ID A0A256CIZ4_9GAMM Unreviewed; 861 AA.
AC A0A256CIZ4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B9T19_08430 {ECO:0000313|EMBL:OYQ78083.1};
OS Ignatzschineria sp. F8392.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Ignatzschineria.
OX NCBI_TaxID=1980117 {ECO:0000313|EMBL:OYQ78083.1, ECO:0000313|Proteomes:UP000215803};
RN [1] {ECO:0000313|EMBL:OYQ78083.1, ECO:0000313|Proteomes:UP000215803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8392 {ECO:0000313|EMBL:OYQ78083.1,
RC ECO:0000313|Proteomes:UP000215803};
RA Gulvik C.A.;
RT "Wohlfahrtiimonas and Ignatzschineria genomes.";
RL Submitted (APR-2017) 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:RU363035}.
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:OYQ78083.1}.
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DR EMBL; NEFF01000005; OYQ78083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256CIZ4; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000215803; 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; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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 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; PF00133; tRNA-synt_1; 2.
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 39..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..402
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 417..576
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 622..662
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 705..825
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 623..627
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 861 AA; 97613 MW; 0CE9C2BA8EBEB041 CRC64;
MKPTYEAAVI EASAQEFWEK NASFKVEDKT DKPNYYCLSM FPYPSGRLHM GHVRNYTIGD
VITRYKKMSG YNVMQPIGWD AFGMPAENAA IDNKVSPNDW TQKNIVYMRK QFRELGFGFD
WSREFSTCDP EYYGWEQWFF LQLYKKGVIY RKKGIVNWDP VDQTVLANEQ VIDGRGWRSD
ALVERREIPM YYFKITDYAD ELLEDLALLE EWPEQVRTMQ ANWIGRSEGM EVTFLHEGGQ
FNVFTTRPDT LMGVTYVAVA PEHPIAAKAA EKNPQLAEFI KECQKTGTSE ADFATQEAKG
MPTGEFATHP LTGEKVEIWV ANYVLMAYGD GAVMAVPAHD ARDFAFAKKY NLPIKVVIKP
ENGDISTDTW HESLAEHGTL INSGEFDGLN FEEAFSKIGT ALESKGLGKP KTQYRLRDWG
ISRQRYWGCP IPIINCPSCG EVPVPEKDLP VVLPTDCIPD GSGNPLNKLD SFKNVACPKC
GGAAERETDT MDTFVESSWY YARFACSNYE KGMIDPEAAT AWLPVDQYIG GVEHAILHLL
YSRFFHKLMR NEGLLGDIEK VGPEPFKALL TQGMVVSPSF FRHSSKGYEW FNIKDVEVRE
NNGEKEYFLK ADGEPVTYYG IQKMGKSKNN GVDPEAIVKE YGADVSRLFM MFTSPPEQTL
EWSASGLEGA DRFLRRVWNF AYENQAILKD LTLSCEALTE KNAKDARREI HQELKKALYD
YERFHFNTVI SANMIMLNIL SKLGDSRDEA AVKQEGFSIM LRLLSPIVPH ITHTIWETLF
GDDILNHPLP EVVAEALVSD EVKYMVQVNG RLRGEIIVPA SASKEEIEKA ALANENAAKF
IEGEIRRIIV VPNRLVNIVA N
//
