ID F8A1S3_CELGA Unreviewed; 974 AA.
AC F8A1S3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Celgi_1211 {ECO:0000313|EMBL:AEI11730.1};
OS Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI11730.1, ECO:0000313|Proteomes:UP000000485};
RN [1] {ECO:0000313|Proteomes:UP000000485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL Submitted (APR-2011) 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; CP002665; AEI11730.1; -; Genomic_DNA.
DR RefSeq; WP_013883249.1; NC_015671.1.
DR AlphaFoldDB; F8A1S3; -.
DR STRING; 593907.Celgi_1211; -.
DR KEGG; cga:Celgi_1211; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000000485; Chromosome.
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:UP000000485}.
FT DOMAIN 74..155
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 316..511
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 826..934
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 746..750
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 749
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 974 AA; 107244 MW; A10E69839DD712E0 CRC64;
MTSTPATASQ PTADRGDDVP FRYTADLARE IELRWQDEWQ ERGTFHAANP TGSLTDGDGR
HADPSRRSFF VMDMFPYPSG AGLHIGHPLG YIATDVVARF RRMQGDNVLH ALGFDAFGLP
AEQYAVQTGQ HPRVTTEANI AIMQRQLRRL GLAHDPRRSF ATIDPDYVRW TQWIFLQIFG
AWYDEDAERA DGGRGKARPI TELEAELAAG TRPVPAVADV PAGVAWQDLD AVARRRVLDA
HRLAYVSETP VNWCPGLGTV LANEEVTSDG RSERGNFPVF QRSLRQWNMR ITAYADRLAD
DLDHIDWPEK VKSMQRNWIG RSSGARVRFA VEGGSQVEVF TTRPDTLFGA TFMVVAPEHP
LLDEVPPSWP DGTHAAWTGG HASPAEAVAA YRAEAAAKTA VERQADAGRK TGVFTGHLAI
NPVNGQPLPV FTADYVLMGY GTGAIMAVPG GDERDFAFAQ AYELPVVYTT AGDVTDAART
GDGVVINSSN DELSLDGLGV AEAKERMIAW LTAAGIGEGT ITYRLRDWLF SRQRYWGEPF
PVVYDEHDLP IALPAELLPV ALPDVPDYAP RTFDPEDSAS SPEPPLGRND EWVTVTLDLG
DGPRQYRRDT NTMPNWAGSC WYYLRYLDPT SDEVLVDPEL ERFWMGPGHN GDPADTVGGV
DLYVGGVEHA VLHLLYARFW HKVLFDLGHV SGGEPFHQLF NQGYIQAYAY TDARGVHVPA
DEVVEDEASP TGFTWQGEPV NREYGKMGKS LKNMVTPDEM YAEYGADTLR VYEMSMGPLD
LSRPWETRAV VGSQRFLQRL WRNVVSEADG TLVVSEDAPS DETSRVLHRT IADVTEDMAA
MRINTAIAKL IVLNNHLTTL PAAPRAAVEA LVLMTAPIAP HVAEEIWARL GHERSLAYEP
YPVADPAFLV EETVTCVFQV AGKVRGRAEV AVDSSDDALR ELALADAGVQ RALDGRGVRT
VIVRAPRLVN VVPA
//
