UniProt: A8XZU2

Database: UniProt
Entry: A8XZU2_CAEBR

LinkDB:  A8XZU2_CAEBR 
Original site:  A8XZU2_CAEBR

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   WORMBASE (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   A8XZU2_CAEBR            Unreviewed;       787 AA.
AC   A8XZU2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00019404};
DE            EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
DE   AltName: Full=Diadenosine tetraphosphate synthetase {ECO:0000256|ARBA:ARBA00030057};
GN   Name=gars-1 {ECO:0000313|WormBase:CBG21320};
GN   Synonyms=Cbr-gars-1 {ECO:0000313|EMBL:CAP38159.2};
GN   ORFNames=CBG21320 {ECO:0000313|WormBase:CBG21320}, CBG_21320
GN   {ECO:0000313|EMBL:CAP38159.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP38159.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP38159.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP38159.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H(+) = diphosphate + P(1),P(4)-bis(5'-adenosyl)
CC         tetraphosphate; Xref=Rhea:RHEA:34935, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58141;
CC         Evidence={ECO:0000256|ARBA:ARBA00000713};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34936;
CC         Evidence={ECO:0000256|ARBA:ARBA00000713};
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:ARBA00001768};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16014;
CC         Evidence={ECO:0000256|ARBA:ARBA00001768};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; HE600993; CAP38159.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XZU2; -.
DR   STRING; 6238.A8XZU2; -.
DR   WormBase; CBG21320; CBP39486; WBGene00040130; Cbr-gars-1.
DR   eggNOG; KOG2298; Eukaryota.
DR   HOGENOM; CLU_015515_1_0_1; -.
DR   InParanoid; A8XZU2; -.
DR   OMA; MEMQYFV; -.
DR   OrthoDB; 546660at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070150; P:mitochondrial glycyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00774; GlyRS-like_core; 1.
DR   CDD; cd00858; GlyRS_anticodon; 1.
DR   CDD; cd00935; GlyRS_RNA; 1.
DR   Gene3D; 3.30.40.230; -; 1.
DR   Gene3D; 3.30.720.200; -; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR   InterPro; IPR033731; GlyRS-like_core.
DR   InterPro; IPR002315; tRNA-synt_gly.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   InterPro; IPR000738; WHEP-TRS_dom.
DR   NCBIfam; TIGR00389; glyS_dimeric; 1.
DR   PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF00458; WHEP-TRS; 1.
DR   PRINTS; PR01043; TRNASYNTHGLY.
DR   SMART; SM00991; WHEP-TRS; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS51185; WHEP_TRS_2; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          115..171
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          172..665
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   787 AA;  89698 MW;  F84F72F90FF9CA37 CRC64;
     MLSGYLFKNI RTTQRLLRNF SSDAKFFKVR KPSRKQNKLG LEKEKRRKNK LQSTQFFYIA
     ARARSPYQEV EVVSNNRKAP LQTQRKSIAP RFEKKTRQKI SDYLKQMATP EIEAQLAPLR
     AAVKEYGDLI RDLKAKQAPK IDIDKAVVEL KARKKLLEET EIALAPKEAS FDRLKLEDLL
     KRRFFYDQSF AIYGGVTGLY DFGPMGCALK ANMLQQWRKH FILEEGMLEV DCTSLTPEPV
     LKASGHVDRF ADWMVKDTKN GECFRADHLI KNSIEKLMNV SKIDKKVSAE IKKDGEDVLA
     RLEGFDDKDM HEVITRFKFK SPITGNDLTE PIAFNLMFPT QIGPTGDFKA FLRPETAQGI
     FVNFKRLLEF NQGKLPFAAA QIGLGFRNEI SPRQGLIRVR EFTMCEIEHF VDPEDKRFPK
     FAKVADEKLV LFSACNQLDG APAREVAIGE AVANKTVANE TLGYYMARCH QFLMKVGIDG
     RRLRFRQHLS NEMAHYAQDC WDAEILTSYG WIECVGNADR ACYDLQQHYK ATNVKLVAEK
     KLPEPVDVDI VEAQANMALL GKKYKKEAKK IQTALQQLTS EQVTAIEAEL VAKQLYNLDI
     NGEKFELAPD LVNIKKYSKK IHVQEITPSV IEPSYGIGRI MYALLEHSFR QREGDEQRTF
     LAFKPLVAPI KCSILPISAN DTLVPVMDAV KEELSHYELS YKVDDSSGTI GRRYARTDEI
     GIPFGITVDF ESGKTTPYTV TIRHAETMSQ IRLEVSELGR LISDLVSGRQ QWSDAQAKYP
     KFEASAE
//

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