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SYQ_ARATH
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   03-AUG-2022, entry version 141.
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.AT1G25350.2; -.
DR   iPTMnet; Q8W4F3; -.
DR   PaxDb; Q8W4F3; -.
DR   PRIDE; Q8W4F3; -.
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   eggNOG; KOG1148; Eukaryota.
DR   HOGENOM; CLU_001882_2_3_1; -.
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   Gene3D; 1.10.10.2420; -; 1.
DR   Gene3D; 1.10.8.1290; -; 1.
DR   Gene3D; 2.40.240.10; -; 2.
DR   Gene3D; 3.40.50.620; -; 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_L25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR   Pfam; PF04557; tRNA_synt_1c_R2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   TIGRFAMs; TIGR00440; glnS; 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
 
 
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