UniProt: A0A151IJY4

Database: UniProt
Entry: A0A151IJY4_9HYME

LinkDB:  A0A151IJY4_9HYME 
Original site:  A0A151IJY4_9HYME

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Ontology (5)   
   GO (5)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
All databases (22)   

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ID   A0A151IJY4_9HYME        Unreviewed;       510 AA.
AC   A0A151IJY4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   ORFNames=ALC62_05260 {ECO:0000313|EMBL:KYN03959.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN03959.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYN03959.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYN03959.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN03959.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KQ977294; KYN03959.1; -; Genomic_DNA.
DR   RefSeq; XP_018394238.1; XM_018538736.1.
DR   AlphaFoldDB; A0A151IJY4; -.
DR   STRING; 456900.A0A151IJY4; -.
DR   GeneID; 108773031; -.
DR   OrthoDB; 5404395at2759; -.
DR   Proteomes; UP000078542; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
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:UP000078542}.
FT   DOMAIN          24..335
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          377..508
FT                   /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19269"
SQ   SEQUENCE   510 AA;  58767 MW;  C21622E8E908D194 CRC64;
     MQRNILRATS LQLLQRRLFK KYHVRVRFAP SPTGHLHLGG LRTALYNYLF ARSNNGAFIL
     RIEDTDQTRT ISGAIEKIQD DLLWAGIISD EDPTRGGPVG PYVQSSRLEL YKEQVLKLLN
     NGSAYYCFCT EKRLDLLRKE AMKCGQIPKY DNRCRHLTKD EVKEMLRKNL AYCIRFKLTS
     TSEVFHDLVY GDVFHDITKS EGDPVIIKSD GYPTYHFANV VDDHFMEISH VLRGVEWQVS
     TPKHIMLHKA FGWNPPIYGH LPLIMNSDGS KLSKRQGDIK IDSFRKQGIF PLALLNYVIG
     AGGGFHKEQE SQDLYTYQEL IKQFDITKIK PSSGKLMPDK LWEFNKLEMT NLLQNERNHK
     FFIERIKKLV SEAFPEWKND GNLQLDDDHI ITTFKWAQNR VTTLNDLVKK DLAFLWIIPS
     SIPNVKQDGY SDTIKLLNAE LVEIDANNYN TDWMTPYLKE FAKKNGIPFP ALMKTLRSVM
     SGVNVGPPVA EMMEILGKDR TLSRLQRCVS
//

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