SYL1_RHIL3
ID SYL1_RHIL3 Reviewed; 838 AA.
AC Q1MFI6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Leucine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS 1 {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS1 {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=RL2798;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; AM236080; CAK08288.1; -; Genomic_DNA.
DR RefSeq; WP_011652325.1; NC_008380.1.
DR AlphaFoldDB; Q1MFI6; -.
DR SMR; Q1MFI6; -.
DR STRING; 216596.RL2798; -.
DR EnsemblBacteria; CAK08288; CAK08288; RL2798.
DR KEGG; rle:RL2798; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; DIDWADV; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000006575; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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 PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..838
FT /note="Leucine--tRNA ligase 1"
FT /id="PRO_0000334802"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 608..612
FT /note="'KMSKS' region"
FT BINDING 611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 838 AA; 94069 MW; 7C2AC9CEACE16F9F CRC64;
MPYDPTKIEP KWQAYWAGHH IFRVEIDPAR PKFYALDMFP YPSGAGLHVG HPLGYTATDI
MCRYKRMRGF NVLHPMGWDS FGLPAERHAM RTGVHPDITT KRNIETFRGQ VQRLGFSYDW
SREFATTDPA YVRWTQWIFL KLFENGLAYQ AEVAVNWCPA QNAVLADEEV KDGRYVETGD
PVIRRRMRQW MLRITAYADR LLQGLDGLDW PENLKAMQRN WIGRSEGAEI RFPLEHGKGV
ITVFTTRPET LFGASYILLA PEHPAVAAIV EPEMSEAVAA YIAEAEGLEE TVRADAGREK
TGVFTGAYAI NPANGARLPV WVADYVLAGY GTGALMAVPA HDARDYAFAH SHELPIIRVI
DSEADIEKGA YEGEGAMVNS GFLSGLGSPE ARSAIVAWLQ ANGTGWPKVM YRLRDWLFSR
QRYWGEPIPV LHLADGSVMP LPEECLPLLP PELDDYAPTP DGEPPLARAQ AWVETIVPGT
DIPARRETNT MPQWAGSCWY YLRFLDPENT SEPVGREAER YWMPVDLYVG GAEHAVLHLL
YARFWHKVLY DIGVVSTEEP FQRLFNQGMI LAHSYRDAAG RYYAPSSVVE EEGRWFAGSV
EVQRAVEKMS KSQLNVVNPD DVVHQFGADA LRLYEMFMGP LDAAKPWQTA GVIGVRRFLE
RAWRIVCDES DGLSPVVLEA APSPQLLRLR HQTVKTVTAD IEAIRFNTAV SRLMELANAL
TAEAARPREV VETFVLLLAP FAPHIAEELW SKLGHGETLT WVSWPTFDPA LIEMETREYV
VQINGKVRHR FEAAADLGEA LLAAARSEPS VMALLDGKTV VKEVLVPGRL VNFVVEDL
