ID A0A1G7VTJ1_9SPHI Unreviewed; 934 AA.
AC A0A1G7VTJ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN ORFNames=SAMN05192573_104174 {ECO:0000313|EMBL:SDG62997.1};
OS Mucilaginibacter gossypii.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=551996 {ECO:0000313|EMBL:SDG62997.1, ECO:0000313|Proteomes:UP000199705};
RN [1] {ECO:0000313|EMBL:SDG62997.1, ECO:0000313|Proteomes:UP000199705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gh-67 {ECO:0000313|EMBL:SDG62997.1,
RC ECO:0000313|Proteomes:UP000199705};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; FNCG01000004; SDG62997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7VTJ1; -.
DR STRING; 551996.SAMN05192573_104174; -.
DR Proteomes; UP000199705; Unassembled WGS sequence.
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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
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|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 38..155
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 277..465
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 784..898
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 707..711
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 710
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 934 AA; 106788 MW; 99E462F46D022934 CRC64;
MDYQFKEIEQ KWQQFWAQNQ TFKAEDKSSK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
FARYKRLKGF NVLHPMGYDS FGLPAEQYAI QTGQHPAITT EDNIATYRRQ LDQIGFSFDW
SREVRTSSPD YYKWTQWIFM QLFNSWYNKD ADKAQSIDQL VAHFETKGSA GINAVCDDEI
LSFTADEWKA FSNQQQQDEL LKYRLTYLRE STVNWCPALG TVLANDEVKD GFSERGGYPV
EQKKMTQWSM RITAYAERLL QGLDTIDWPE PLKEMQRNWI GKSTGASVKF PIDKSGHNAA
LGTDFIEVFT TRVDTIFGVT FLVIAPEHEL VSALTTPEQK AEIEAYITQT KKKSELDRMA
DAKTVSGAFT GSYVLNPLNG QQIPIWIADY VLAGYGTGAV MAVPSGDQRD YLFAKHFNLP
VVQILDIQNI ETEADPTKEG TYINSDFING LAYKEATAAV VAKLEEINAG KAKVNFRMRD
AIFGRQRYWG EPVPVYFKEG LPHLINESHL PLLLPEIDKY LPTETGEPPL GRAEDWKYEG
GLPYELSTMP GWAGSSWYWY RYMDAKNDKE FASREAIEYW KDVDLYIGGS EHATGHLLYS
RFWNKFLKDL DLVVEEEPFK KLINQGMIQG RSNFVYRLID EEGRGTNTLV SHGLIKQYKT
SPLHVDVNIV ENEILNIEKF KQWRPEFTDA EFVLEGGKYI CGVEVEKMSK SKFNVVNPDD
IISRFGADTL RMYEMFLGPL EQSKPWNTNG IEGVFKFLRK FWRLFHNDAW EFGVNNAAPS
KAELKSLHKI IKKVEEDIER FSFNTSVSSF MIAVNELTDL KCNNRAILQD MVIILSPYAP
HICEELWSLL GNADGTLSYA PFPKFNAEYL VEDEFAYPIS INGKMKMNLS ISLSLDVKEI
EAFVLANADV QKYLDGKTPK KLIVVKGRIV NMVV
//
