SYQ_YEAST
ID SYQ_YEAST Reviewed; 809 AA.
AC P13188; D6W2M6; Q12005;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Glutamine--tRNA ligase;
DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE AltName: Full=Glutaminyl-tRNA synthetase;
DE Short=GlnRS;
GN Name=GLN4; OrderedLocusNames=YOR168W; ORFNames=O3601;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3301841; DOI=10.1016/s0021-9258(18)61034-8;
RA Ludmerer S.W., Schimmel P.;
RT "Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal
RT extension and provides a strong confirmation of the signature sequence for
RT a group of the aminoacyl-tRNA synthetases.";
RL J. Biol. Chem. 262:10801-10806(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RX PubMed=8972579;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1563::aid-yea44>3.0.co;2-m;
RA Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
RT "Analysis of a 22,956 bp region on the right arm of Saccharomyces
RT cerevisiae chromosome XV.";
RL Yeast 12:1563-1573(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 -!- MISCELLANEOUS: Present with 37500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; M29184; AAA34646.1; -; Genomic_DNA.
DR EMBL; M29185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U55021; AAB47415.1; -; Genomic_DNA.
DR EMBL; Z75076; CAA99374.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10942.1; -; Genomic_DNA.
DR PIR; S67056; SYBYQT.
DR RefSeq; NP_014811.3; NM_001183587.3.
DR PDB; 3TL4; X-ray; 2.30 A; X=1-187.
DR PDB; 4H3S; X-ray; 2.15 A; A=1-809.
DR PDBsum; 3TL4; -.
DR PDBsum; 4H3S; -.
DR AlphaFoldDB; P13188; -.
DR SMR; P13188; -.
DR BioGRID; 34564; 264.
DR IntAct; P13188; 1.
DR MINT; P13188; -.
DR STRING; 4932.YOR168W; -.
DR iPTMnet; P13188; -.
DR MaxQB; P13188; -.
DR PaxDb; P13188; -.
DR PRIDE; P13188; -.
DR EnsemblFungi; YOR168W_mRNA; YOR168W; YOR168W.
DR GeneID; 854339; -.
DR KEGG; sce:YOR168W; -.
DR SGD; S000005694; GLN4.
DR VEuPathDB; FungiDB:YOR168W; -.
DR eggNOG; KOG1148; Eukaryota.
DR GeneTree; ENSGT00940000168831; -.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; P13188; -.
DR OMA; INNFCAQ; -.
DR BioCyc; YEAST:G3O-33684-MON; -.
DR BRENDA; 6.1.1.18; 984.
DR BRENDA; 6.3.5.7; 984.
DR PRO; PR:P13188; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P13188; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..809
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_0000195866"
FT REGION 185..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 258..268
FT /note="'HIGH' region"
FT MOTIF 495..499
FT /note="'KMSKS' region"
FT COMPBIAS 185..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 265..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 291
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 440
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 488..489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 496..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 179
FT /note="G -> Q (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:3TL4"
FT TURN 110..114
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3TL4"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 267..281
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 300..312
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:4H3S"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 440..450
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 466..475
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 498..506
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 521..527
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 531..541
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 552..566
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 572..581
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 590..597
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 648..655
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 661..668
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 698..706
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 709..713
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 722..725
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 730..739
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 743..748
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 755..758
FT /evidence="ECO:0007829|PDB:4H3S"
FT HELIX 771..773
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:4H3S"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 782..786
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:4H3S"
FT STRAND 796..801
FT /evidence="ECO:0007829|PDB:4H3S"
SQ SEQUENCE 809 AA; 93133 MW; C7AB13D02BC483F6 CRC64;
MSSVEELTQL FSQVGFEDKK VKEIVKNKKV SDSLYKLIKE TPSDYQWNKS TRALVHNLAS
FVKGTDLPKS ELIVNGIING DLKTSLQVDA AFKYVKANGE ASTKMGMNEN SGVGIEITED
QVRNYVMQYI QENKERILTE RYKLVPGIFA DVKNLKELKW ADPRSFKPII DQEVLKLLGP
KDERDLIKKK TKNNEKKKTN SAKKSSDNSA SSGPKRTMFN EGFLGDLHKV GENPQAYPEL
MKEHLEVTGG KVRTRFPPEP NGYLHIGHSK AIMVNFGYAK YHNGTCYLRF DDTNPEKEAP
EYFESIKRMV SWLGFKPWKI TYSSDYFDEL YRLAEVLIKN GKAYVCHCTA EEIKRGRGIK
EDGTPGGERY ACKHRDQSIE QNLQEFRDMR DGKYKPGEAI LRMKQDLNSP SPQMWDLIAY
RVLNAPHPRT GTKWRIYPTY DFTHCLVDSM ENITHSLCTT EFYLSRESYE WLCDQVHVFR
PAQREYGRLN ITGTVLSKRK IAQLVDEKFV RGWDDPRLFT LEAIRRRGVP PGAILSFINT
LGVTTSTTNI QVVRFESAVR KYLEDTTPRL MFVLDPVEVV VDNLSDDYEE LATIPYRPGT
PEFGERTVPF TNKFYIERSD FSENVDDKEF FRLTPNQPVG LIKVSHTVSF KSLEKDEAGK
IIRIHVNYDN KVEEGSKPKK PKTYIQWVPI SSKYNSPLRV TETRVYNQLF KSENPSSHPE
GFLKDINPES EVVYKESVME HNFGDVVKNS PWVVDSVKNS EFYVEEDKDS KEVCRFQAMR
VGYFTLDKES TTSKVILNRI VSLKDATSK
