(data stored in SCRATCH zone)

SWISSPROT: E6V4C2_VARPE

ID   E6V4C2_VARPE            Unreviewed;       876 AA.
AC   E6V4C2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=Varpa_0446 {ECO:0000313|EMBL:ADU34668.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34668.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34668.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34668.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-
CC         leucyl-tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613,
CC         Rhea:RHEA-COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57427, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC         ChEBI:CHEBI:456215; EC=6.1.1.4; Evidence={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
CC       family. {ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; CP002417; ADU34668.1; -; Genomic_DNA.
DR   RefSeq; WP_013538914.1; NC_014931.1.
DR   STRING; 595537.Varpa_0446; -.
DR   EnsemblBacteria; ADU34668; ADU34668; Varpa_0446.
DR   GeneID; 29717734; -.
DR   KEGG; vpe:Varpa_0446; -.
DR   eggNOG; ENOG4105C8T; Bacteria.
DR   eggNOG; COG0495; LUCA.
DR   HOGENOM; HOG000200747; -.
DR   KO; K01869; -.
DR   OMA; ALSMFPY; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; VPAR595537:G1GQO-447-MONOMER; -.
DR   Proteomes; UP000008917; 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; -; 1.
DR   Gene3D; 3.90.740.10; -; 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   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;
DR   PRODOM; E6V4C2.
DR   SWISS-2DPAGE; E6V4C2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000313|EMBL:ADU34668.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917}.
FT   DOMAIN       38    171       tRNA-synt_1g. {ECO:0000259|Pfam:PF09334}.
FT   DOMAIN      222    415       tRNA-synt_1_2. {ECO:0000259|Pfam:
FT                                PF13603}.
FT   DOMAIN      431    586       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      714    838       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        42     52       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00049}.
FT   MOTIF       634    638       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00049}.
FT   BINDING     637    637       ATP. {ECO:0000256|HAMAP-Rule:MF_00049}.
SQ   SEQUENCE   876 AA;  97627 MW;  CD7716AEA8066C1C CRC64;
     MNPSYKPSDV ESAAQAQWSA ADAYRVTEDA SRKKYYACSM LPYPSGKLHM GHVRNYTIND
     MLTRYLRMSG YNVLMPMGWD AFGLPAENAA LKNGVPPAKW TYENIDYMRG QLQAMGLAID
     WSREIATCDP SYYKWNQWLF LKMLEKGVAY RKTQVVNWDP VDQTVLANEQ VIDGKGWRTG
     ATVERREIPG YYLKISDYAE ELLEHTQHKL PGWPERVKLM QENWIGKSEG VRFAFTHDIQ
     DASGQLIQDG RMYVFTTRAD TIMGVTFCAV APEHPLAAHA ATLDPKVAAF IEECKNGGTT
     EAELATQEKK GVPTGLTVKH PITEEQVPVW VGNYVLIGYG DGAVMGVPAH DERDFAFANK
     YGIEIIQVVL VDDEPHFDYH KWQDWYGDKQ RGVTINSDNF SGMTYKEAVA AVAHALGQKG
     LGELQTTWRL RDWGVSRQRY WGTPIPIIHC EEHGAVPVPE KDLPVVLPTD CVPDGSGNPL
     NKHEGFHAGV VCPVCGKAAR RETDTMDTFV DSSWYFMRYC DPKNDQAMVA EGADYWMPMD
     QYIGGIEHAI LHLLYARFWT KVMRDLGLVK ADEPFAKLLT QGMVLNHIFY KRNEKGGKDY
     FPPLEVTPVL DAQGRITGGT TADGTKVEYG GVGKMGKSER NGVDPQDLIE KYGADTARLY
     TMFTAPPEAT LEWNDAAVEG SYRFLRRVWN FGVTQADVAP AKAGTQAFGK AAQALRREVH
     TVLRQVDYDY QRMQYNTVVS GAMKLLNALE GFKPDGSAGD AAAVREGFGI LLRCLYPATP
     HIAQQLWTEL GYDKDLGGLL DAAWPTVDVE ALVQDEIELM LQVNGKLRGK LLVPAGASKD
     EIEKLALACD DFVAFAEGAP PKRVIVVPGR LVNVVL
//

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