SYL_FRAAA
ID SYL_FRAAA Reviewed; 1069 AA.
AC Q0RCJ1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=FRAAL6210;
OS Frankia alni (strain ACN14a).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CT573213; CAJ64833.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0RCJ1; -.
DR SMR; Q0RCJ1; -.
DR STRING; 326424.FRAAL6210; -.
DR KEGG; fal:FRAAL6210; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000657; 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; -; 3.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 2.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..1069
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334758"
FT REGION 19..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 107..118
FT /note="'HIGH' region"
FT MOTIF 838..842
FT /note="'KMSKS' region"
FT COMPBIAS 23..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 841
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 1069 AA; 116994 MW; 392D3E9F711BC099 CRC64;
MSQGRRTNEL GWHERMSETA EHGTGAANAT ASPSGAVPPS GATATAGTGD EPGFRYDARL
AADIERRWQR RWADEGTFNS PNPVGPLAAG FDEVAGREPF YIMDMFPYPS GTGLHVGHPL
GYIGTDVFAR YLRMSGRHVL HPFGYDAFGL PAEQYAINTG QHPRTTTDAN IANMRRQLSR
LGLGHDTRRE IATTDVGYYR WTQWIFEQIF DAWYDPQAGR ARPIAELIAE FEAGTRSPAA
GPAAGTTAVS VDAVRAANPT GLPWAELDRV TRRRVVDAHR LAYISEQLVN WCPGLGTVLA
NEEVTAEGRS DIGNYPVFRR PLRQWVLRIT AYAERLVDDL DLVDWSDSIK QMQRNWIGPS
DGAGVEFAVV PPSGSAGAAP GQRIEVYTTR PDTLAGATFL VLAPEHPQVD ALVADAWPAG
TPGAWRFPAG RGPAVGEAAE VAAEEVAAEE VGAAEVEAAA ADPAWTPRAA VEAYRAFAAR
RSDRQRGEEV DRTGVFTGAY VRNPVGGGLL PVFLADYVLV GYGTGAIMAV PAHDSRDFSF
ARAFDLPIPA VLAPDEQWYA EHRVTPGAPP SAWPEAFGGE GAYLPGPAGT PVLAGLTKPD
AIKTTVRWLE DGGHGRLARS YRLRDWLFSR QRYWGEPFPI VFDDDGLPYA VPDELLPVEL
PEMTDFRPTA MAEDDESDPV PPLARVADWA SVTLDLGDGP KRYRRETNTM PQWAGSCWYH
LRYLDPTNTE RFVDETVERY WLAKPGAAAG DGGVDLYVGG VEHAVLHLLY ARFWQKVLYD
LGHVSSKEPF KRLFNQGYIQ ADAFTDARGM YVPAAEVKQT DDGRFTHHGA PVDRRSGKMG
KSLKNSVSPD EMYERFGADT LRVYEMAMGP LDADRPWHTD DIVGSHRFLQ RLWRAVVDEG
SGTVAVSDEQ LDAEATRVLH RTIITLAAEY AGLRFNTAVA RLIELTNYVS KRYGQAATPR
ALAEPLVLMV APLAPHIAEE LWTRLGHSES VSRAAFPVGD PALAAESERT IPVQVNGKVR
FTLQVPDGAA EPVIRELLTA HPDYARQTEG RTIKKTIIVP GRIVNIALG
