ID A0A1W6CVR1_9RHOB Unreviewed; 770 AA.
AC A0A1W6CVR1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=B0A89_04180 {ECO:0000313|EMBL:ARJ68947.1};
OS Paracoccus contaminans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ68947.1, ECO:0000313|Proteomes:UP000193017};
RN [1] {ECO:0000313|EMBL:ARJ68947.1, ECO:0000313|Proteomes:UP000193017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC {ECO:0000313|Proteomes:UP000193017};
RA Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT "Genome sequence of Paracoccus contaminans isolated from a water
RT microcosm.";
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}.
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DR EMBL; CP020612; ARJ68947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6CVR1; -.
DR STRING; 1945662.B0A89_04180; -.
DR KEGG; pcon:B0A89_04180; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000193017; 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:UP000193017}.
FT DOMAIN 658..758
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 770 AA; 83858 MW; 548C2170A0D264D8 CRC64;
MMDLLIELFS EEIPARMQAR ARQDLQRLVT EGLVDAGLTY RSAGAFSTPR RLALAVEGLD
AASKPVREER KGPRTDAPDA ALQGFLRSTG LTLDQLERRA DKKAEVYFAV ITRPGRPAAA
IVAEVLERTI RDFPWPKSMR WGSGTLRWVR PLHSIIALLT DEAGAQVVPL TVDGITAGDT
TRGHRFMAPD AFSVTGFDDY AAKLRRARVM LDPAEREAAI RQEAANLAFA RGWEIVPDDA
LMTELAGLVE WPVPLMGVIE ERFLSLPSEV LQTSMKEHQK FLSARNPATG RIEGYVTVAN
IETPDQGATI LHGNQRVLAA RLSDAAFFWS NDLREAKAGM KDWAEGLKAV TFHAKLGSQH
DRIERIAALA REIAPAVGAD PALAEQAARV AKLDLRSAMV GEFPELQGTM GRYYALEAGL
DAAVADAARD HYSPLGPSDA VPSAPVSVAV ALADKLDTLT GFWAIDEKPT GSKDPYALRR
AALGVIRLVL GNGVRVGVNQ IVQSASSGCW YYSTLSEGIA VHSSQSGPAK DWRRLGVPDP
QTGVVEHCLS FEDFRQALLE DRVRDFYGTV FDDLDADGAG GENRIVSGDD RLHRLNSDLL
AFLHDRLKVH LREQGIRHDV IDAVLAMPGS DDLTLVVARA TALNAMLATE DGTNLLQGLK
RAANILAQAE DKDGVEYSFG ADPKFAETDA ERALFAALDA AEPRIEAAMQ AEDFPAAMSA
IAALRAPIDA FFGSVQVNTD NQMVRRNRLN LLHRIRETGR RIADFSRIEG
//
