ID SYQ_ARATH Reviewed; 795 AA.
AC Q8W4F3; A4UVN3;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 149.
DE RecName: Full=Glutamine--tRNA ligase, cytoplasmic {ECO:0000305};
DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000305};
DE Short=GlnRS {ECO:0000305};
DE AltName: Full=Protein OVULE ABORTION 9 {ECO:0000303|PubMed:16297076};
GN Name=OVA9 {ECO:0000303|PubMed:16297076};
GN OrderedLocusNames=At1g25350 {ECO:0000312|Araport:AT1G25350};
GN ORFNames=F4F7.26 {ECO:0000312|EMBL:AAG28806.2};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA Berg M., Rogers R., Muralla R., Meinke D.;
RT "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT development in Arabidopsis.";
RL Plant J. 44:866-878(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
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:0000250|UniProtKB:P47897};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277,
CC ECO:0000305|PubMed:16297076}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8W4F3-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Lethal. In heterozygous plants, aborted ovules.
CC {ECO:0000269|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG28806.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079374; AAG28806.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30610.1; -; Genomic_DNA.
DR EMBL; AY062594; AAL32672.1; -; mRNA.
DR EMBL; AY114653; AAM47972.1; -; mRNA.
DR PIR; D86381; D86381.
DR RefSeq; NP_173906.2; NM_102345.4. [Q8W4F3-1]
DR AlphaFoldDB; Q8W4F3; -.
DR SMR; Q8W4F3; -.
DR STRING; 3702.Q8W4F3; -.
DR iPTMnet; Q8W4F3; -.
DR PaxDb; 3702-AT1G25350-2; -.
DR ProteomicsDB; 228054; -. [Q8W4F3-1]
DR EnsemblPlants; AT1G25350.1; AT1G25350.1; AT1G25350. [Q8W4F3-1]
DR GeneID; 839120; -.
DR Gramene; AT1G25350.1; AT1G25350.1; AT1G25350. [Q8W4F3-1]
DR KEGG; ath:AT1G25350; -.
DR Araport; AT1G25350; -.
DR TAIR; AT1G25350; OVA9.
DR eggNOG; KOG1148; Eukaryota.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; Q8W4F3; -.
DR PhylomeDB; Q8W4F3; -.
DR PRO; PR:Q8W4F3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W4F3; baseline and differential.
DR Genevisible; Q8W4F3; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..795
FT /note="Glutamine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000433534"
FT REGION 188..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 277..287
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 505..509
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT COMPBIAS 188..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 278..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 284..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 310
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 450
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 498..499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 506..508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
SQ SEQUENCE 795 AA; 91247 MW; 3B5D9FE912B54376 CRC64;
MVLKDDNSEK SIELFISIGL DEKTARNTIN NNKVTANLTA VIHEAAVTDG CDRNTGNLLY
SVATKFPTNA LVHRPTLLKY IVNSKIKTPA QLEAAFAFFA STGPEDFKLN EFEEACGVGI
EVSPEDIEKA VKGIFEENKK TILEQRYRTN VGELFGHVRK SLPWADPKIV KKLIDEKMYE
LLGEKTAADN EKPTKKKEKK EKPAKVEEKK AVVETTAEPS EEELNPYTIF PQPEQNFMVH
TEVFFSDGSI LRCSNTKEVL DKHLKVTGGK VYTRFPPEPN GYLHIGHAKA MFVDFGLAKE
RGGCCYLRYD DTNPEAEKEE YINHIEEIVK WMGWEPFKIT YTSDYFQELY DLAVELIRRG
HAYVDHQTAD EIKEYREKKM NSPWRDRPIE ESLKLFDEMR RGIIEEGKAT LRMKQDMQSD
NFNMYDLIAY RIKFAPHPKA GDKWCIYPSY DYAHCTVDSL ENITHSLCTL EFETRRASYY
WLLHSLSLYM PYVWEYSRLN VTNTVMSKRK LNYIVTNKYV DGWDDPRLLT LSGLRRRGVT
STAINAFVRG IGITRSDGSM IHVSRLEHHI REELNKTAPR TMVVLNPLKV VITNLESDKL
IELDAKRWPD AQNDDPSAFY KVPFSRVVYI DQSDFRMKDS KDYYGLAPGK SVLLRYAFPI
KCTNVVFADD NETVREIHAE YDPEKKSKPK GVLHWVAESS PGEEPIKVEV RLFEKLFNSE
NPAELNDAWL TDINPNSKMV ISGAYAVSTL KDAAVGDRFQ FERLGYYAVD KDSEPGKLVF
NRTVTLRDSY GKGGK
//
