ID   A4HWN1_LEIIN            Unreviewed;       570 AA.
AC   A4HWN1; A0A2K4YQL7; A0A381MDX5;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 104.
DE   RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE            EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN   ORFNames=LINJ_15_1490 {ECO:0000313|EMBL:CAM66861.1};
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM66861.1, ECO:0000313|Proteomes:UP000008153};
RN   [1] {ECO:0000313|EMBL:CAM66861.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM66861.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM66861.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM66861.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Gln) + L-glutamine + ATP = L-glutaminyl-tRNA(Gln) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662, Rhea:RHEA-
CC         COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78521, ChEBI:CHEBI:456215;
CC         EC=6.1.1.18; Evidence={ECO:0000256|ARBA:ARBA00048270};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363037}.
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DR   EMBL; FR796447; CAM66861.1; -; Genomic_DNA.
DR   RefSeq; XP_001464472.1; XM_001464435.1.
DR   AlphaFoldDB; A4HWN1; -.
DR   SMR; A4HWN1; -.
DR   FunCoup; A4HWN1; 608.
DR   STRING; 5671.A4HWN1; -.
DR   GeneID; 5067867; -.
DR   KEGG; lif:LINJ_15_1490; -.
DR   VEuPathDB; TriTrypDB:LINF_150022500; -.
DR   eggNOG; KOG1148; Eukaryota.
DR   InParanoid; A4HWN1; -.
DR   OMA; TWCIYPM; -.
DR   Proteomes; UP000008153; Chromosome 15.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR   FunFam; 3.40.50.620:FF:000037; Glutamine--tRNA ligase cytoplasmic; 1.
DR   FunFam; 2.40.240.10:FF:000037; Putative glutaminyl-tRNA synthetase; 1.
DR   FunFam; 2.40.240.10:FF:000038; Putative glutaminyl-tRNA synthetase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.240.10; Ribosomal Protein L25, Chain P; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004514; Gln-tRNA-synth.
DR   InterPro; IPR050132; Gln/Glu-tRNA_Ligase.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   NCBIfam; TIGR00440; glnS; 1.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 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:UP000008153}.
FT   DOMAIN          51..351
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          354..453
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          465..536
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
SQ   SEQUENCE   570 AA;  66010 MW;  8960B8D753616A43 CRC64;
     MAGPAAAEVK EMETKRDLSI LQNGRPVPGC RNTRELLEAH EKVTGGKPYF RFPPEPNGFL
     HIGHAKSMNL NFGSARAHGG KCYLRYDDTN PESEDQVYID AIMEMVDWMG WKPDWVTFSS
     DYFDQLHTFA VQLIKDGKAY VDHSTPDELK QQREQREDSP WRNRSVEENL LLFKHMRQGR
     YAEGEATLRV KADMKSDNPN MRDFIAYRVK YVEHPHIKDK WCIYPSYDFT HCLIDSLEDI
     DYSLCTLEFE TRRESYFWLL NELNLWRPYV WEFSRLNVTG SLLSKRKINV LVRKGIVRGF
     DDPRLLTLAG MRRRGYTPAA INRFCELVGI TRSMNVIQIS MLENTLREDL DERCERRLMV
     IDPIKVVVDN WKGERIFECP NHPRKPELGS RALTFTDTFY VDRSDFHTDD DNSKFYGLAP
     GPRVVGLKYS GNVVCKSFEV DAKGQPMVIH VDIDFERKDK PKTNISWVSA TACTPVEVRL
     YNALLKDDRA AIDPEFLKFI DEKSEVVSHG YAEKGVENFK HFESVQAERF GYFVVDPDTT
     ADHLVMNRVL GLREDKSKAT VAEPVPAKRK
//