ID A0A0M0BWS0_9ARCH Unreviewed; 960 AA.
AC A0A0M0BWS0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=AC479_06300 {ECO:0000313|EMBL:KON32899.1};
OS miscellaneous Crenarchaeota group-6 archaeon AD8-1.
OC Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia.
OX NCBI_TaxID=1685126 {ECO:0000313|EMBL:KON32899.1, ECO:0000313|Proteomes:UP000037259};
RN [1] {ECO:0000313|EMBL:KON32899.1, ECO:0000313|Proteomes:UP000037259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD8-1 {ECO:0000313|EMBL:KON32899.1};
RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA Teske A.P.;
RT "New insights into the roles of widespread benthic archaea in carbon and
RT nitrogen cycling.";
RL Submitted (JUN-2015) 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|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:KON32899.1}.
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DR EMBL; LFWW01000038; KON32899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0BWS0; -.
DR STRING; 1685126.AC479_06300; -.
DR PATRIC; fig|1685126.3.peg.1710; -.
DR Proteomes; UP000037259; 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 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; 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; 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 Pfam; PF09334; tRNA-synt_1g; 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 11..507
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 590..675
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 704..832
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 39..49
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 630..634
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 960 AA; 112219 MW; 52DA1A123B0BB8EA CRC64;
MSHIKQIEEK WRKKWDKAKI FQANPKNGKK KIFVTFPYPY MNGPLHVGHT FTASRVDVYA
RFKRMQGYNV LWPWAWHWTG QPLLGASQRV AKGDKEYIRV LRDIDGVPAE ELKKFVDPLY
MAQYYTNEGR LVAKRIGFSI DWRREFTTVM PAYQKFIEWQ YNNLKKEGYV TKGTHPVVWC
PKDNSPTGDH DRQIGEGVTP EEYTLIKYRL DDERFLPAAT FRPETIYGVT NIWINPDAKY
VEALVDKEIW IISKEAAMKL KEQEKEIHVR RTFKGKEIIG QKFENPLSKK KYFILPGWFV
DSNQGTGVVY SVPAHAPFDW LALKDLQAKP EFIKKYNLNI DQIQKIKPIS IIATEGENAY
PAVDIVEKMA IINQNDPRAE EATKIIYKKE FHSGKLKDNC GPYAGKLVSE VKDLLIKDFK
KIGIADVMYD LPQSVVCRCL TPCIVKILSE QWFLNYSNLN WKKKSKEVIS TMNIFPESAR
PWFIAVIDWL KEWACARTTG FGTPLPWGKG WIIETLSDST VYMAFYTIYN HIVENRINPK
NLTPEIFNYI FYGKGSSYNL SKQSQIKESL LRKMRDEFLY WYPFDLRISA KELVPNHLTF
CVFHHAALFP PEHWPRGIGV NGMLMIEGKQ MHKSKGNFVT MKNAVDTYGA DATRCALLIG
AEAMDDPDWR NENAKTLKEK IENLSKFIIN LIDAPNQNQN GHLERWLNSK IQSRITQVTE
NLENLKTRTS LEIALYETWN DFRWYINRKQ NKNTISLSSA LAIWIRLLAP FAPYISEELW
SYLRKDNFVS IANWPKSDID KINLEAEEKE NIIVDLVDDT FNILKATKIS PKKIYYYCAA
EWKREIYQRL LKETVKGQIA FKDVMKELAK DPSLRKKMNL VVSYVQRTLK ILNKYPIDRK
KRLFKTNILD EKDFIESAKD FFENRYKTKI YVYSEDDSEK YDPKQRAKLA IPGQPAIFIE
//
