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Database: UniProt
Entry: A0A0J0YUQ4_9NEIS
LinkDB: A0A0J0YUQ4_9NEIS
Original site: A0A0J0YUQ4_9NEIS 
ID   A0A0J0YUQ4_9NEIS        Unreviewed;       881 AA.
AC   A0A0J0YUQ4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:KLT73829.1};
GN   ORFNames=PL75_00340 {ECO:0000313|EMBL:KLT73829.1};
OS   Neisseria arctica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1470200 {ECO:0000313|EMBL:KLT73829.1, ECO:0000313|Proteomes:UP000036027};
RN   [1] {ECO:0000313|EMBL:KLT73829.1, ECO:0000313|Proteomes:UP000036027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1503 {ECO:0000313|EMBL:KLT73829.1,
RC   ECO:0000313|Proteomes:UP000036027};
RA   Hansen C.M., Hueffer K., Choi S.C.;
RT   "Genome of a novel goose pathogen.";
RL   Submitted (NOV-2014) 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:RU363035}.
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:KLT73829.1}.
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DR   EMBL; JTDO01000001; KLT73829.1; -; Genomic_DNA.
DR   RefSeq; WP_047759921.1; NZ_JTDO01000001.1.
DR   AlphaFoldDB; A0A0J0YUQ4; -.
DR   STRING; 1470200.PL75_00340; -.
DR   PATRIC; fig|1470200.3.peg.77; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000036027; 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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; 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:UP000036027}.
FT   DOMAIN          39..171
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          221..415
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          429..605
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          630..673
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          719..845
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           634..638
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   881 AA;  98916 MW;  051EE01FF46876B2 CRC64;
     MQEHYQPSAI ETAAQEKWEK ARLFNVSEDS SKPKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VLSRFKLLNG YNVMQPMGWD AFGMPAENAA MKHQVAPAKW TYENISYMKQ QLKSLGFAID
     WEREIATCTP EYYRWEQWLF TKLFEKGIVY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALIEKREIPM YYFKITDYAE ELLADLDKLE NWPEQVKTMQ RNWIGKSRGM QVRFKVDADS
     RSGLEGEYAD YLQVYTTRPD TLMGATYVAV AAEHPLATAA AADKPELQAF IAECKSGSVA
     EADMATMEKK GVPTGRYVIN PLNGDKLEVW IANYVLWGYG DGAVMAVPAH DERDFEFAAK
     YALPIKQVIA VAGETFDATK WQEWYADKEN GTLINSGKYD GMNFQTAFDT MAADLQAAHA
     GAPKTQYRLR DWGISRQRYW GCPIPIIHCD CCGDVPVPAE QLPVVLPEDV VPDGTGSPLA
     KMPEFYETTC PKCGAPAKRE TDTMDTFMES SWYPFRYMSP RFEEGMVEPQ AAAYWGAVDQ
     YIGGIEHAIL HLLYARFFTK LMRDEGLINV DEPFERLLTQ GMVVCDTYYR EGENGSKNWI
     NPADVELTFD EKGRPVSAVL KADGLPVIIS GTEKMSKSKN NGVDPQALID AYGADTARLF
     MMFASPPEQS LEWSDSGVEG AHRFLRRLWR TVYEYTTKDN TVAAFAGDQS GLSKALKELR
     FKLHSTIAKV GDDYGRRLQF NTAIAAVMEL LNQYDACVKN GDCDSAEGRA VAQEVLEAAV
     RLLWPIVPHI CETLWSELRP GTALWEAAWP QTDEDALVKS EIEIMVQVNG KLRGKITVAA
     DASKDTVEAA ALASDGAVKF MEGKPAKKVI VVPRRLVNIV V
//
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