ID SYG_SCHPO Reviewed; 652 AA.
AC Q10179;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Putative glycine--tRNA ligase;
DE EC=6.1.1.14 {ECO:0000250|UniProtKB:P41250};
DE AltName: Full=Diadenosine tetraphosphate synthetase;
DE Short=Ap4A synthetase;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P41250};
DE AltName: Full=Glycyl-tRNA synthetase;
DE Short=GlyRS;
GN Name=grs1; ORFNames=SPAC3F10.03;
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 -!- FUNCTION: Catalyzes the ATP-dependent ligation of glycine to the 3'-end
CC of its cognate tRNA, via the formation of an aminoacyl-adenylate
CC intermediate (Gly-AMP). Also produces diadenosine tetraphosphate
CC (Ap4A), a universal pleiotropic signaling molecule needed for cell
CC regulation pathways, by direct condensation of 2 ATPs. Thereby, may
CC play a special role in Ap4A homeostasis.
CC {ECO:0000250|UniProtKB:P41250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC EC=6.1.1.14; Evidence={ECO:0000250|UniProtKB:P41250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H(+) = diphosphate + P(1),P(4)-bis(5'-adenosyl)
CC tetraphosphate; Xref=Rhea:RHEA:34935, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58141;
CC Evidence={ECO:0000250|UniProtKB:P41250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P41250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA93301.1; -; Genomic_DNA.
DR PIR; T38704; T38704.
DR RefSeq; NP_593935.1; NM_001019363.2.
DR AlphaFoldDB; Q10179; -.
DR SMR; Q10179; -.
DR BioGRID; 279611; 4.
DR STRING; 284812.Q10179; -.
DR iPTMnet; Q10179; -.
DR MaxQB; Q10179; -.
DR PaxDb; 4896-SPAC3F10-03-1; -.
DR EnsemblFungi; SPAC3F10.03.1; SPAC3F10.03.1:pep; SPAC3F10.03.
DR GeneID; 2543181; -.
DR KEGG; spo:SPAC3F10.03; -.
DR PomBase; SPAC3F10.03; grs1.
DR VEuPathDB; FungiDB:SPAC3F10.03; -.
DR eggNOG; KOG2298; Eukaryota.
DR HOGENOM; CLU_015515_1_0_1; -.
DR InParanoid; Q10179; -.
DR OMA; HFVNFQR; -.
DR PhylomeDB; Q10179; -.
DR PRO; PR:Q10179; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IGI:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; IGI:PomBase.
DR GO; GO:0005524; F:ATP binding; ISO:PomBase.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IGI:PomBase.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IGI:PomBase.
DR GO; GO:0070150; P:mitochondrial glycyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00774; GlyRS-like_core; 1.
DR CDD; cd00858; GlyRS_anticodon; 1.
DR Gene3D; 3.30.40.230; -; 1.
DR Gene3D; 3.30.720.200; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR NCBIfam; TIGR00389; glyS_dimeric; 1.
DR PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1.
DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..652
FT /note="Putative glycine--tRNA ligase"
FT /id="PRO_0000073004"
FT REGION 119..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 253..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 264..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 272
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 380..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 499..501
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
SQ SEQUENCE 652 AA; 74005 MW; 3B7041D0616D2527 CRC64;
MTEVSKAAAF DRTQFEELMK KRFFFSPSFQ IYGGISGLYD YGPPGSALQS NLVDIWRKHF
VIEESMLEVD CSMLTPHEVL KTSGHVDKFA DWMCKDPATG EIFRADHLVE EVLEARLKGD
KEARGQNSND QPEESDDKKK RKKKVKEIRA TRLDDKTVEE YEFILAQIDN YDGDQLGELM
KKYDIRNPAT NGELETPRQF NLMFETQIGP SGGLKGYLRP ETAQGQFLNF SRLLEFNNGK
VPFASAMVGK AFRNEISPRS GLLRVREFLM AEVEHFVDPK NKEHDRFDEV SHMPLRLLPR
GVQLEGKTDI LEMPIGDAVK KGIVDNTTLG YFMARISLFL EKIGIDMNRV RFRQHMSNEM
AHYACDCWDA EIQCSYGWIE CVGCADRSAY DLSVHSKATK TPLVVQEALP EPVVVEQFEV
EVNRKKFGPR FKRDAKAVEE AMISWPESEK VEKSAQLVAE GKIIVNVNGV EHTVESDLVT
IEKRKHTEHI RTYTPNVIEP SFGLGRILYV LMEHAYWTRP EDVNRGVLSF PASIAPIKAL
IVPLSRNAEF APFVKKLSAK LRNLGISNKI DDSNANIGRR YARNDELGTP FGLTVDFETL
QNETITLRER DSTKQVRGSQ DEVIAALVSM VEGKSSFEDA LAKFGEFKST QE
//
