UniProt: C3YJE6

Database: UniProt
Entry: C3YJE6_BRAFL

LinkDB:  C3YJE6_BRAFL 
Original site:  C3YJE6_BRAFL

All links

Ontology (6)   
   GO (6)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (25)   

Download RDF

ID   C3YJE6_BRAFL            Unreviewed;       543 AA.
AC   C3YJE6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial {ECO:0000256|ARBA:ARBA00044142};
DE            EC=6.1.1.17 {ECO:0000256|ARBA:ARBA00012835};
DE            EC=6.1.1.24 {ECO:0000256|ARBA:ARBA00044054};
DE   AltName: Full=Glutamate--tRNA(Gln) ligase EARS2, mitochondrial {ECO:0000256|ARBA:ARBA00044313};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030865};
DE   AltName: Full=Mitochondrial glutamyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00044251};
GN   Name=LOC118427702 {ECO:0000313|RefSeq:XP_035693497.1};
GN   ORFNames=BRAFLDRAFT_265112 {ECO:0000313|EMBL:EEN59545.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN59545.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59545.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN59545.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
RN   [2] {ECO:0000313|RefSeq:XP_035693497.1}
RP   IDENTIFICATION.
RC   STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035693497.1};
RC   TISSUE=Testes {ECO:0000313|RefSeq:XP_035693497.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Gln) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Gln); Xref=Rhea:RHEA:64612, Rhea:RHEA-COMP:9662,
CC         Rhea:RHEA-COMP:9684, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00043804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64613;
CC         Evidence={ECO:0000256|ARBA:ARBA00043804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00043725};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23541;
CC         Evidence={ECO:0000256|ARBA:ARBA00043725};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Glx) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glx); Xref=Rhea:RHEA:18397, Rhea:RHEA-COMP:9713,
CC         Rhea:RHEA-COMP:9716, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00043717};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18398;
CC         Evidence={ECO:0000256|ARBA:ARBA00043717};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007894}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG666520; EEN59545.1; -; Genomic_DNA.
DR   RefSeq; XP_002603534.1; XM_002603488.1.
DR   RefSeq; XP_035693497.1; XM_035837604.1.
DR   STRING; 7739.C3YJE6; -.
DR   KEGG; bfo:118427702; -.
DR   eggNOG; KOG1149; Eukaryota.
DR   InParanoid; C3YJE6; -.
DR   OMA; EAFKWVG; -.
DR   OrthoDB; 5404395at2759; -.
DR   Proteomes; UP000001554; Chromosome 12.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00808; GluRS_core; 1.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR   InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR033910; GluRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363037};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363037};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001554}.
FT   DOMAIN          43..358
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          400..527
FT                   /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19269"
SQ   SEQUENCE   543 AA;  62209 MW;  F171678411FE3CE0 CRC64;
     MQINSFGGTM RLLLKIPQYS SLGLHHSVRG VCCSRALLSC SDVRVRFAPS PTGMLHLGGL
     RTALYNYLFA KAHNGSFIIR IEDTDRTRLV PGSEESLEEM LRWAGLEPDE GPTKSGKFGP
     YRQSERVHIY KEKTQELIER GSAYYCFCTP HRLELLRKEA ARRKEVPRYD NRCRQLSQEE
     CRRRLEDGVP HVVRFKLEEN AQPFTDLVFG ITRHDVASVE GDPVIMKGDG FPTYHLANVV
     DDHLMQISHV LRGQEWLIST GKHLMLYRAF GWTPPQFAHL PLLVNKDGTK LSKRQGDIFA
     NHFREKGYLP QAVLNFITFC GAGFHDNRKV RTLEDMVAEF SLARVVEHPA RLDWDRLQEF
     QREHLARLFG THHGQTQIVQ NLRELIVQQY GERFSGSSIL LDEYILKVLE TRMGHFTLLS
     DLVSPDFQYL WGQPDITVQE LSMITCHASS VLRTVHKALQ DMSTNQFTLE EVGIKLRDVS
     KTHKAVKYST LMKMLRFVLS GRQVGPSVAE MMTTLGQTET LKRLINALSL LDNGTKTKDT
     ERR
//

DBGET integrated database retrieval system