ID L9VFJ8_9EURY Unreviewed; 886 AA.
AC L9VFJ8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 Name=leuS {ECO:0000313|EMBL:ELY35747.1};
GN ORFNames=C496_23001 {ECO:0000313|EMBL:ELY35747.1};
OS Natronorubrum tibetense GA33.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1114856 {ECO:0000313|EMBL:ELY35747.1, ECO:0000313|Proteomes:UP000011599};
RN [1] {ECO:0000313|EMBL:ELY35747.1, ECO:0000313|Proteomes:UP000011599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA33 {ECO:0000313|EMBL:ELY35747.1,
RC ECO:0000313|Proteomes:UP000011599};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY35747.1}.
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DR EMBL; AOHW01000055; ELY35747.1; -; Genomic_DNA.
DR RefSeq; WP_006092904.1; NZ_KB913017.1.
DR AlphaFoldDB; L9VFJ8; -.
DR STRING; 1114856.GCA_000383975_01404; -.
DR PATRIC; fig|1114856.3.peg.4755; -.
DR eggNOG; arCOG00808; Archaea.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000011599; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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 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}.
FT DOMAIN 223..402
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 416..614
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 653..769
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 866..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 100200 MW; 2749468238D8C1E6 CRC64;
MSDAGYDHAA VERRWQEAWD DEDAYRTPDD VEDPTYVLGM YPYPSGKLHM GHVRNYTITD
AYARFRRMCG DEVLHPMGWD AFGLPAENAA KERDTNPRDW TFDCIDTMTD QMESMGFGYD
WDREIATCTP EYYQWNQWLF SRFHEEGLVE RRDAEVNWCP HCETVLADEQ VEGEAELCWR
CDTPVEQREL EQWFLRITEY ADELLEAIDD LEGWPNSVRQ MQRNWIGRQF GTELEFQVAG
HGSVEAFTTR VDTIHGATFF ALAPDHPISE ELAEVDDDVH QFVEHEADPE GDEPNGVATD
LTATNPVTGE EIPVYVADFV LSDVGTGALM AVPGHDERDH AFATKMDEEI KPVIAPKPDD
WDGETVPDAP DVSEEAFTDD GVLVNSGEYS GLESAEARER LTVDIDSAEE STQYQLRDWG
ISRQRYWGTP IPIVHCHDDC GAVPVPEDEL PVELPEFINT TGNPLDAAEE WKQTTCPACG
GEATRETDTM DTFVDSSWYF LRYVSPGLED APFDLERAND WMPVDQYVGG IEHAVMHLLY
SRFFTKVLAD HEGLEHREPF TNLLAQGMVQ LEGEKMSKSK GNTVSPQRIV EEYGADTARL
FMMQAAQPER DFDWSEEGVR STYAFLSRLQ EMVEGYVSDD PKGEDDAIAS YVDAEIDATI
AIASGEYDEL RFNRALRETQ DLTRTLRQYA DYTDPHAETY ERGLSAVVRL LAPVAPHLAE
ELWDELGYDG FVVDAEWPTA QVDRDYVAKR RRLVQNTRED IRDIVEVAGI EDPEAIDVVV
APDWMYDALE IAIESDADNL IGELMQESHI REQGDDAASY GQDLQAEREA LSMTLGPDDE
HAALESAAWL IEREFDAPVS VVHAEKADDS AIKNAEPGRP AIEIDD
//
