(data stored in ACNUC7421 zone)

SWISSPROT: C6B3G6_RHILS

ID   C6B3G6_RHILS            Unreviewed;       704 AA.
AC   C6B3G6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   OrderedLocusNames=Rleg_0583 {ECO:0000313|EMBL:ACS54887.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54887.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54887.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54887.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly). {ECO:0000256|HAMAP-Rule:MF_00255,
CC       ECO:0000256|SAAS:SAAS00696787}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00255, ECO:0000256|SAAS:SAAS00696785}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255,
CC       ECO:0000256|SAAS:SAAS00696779}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00255,
CC       ECO:0000256|SAAS:SAAS00696776}.
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DR   EMBL; CP001622; ACS54887.1; -; Genomic_DNA.
DR   RefSeq; WP_012756263.1; NC_012850.1.
DR   ProteinModelPortal; C6B3G6; -.
DR   EnsemblBacteria; ACS54887; ACS54887; Rleg_0583.
DR   KEGG; rlg:Rleg_0583; -.
DR   HOGENOM; HOG000264304; -.
DR   KO; K01879; -.
DR   OMA; KENQRYF; -.
DR   OrthoDB; POG091H00US; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.730.10; -; 1.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   TIGRFAMs; TIGR00211; glyS; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B3G6.
DR   SWISS-2DPAGE; C6B3G6.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00255,
KW   ECO:0000256|SAAS:SAAS00696784, ECO:0000313|EMBL:ACS54887.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00255,
KW   ECO:0000256|SAAS:SAAS00696781};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255,
KW   ECO:0000256|SAAS:SAAS00696778};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00255,
KW   ECO:0000256|SAAS:SAAS00696783, ECO:0000313|EMBL:ACS54887.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00255,
KW   ECO:0000256|SAAS:SAAS00696777};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00255,
KW   ECO:0000256|SAAS:SAAS00696782}.
FT   DOMAIN      595    691       DALR_1. {ECO:0000259|Pfam:PF05746}.
SQ   SEQUENCE   704 AA;  77132 MW;  91138D0AD4A9D0E3 CRC64;
     MPNLLLELRS EEIPARMQRK AAGDLKKLVT DALVEAGLSY EGAREYWTPR RLALDIHGLT
     ARSADVREER KGPRTDANEK AIEGFLRGAG LSSVSEAQVV SDPKKGDFYV AVISKPGRAT
     EEIVSDVMPG IIRDFPWPKS MRWGKASSKP GALRWVRPLQ SIVCTFGPEH EETTVIPFEI
     DGITASNITY GHRFHAPEAI TVRRFDDYAA NLEKAKVILD AERRKDIILH DARDIAFANG
     LELVEDEGLL EEVSGLVEWP QVLMGSFEED YLSIPSEIIR LTIKTNQKCF VTRPQGGETL
     SNKFILVSNI QASDGGKEIV HGNGKVVRAR LSDALHFWKR DQGNLPDLET LEASAAKFGL
     DLKKPLDQRM AKLDALDVTF HAKLGTQGAR VARIRTLAKE LADITGADAA LIDRAAVLAK
     ADLRTEAVGE FPELQGLMGR KYAVLQGEDA SVAAAIEDHY KPQGPSDRVP EDRVAITIAL
     ADKLDTLIGF WAIDEKPTGS KDPFALRRAA LGVVRILLER RIRLPLLATT KDGDLLSFFH
     DRLKVYLRDQ GARHDLIDAV LTSDADDLLM VARRVEALTA FITSEDGKNL LSGTKRATQL
     LAAEEKKGTV IADGVSPALL TLDAEKELFA AISGASKDAS DAVAGEDFRS AMEALSKLRG
     PVDRFFEDVL VNDEDAAIRA NRLALLRLIR EATGTVADFS KISG
//

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