ID A0A139CVD0_9EURY Unreviewed; 962 AA.
AC A0A139CVD0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=AWU59_26 {ECO:0000313|EMBL:KXS45162.1};
OS Methanolobus sp. T82-4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=1794908 {ECO:0000313|EMBL:KXS45162.1, ECO:0000313|Proteomes:UP000074030};
RN [1] {ECO:0000313|EMBL:KXS45162.1, ECO:0000313|Proteomes:UP000074030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T82-4 {ECO:0000313|EMBL:KXS45162.1};
RA Wolfe R., Daly R., Wrighton K.;
RT "Methanolobus T82 Annotated.";
RL Submitted (FEB-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|HAMAP-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|HAMAP-Rule:MF_00049, 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:KXS45162.1}.
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DR EMBL; LSRV01000001; KXS45162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139CVD0; -.
DR STRING; 1794908.AWU59_26; -.
DR PATRIC; fig|1794908.3.peg.105; -.
DR Proteomes; UP000074030; 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; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR020791; Leu-tRNA-lgase_arc.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
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}; 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 13..670
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 709..837
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 631..635
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 962 AA; 110280 MW; CDAC66A750FE2ECE CRC64;
MEQDYNPHAI EKKWQNRWNE SRVFEPEPDE REKFFITIPY PYLNGNLHAG HTRTFTIGDV
VARHRRMLGY NVLYPMGFHV TGTPIVGLAE LIANRDPQTM DVYSRLHKIP ENILPSLDTP
EKIVDYFSVE AEIAMRSIGY SIDWRRKFTT TDHTYKKFIE WQFNLLHDKG LIVKGSHPVK
WCPNDNNPVE DHDILHGEEA TIVDYTFIKF EYDGMILPCA TLRPETIFGV TNLWVNPDIE
HVKVKVKQDG KEEFWVVSRE AYNKLTYTDR EVELVENVPS ESIIGIKVKN PLTGKEIITL
PASFVKGGNG SGIVMSVPAH APYDYLAVKD LYDRDLSEYG ITENIRDIEF ISLIEVKDFG
EYPAIDAVEQ LGVEDQKDPK AEEATKLVYR REFHGGVLKE NTGEYAGIAV SKIKDVLTRD
LLDKGIGEIF YEFSEPVVCR CGTPCVVNMV KGQWFLNYSN PEWKDKVYRC IENMEIIPEE
IRVEFNNKVD WLKDKACARK KGLGTRLPFD TDWLIESLGD STIYMSYYIT NKFFSNGILP
EQLKPSLFDY VLLGKGTVQQ VAKDTGLDEP LIANMKSDFD YWYPVDLRSS GKDLVPNHLL
FFLFHHVAIF DEDRWPRALA VNGFVSLEGQ KMSKSKGPIL TLKEAVDTYG ADVSRMYILS
SAEQTQDADW RNAGVESAKK QMERFYKLAR EIIDSGASSG IDGELQLIDR WMLSRLQQFV
RDTNNDMTSI RTRGALQNSF FLLYNDVKWY QRRGGSAVLY DVLDTWVRLM APFTPHICEE
IWSAMGHGAG DYASLAPYPI FNPEYVDNDA ELAEELIGNT LSDIEEIIKV TKLTPKKAVL
YTAPSWKTEA FKLALKMLHE EDLNPGKLIK TLMSDPENRK YGKEIPKYVQ KLVPDIKSMK
TERLEKLLGF DLDEQSILKE NDRCLENEIG CPVEVYTADD PAYDPENKAR FAAPLRPAIY
LE
//
