ID K9QTY3_NOSS7 Unreviewed; 887 AA.
AC K9QTY3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Nos7524_2415 {ECO:0000313|EMBL:AFY48257.1};
OS Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY48257.1, ECO:0000313|Proteomes:UP000010378};
RN [1] {ECO:0000313|Proteomes:UP000010378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:RU363035}.
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DR EMBL; CP003552; AFY48257.1; -; Genomic_DNA.
DR AlphaFoldDB; K9QTY3; -.
DR STRING; 28072.Nos7524_2415; -.
DR KEGG; nop:Nos7524_2415; -.
DR PATRIC; fig|28072.8.peg.2633; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_3; -.
DR Proteomes; UP000010378; 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 CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 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; 2.
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:UP000010378}.
FT DOMAIN 54..187
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 237..437
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 451..607
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 649..688
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 729..849
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 56..66
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 648..652
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 651
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 887 AA; 100175 MW; E4ADF6796B2564FB CRC64;
MEADKITEPV GEFSVDSRYN AAAIEEKWQQ AWAELGLDKT PTDSNQPKFY ALSMFPYPSG
SLHMGHVRNY TITDVIARLK RMQGYRVLHP MGWDAFGLPA ENAAIDRGVP PAKWTYQNIA
QMRQQLQRLG LSIDWDSEVA TCSPDYYKWT QWIFLQFLQM GLAYQKEAAV NWDPIDQTVL
ANEQVDSEGR SWRSGAKVER KLLRQWFLKI TDYAEQLLND LDKLTGWPER VKLMQANWIG
KSTGAYLEFP IVGSSEKIAV YTTRPDTVFG VSYVVLAPEH PLTKQVTSKA QQATVEAFIH
EVTNQSELER TAEDKPKRGV PTGGKVVNPF TGEEVPIWIA DYVLYEYGTG AVMGVPAHDA
RDFKFAQRYD LPIDFVIADP KDVAGFDLTP TSDGEEVTQL VQIEYNDAYT EPGILINSGA
FTGLNSTDAK QAITKYAEEN SFGKERVQYR LRDWLISRQR YWGAPIPVIH CPNCGIVPVP
DKDLPVQLPE EVEFTGRGGS PLAQLESWVN VPCPTCGTPA KRETDTMDTF IDSSWYFLRY
PDAQNEQQIF ELGKTNDWMP VDQYVGGIEH AILHLLYSRF FTKVLRDRGL LNFDEPFERL
LTQGMVQGLT YMNPNKGGKD KWIPSSLVNP NDPRDPQTGE PLQRLYATMS KSKGNGVAPE
DVIAKYGVDT ARMFILFKAP PEKDLEWDEA DVEGQFRFLN RVWRLVTEYV AAGVCRKQAQ
LDNLSKPEKE LRRAIHTAIQ AVTEDLEDEY QFNTAVSELM KLSNAITDAN CQNSPIYAEG
MRTLVVLLAP FAPHIADELW HLLGNKESVH TQSWPSFDPE ALVADEVTVV IQINGKKRAD
IQVPAQADKA ALEKFALESE VTQRYIEGKE IKKVIVVPGK LVNFVVV
//
