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Database: UniProt
Entry: V4JUW4_9GAMM
LinkDB: V4JUW4_9GAMM
Original site: V4JUW4_9GAMM 
ID   V4JUW4_9GAMM            Unreviewed;       604 AA.
AC   V4JUW4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE   Flags: Fragment;
GN   ORFNames=N838_27505 {ECO:0000313|EMBL:ESQ16070.1};
OS   Thiohalocapsa sp. PB-PSB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiohalocapsa.
OX   NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ16070.1, ECO:0000313|Proteomes:UP000017935};
RN   [1] {ECO:0000313|EMBL:ESQ16070.1, ECO:0000313|Proteomes:UP000017935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA   Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA   Orphan V.J.;
RT   "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT   consortia of the Sippewissett salt marsh.";
RL   Submitted (AUG-2013) 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};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, 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:ESQ16070.1}.
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DR   EMBL; AVFR01000267; ESQ16070.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4JUW4; -.
DR   Proteomes; UP000017935; Unassembled WGS sequence.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; 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; 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|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017935}.
FT   DOMAIN          39..171
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          221..403
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          417..566
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   NON_TER         604
FT                   /evidence="ECO:0000313|EMBL:ESQ16070.1"
SQ   SEQUENCE   604 AA;  68418 MW;  9D66BF0A3DBCC0AF CRC64;
     MQTEYDPRAV EAAAQRDWEE NHSFRAVEDP TREKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VIARYQRMQG KNVLQPMGWD AFGLPAENAA IKQGIPPSRW TRANVAYMKG QLKQLGFGYD
     WERELATCDP DYYRWEQWLF TRLMQKGLAY RASATVNWDP IDQTVLANEQ VIDGKGWRSG
     APVEKREIEQ WFLRITDYAQ ELLDATEGLD GWPEQVRTMQ RNWIGRSEGV YMKFGIQGRD
     DVLGIYTTRP DTLMGVTYVA VAAEHPLARD TAKHDPALAA FIDECRMGGT SEAELETMEK
     KGYRLGLDAL HPVTGEPVPM FAANFVLMGY GTGAIMAVPA HDQRDWEFAE RYDIPKKQVI
     VAADGGACGI DAGAYIDKGV LVESGPFTGL SSEQAFTAIA DWLSRHDKGE KRVNFRLRDW
     GVSRQRYWGC PIPVVHTADG ELYAETELPV RLPEDVVVDG SGSPLSKISA FSQLPGGAVR
     ETDTFDTFFE SSWYYARFCC TDCNDAMLDQ RANYWLPVDQ YIGGIEHAVL HLLYARFFHR
     LMRDEGLLNC DEPFANLLTQ GMVVAETWYR EDADGRKRWF NPSEVEAVRD DKGKLLSAVL
     QSDG
//
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