(data stored in SCRATCH zone)

SWISSPROT: D3UYL7_XENBS

ID   D3UYL7_XENBS            Unreviewed;       689 AA.
AC   D3UYL7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
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   ECO:0000313|EMBL:CBJ79395.1};
GN   OrderedLocusNames=XBJ1_0244 {ECO:0000313|EMBL:CBJ79395.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79395.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79395.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79395.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522,
CC         ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00255, ECO:0000256|SAAS:SAAS01120476};
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; FN667741; CBJ79395.1; -; Genomic_DNA.
DR   RefSeq; WP_012986857.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0244; -.
DR   EnsemblBacteria; CBJ79395; CBJ79395; XBJ1_0244.
DR   GeneID; 8829867; -.
DR   KEGG; xbo:XBJ1_0244; -.
DR   PATRIC; fig|406818.4.peg.225; -.
DR   eggNOG; ENOG4105C38; Bacteria.
DR   eggNOG; COG0751; LUCA.
DR   HOGENOM; HOG000264302; -.
DR   KO; K01879; -.
DR   OMA; LPIPKRM; -.
DR   BioCyc; XBOV406818:XBJ1_RS01065-MONOMER; -.
DR   Proteomes; UP000002045; 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-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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   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; D3UYL7.
DR   SWISS-2DPAGE; D3UYL7.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00255,
KW   ECO:0000256|SAAS:SAAS00696784, ECO:0000313|EMBL:CBJ79395.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00255,
KW   ECO:0000256|SAAS:SAAS00696781};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
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:CBJ79395.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN      582    678       DALR_1. {ECO:0000259|Pfam:PF05746}.
SQ   SEQUENCE   689 AA;  76806 MW;  73E6AE49B179736E CRC64;
     MIQQTFLVEI GTEELPPKAL RSLAESFAAN FEAELKNANL GHGEISWFAA PRRLALKVAN
     LAVAQADREV EKRGPAIAQA FDAEGKPTKA AEGWARGCGI TVDQAERMVT DKGEWLLYRA
     QVKGREAKEL LADMVSSSLG KLPIPKLMRW GDKETQFVRP VHTVTMLLGS DVIDGEILGI
     KSDRIIRGHR FMGEAEFAID NAEQYPTILQ ERGRVIADYY ARKALIKRDA EQAAMQLGGV
     ADLTDSLLEE VTSLVEWPVV LTAKFEEKFL EVPAEALVYT MKGDQKYFPV YDKSGKLMAN
     FIFVANIESS DPQQIISGNE KVVRPRLADA EFFFKTDRKQ RLEDNLLRLE TVLFQKQLGT
     LRDKTDRIQA LAGWIAEKIG ADVTHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
     GEAEDVALAL NEQYQPRFSG DELPSTAVSC AVAIADKMDT LAGIFGIGQH PKGDKDPFAL
     RRAALGVLRI IVEKKLPLDL QTLAEEAVRL YGDKLTNENV VDDVVEFMLG RFRTWYQEQG
     YSVDAIQAVL ARRPTQPADF DARMKAVTHF RTLDEAVSLA AANKRVSNIL AKSEEKLNDC
     VLASVLKAAE EIQLATHLVV LKDKLAPLFA EGNYQDALVE LASLREVVDA FFDNVMVMDE
     DQQVRINRLT LLSELRELFL RVADISLLQ
//

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