ID A0A1Y0N2S6_9FLAO Unreviewed; 1119 AA.
AC A0A1Y0N2S6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=BTO07_13640 {ECO:0000313|EMBL:ARV16120.1};
OS Polaribacter sp. SA4-12.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1312072 {ECO:0000313|EMBL:ARV16120.1, ECO:0000313|Proteomes:UP000195470};
RN [1] {ECO:0000313|EMBL:ARV16120.1, ECO:0000313|Proteomes:UP000195470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-12 {ECO:0000313|EMBL:ARV16120.1,
RC ECO:0000313|Proteomes:UP000195470};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-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; CP019334; ARV16120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0N2S6; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000195470; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 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; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR007569; DUF559.
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; 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.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000195470}.
FT DOMAIN 38..143
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 312..407
FT /note="DUF559"
FT /evidence="ECO:0000259|Pfam:PF04480"
FT DOMAIN 422..584
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 970..1083
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 303..333
FT /evidence="ECO:0000256|SAM:Coils"
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 1119 AA; 127109 MW; 97827DC75190D551 CRC64;
MQYNHLDIEK KWQKFWAENQ TFKASNESEK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
YARYKRHKGF NVLHPQGYDS FGLPAEQYAI QTGQHPAKTT EENVATYRRQ LDNIGFSFDW
SREVRTSSPE YYKWTQWIFI QLFDSWYNKD TDKAEDVSTL IKIFKKEGNA TVNAVADEEI
TIFSADEWKA FSKVEQEEIL LQYRLTFLSD TEVNWCPALG TVLANDEIVN GVSERGSHPV
IRKKMTQWSM RISAYAQRLL DGLEKIDWPQ PLKDSQTNWI GRSQGAMVSF NVDNGAEKSS
SEVKLTYKEL EALKELRQNL SKAESRLWDE LKNKKGASKF RKKYTIGTFL VDYVCISKNI
IVEFSGKEDE AARTEFFNNE GFNVIRFTNE EVIENVLGVV SKINSAIQFP KAIEKTEKKE
VAVKEENQYK IDVFTTRPDT IYGVSFMTLA PEHELVSKIT TDAQKSEVEA YITATAKRSE
RDRMADVKTI SGAFTGAYAI HPFSGEKVQI WIGDYVLANY GTGAVMAVPC GDQRDYDFAK
HFGIPIPNIF EGVDISEAAH TGKDGTKIAN SDFLSGLKYK KALKLAIFEM EKRGFGYGKI
NYRLRDAVFS RQRYWGEPFP VYYKDGMPQM IDAEHLPIVL PEVEKYLPTE DGKPPLGNAT
EWAWDSRGKK VVSNDKLKNK TVYPLELNTM PGWAGSSWYF NRYMDATNSN EFASKESLEY
WKEVDLYIGG SEHATGHLLY ARFWQKFLFD KGIVPVDEFA KKLINQGMIL GTSAFVYKAT
PFVKNGCGCS DEKSNDDVIA KIPTVIVSKN LFNSDDEFET VVKNYLLDNK FLDPNFADLV
MITKTALHAD VSLVNASDEL DVDGFKNHAL NSDYKNAEFI LEDGVYKVGR EVEKMSKSKY
NVVNPDAICE EYGADSLRLF EMFLGPLEQA KPWKTSGISG VSSFLKKLWK LYFNGETFEV
SDAEPTKDEL KTLHKTIKKV EEDIENFSFN TSVSTFMIAV NELTALKCNK RAILEPLATL
VSPYAPHIAE ELWSLLGHKE SISTAGFPVF EASHLVESAK NYPISFNGKM RFTLELPLDL
SKEEIEKTVM ENEKTIAQLE GKSPKKVIIV PGKIINIVI
//
