UniProt: G4QEE0

Database: UniProt
Entry: G4QEE0_GLANF

LinkDB:  G4QEE0_GLANF 
Original site:  G4QEE0_GLANF

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   G4QEE0_GLANF            Unreviewed;       693 AA.
AC   G4QEE0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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:AEP28168.1};
GN   OrderedLocusNames=GNIT_0008 {ECO:0000313|EMBL:AEP28168.1};
OS   Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP28168.1, ECO:0000313|Proteomes:UP000009282};
RN   [1] {ECO:0000313|EMBL:AEP28168.1, ECO:0000313|Proteomes:UP000009282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC   {ECO:0000313|Proteomes:UP000009282};
RX   PubMed=22123761; DOI=10.1128/JB.06296-11;
RA   Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT   FR1064T.";
RL   J. Bacteriol. 193:7006-7007(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, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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DR   EMBL; CP003060; AEP28168.1; -; Genomic_DNA.
DR   RefSeq; WP_014107047.1; NC_016041.1.
DR   AlphaFoldDB; G4QEE0; -.
DR   STRING; 1085623.GNIT_0008; -.
DR   KEGG; gni:GNIT_0008; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000009282; 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   NCBIfam; TIGR00211; glyS; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00255};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00255};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000009282}.
FT   DOMAIN          582..682
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   693 AA;  75961 MW;  C72E59BA2E1E6C42 CRC64;
     MTVIKQNLLI ELGTEELPPK SLKKLSESFT QNIKDELSKA GFEFDDIQPF AAPRRLAVIV
     QNCAGSQPDS RVEKRGPAVS AAFDADGNPT RAAQGWAKGN GIDVAQASRL KTDKGEWLLH
     IAEVKGKALK DVLQDVLHTT VKKLPIPKPM RWGSSSAEFI RPVHTLCVMF GTEVLPVSLF
     GLSSANQLSG HRFHGERRFT LDHADNYASA LTAQYVVADY AQRTDTIEDG LSKKAKELGL
     SPDYDLSLLE EISSLVEWPV VLTAKFEADF LDVPKEALIY TMKDDQKYVP LLDSDGQLSS
     TFLFVTNIES KDPKQIIVGN QKVIRPRLAD AKFFFENDKK TTLESKAEKL ATVLFQKELG
     TVAEKTARLV AISKSIAEVL GIDSTHVARA AALAKADLLS DMVMEFPSVQ GIMGHHYALH
     DGEHAEVALA IEEQYLPRFA GDKLPTSTAG YILSLAEKLD TLVGIFGIGK LPKGDKDPFA
     LRRSAIGILR ILVENKLPLE LKAMVDSVVN IYGAKLSNAE TASQVHTFLL DRFKPFYQDQ
     EIAGDVVMAV MTQQPTTAID FDARIKAVTA FKEMESAVDL VAANKRVANI LNKNDIDINA
     LPAIDSALFS EEAEKVLFLS LESAETQVAS LIEKLSYDEV LASLTVLKTP LNNFFDDVMI
     MADDEKVKSN RVALVGKARQ LFLSVADVSV LAV
//

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