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Database: UniProt
Entry: W7QF81_9GAMM
LinkDB: W7QF81_9GAMM
Original site: W7QF81_9GAMM 
ID   W7QF81_9GAMM            Unreviewed;       634 AA.
AC   W7QF81;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
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:EWH02799.1};
GN   ORFNames=Q427_06530 {ECO:0000313|EMBL:EWH02799.1};
OS   Halomonas sp. BC04.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1403540 {ECO:0000313|EMBL:EWH02799.1, ECO:0000313|Proteomes:UP000019279};
RN   [1] {ECO:0000313|EMBL:EWH02799.1, ECO:0000313|Proteomes:UP000019279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC04 {ECO:0000313|EMBL:EWH02799.1,
RC   ECO:0000313|Proteomes:UP000019279};
RA   Farooqui S., Greene A.C., Patel B.K.;
RT   "Draft Genome Sequence of Halomonas Strain BC04, an Aromatic-degrading
RT   moderate Halophilic Bacterium.";
RL   Submitted (DEC-2013) 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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWH02799.1}.
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DR   EMBL; AZQX01000073; EWH02799.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7QF81; -.
DR   PATRIC; fig|1403540.3.peg.1228; -.
DR   Proteomes; UP000019279; Unassembled WGS sequence.
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:UP000019279}.
FT   DOMAIN          524..618
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   634 AA;  69562 MW;  8286B122BB03F1AE CRC64;
     MQVSELADKQ PDREVERRGP ALAAAFKDGE PTKAAHGFAR SCGVDVAELI HLETDKGTWL
     GYRERQSGEA TTALLPDIVA KAVASLPVPK NMRWGASRIE FSRPVHWLVM LYGSDIVEAE
     VLGLTAGRTT RGHRFHAPDA IELAHAEDYL AALENAWVLA DRQRRRESIR EQVLAEAEVQ
     EATAVIGEAL LTEVSGLVEW PVALAGSFDE RFLEVPAECL ISSMKANQKY FHLLDNSGRL
     KPLFITIANI DSQDPQQVIE GNEKVIRPRL ADAAFFYDTD RKQPLATRIS GLSSVLFQKQ
     LGSLADKAHR TAAVAAFIAG RIGGEVAHAR RAAELGKCDL ITEMVLEFPE LQGIMGRYYA
     TLDGEPSDVA QALEEQYLPR FATDAIPETP TGLALALADR LDTLTGIFGI GARPTGTKDP
     FALRRASIGV LNILVKGELD LDLRELLELA AAQHQELPYA ENLVEEVLSY MLDRFRAWGQ
     DEGIEAEVYL AVRARPVTRP LDFARRLRAV HAFAQRVEAG SLAAANKRVA NILAKQESGS
     TPNRVDPGLL QETAEEALFE ALAAKREAVM PLFAEGRYHD ALDALATLRD PVDTFFDQVM
     VMAEDDDIRA NRLALLAGLQ GLFLEVADIA LLQQ
//
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