.4.33;
DE AltName: Full=tRNA adenosine deaminase arginine;
DE AltName: Full=tRNA arginine adenosine deaminase;
DE Flags: Precursor;
GN Name=TADA; OrderedLocusNames=At1g68720; ORFNames=F14K14.18, F24J5.5;
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP 3D-STRUCTURE MODELING, AND DOMAIN.
RX PubMed=19602623; DOI=10.1105/tpc.109.066654;
RA Delannoy E., Le Ret M., Faivre-Nitschke E., Estavillo G.M., Bergdoll M.,
RA Taylor N.L., Pogson B.J., Small I., Imbault P., Gualberto J.M.;
RT "Arabidopsis tRNA adenosine deaminase arginine edits the wobble nucleotide
RT of chloroplast tRNAArg(ACG) and is essential for efficient chloroplast
RT translation.";
RL Plant Cell 21:2058-2071(2009).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19460869; DOI=10.1261/rna.1600609;
RA Karcher D., Bock R.;
RT "Identification of the chloroplast adenosine-to-inosine tRNA editing
RT enzyme.";
RL RNA 15:1251-1257(2009).
CC -!- FUNCTION: Deaminates adenosines to inosines in tRNA-Arg(ACG).
CC Exclusively involved in A-to-I editing of the prokaryote-type
CC chloroplast-tRNA and not involved in C-to-U editing.
CC {ECO:0000269|PubMed:19460869, ECO:0000269|PubMed:19602623}.
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:19602623};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19460869, ECO:0000269|PubMed:19602623}.
CC -!- DOMAIN: The C-terminus (843-1307) is sufficient for the deamination.
CC {ECO:0000269|PubMed:19602623}.
CC -!- DISRUPTION PHENOTYPE: Loss of cp-tRNA editing, decreased chloroplast
CC translation and impaired photosynthesis. {ECO:0000269|PubMed:19602623}.
CC -!- MISCELLANEOUS: Since the absence of A-to-I editing is compatible with
CC plant survival, a limitted two out of three codon recognition occurs in
CC chloroplasts, though this mechanism is less efficient than wobble
CC pairing. {ECO:0000305|PubMed:19602623}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AC008075; AAD49971.1; -; Genomic_DNA.
DR EMBL; AC011914; AAG52046.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34831.1; -; Genomic_DNA.
DR EMBL; AK117889; BAC42528.1; -; mRNA.
DR EMBL; BT010731; AAR23701.1; -; mRNA.
DR PIR; G96711; G96711.
DR RefSeq; NP_177039.1; NM_105544.3.
DR AlphaFoldDB; Q9S7I0; -.
DR SMR; Q9S7I0; -.
DR STRING; 3702.AT1G68720.1; -.
DR iPTMnet; Q9S7I0; -.
DR PaxDb; Q9S7I0; -.
DR PRIDE; Q9S7I0; -.
DR ProteomicsDB; 234118; -.
DR EnsemblPlants; AT1G68720.1; AT1G68720.1; AT1G68720.
DR GeneID; 843202; -.
DR Gramene; AT1G68720.1; AT1G68720.1; AT1G68720.
DR KEGG; ath:AT1G68720; -.
DR Araport; AT1G68720; -.
DR TAIR; locus:2012408; AT1G68720.
DR eggNOG; KOG1018; Eukaryota.
DR HOGENOM; CLU_006132_0_0_1; -.
DR InParanoid; Q9S7I0; -.
DR OMA; EEDMEIH; -.
DR OrthoDB; 1616309at2759; -.
DR PhylomeDB; Q9S7I0; -.
DR BRENDA; 3.5.4.33; 399.
DR PRO; PR:Q9S7I0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7I0; baseline and differential.
DR Genevisible; Q9S7I0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IDA:TAIR.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IDA:TAIR.
DR HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR Pfam; PF14437; MafB19-deam; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Coiled coil; Hydrolase; Metal-binding; Plastid;
KW Reference proteome; Transit peptide; tRNA processing; Zinc.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..1307
FT /note="tRNA(adenine(34)) deaminase, chloroplastic"
FT /id="PRO_0000305189"
FT DOMAIN 1108..1230
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 245..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..309
FT /evidence="ECO:0000255"
FT COMPBIAS 249..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1161
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 1159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 883
FT /note="L -> S (in Ref. 4; BAC42528/AAR23701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1307 AA; 146564 MW; 8CDAD95ABAB24719 CRC64;
MFNTYTNSLQ WPIRSRNQQD YCSLLPERSE SYKLSKAYTS SRCYCVSSRS SCCCCCSTPS
SSSFVKPKVL INPGFVLYGV RQSTLIQWPS FQRRLLVGGG RLMGCEVYSS CDGIRRKNRS
FKLRCLEESD ECCGGRSCSD DVEAMISFLS EELIDEERKW NLVSRVKEKK KVGNVRKVSV
EGSNSYGNGR VSQRVKKPEG FGRRKEIKED VKLNERYDCE HCGRRKKSSE LESESRRGSK
LVTGEYIGKS YRGDEEREVR PRRRKSSSCS SYYSLASSGE FESDTEDQEE DVEIYRENVR
SSEKKVVDQS AKRLKSRKEA SQMHSRKKRD ESSTGVDSRY QKQIFEEGEN SNQAVTLNQR
RRKKFSQTEN RVSESTGNYE EDMEIHEVHV NDAETSSQNQ KLFNEREDYR VHSIRNDSGN
ENIESSQHQL KERLETRYSS EDRVSEMRRR TKYSSSQEEG INVLQNFPEV TNNQQPLVEE
RISKQAGTRR TTEHISESSE IHDIDIRNTY VSQREDQIRN QEVHAGLVSG LQSERKQQDY
HIEHNPLQTT QSDRTSVSVS HTSDAVRYTE IQRKSEKRLI GQGSTTAVQS DSKVEKNGAQ
KEDSRLDHAN SKKDGQTTLG LQSYQSKLSE EASSSQSSLM ASRTKLQLVD LVSEEMQGSE
TTLIPPSSQL VSRRSGQSYR TGGVSIQEIS HGTSESGYTT AFEHPRAGAS VNSQSAGELM
GFTSHEDAMG SAHRLEQASE KYVGEFVKKA KHGVINPETE EQRAESNQLK RRDSRRSSGG
SGAKGPSDEM WVTDSAQGTP HPGATEGNAA VGNAIFKRNG RSLWNVIADI ARLRWGSRAG
SPDSSAKPAG RSSPNESVSS ATWFSGREHD GSSDDNTKGD KVLPQEAPSL HQVEVGQTSP
RSQSEYPGTT KLKQRSERHE GVVSSPSSTI LEGGSVSNRM SSTSGNQIVG VDEEEGGNFE
FRLPETALTE VPMKLPSRNL IRSPPIKESS ESSLTEASSD QNFTVGEGRR YPRMDAGQNP
LLFPGRNLRS PAVMEPPVPR PRMVSGSSSL REQVEQQQPL SAKSQEETGS VSADSALIQR
KLQRNKQVVR DSFEEWEEAY KVEAERRTVD EIFMREALVE AKKAADTWEV PVGAVLVHDG
KIIARGYNLV EELRDSTAHA EMICIREGSK ALRSWRLADT TLYVTLEPCP MCAGAILQAR
VNTLVWGAPN KLLGADGSWI RLFPGGEGNG SEASEKPPPP VHPFHPKMTI RRGVLESECA
QTMQQFFQLR RKKKDKNSDP PTPTDHHHHH LPKLLNKMHQ VLPFFCL
