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   27-MAR-2024, entry version 152.
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; 284812.Q9Y7Y8; -.
DR   iPTMnet; Q9Y7Y8; -.
DR   MaxQB; Q9Y7Y8; -.
DR   PaxDb; 4896-SPBC342-02-1; -.
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; TWCIYPM; -.
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   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; 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
//