ID A0A0R2X035_9FLAO Unreviewed; 1124 AA.
AC A0A0R2X035;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=ABS28_05380 {ECO:0000313|EMBL:KRP29311.1};
OS Cryomorphaceae bacterium BACL22 MAG-120619-bin32.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655630 {ECO:0000313|EMBL:KRP29311.1, ECO:0000313|Proteomes:UP000052139};
RN [1] {ECO:0000313|EMBL:KRP29311.1, ECO:0000313|Proteomes:UP000052139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL3 MAG-120619-bin32 {ECO:0000313|EMBL:KRP29311.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRP29311.1}.
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DR EMBL; LIDG01000059; KRP29311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2X035; -.
DR Proteomes; UP000052139; 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 CDD; cd01038; Endonuclease_DUF559; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR Gene3D; 3.40.960.10; VSR Endonuclease; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR007569; DUF559.
DR InterPro; IPR047216; Endonuclease_DUF559_bact.
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; IPR011335; Restrct_endonuc-II-like.
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:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF04480; DUF559; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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}; Cytoplasm {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 44..150
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 323..426
FT /note="DUF559"
FT /evidence="ECO:0000259|Pfam:PF04480"
FT DOMAIN 438..600
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 891..920
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 974..1088
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 894..898
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 897
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 1124 AA; 128116 MW; 9875BE8EEE8D944B CRC64;
MQYNHKDIEE YWQKYWAENK TFKSKNPPPL GELEGAPKYY VLDMFPYPSG SGLHVGHPLG
YIASDIYARY KRHKGFNVLH PQGYDSFGLP AEQYAIQTGQ HPAQTTEENI KTYRKQLDKI
GFSFDWDREV RTSNPEYYKW TQWIFIQLFN SWYNKDSNKA EDISTLISLF EKQGNAKINA
VCDENILSFS AEEWHQFSDS KKQAVLLQYR LTFLSDTEVN WCPALGTVLA NDEIINGVSE
RGGHPVIRKK MTQWSMRISA YAQRLLDGLS TIDWPQPLKD SQTNWIGRSQ GAMVEFPILS
FPKGEENTSK GYLTGGNNAH LLQEKAKEMR ANPTQAEAIL WQQLRGKGLG YKFRQQHLID
DFIADFVCLS KKLIIEVDGK IHDFQQEKYA ERTQILENLG YKVIRFTNEE VIGNLDKVLE
TIKLNLDQAP LSFGKGLGDR ISVFTTRPDT IFGVSFMTLA PEHELVSKIT TDEQKAAVKN
YIEVTAKRSE RERMADVKTV SGVFTGGYAE HPFTKKPIPI WIGDYVLAGY GTGAVMAVPC
GDQRDYNFAK QFGIEIPNIF ENLDISEAAH ADKEGTVIAN SDFLSGLSYK KALQKAIESL
EENGFGYGKV NYRLRDAVFS RQRYWGEPFP VYYKDGMPQM IDEKYVPIVL PEVEKYLPTE
DGKPPLGNAE VWAWCTKTNS IVDNSKIDNT TVFSLELNTM PGWAGSSWYF NRYMDAKNPT
EFASKEALNY WKEVDLYIGG SEHATGHLLY ARFWQKFLFD RGFVPVEEFA KKLINQGMIL
GESAFVYSWN YNNLDNPPNK KTIFISKNII QKSISEKSIL VNGNKDIDDL SFGIKILISN
TEWSHFNPIH VDVSLVNSSD ELDIEGFKNW RPEYKDAEFI LENGVYKVGR EVEKMSKSKY
NVVNPDDIVA EYGADALRLF EMFLGPLEQT KPWKTSGISG VYSFLKKLWK LYHSGENGTF
YVDNSPLLEG LGEALKVLHK TIKKVEEDIE NFSFNTSVST FMIAVNELTA LQCNKSSILE
PLLILLSPYA PHITEELWSK LGHTTSISTA EFPKFEPKYL VESTKIYPIS FNGKMRFTIE
LSLDLSKEEI EKEVMSNEKT IAQLEGKTPK NVIIVPGKIV NIVG
//
