ID S5YWT5_PARAH Unreviewed; 703 AA.
AC S5YWT5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=JCM7686_2603 {ECO:0000313|EMBL:AGT09671.1};
OS Paracoccus aminophilus JCM 7686.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT09671.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT09671.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT09671.1};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(2014).
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; CP006650; AGT09671.1; -; Genomic_DNA.
DR RefSeq; WP_020951309.1; NC_022041.1.
DR AlphaFoldDB; S5YWT5; -.
DR STRING; 1367847.JCM7686_2603; -.
DR KEGG; pami:JCM7686_2603; -.
DR PATRIC; fig|1367847.3.peg.2609; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000015480; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000015480}.
FT DOMAIN 591..690
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
FT REGION 57..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..224
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 703 AA; 76579 MW; 32114C2CB98D0483 CRC64;
MPDLLIELFS EEIPARMQAR AREDLKKLVT DGLVEAGLTY ASAGAFSTPR RLTLAIEGLS
AQSPTTREER KGPRTDAPEA ALEGFLRSTG LSRDQLEARD EKKGQVWFAT ITKPGRPAAE
IIAEVLEATI RNFPWPKSMR WGAGSLRWVR PLHTILCILT DEAGAQVVPL SVEGVTSGDT
TRGHRFMAPD AFAVTSFDDY ATKLRRARVM LDSAERQAAI WQEAQNLAFA RGWEIVEDQG
LLAEVAGLVE WPVPLMGQIE ERFLALPPEV LQTSMKEHQK FFSARNPKTG RIEGFVTVAN
IEAPDHGETI LKGNQRVLAA RLSDAAFFWD LDLREAKAGM QDWAEGLKSV TFQSKLGSQA
DRISRIAALA REIAPLVGAD PDQAEEAAKI AKLDLRSAMV GEFPELQGTM GRYYALEAGK
APEVADAARD HYSPLGPSDA VPSAPVSVAV ALADKLDTLT GFWAIDEKPT GSKDPFALRR
AALGVIRLVL GNGVRAKLAT VVANYQNYID DETGIIWEEA GEDYIGNTTQ GLLSFFHDRL
KVFLKDEGIR HDIIDAVLAM PGNDDLVLLV NRARALSDVL KTEDGTNLLQ GLKRAANILA
QAEAKDGVEY SYGADPKFAE TEEERALFAA LTTAEPAIKA AVNAEDFPAA TSAIAALRAP
IDAFFEAVQI NTDNQTVRRN RLNLLSQIRQ AGALIADFSK IEG
//
