ID R0IAV3_9BRAS Unreviewed; 1095 AA.
AC R0IAV3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN ORFNames=CARUB_v10008148mg {ECO:0000313|EMBL:EOA39529.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA39529.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; KB870805; EOA39529.1; -; Genomic_DNA.
DR RefSeq; XP_006306631.1; XM_006306569.1.
DR AlphaFoldDB; R0IAV3; -.
DR STRING; 81985.R0IAV3; -.
DR GeneID; 17900228; -.
DR KEGG; crb:17900228; -.
DR eggNOG; KOG0437; Eukaryota.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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 NCBIfam; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT DOMAIN 21..103
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 192..754
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 794..924
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1095 AA; 123799 MW; 1D8E6603753C7923 CRC64;
MASDSKSYAR RDRLLEIEVA VQKWWEDEQV FKAESRENLP KPGEKFFSTF PFPYMNGYLH
IGHAFSLSKV DFASAYHRLR GANVLLPFGF HCTGMPIKAS ADKLSREIQQ FGNPPVFTAD
DTKTNQAPQV LEESSDTPAL PGQFKGKKSK VAAKSGGQVY QWEIMRSFGL TDSEIAEFQD
PYKWLYYFPP LAMEDLKAYG LGCDWRRSFV TTDVNPFYDA FVRWQMRKLK SMGKVVKDRR
YTIFSPLDGQ PCADHDRATG EGVQPQEYTL IKMEVVKPFP LKLGPLEGKR VYLAAATLRP
ETMYGQTNAW VLPDGKYGAY EINETDVFIL TERAALNLAY QNFSKIHQKP SCLVELTGYD
LIGLPLRSPL AVNDIIYALP MMTILTNKGT GIVTSVPSDA PDDYMALKDL NGKPAFREKY
GVKQEWLPSE IIPIINIPEF GDKAAERVCL DLKIASQNDK DKLVEAKRLT YLKGFTEGTM
LIGEFVGRRV QDIKPIIKTK LIETGEAIIY SEPEKPVMSR SGDECVVALT DQWYITYGEP
EWRKMAEECL SKMNLYSDET RHGFEHTLSW LNQWACSRSF GLGTRIPWDE QFLVESLSDS
SLYMAYYTVS HFFHGGGDMY KGSKSLISPQ QMNDDVWEYL FCDGPYPKSS DISSAVLSKM
KQEFDYWYPL DLRVSGKDLI QNHLTFFIYN HTALMANRNW PRGIRCNGHI MLNSEKMSKS
TGNFRTLRQA IEEFSATATR FSLADAGDGV DDANFVFETA NAAILRLTKE LTWMEEVLAA
ESSLRTGPPS TYADKVFEND MNIAIRLTEK AYKDCLFREA LKNGFYDLQA ARDEYRLSCG
SGGMNHDLIL TFMDVQTRLI EPICPQFAEY VWRKLLKKEG CVVTAGWPTS SEPDLVLKSA
NKYLQDSIVL MRKLLQKQLV GSKKGSKKGA QVTAVPEGKL KGLVYVNEQF DGWRAHCLRI
LQSNFDQQTC RFAPDAETLA ELREILEKEG QKPETFKKIQ MICMPFLKFK KDEAISIGIQ
ALNLRLPFGE MDVLKSNMDL IKRQLGLEEV EIYSASNTDD VSKAGPLASV LTQTPPSPGS
PTAIFVTSTS VCPPA
//
