ID K1E9W8_9MICO Unreviewed; 964 AA.
AC K1E9W8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 ECO:0000313|EMBL:EKA62207.1};
GN ORFNames=B277_04145 {ECO:0000313|EMBL:EKA62207.1}, CWN80_02675
GN {ECO:0000313|EMBL:RWU85072.1};
OS Janibacter hoylei PVAS-1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1210046 {ECO:0000313|EMBL:EKA62207.1, ECO:0000313|Proteomes:UP000004474};
RN [1] {ECO:0000313|EMBL:RWU85072.1, ECO:0000313|Proteomes:UP000288711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU85072.1,
RC ECO:0000313|Proteomes:UP000288711};
RX PubMed=19643890; DOI=10.1099/ijs.0.002527-0;
RA Shivaji S., Chaturvedi P., Begum Z., Pindi P.K., Manorama R.,
RA Padmanaban D.A., Shouche Y.S., Pawar S., Vaishampayan P., Dutt C.B.,
RA Datta G.N., Manchanda R.K., Rao U.R., Bhargava P.M., Narlikar J.V.;
RT "Janibacter hoylei sp. nov., Bacillus isronensis sp. nov. and Bacillus
RT aryabhattai sp. nov., isolated from cryotubes used for collecting air from
RT the upper atmosphere.";
RL Int. J. Syst. Evol. Microbiol. 59:2977-2986(2009).
RN [2] {ECO:0000313|EMBL:EKA62207.1, ECO:0000313|Proteomes:UP000004474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:EKA62207.1,
RC ECO:0000313|Proteomes:UP000004474};
RX PubMed=23144385; DOI=10.1128/JB.01728-12;
RA Pawar S.P., Dhotre D.P., Shetty S.A., Chowdhury S.P., Chaudhari B.L.,
RA Shouche Y.S.;
RT "Genome Sequence of Janibacter hoylei MTCC8307, Isolated from the
RT Stratospheric Air.";
RL J. Bacteriol. 194:6629-6630(2012).
RN [3] {ECO:0000313|EMBL:RWU85072.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU85072.1};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RL Submitted (NOV-2017) 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:RU363039}.
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:EKA62207.1}.
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DR EMBL; ALWX01000014; EKA62207.1; -; Genomic_DNA.
DR EMBL; PIPF01000002; RWU85072.1; -; Genomic_DNA.
DR RefSeq; WP_007925408.1; NZ_PIPF01000002.1.
DR AlphaFoldDB; K1E9W8; -.
DR STRING; 1210046.B277_04145; -.
DR PATRIC; fig|1210046.3.peg.808; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000004474; Unassembled WGS sequence.
DR Proteomes; UP000288711; 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 Gene3D; 3.40.50.620; HUPs; 3.
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; 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; 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 58..158
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 295..498
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 816..924
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 551..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 737..741
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 740
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 964 AA; 107128 MW; C884DFA95BC2DA89 CRC64;
MSETPYRYTA EMAGRIETGW QDRWEELGTF RAPNPAGPWA EPERVQQHEG HQLILDMFPY
PSGAGLHVGH PLGYIATDVY ARYQRMLGKN VLHCLGYDAF GLPAEQFAVQ TGQHPRVTTE
ANMDTMRRQL RRLGLGHDDR RAFATIDPDY YRWTQWIFLQ IFNAWYDEDA VRPDGGRGRA
RPIAELVEAF ASGERPLPEG ETRTWADLSP KERSDVLDGY RLAYSAEAPV NWAPGLGSVV
ANEEVTSDGR SERGNFPVFR TNLRQWMMRI TAYADRLADD LDRVEWPDKV KAMQRNWIGR
SEGAQVIFTA TGTDGAEHPI EVFTTRPDTL FGATFMVLAP EHPLVDALVP EGGWPEGTLD
AWTGGADTPF AAVSAYREEA RRKSDVERQI ETKDKTGVFT GGWATNPVSG ARIPVFVADY
VLMGYGTGAI MAVPSGDQRD FDYATAFGLD IIPTVAAPEG HEGAWSGDGE IINSVSDSIS
LDGLTVAEGK AAITTWLEEH GVGRGTVNYK LRDWLFSRQR YWGEPFPIVF DDDGVAHAVP
ESMLPVELPE VDDYSPRTFD PDDASSQPEP PLGRATEWVE VELDLGDGPR RYRRETNTMP
NWAGSCWYYL RYLDPANDEA LVDPANEAYW VGPRETPVPG APAGTRDPGG VDLYIGGVEH
AVLHLLYARF WHKILFDLGH VSSEEPFRRY FSQGYIQAHA YRDDRGQPVP AAEVVEDASA
PTGFTWQGQP VTQEYGKIGK SLKNAVSPDE MYEQYGADTF RVYEMSLGPL EQSKPWETRA
VVGSQRFLQR LWRNVVDEET GEVRVTDGAL DAQTERLLHQ TIAAVGADYA SLGFNTAIAR
LIELNNALTK LGEVPRAAVE PLVLMVAPIA PHLAEELWSR LGHEHSLSAE PFPVADESKM
VEASVTCVIQ IKGKVRDRVE VPSDIGEDEL RELALDRDKI KAATEGGIRT VIVRAPKLVN
VVPA
//
