ID A0A1Z5HDF0_9GAMM Unreviewed; 814 AA.
AC A0A1Z5HDF0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=bplSymb_SCF09401P003 {ECO:0000313|EMBL:GAW87496.1};
OS Bathymodiolus platifrons methanotrophic gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=113268 {ECO:0000313|EMBL:GAW87496.1, ECO:0000313|Proteomes:UP000196430};
RN [1] {ECO:0000313|EMBL:GAW87496.1, ECO:0000313|Proteomes:UP000196430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPD1508-B01-01 {ECO:0000313|EMBL:GAW87496.1,
RC ECO:0000313|Proteomes:UP000196430};
RX PubMed=28453654; DOI=10.1093/gbe/evx082;
RA Takishita K., Takaki Y., Chikaraishi Y., Ikuta T., Ozawa G., Yoshida T.,
RA Ohkouchi N., Fujikura K.;
RT "Genomic Evidence that Methanotrophic Endosymbionts Likely Provide Deep-Sea
RT Bathymodiolus Mussels with a Sterol Intermediate in Cholesterol
RT Biosynthesis.";
RL Genome Biol. Evol. 9:1148-1160(2017).
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:GAW87496.1}.
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DR EMBL; BDMN01000353; GAW87496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5HDF0; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000196430; 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; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000196430}.
FT DOMAIN 39..184
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..403
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 416..613
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 655..777
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 574..578
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 814 AA; 92300 MW; 3B862F91CD7C42A4 CRC64;
MQENYKPLEI ESEVQAQWEQ SGIFQASDDE SKEKYYCLSM FPYPSGRLHM GHVRNYTIGD
VISRYQRMQG KNVMQPMGWD AFGLPAENAA MKHNVHPAEW TYENIDYMRD QLKQLGFGYD
WSRELATCDP DYYRWEQWFF LQLLDKDLVY KKTSAVNWCP HDQTVLANEQ VIDGCCWRCD
TAVEKKDISQ WFLRITAYAD ELLTSLDKMP GWPEQVKTMQ ANWIGRSEGL EMSFAVDGFD
DVEIYTTRPD TLMGVTYLAV AAEHPLALKA AQDNTEIADF LEECRHTETS EAALDTMEKK
GIDSGFQAKH PVSGELVPVW IANFVLMSYG TGAVMSVPAH DQRDYEFAKK YGIAIKQVIF
SASDSDDSIV EQAFTEKGKL QNSAEFDGLS SAEAVSAIAD KLESQSKGQR KTNFRLHDWG
VSRQRYWGAP IPIIYCDDCG TVPVPESDLP VELPKDVVLD GSNSPLVTHK AFLHVDCPKC
GKGAKRETDT FDTFMESSWY FARFASSKAD SMLDESAKYW LPVDQYIGGI EHAILHLLYA
RFFTKLMRDE GLLVCDEPFK DLLTQGMVLM DGTKMSKSKG NTVDPQGLIA EYGADTVRLF
IMFAAPPEQS LEWSDSGVEG SFRFLKRLWR QVYLHVDAGH SVPLLDKQNL TNVEKELRRH
VHHAIEKVTD DIGRRHHFNT AIATNMELLN TFTKFNAQSD NATAIRQEAL EMIVLMLYPI
VPHICQELWV GLGKEQDINR TWPELDKSAL VQDELQMVVQ VNGKVRGKIM VASDASKEDI
EAQALAEESV IRFLDGKAVK KLIVVPKKLV SIVV
//
