ID A0A0F8CKI9_9EURY Unreviewed; 894 AA.
AC A0A0F8CKI9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN ORFNames=FK85_28665 {ECO:0000313|EMBL:KKF39417.1};
OS Halorubrum saccharovorum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=2248 {ECO:0000313|EMBL:KKF39417.1, ECO:0000313|Proteomes:UP000053331};
RN [1] {ECO:0000313|EMBL:KKF39417.1, ECO:0000313|Proteomes:UP000053331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KKF39417.1,
RC ECO:0000313|Proteomes:UP000053331};
RA Rozanov A.S., Kotenko A.V., Bryanskaya A.V., Malup T.K., Peltek S.E.;
RT "Full genome sequence of Halorubrum H3 strain isolated from Burlinskoye
RT Salt Lake (Altai Krai, Russia).";
RL Submitted (MAR-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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, 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:KKF39417.1}.
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DR EMBL; JNFH02000053; KKF39417.1; -; Genomic_DNA.
DR RefSeq; WP_050025760.1; NZ_JNFH02000053.1.
DR AlphaFoldDB; A0A0F8CKI9; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000053331; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 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; 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|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000053331}.
FT DOMAIN 40..174
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 223..405
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 416..612
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 658..778
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 894 AA; 100515 MW; 0E4D54FB37FF1E76 CRC64;
MSQEAYDHTA VEKRWQEAWD DASVYRTPDE VDDPTYVLGM YPYPSGKLHM GHVRNYTITD
AYARYRRMRG DDVLHPMGWD AFGLPAENAA KERDTNPRDW TFDCIDTMRG QMKSMGFGYD
WDREVTTCTP EYYQWNQWLF RRFHEAGLVE RRDAEVNWCP SCETVLADEQ VEGDDELCWR
CDTPVETRDL DQWFLEITEY ADELIDAIDG LEGWPDSVRQ MQRNWIGRQH GTTLDFHIDG
HGPVEAFTTR VDTIHGATFF ALAPDHPISE ELAAENDDIH QFVHHEADPE GDEPNGVATG
LTATNPATGE EIPVFVADFV LSDVGTGALM AVPGHDERDH AFAEKMGVDI EPVIAPEPDD
WDGETVPDAP DVSEAAFTDD GVVIDSGEYS GLDSETARER LTEEIESAEA TTQYRLRDWG
ISRQRYWGTP IPVVHCDDCG SVLVPEEELP VELPEFINTT GNPLDAAEEW KETTCPECGG
PATRETDTMD TFVDSSWYYL RYVSPGLDDA PFDLDRANDW MPVDQYVGGI EHAVMHLLYS
RFVTKVLADE EGLEHREPFT NLLAQGMVQL EGEKMSKSKG NTVSPQRIVE EYGADTARLF
MMQAAQPERD FDWAEEGVKS THRFLARLTD LVEEYAAGEV ALAGDGDPEA ADHDEIDDYV
ADEIDAAVAI AGAEYDDLTF NVALREAQDL VGTLRSYRGH ADPHPETYER GLDVAVRLLA
PVVPHLAEEL WDTLDRDGFV VEAEWPTATV DRETVERRRR LVANTREDVR DIVEVAGIED
PERIDVVVAP DWKYDALAIA IGSDADNLIS ELMGENHIRE QGDDAASYGQ DLQANREALQ
ETLSSDAEYD ALRAASWLIE REFDAPVRVE RAEDADDAVV RKAEPGRPAI DIVE
//
