ID A0A1Z1FEQ4_9SPHN Unreviewed; 698 AA.
AC A0A1Z1FEQ4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=A9D14_06405 {ECO:0000313|EMBL:ARU17299.1};
OS Croceicoccus marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=450378 {ECO:0000313|EMBL:ARU17299.1, ECO:0000313|Proteomes:UP000195807};
RN [1] {ECO:0000313|EMBL:ARU17299.1, ECO:0000313|Proteomes:UP000195807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E4A9 {ECO:0000313|EMBL:ARU17299.1,
RC ECO:0000313|Proteomes:UP000195807};
RA Wu Y.-H., Cheng H., Xu L., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT "Complete genome sequence of esterase-producing bacterium Croceicoccus
RT marinus E4A9.";
RL Submitted (JAN-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}.
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DR EMBL; CP019602; ARU17299.1; -; Genomic_DNA.
DR RefSeq; WP_066848458.1; NZ_CP019602.1.
DR AlphaFoldDB; A0A1Z1FEQ4; -.
DR STRING; 450378.GCA_001661675_01284; -.
DR KEGG; cman:A9D14_06405; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000195807; 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:UP000195807}.
FT DOMAIN 562..688
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 698 AA; 75740 MW; A488A570E0B86B0B CRC64;
MTDFLLELLC EEIPARMQAG ARADLERLFR AEMEAAGVAH GALTVWSTPR RLAMIAADMP
ERTEAVSEEA KGPPEGAPDA AIDGFCKKNG VTRDQLELRE VKGRNTWFAV RNVPGRAVAD
VLAEAIPSIV RAFPWPKSMR WGDASISTES LRWVRPLQGI VAILGEELVS CEVGGVASSY
ATVGHRFHHS GEVTIGGAND YAEKLRACHV IVDHAERQDM IRTKAREAAE ASGLTLVEDE
GLVVENAGLT EWPEPLLGLF DEDYLAVPPE VIQLTARVNQ KYFVCEDGAG RLANAFVCTA
NISAADPAVV VDGNRKVLAA RLSDARFFWD TDRKVPLGEQ ASKLARITFH EKLGTLADKV
ERVAKLARQL AEEGIVPAAD PDRAELAARL AKADLVTEMV GEFPELQGLM GGYYARAEGL
PDAVADAIRD HYKPVGQGDA VPTAPVTVAV SLADKLDNLR SFFAIDEKPT GSKDPFALRR
AALGVIRIVT QNRLRLAIAD GDLLDFLADR LKVQQREAGV RHDLIDAVFA LGEEDDLVRL
LARVHALQSF MENEDGANLL AGYKRAANIL KKEDYKGTDD RIARTGEEDP LALVDDPELG
SILAQRGHTN PDHAPEPAEA ELIAALDKAA PAASDAVESE RFEEAMAALA SLRGPIDAFF
DHVTVNDPDP ATREARLALL DRFRAAVHKV ADFSRIEG
//