ID U2V7S8_9FUSO Unreviewed; 892 AA.
AC U2V7S8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=HMPREF9108_01028 {ECO:0000313|EMBL:ERL26393.1};
OS Leptotrichia sp. oral taxon 225 str. F0581.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321774 {ECO:0000313|EMBL:ERL26393.1, ECO:0000313|Proteomes:UP000016631};
RN [1] {ECO:0000313|EMBL:ERL26393.1, ECO:0000313|Proteomes:UP000016631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0581 {ECO:0000313|EMBL:ERL26393.1,
RC ECO:0000313|Proteomes:UP000016631};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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: 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:ERL26393.1}.
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DR EMBL; AWVS01000065; ERL26393.1; -; Genomic_DNA.
DR AlphaFoldDB; U2V7S8; -.
DR PATRIC; fig|1321774.3.peg.980; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_0; -.
DR Proteomes; UP000016631; 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 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 40..177
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 224..429
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 442..596
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 634..675
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 722..854
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 636..640
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 892 AA; 103022 MW; 23C18C979202DEA5 CRC64;
MIKEYKPSEI EKKWQDKWFE EDVFKSENKI EGKENYYVLE MFAYPSGKLH VGHLRNYAIG
DAIARYKKMK GFNVLHPFGW DSFGLPAENA AIDNGAHPGK WTKANIDNMR RQMKLMGLSY
DWNRELSTYT PEYYKWNQKF FIEMYKKGLV YKKKSYVNWC PDCNTVLANE QVEGGKCWRH
GKTDVIQKEL SQWYFKITEY AEELLQGHEE LRGHWPEQVL TMQKNWIGKS TGSEVDFILD
YKFENDGNSH LKLNDNGEVV ISVFTTRPDT LYGVTYATVA PEHPLVEEII LKENPSIREA
VERMINEDKI ARTAEDKEKE GVFSGLYVIN PVNGEKVQLW IANYVLMDYG TGAVMAVPAH
DERDFQFSKK YNLDLKIVVN PVDKNGNLEE VSVEKMENAL VNSGVLVNSE EFNGLNSNEA
KEKITEKLEK IGLGKKTVNY RLHDWLISRQ RYWGTPIPVI YDEDGNIYLE EEVNLPVKLP
TDIEFSGKGN PLETSEEFKN VILPNGKKGR RETDTMDTFV DSSWYYLRYL DSHNDKEPFK
KEDADNWTPV HQYIGGIEHA VMHLLYARFF HKSLRDLGYV DTNEPFKRLL TQGMVLGPSY
YSQNERRYLF PREVEMKDGK PVSKETEEEL ATKVEKMSKS KNNGVDPEEI VKEYGADSSR
VFTLFAAPPE KELEWNMNGL AGAYRFINRL YLLISSTADF AYKNATKEDN YGINLDARSE
KDKEIQKKLH QTVKKVTDSI EDDFHFNTAI AAIMELLNDM TTYKQNVIDK NDISSESKKV
WHEVLEKVIL LIAPFAPHVA DELWSDLGNT TLTFEQEWPT FDEKLTVENN FNLVLQVNGK
VRDMVPAQIG ISKDDAEKLA FSSEKVQKFV DGKEVIKVIV VPNKLVNIVI KG
//
