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Database: UniProt
Entry: A0A1G9CH56_9RHOB
LinkDB: A0A1G9CH56_9RHOB
Original site: A0A1G9CH56_9RHOB 
ID   A0A1G9CH56_9RHOB        Unreviewed;       763 AA.
AC   A0A1G9CH56;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN04487971_101214 {ECO:0000313|EMBL:SDK50824.1};
OS   Paracoccus chinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=525640 {ECO:0000313|EMBL:SDK50824.1, ECO:0000313|Proteomes:UP000199555};
RN   [1] {ECO:0000313|EMBL:SDK50824.1, ECO:0000313|Proteomes:UP000199555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7655 {ECO:0000313|EMBL:SDK50824.1,
RC   ECO:0000313|Proteomes:UP000199555};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNGE01000001; SDK50824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9CH56; -.
DR   STRING; 525640.SAMN04487971_101214; -.
DR   Proteomes; UP000199555; 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          651..749
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   763 AA;  83089 MW;  2DA7CDED69E012BB CRC64;
     MDLLIELFSE EIPARMQPRA REDLKRLITD GLVDAGLTYA SAGAFSTPRR LALAVEGLTA
     ESKPVREERK GPRTDAPEKA IEGFLRSTGL TLDQLERRAE KKGEVFFAVI EKPGRKAADI
     VAEVLEATIR DFPWPKSMRW GSGSLRWVRP LHSIIAILSD EGGAQVVPLT VDGIAAGDTT
     RGHRFMAPDA FRVTGFDDYA AKLRRAKVML DPAEREAAIR QEAANLAFAR GWEIVSDEGL
     MTELAGLVEW PVPLMGVIEQ RFLDLPPEVL QTSMKEHQKF LSARNPKTGR IEGYVTVANI
     ETPDHGATIL AGNQRVLAAR LSDAAFFWEN DLREARAGMQ AWAEGLKAVT FHAKLGSQAD
     RVERIAALAR EIAPAVGADP DQAEQAAKVA KLDLRSAMVG EFPELQGTMG RYYAQAAGLP
     DAVADAARDH YSPLGPSDEV PSAPVSVAVA LADKYNILGH FFAAKEKPTG SKDPFALRRA
     ALGMIRLIVD NSVRLSLEYL VSKDIDGASF VYAMHNGAAL MTGQPDGSTV ITDFNSAMVL
     GNQFPDTFGR ARSQMLEMFE TGHDDFVKLV DDKPAGRFPT KREVLELLAA DLLAFLHDRL
     KVHLRDQGIR HDVIDAVLAM LGSDDLTLVV RRATALNGML GTGDGPNLLQ GLKRAANILA
     QAEEKDGVEY SFGADPKFAE TDEERALFAA LDAAEPKIAA AMRAEDFPAA MSAIAALRAP
     IDAFFEAVQV NTDNQVVRRN RLNLLSRIRE AGRLIADFGR IEG
//
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