SYL_ACAM1
ID SYL_ACAM1 Reviewed; 855 AA.
AC B0C1R1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=AM1_1037;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; CP000828; ABW26077.1; -; Genomic_DNA.
DR RefSeq; WP_012161635.1; NC_009925.1.
DR AlphaFoldDB; B0C1R1; -.
DR SMR; B0C1R1; -.
DR STRING; 329726.AM1_1037; -.
DR EnsemblBacteria; ABW26077; ABW26077; AM1_1037.
DR KEGG; amr:AM1_1037; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_3; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000268; 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 Gene3D; 3.40.50.620; -; 2.
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 PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..855
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000074823"
FT REGION 292..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 614..618
FT /note="'KMSKS' region"
FT COMPBIAS 292..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 855 AA; 95949 MW; 6BEA950C874A35F9 CRC64;
MESRYNPTEI EPKWQASWAK QGLDATPEDT SKPKFYALSM FPYPSGSLHV GHTRNYVITD
VIARLKRMQG YRVLQPMGWD AFGLPAENAA IARGIHPAEW TYANMAQMKK QLEPLGLSID
WSREIATCSP DYYRWTQWIF LQFLDMGLAY QKEAAVNWDP VDQTVLANEQ VDNEGRSWRS
GAKVERKLLR QWFLKITDYA EELLTDLDKL TGWPERVKTM QANWIGKSVG AYLEFPIVGM
DEKVAVFTTR PDTVYGVTYV VLAPEHPLTP QVTSKAQKKA VDKFIEAVGA ESEMDRTAED
KPKKGIPTGG KAINPFTGEE IPIWIADYVL YEYGTGAVMG VPAHDTRDFV FAQQNKLPIQ
TVIVPEGGDA ETPLEAAYTE PGLMVNSGEF DGKVSTEGKQ AIIAKAETKG WGKARVQYRL
RDWLISRQRY WGVPIPVIHC PNCGAVPVPE ADLPVELPED VEFSAQGGSP LAKLESWVNV
ACPNCGADAK RETDTMDTFI DSSWYFLRYP DAKNDKAVFD SAKTNDWLPV DQYVGGIEHA
ILHLLYSRFF TKVMRDRKLL NFDEPFKKLL TQGMVQALTY KNPETGQYIA PINVDADDPK
DPETGAPLEA FYEKMSKSKY NGVPPEEVTN KYGADTARLF TLFKAPPEKD LEWEGADVEG
QFRFLNRVWR LVSEHAAQAK GKKAKVNKAK LSKTEKELRR SIHIAIKETS EDLDGDYQFN
TAVSELMKLS NALSDSKEKA SPVYAEGVET LLLLLTPFAP HISEELWENL GHSESILGQT
WPQVDEEALV ADEITLVIQI MGKTRGTIQV PAGSSREDLE QLARESEVAQ RYIAGKEVKK
VIVVPGKLVN FVVPK
