(data stored in ACNUC1104 zone)

SWISSPROT: E6V4F5_VARPE

ID   E6V4F5_VARPE            Unreviewed;       561 AA.
AC   E6V4F5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000256|HAMAP-Rule:MF_00123};
GN   OrderedLocusNames=Varpa_0479 {ECO:0000313|EMBL:ADU34701.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34701.1, 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:ADU34701.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34701.1,
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-arginine + tRNA(Arg) = AMP + diphosphate + L-
CC         arginyl-tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658,
CC         Rhea:RHEA-COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513,
CC         ChEBI:CHEBI:456215; EC=6.1.1.19; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00123,
CC       ECO:0000256|RuleBase:RU363038}.
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DR   EMBL; CP002417; ADU34701.1; -; Genomic_DNA.
DR   RefSeq; WP_013538947.1; NC_014931.1.
DR   STRING; 595537.Varpa_0479; -.
DR   EnsemblBacteria; ADU34701; ADU34701; Varpa_0479.
DR   GeneID; 29717518; -.
DR   KEGG; vpe:Varpa_0479; -.
DR   eggNOG; ENOG4105C75; Bacteria.
DR   eggNOG; COG0018; LUCA.
DR   HOGENOM; HOG000247214; -.
DR   KO; K01887; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   BioCyc; VPAR595537:G1GQO-480-MONOMER; -.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR11956; PTHR11956; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6V4F5.
DR   SWISS-2DPAGE; E6V4F5.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:ADU34701.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:ADU34701.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917}.
FT   DOMAIN        6     92       Arg_tRNA_synt_N. {ECO:0000259|SMART:
FT                                SM01016}.
FT   DOMAIN      444    561       DALR_1. {ECO:0000259|SMART:SM00836}.
FT   MOTIF       128    138       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00123}.
SQ   SEQUENCE   561 AA;  61311 MW;  03C8352DAF9DD239 CRC64;
     MLLVKQELLA ALANTLESLS PGAGAKAAFE SPKVAAHGDF ASTAAMQLAK PLAKKPRELA
     EQLSAALLAT PAFGQWVEAI EIAGPGFLNI RLKTAAKQQI VREVLAAGNT FGQQPATGEK
     VLVEFVSANP TGPLHVGHGR QAALGDAICN LRASQGDSVW REFYYNDAGV QIQTLANSTQ
     LRARGFKPGD PEWPSGEKAP AYNGDYIADI AEDFKAKKTV KSDDREYTAS GDIDDIDSIR
     EFAVAYLRRE QDLDLQAFRV RFDNYYLESS LYTSGRVEAA VGKLVAAGKT YEEDGALWLK
     STDYGDDKDR VMKKKDGTYT YFVPDVAYHI AKWERGFHKV VNIQGTDHHG TIARVRAGLQ
     AAGEGIPEGY PDYVLHTMVR VMKGGEEVKI SKRAGSYVTL RDLIEWTSTD AVRFFLLSRK
     PDTEYTFDVD LAVTKNNDNP VYYVQYAHAR ICSVLAGWGG DAATLKDVDL SPLKSPAAQA
     LMLLLAKYPA MLTAASKDFA PHDVTFYLRE LAASYHSYYD AERILVDDEK VKLARLALVA
     ATAQVLHNGL AILGVSAPNK M
//

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