SYIM_ARATH
ID SYIM_ARATH Reviewed; 1093 AA.
AC Q8RXK8; B9DF95; F4K4Q4; Q9FI67;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Isoleucine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.5 {ECO:0000305};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000305};
DE Short=IleRS {ECO:0000305};
DE AltName: Full=Protein OVULE ABORTION 2 {ECO:0000303|PubMed:16297076};
DE Flags: Precursor;
GN Name=OVA2 {ECO:0000303|PubMed:16297076};
GN OrderedLocusNames=At5g49030 {ECO:0000312|Araport:AT5G49030};
GN ORFNames=K19E20.18 {ECO:0000312|EMBL:BAB10327.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP 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 [6]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC ChEBI:CHEBI:456215; EC=6.1.1.5; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16251277}. Mitochondrion
CC {ECO:0000269|PubMed:16251277}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RXK8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RXK8-2; Sequence=VSP_057806, VSP_057807;
CC -!- DISRUPTION PHENOTYPE: Lethal. In heterozygous plants, aborted ovules.
CC {ECO:0000269|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10327.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB017061; BAB10327.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95762.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95763.1; -; Genomic_DNA.
DR EMBL; AY080830; AAL87306.1; -; mRNA.
DR EMBL; AY142605; AAN13174.1; -; mRNA.
DR EMBL; AK316685; BAH19412.1; -; mRNA.
DR RefSeq; NP_001032042.1; NM_001036965.2. [Q8RXK8-2]
DR RefSeq; NP_199714.2; NM_124280.4. [Q8RXK8-1]
DR AlphaFoldDB; Q8RXK8; -.
DR SMR; Q8RXK8; -.
DR STRING; 3702.AT5G49030.3; -.
DR iPTMnet; Q8RXK8; -.
DR PaxDb; Q8RXK8; -.
DR PRIDE; Q8RXK8; -.
DR ProMEX; Q8RXK8; -.
DR ProteomicsDB; 234106; -. [Q8RXK8-1]
DR EnsemblPlants; AT5G49030.1; AT5G49030.1; AT5G49030. [Q8RXK8-1]
DR EnsemblPlants; AT5G49030.2; AT5G49030.2; AT5G49030. [Q8RXK8-2]
DR GeneID; 834962; -.
DR Gramene; AT5G49030.1; AT5G49030.1; AT5G49030. [Q8RXK8-1]
DR Gramene; AT5G49030.2; AT5G49030.2; AT5G49030. [Q8RXK8-2]
DR KEGG; ath:AT5G49030; -.
DR Araport; AT5G49030; -.
DR TAIR; locus:2154349; AT5G49030.
DR eggNOG; KOG0433; Eukaryota.
DR OMA; HLGTAWN; -.
DR PhylomeDB; Q8RXK8; -.
DR PRO; PR:Q8RXK8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RXK8; baseline and differential.
DR Genevisible; Q8RXK8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast;
KW Ligase; Metal-binding; Mitochondrion; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..1093
FT /note="Isoleucine--tRNA ligase,
FT chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433537"
FT REGION 69..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..165
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 723..727
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT COMPBIAS 89..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 682
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000250|UniProtKB:P41972"
FT BINDING 726
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1050
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P41972"
FT BINDING 1053
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P41972"
FT BINDING 1070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P41972"
FT BINDING 1073
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P41972"
FT VAR_SEQ 951..955
FT /note="LRTEV -> VSKLS (in isoform 2)"
FT /id="VSP_057806"
FT VAR_SEQ 956..1093
FT /note="Missing (in isoform 2)"
FT /id="VSP_057807"
FT CONFLICT 223
FT /note="K -> M (in Ref. 4; BAH19412)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="P -> T (in Ref. 4; BAH19412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1093 AA; 123008 MW; A92A637F087812B6 CRC64;
MSSFFKSFAG NPREAAAMAM VQSSSYRVLS GKSCSNLRRN TPLDSFLAKG RSSVKAFSFL
YVSRFSTEPN NEFGHSSKRR SRGPVMAAKK ASEGEKQEDG KYKQTVDLPK TGFGMRANSL
TREPELQKLW EENQVFKRVS DNNNGGSFIL HDGPPYANGD LHMGHALNKI LKDIINRYKL
LQNYKVQYVP GWDCHGLPIE LKVLQSLDQE VRKELTPLKL RAKAAKFAKA TVKTQMESFK
RFGVWADWNN PYLTLDPEYE AAQIEVFGQM ALKGYIYRGR KPVHWSPSSR TALAEAELEY
PEGHISKSIY AIFKLVGGAK TSLLDEFIPN IYLAVWTTTP WTMPANAAVA VNAKLQYSVV
EVQSFSEDES TVTSNKKKIP GKVLKNQQKL FVIVATDLVP ALEAKWGVKL SISKTFLGSD
LENCRYTHPI DNRDCPVVIG GDYITTESGT GLVHTAPGHG QEDYATGLKY GLPLVSPVDD
EGKFTEEAGQ FRGLSVLGEG NTAVVSYLDE NMSLVMEESY AHKYPYDWRT KKPTIFRATE
QWFASVEGFR TATMDAINNV KWVPHQAVNR ISAMTSSRSD WCISRQRTWG VPIPAFYHVK
TKEPLMNEET INHVKSIISQ KGSDAWWYMS VEDLLPEKYR DKAADYEKGT DTMDVWFDSG
SSWAGVLGKR EGLSFPADVY LEGTDQHRGW FQSSLLTSIA TQGKAPYSAV ITHGFVLDEK
GMKMSKSLGN VVDPRLVIEG GKNSKDAPAY GADVMRLWVS SVDYTGDVLI GPQILRQMSD
IYRKLRGTLR YLLGNLHDWR VDNAVPYQDL PIIDQHALFQ LENVVKNIQE CYENYQFFKI
FQIIQRFTIV DLSNFYFDIA KDRLYTGGTS SFTRRSCQTV LSTHLLSILR VIAPIVPHLA
EDVWQNLPFE YRNEDGSAAE FVFELKWPTL NEQWLSFPAE DVLFWQRLLE LRTEVNKVLE
LARNEKMIGS SLEAKVYLHT ADAGMAAKLL EMSEAKNEAD TLQRIFITSQ VEVLSSMEKE
MISSVQHTGE YVEGENKVWI GVSRAEGSKC ERCWNYSGQV GSFSDHPTLC GRCFSVIVAN
PPEPAVAAVN SLA
