ID A0A0P7J5W5_9RHOB Unreviewed; 771 AA.
AC A0A0P7J5W5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AKJ29_12725 {ECO:0000313|EMBL:KPN63503.1};
OS Aliiroseovarius crassostreae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=154981 {ECO:0000313|EMBL:KPN63503.1, ECO:0000313|Proteomes:UP000050471};
RN [1] {ECO:0000313|EMBL:KPN63503.1, ECO:0000313|Proteomes:UP000050471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV919-312 {ECO:0000313|EMBL:KPN63503.1,
RC ECO:0000313|Proteomes:UP000050471};
RA Kessner L., Spinard E., Nelson D.;
RT "Draft genome sequence of Aliiroseovarius crassostreae CV919-312TSm, the
RT causative agent of Roseovarius Oyster Disease (formerly Juvenile Oyster
RT Disease).";
RL Submitted (SEP-2015) 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:KPN63503.1}.
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DR EMBL; LKBA01000006; KPN63503.1; -; Genomic_DNA.
DR RefSeq; WP_055189911.1; NZ_LKBA01000006.1.
DR AlphaFoldDB; A0A0P7J5W5; -.
DR STRING; 154981.AKJ29_12725; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000050471; 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:UP000050471}.
FT DOMAIN 659..759
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 771 AA; 84699 MW; 9322BB088694DF6F CRC64;
MPDLLIELFS EEIPARMQTR AAQDLKKLVT DGLVEAGLTY AGAHALSTPR RLTLAIDGLL
AASPDTREER KGPKVGAPDK AIEGFLRGAG LTRDQLVERD TPKGPVYFAM IENKGRPAAE
IIAEVLEKTI RNFPWPKSMR WGSGSLKWVR PLHSILCILS DEAGAEVVPM EVDGIRSGDT
TQGHRFMAPG TITVSGFEDY ATKLKSAKVV LDPQERADHI WEDAKNAAFA QGLEIVEDTA
LLREVAGLVE WPVVLMGDIA DDFIPLPPEV LQTSMREHQK FFSVKNPKTD RIEKFITVAN
VETADNGATI LAGNQKVLFA RLADAKFFWE NDIREAEAGG QKWLDSLTNV TFHNKLGTQA
ARIDRIASLA RAIAPSIGAD PDLSERAARW AKADLSSEMV YEFPELQGLM GKYYAGPAGH
PVEVANAATE HYSPLGPSDD VPSAPTSVAV ALADKLDTLT GFWAIDEKPT GSKDPFALRR
AALGVIRLVL ENGHRVGLSG LAKESQAISD MPRVERLKNS VYSEIHNSWE YGDSLPEHIV
IKVGEDGSDL VKRISEGYPI RPAAKFRHIA QQADELADLY AEKDKVEKWL NSFDPQRSNL
LSFFHDRLKV YLKDQGIRHD VIDACLAMPG NDDLTLLVKR AEALSGLLKT DDGENLLQGF
KRANNILTQA EEKDGVEYSY GADVKFAEDD SEKALFAALD TAEAAIQPAM QTEDFAAAMT
SMAALRAPID AFFEAVQINT ENEIIRRNRL NLLSRIRQIC LSVADLTKVE G
//
