SYEC_SCHPO
ID SYEC_SCHPO Reviewed; 716 AA.
AC O13775;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable glutamate--tRNA ligase, cytoplasmic;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
DE Short=GluRS;
GN Name=gus1; Synonyms=ers1; ORFNames=SPAC17A5.15c;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17;
CC -!- SUBUNIT: Component of a yeast aminoacyl-tRNA synthase (aaRS) complex
CC formed by methionyl-tRNA synthase, glutamyl-tRNA synthase and the tRNA
CC aminoacylation cofactor arc1 in a stoichiometric complex. Interacts
CC with arc1/SPAC30C2.04 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB11515.1; -; Genomic_DNA.
DR PIR; T37830; T37830.
DR RefSeq; NP_593483.1; NM_001018916.2.
DR AlphaFoldDB; O13775; -.
DR SMR; O13775; -.
DR BioGRID; 278872; 7.
DR STRING; 4896.SPAC17A5.15c.1; -.
DR iPTMnet; O13775; -.
DR MaxQB; O13775; -.
DR PaxDb; O13775; -.
DR PRIDE; O13775; -.
DR EnsemblFungi; SPAC17A5.15c.1; SPAC17A5.15c.1:pep; SPAC17A5.15c.
DR GeneID; 2542408; -.
DR KEGG; spo:SPAC17A5.15c; -.
DR PomBase; SPAC17A5.15c; gus1.
DR VEuPathDB; FungiDB:SPAC17A5.15c; -.
DR eggNOG; KOG1147; Eukaryota.
DR HOGENOM; CLU_001882_1_2_1; -.
DR InParanoid; O13775; -.
DR OMA; NLTRWFT; -.
DR PhylomeDB; O13775; -.
DR PRO; PR:O13775; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IPI:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005844; C:polysome; EXP:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; ISS:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; ISS:PomBase.
DR Gene3D; 1.10.1160.10; -; 1.
DR Gene3D; 2.40.240.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
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; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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 PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00463; gltX_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..716
FT /note="Probable glutamate--tRNA ligase, cytoplasmic"
FT /id="PRO_0000119738"
FT MOTIF 215..224
FT /note="'HIGH' region"
FT MOTIF 441..445
FT /note="'KMSKS' region"
FT BINDING 210..212
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 386..390
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 441..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 716 AA; 80750 MW; 2ACE0A35ED393227 CRC64;
MSVSVALKAK PIAYGAVACA NYVNLSGAGS ISVKYEDVAL LDKQNKESNV SIQLNGSDSP
VFGSKLALQT FSQVYPKLFI GENDRSLVES WVETASALAG NHNFLELSSL LAQLDDHLIM
RSLFVGYSLT SADFSIWGAL KSNNMAAGAV RTGQYFNLAR WYKFMDSQNA VSVTMEEFTK
AVNISKKQKS SGPNYEIGLP DAIDGKVVTR FPPEPSGYLH IGHAKAALLN QYFANKYHGK
LIVRFDDTNP SKENSEFQDA ILEDVALLGI KPDVVTYTSD YLDTIHQYCV DMIKSGQAYA
DDTDVETMRH ERTEGIPSKH RDRPIEESLE ILSEMDKGSD VGLKNCIRAK ISYENPNKAM
RDPVIYRCNL LPHHRTGTKY RAYPTYDFAC PIVDSLEGVT HALRTTEYRD RNPLYQWMIK
AMNLRKIHVW EFSRMNFVRT LLSKRKLTEI VDHGLVWGWD DPRFPTVRGV RRRGMTIEAL
QQYIVSQGPS KNILTLDWTS FWATNKKIID PVAPRHTAVE SGDVVKATIV NGPAAPYAED
RPRHKKNPEL GNKKSIFANE ILIEQADAQS FKQDEEVTLM DWGNAYVREI NRDASGKVTS
LKLELHLDGD FKKTEKKVTW LADTEDKTPV DLVDFDYLIT KDKLEEGENY KDFLTPQTEF
HSPVFADVGI KNLKKGDIIQ VERKGYYIVD VPFDGTQAVL FNIPDGKTVN RYGVKN
