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Database: UniProt
Entry: A0A238JQ29_9RHOB
LinkDB: A0A238JQ29_9RHOB
Original site: A0A238JQ29_9RHOB 
ID   A0A238JQ29_9RHOB        Unreviewed;       287 AA.
AC   A0A238JQ29;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Glutamate--tRNA ligase {ECO:0000313|EMBL:SMX32769.1};
DE            EC=6.1.1.17 {ECO:0000313|EMBL:SMX32769.1};
GN   Name=gltX_1 {ECO:0000313|EMBL:SMX32769.1};
GN   ORFNames=PEV8663_00105 {ECO:0000313|EMBL:SMX32769.1};
OS   Pelagimonas varians.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Pelagimonas.
OX   NCBI_TaxID=696760 {ECO:0000313|EMBL:SMX32769.1, ECO:0000313|Proteomes:UP000220836};
RN   [1] {ECO:0000313|EMBL:SMX32769.1, ECO:0000313|Proteomes:UP000220836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8663 {ECO:0000313|EMBL:SMX32769.1,
RC   ECO:0000313|Proteomes:UP000220836};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363037}.
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DR   EMBL; FXYH01000001; SMX32769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238JQ29; -.
DR   OrthoDB; 9807503at2; -.
DR   Proteomes; UP000220836; 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:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF1; GLUTAMYL-Q TRNA(ASP) SYNTHETASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 2.
DR   PRINTS; PR00987; TRNASYNTHGLU.
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|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220836}.
FT   DOMAIN          3..104
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          188..278
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
SQ   SEQUENCE   287 AA;  31908 MW;  BB2B5F0BE3200299 CRC64;
     MLITRFAPSP TGPLHLGHAY SAIVAHDMAR QAKGRFLLRI EDIDQTRSRP RWETQIYEDL
     AWLGIRWDDS PVRQSDRITS YVDALKQLWS RGFVYPCHCR RKDILAAASA PQEGVEPAYG
     PDGLVYPGTC RPSGLGGLGE MPTDTVLRLN MHRALAECDD LSFTEIGPLG YKTGQNIGIS
     RTELVDCVGD IILSRKDFAG SYHLSVVLDD AAQGITHVIR GQDLFEATKI HVVLQQLLGL
     PTPVYLHHPL IRDENGKRLA KRDDARAISK YRDDGVTAGE IRKMVGL
//
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