SYYC2_ARATH
ID SYYC2_ARATH Reviewed; 748 AA.
AC F4HWL4; Q9SGN2;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Tyrosine--tRNA ligase 2, cytoplasmic {ECO:0000305};
DE EC=6.1.1.1 {ECO:0000305};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000305};
DE Short=TyrRS {ECO:0000305};
GN OrderedLocusNames=At1g28350 {ECO:0000312|Araport:AT1G28350};
GN ORFNames=F3M18.22 {ECO:0000312|EMBL:AAF16759.1};
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 SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA Berg M., Rogers R., Muralla R., Meinke D.;
RT "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT development in Arabidopsis.";
RL Plant J. 44:866-878(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr).
CC {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277,
CC ECO:0000305|PubMed:16297076}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF16759.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010155; AAF16759.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30961.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58265.1; -; Genomic_DNA.
DR PIR; A86410; A86410.
DR RefSeq; NP_001319097.1; NM_001332810.1.
DR RefSeq; NP_174157.4; NM_102601.6.
DR AlphaFoldDB; F4HWL4; -.
DR SMR; F4HWL4; -.
DR STRING; 3702.AT1G28350.1; -.
DR iPTMnet; F4HWL4; -.
DR PaxDb; F4HWL4; -.
DR PRIDE; F4HWL4; -.
DR ProteomicsDB; 245301; -.
DR EnsemblPlants; AT1G28350.1; AT1G28350.1; AT1G28350.
DR EnsemblPlants; AT1G28350.2; AT1G28350.2; AT1G28350.
DR GeneID; 839731; -.
DR Gramene; AT1G28350.1; AT1G28350.1; AT1G28350.
DR Gramene; AT1G28350.2; AT1G28350.2; AT1G28350.
DR KEGG; ath:AT1G28350; -.
DR Araport; AT1G28350; -.
DR TAIR; locus:2032164; AT1G28350.
DR eggNOG; KOG2144; Eukaryota.
DR HOGENOM; CLU_010604_0_0_1; -.
DR InParanoid; F4HWL4; -.
DR OMA; CIHDDEL; -.
DR OrthoDB; 852081at2759; -.
DR PRO; PR:F4HWL4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HWL4; baseline and differential.
DR Genevisible; F4HWL4; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 3.40.50.620; -; 4.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00579; tRNA-synt_1b; 2.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..748
FT /note="Tyrosine--tRNA ligase 2, cytoplasmic"
FT /id="PRO_0000433554"
FT MOTIF 441..449
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 623..627
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 564
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 568
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 571
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 586
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:P54577"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 748 AA; 84717 MW; 14FEEFFFFF8B2D82 CRC64;
MEALSINAPT QASTLPSGLQ ISKEVEKRYN VVRSVGEQCI HDDELKDLLA KKAAPVCYDG
FEPSGRMHIA QGLMKIMNVN KLTSAGCRVK IWIADWFAYM NNKLGGDLKK IRVVGEYFKE
IFQAAGMNSE NVEFLWSSDE INAKGDEYWP LVMDIACRNS LAQIKRCMPI MGLSENEELS
AAHILYVCMQ CADTFFLEAD ICQLGMDQQT VNLLARDYCD VVKRENKPVI LSHHMLPGLQ
QGQKKMSKSD PSSAIFMEDE EAEVNVKIKK AYCPPDIVEG NPCLEYVKHI ILPWFSEFTV
ERDEKYGGNR TFKSFEDITT DYESGQLHPK DLKDALSKAL NKILQPVRDH FKTNSRAKNL
LKQVKGYKVT RVIPTASSTK EEDLSINTSA SSSAAGLQMS EEAEMKYKIV RSIGEECIQE
DELKNLLAKK PAPICYDGFE PSGRMHIAQG VMKVTNVNKL TSAGCQVKIW IADWFAQLNN
KLGGDLERIR VVGEYFKEIW QAGGMNNDKV EFLWASDEIN GKGSKYWPLV MDIARRNNLR
RILRCGQIMG RSETEVLSAA QILYPCMQCA DIFLLEADIC QLGMDQRKVN MLAREYCADI
KRKNKPIILS HHMLPGLQQG QEKMSKSDPS SAIFMEDEEA DVNEKISKAY CPPKTVEGNP
CLEYVKYIVL PRFNEFKVES EKNGGNKTFN SFEDIVADYE TGELHPEDLK KALMKALNIT
LQPVRDHFKT NERAKNLLEQ VKAFRVTR
