ID A0A0D2QT74_GOSRA Unreviewed; 779 AA.
AC A0A0D2QT74;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030466};
GN ORFNames=B456_009G347600 {ECO:0000313|EMBL:KJB61242.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB61242.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB61242.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000948};
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; CM001748; KJB61242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2QT74; -.
DR EnsemblPlants; KJB61242; KJB61242; B456_009G347600.
DR Gramene; KJB61242; KJB61242; B456_009G347600.
DR Proteomes; UP000032304; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR CDD; cd00807; GlnRS_core; 1.
DR Gene3D; 1.10.10.2420; -; 1.
DR Gene3D; 1.10.8.1290; Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1, domain 1; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
DR InterPro; IPR042559; Gln-tRNA-synth_Ib_RNA-bd_N_2.
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 Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR Pfam; PF04557; tRNA_synt_1c_R2; 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:UP000032304}.
FT DOMAIN 10..167
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04558"
FT DOMAIN 171..247
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04557"
FT DOMAIN 270..574
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 577..681
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT DOMAIN 691..749
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 185..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 89362 MW; 40DFA3BDEE70F361 CRC64;
MVVKGEESDK ILELFLKIGL DERTARNTIA NNKVTANLTA VIHEAALANG CDRAIGNFLY
TVATKYPANA LVHRPKLLEY VVSSKIKTPA QLEAAFSFLS NVASEEFKRN EFEEACGVGV
EVSLEELTQT VNEIFEENKA VILERRYRTN VGELFGSIRK KHPWADPKMA KQLVDAKMYE
LLGERTAADD EKPSKKKEKK EKPAKVEKAV VDETPAQPSE EELNPFSIFP APEDNIKVHT
EVFFSNGSVL RCCNTRERLD NHLKVTGGRV FTRFPPEPNG YLHIGHAKAM FVDFGLAKER
GGCCYLRYDD TNPEAEKKEY INHIEEIVQW MGWEPFKITY TSDYFPELYE LAVELIRRGH
AYVDHQTPEE IKEYREKKMN SPWRDRPIAE SLKLFDDMKR GLIEEGKATL RMKQDMQSDN
FNMYDLIAYR IKFTPHPHAG DKWCIYPSYD YAHCIVDSLE NITHSLCTLE FETRRASYYW
LLHVLDLYQP YVWEYSRLNV TNTVMSKRKL NYIVTNKYVD GWDDPRLMTL AGLRRRGVTS
TAINSFVRGI GITRSDCSMI RLDRLEYHIR EELNKTAPRV LVVLHPLKVV ITNLESGSVL
DLDAKKWPDA RTDDTSAFYK VPFSNVVYIE RSDFRMKDSK DYYGLAPGKS ALLRYAFPIK
CTDVILADDK ETVLEIRAEY DASKKSKPKG VLHWVAEPSP GSYPLKIEVR LFDKLFNSEN
PAELDNWLTD LNPNSKVVVT TAYAVPSLGY FTVDKDSTAE KLVFNRTVTL KDTYSKGGK
//
