ID A0A1H1RSY0_9CELL Unreviewed; 986 AA.
AC A0A1H1RSY0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=SAMN04489860_1435 {ECO:0000313|EMBL:SDS38656.1};
OS Paraoerskovia marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Paraoerskovia.
OX NCBI_TaxID=545619 {ECO:0000313|EMBL:SDS38656.1, ECO:0000313|Proteomes:UP000185663};
RN [1] {ECO:0000313|EMBL:SDS38656.1, ECO:0000313|Proteomes:UP000185663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22126 {ECO:0000313|EMBL:SDS38656.1,
RC ECO:0000313|Proteomes:UP000185663};
RA de Groot N.N.;
RL Submitted (OCT-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|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}.
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DR EMBL; LT629776; SDS38656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1RSY0; -.
DR STRING; 545619.SAMN04489860_1435; -.
DR eggNOG; COG0495; Bacteria.
DR Proteomes; UP000185663; Chromosome i.
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}; Reference proteome {ECO:0000313|Proteomes:UP000185663}.
FT DOMAIN 74..156
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 310..524
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 836..948
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 759..763
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 986 AA; 108478 MW; C5462A920CA67CE6 CRC64;
MSTPETTPRS TDAAGAPGEP SFRYTPAMAE EIELRWQDRW ESSGTFYAAN PSGALTDGNG
EHAGDRPPFF IMDMFPYPSG AGLHVGHPLG YIATDVVGRF RRMQGDNVLH TLGYDAFGLP
AEQFAVQTGQ HPRTTTEANM VNMRRQLRRM GLAHDPRRTF ATIDPEYVRW TQWIFLQMFG
SWYDVDAVRP DGGTGRARPI AELEAEYADG TRAVPGGRSW ADLEAGEQRD VVDSQRLAYV
SEAPVNWCPG LGTVLANEEV TSDGRSERGN FPVFQRSLRQ WNMRITAYAD RLVDDLDLID
WPEKVKAMQR NWIGRSEGAQ VRFALQPSAS AQDAVPGVDG IEVFTTRPDT LFGATFMVVA
PEHPVVDQVP AAWPEGTKDA WTGGHATPRE AVTAYRSEAA AKTAVERQAD AGKKTGVFTG
LFGSNPVDGA AVPVFTADYV LMGYGTGAIM AVPGGDARDF AFAEAFDLPV IYTVAPGGDV
DALDRGEAFT GDGLVVNSAA ASDDGVTLDG LDVATAKRTV IDWLEARGAG TGTVTYRLRD
WLFSRQRYWG EPFPIVYGED GRPLAVPENQ LPVDLPEVPD YAPRVFDADD ADSSPEPPLG
RNQDWVDVEL DLGDGPRTYR RDTNTMPNWA GSCWYYLRYL DPTDDEHVVS PELEKYWLGA
HHNASSGPAG GVDLYVGGVE HAVLHLLYAR FWHKVLHDLG HVSSLEPFGK LFNQGYVQAY
AFRDDRGQPV PAAEVEEHED GGTTTYTWNG QTVTREYGKM GKSLKNVVTP DEMYEQYGAD
TFRVYEMSMG PLDLSRPWET RAVVGAQRFL QRLWRNVVDE TSGRTTVVET PADAATLRAV
HRTIADVTVE MAEMRPNTAI ARLITLNNHL TSLGEVPREA VEPLVLMTAP VAPHIAEELW
QRLGHAESLA HEPFPTALDE YLVEESVTCV VQVKGKVRGK ITVSPSISEE DLRAAALAEP
NVQRQIGDAE IRKVIIRAPK LVNVVV
//
