SYGB_VIBC1
ID SYGB_VIBC1 Reviewed; 693 AA.
AC A7N1D8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255};
GN OrderedLocusNames=VIBHAR_00449;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR EMBL; CP000789; ABU69464.1; -; Genomic_DNA.
DR RefSeq; WP_012126670.1; NC_022269.1.
DR AlphaFoldDB; A7N1D8; -.
DR SMR; A7N1D8; -.
DR EnsemblBacteria; ABU69464; ABU69464; VIBHAR_00449.
DR KEGG; vha:VIBHAR_00449; -.
DR PATRIC; fig|338187.25.peg.2141; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000008152; Chromosome I.
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;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..693
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006420"
SQ SEQUENCE 693 AA; 76679 MW; 338684454AF34EDC CRC64;
MAKEFLIELG TEELPPTQLR TLAEAFAANF EAELKGAELA HEGVKWFAAP RRLALKVAAL
ADSQSDKVVE KRGPAVSAAF DAEGNPTKAA QGWARGCGIT VDQAERMVTD KGEWLLFKQE
VKGQPTSQIV VELAAKALAN LPIAKPMRWG NKTTQFIRPV KTLTMLMGSD LIEGEILGVA
SDRTIRGHRF MGEQEFTIDS AEQYPAILEE RGKVMADYEA RKAIILADAQ KAAAAVGGIA
DLEDDLVEEV TSLVEWPVVL TAKFEEEFLK VPSEALVYTM KGDQKYFPVY SHENGDENKK
LLPNFIFVSN IESKEPRYVI EGNEKVVRPR LADAEFFFNT DRKRPLIDRL PELEQAIFQK
QLGTIKDKTD RITELAGYIA EQIGADVEKS KRAGLLAKCD LMTSMVFEFT DTQGVMGMHY
ARHDGEAEEV AVALNEQYMP RFAGDELPSN GVSTAVAMAD KLDTIVGIFG IGQAPKGSDP
FALRRASLGV LRIIVEYGYN LDLVDLVAKA KSLFGDRLTN DNVEQDVIEF MLGRFRAWYQ
DEGFSVDIIQ AVLARRPTKP ADFDQRVKAV SHFRELEAAE SLAAANKRVG NILAKFDGEL
AADIDLALLQ EDAEKALAES VEVMTEALEP AFATGNYQEA LSKLADLREP VDAFFDNVMV
MADDEALKKN RLTLLNNLRN LFLQIADISL LQK