(data stored in SCRATCH zone)

SWISSPROT: D4YWZ4_SPHJU

ID   D4YWZ4_SPHJU            Unreviewed;       838 AA.
AC   D4YWZ4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 55.
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:BAI94876.1};
GN   OrderedLocusNames=SJA_C1-00420 {ECO:0000313|EMBL:BAI94876.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94876.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94876.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP +
CC       diphosphate + L-leucyl-tRNA(Leu). {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:RU363035}.
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DR   EMBL; AP010803; BAI94876.1; -; Genomic_DNA.
DR   RefSeq; WP_013038719.1; NC_014006.1.
DR   ProteinModelPortal; D4YWZ4; -.
DR   STRING; 452662.SJA_C1-00420; -.
DR   EnsemblBacteria; BAI94876; BAI94876; SJA_C1-00420.
DR   GeneID; 29271752; -.
DR   KEGG; sjp:SJA_C1-00420; -.
DR   eggNOG; ENOG4105C8T; Bacteria.
DR   eggNOG; COG0495; LUCA.
DR   HOGENOM; HOG000200747; -.
DR   KO; K01869; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; POG091H01JZ; -.
DR   Proteomes; UP000007753; Chromosome 1.
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-HAMAP.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.730.10; -; 1.
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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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; D4YWZ4.
DR   SWISS-2DPAGE; D4YWZ4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000313|EMBL:BAI94876.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000313|EMBL:BAI94876.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN       14    171       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      221    406       tRNA-synt_1_2. {ECO:0000259|Pfam:
FT                                PF13603}.
FT   DOMAIN      420    576       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      613    652       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      683    801       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        42     52       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00049}.
FT   MOTIF       614    618       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00049}.
FT   BINDING     617    617       ATP. {ECO:0000256|HAMAP-Rule:MF_00049}.
SQ   SEQUENCE   838 AA;  93238 MW;  4B216891DC73A75B CRC64;
     MQRRFNPLEA DARWQAAWDA KQTFKASDSS EKPRSYVLEM FPYPSGRIHI GHVRNYSMGD
     VLARFRRMTG HEVLHPMGWD AFGMPAENAA MEKNVHPGKW TYENIANMKA QLKKLGFALD
     WSRELATCHP DYYGHEQALF LDMLEAGLVY RKESAVNWDP VDMTVLANEQ VIDGKGWRSG
     APVEKRKLSQ WFLKITQFAD DLLAGLKTLD QWPDKVKLMQ ENWIGKSVGL QFHFRLDAPV
     GEISELEVFS TRPDTIFGAS FAAIAADHPI ALALAEKDAA LAAFAEECRQ TGTAAAEIET
     QEKKGHDTGL SVIHPFTGRK LPLFVANFVL MDYGTGAVMA VPGHDQRDLD FARKYLLPVE
     RVVAAEGDEA KGIGDEAYVG PGRLVNSDFL NGLGVEEAKA EVIRRAESEG WGTGTTVFRL
     RDWGVSRQRY WGTPIPVIHC EDCGPVGVPK DQLPVVLPED VSFDIPGNPL DRHPTWKHVD
     CPTCGKPARR ETDTLDTFAD SSWYFIRFAS QPKDRPFDRE TVEKWLPVGQ YIGGVEHAIL
     HLLYARFWTR ALQHMGQIGF AEPFTGLFTQ GMVTHETYKS PDGAWLAPQE VERQGDRIVM
     VGTGAPVTLG RVEKMSKSKK NVVDPDDIIA QYGADAVRWF MLSDSPPERD LPWTEAGIEG
     SWRFINRLWR LFGEADKGAE GQDKTLDRKL HQTIDGVAKD IEALSFNKAV AKIYELTNAV
     EKARPSASRS AAIRALALLV APMTPHLAEE AWADMGEQGL IAEAAWPAVD PALLVEDEVT
     IACQVMGKLR DTITVPKGTA KEELERLALA APNVVRTLDG ATPKKVIVVP DRLVNLVI
//

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