ID A0A258TSX0_9PROT Unreviewed; 723 AA.
AC A0A258TSX0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=B7Y41_06870 {ECO:0000313|EMBL:OYY94548.1};
OS Hydrogenophilales bacterium 28-61-23.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970530 {ECO:0000313|EMBL:OYY94548.1, ECO:0000313|Proteomes:UP000215898};
RN [1] {ECO:0000313|EMBL:OYY94548.1, ECO:0000313|Proteomes:UP000215898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-61-23 {ECO:0000313|EMBL:OYY94548.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYY94548.1}.
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DR EMBL; NCGJ01000004; OYY94548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258TSX0; -.
DR Proteomes; UP000215898; 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}.
FT DOMAIN 614..713
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 723 AA; 78104 MW; D52E853C298FAD51 CRC64;
MTTKNLLVEL FVEELPPKAL KKLGEAFATA LSEGLKEKKL VNADAGVIPF ASPRRLAVHI
SDVLSTAPDQ EVNEKLMPIS IALDKEGKPT EALRKRLAKV GRAEMADMWP KEEDGPDRLF
IANDGKSDAV FLRSLAKGTS LQVGLQGALE DALAKLPIPK VMTYQLADGW SSVNFVRPAH
SLLALHGAKI VHVSVLGLDA GRETRGHRFE AAIDPISIRD ADSYAAQMRA EGAVIPCFAE
RRAEIERQLN AAAAKVGGGV QPLADDALLD EVTALVERPN VLLCQFEPEF LQVPQECLIL
TMQANQKYFP LLDAAGRLTN QFLIVSNISP ADPSKVIGGN ERVVRPRLAD AKFFFDQDCK
KTLESRVLAL AKVVYHNKLG TQGERVQRVC AIAKAIGKKL GGEALALRAE QAALLAKADL
LTDMVGEFPE LQGIMGRYYA LHDGLSGEIA DAIEDHYKPR FAGDALPRNP VGLAVALADK
LETLVGLFGI GQTPTGDKDP FALRRHALGV VRMLVEAELK LAQSELLQAA VDAFPDTLIA
KESGKDGGKE GGPLWKLVDI YINERAVGYW KEKGYSEQMV DAVLEATHLP IEHALRLAAV
REFNALPEAA ALAAANKRIQ NILKKVDGEV EPVTSPYLFQ EAAEIALNAA LGEVEPVADA
AFDAGDYTAS LKSLAALKAP VDAFFDGVMV NAEDPNLRAN RLGLLARLRR AMNRVADLSR
LAA
//
