SYQ_SCHPO
ID SYQ_SCHPO Reviewed; 811 AA.
AC Q9Y7Y8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable glutamine--tRNA ligase;
DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE AltName: Full=Glutaminyl-tRNA synthetase;
DE Short=GlnRS;
GN Name=qrs1; ORFNames=SPBC342.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB46772.1; -; Genomic_DNA.
DR PIR; T40275; T40275.
DR RefSeq; NP_596745.1; NM_001023765.2.
DR AlphaFoldDB; Q9Y7Y8; -.
DR SMR; Q9Y7Y8; -.
DR BioGRID; 277494; 4.
DR STRING; 4896.SPBC342.02.1; -.
DR MaxQB; Q9Y7Y8; -.
DR PaxDb; Q9Y7Y8; -.
DR EnsemblFungi; SPBC342.02.1; SPBC342.02.1:pep; SPBC342.02.
DR GeneID; 2540978; -.
DR KEGG; spo:SPBC342.02; -.
DR PomBase; SPBC342.02; qrs1.
DR VEuPathDB; FungiDB:SPBC342.02; -.
DR eggNOG; KOG1148; Eukaryota.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; Q9Y7Y8; -.
DR OMA; INNFCAQ; -.
DR PhylomeDB; Q9Y7Y8; -.
DR PRO; PR:Q9Y7Y8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; ISS:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..811
FT /note="Probable glutamine--tRNA ligase"
FT /id="PRO_0000195865"
FT REGION 190..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 269..279
FT /note="'HIGH' region"
FT MOTIF 502..506
FT /note="'KMSKS' region"
FT BINDING 270..272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 276..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 302
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 447
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 495..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 503..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
SQ SEQUENCE 811 AA; 92073 MW; AA346369990F94CE CRC64;
MDQDYEELRA KFTKIGLNET TVKDTLKNKK LSSSLNKVIE ETNVGSSGCD RTIGNLLFTL
ANASLKQKDP KSNAHEAFIA SKIVSGDLKT NLQVNAAITY CKDKDTIDES EFDKETGVGV
VLTPEQIEQL VGDYVAENKS KILEQRYQLL NPSASALRQH ALLKWAPQLE VKQTLDRKFL
ELLGPKTEQD AAAGKKKGAK AKNSKQKTVD SGKAKEQKIV SEQSKKYNMF EEGFLAKLHK
PGGNTQLIPE RMKEHLQATG GGVVTRFPPE PNGYLHIGHS KAIAVNFGFA RYHNGVCYLR
FDDTNPEAEE ERYFESIKDL VAWLGFQPYK ITYSSDYFDK LYELAEELIK RDKAYVCHCT
DAEIKKARGG EERGPRYACV HRDRPIEESL LEFRNMRDGK YQPKEAILRM KQDLSDGNPQ
MWDLIAYRVL NSPHPRTGDK WKIYPTYDFT HCLVDSFENI SHSLCTTEFI LSRVSYEWLC
NALEVYCPAQ REYGRLNVVG TLMSKRKIMK LVKEGYVHGW NDPRLYTLVA LRRRGVPPGA
ILEFVSEVGV TTAVSNIEVA RFENCVRKFL ENSVPRLMFL PDPIKVTLEN LDDSYREQIE
IPFNPKDPSM GSRSAFLTKH IYIDRSDFRE EASSDFFRLT LGQPVGLFRA SHPVVAKRVV
KNDEGEPIEI IAEYDASSSK KPKTFIQWVS RDKESNSPVL IAETRLFNNL FKCDNPAALK
EQELAAQLNP ESEVVLKNSI IEPGIYDLIK SAPWPKTDSS AGVDKAENPE SVRFQAMRVG
YFCLDEDTKK PNHLVLNRIV SLREDSAKNK N
