GARS_BOMMO
ID GARS_BOMMO Reviewed; 732 AA.
AC Q04451; Q2F5I5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=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 Flags: Precursor;
GN Name=GlyRS {ECO:0000305};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=8463296; DOI=10.1016/s0021-9258(18)53008-8;
RA Nada S., Chang P.K., Dignam J.D.;
RT "Primary structure of the gene for glycyl-tRNA synthetase from Bombyx
RT mori.";
RL J. Biol. Chem. 268:7660-7667(1993).
RN [2] {ECO:0000312|EMBL:ABD36382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Niu B.L., Meng Z.Q., Weng H.B., Shen W.F., He L.H., Zheng K.F., Ye S.T.,
RA Lin T.B., Chen J.E.;
RT "Blast silkworm EST database for functional genes.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). Also produces diadenosine
CC tetraphosphate (Ap4A), a universal pleiotropic signaling molecule
CC needed for cell regulation pathways, by direct condensation of 2 ATPs
CC (By similarity). Thereby, may play a special role in Ap4A homeostasis
CC (By similarity). Required for terminal arborization of both dendrites
CC and axons during development (By similarity).
CC {ECO:0000250|UniProtKB:P41250, ECO:0000250|UniProtKB:Q9VUK8}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16014;
CC 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34936;
CC Evidence={ECO:0000250|UniProtKB:P41250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P41250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000250|UniProtKB:Q9VUK8}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q9VUK8}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9VUK8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q04451-2; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q04451-1; Sequence=VSP_060971;
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; L08106; AAA62231.1; -; Genomic_DNA.
DR EMBL; DQ311438; ABD36382.1; -; mRNA.
DR PIR; A46636; A46636.
DR RefSeq; NP_001040293.1; NM_001046828.1.
DR AlphaFoldDB; Q04451; -.
DR SMR; Q04451; -.
DR STRING; 7091.BGIBMGA007637-TA; -.
DR BindingDB; Q04451; -.
DR GeneID; 692991; -.
DR KEGG; bmor:692991; -.
DR eggNOG; KOG2298; Eukaryota.
DR HOGENOM; CLU_015515_1_2_1; -.
DR OrthoDB; 1183820at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
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; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR002315; tRNA-synt_gly.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR PANTHER; PTHR10745; PTHR10745; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Cell projection; Cytoplasm; Direct protein sequencing; Ligase;
KW Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..732
FT /note="Glycine--tRNA ligase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000073001"
FT DOMAIN 61..117
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT BINDING 297
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 329..331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 340..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 348
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 453..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 572..574
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000312|EMBL:AAA62231.1"
FT /id="VSP_060971"
FT CONFLICT 303
FT /note="F -> L (in Ref. 2; ABD36382)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="S -> M (in Ref. 2; ABD36382)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="D -> E (in Ref. 2; ABD36382)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="C -> S (in Ref. 2; ABD36382)"
FT /evidence="ECO:0000305"
FT CONFLICT 497..499
FT /note="NGR -> KAA (in Ref. 2; ABD36382)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="F -> L (in Ref. 2; ABD36382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 83092 MW; 926D1DEFD64FF923 CRC64;
MRHVLSLVYK CSVFSKQVTV FSNHLRLSHS QQWGSNKLHR KIKIPNPFRE IIMADPKIEE
ILAPLRANVK EQGDLVRKLK EEKAPEIDIK KAVAELKTRK KILEDKELSL APAEDLFDRA
KMEDLIKRRF FYDQSFAIYG GITGQFDFGP MGCALKSNMI HLWKKFFILQ EQMLEVECSI
LTPEPVLKAS GHVERFADLM TKDIKTGECF RLDHLIKGHL EKIKSDKNTK IELKAEIEDI
LIKLDGMNAD EMSALMKRFE MKSPISGNDL TPPIEFNLMF NTQIGPSGLV KGFLRPETAQ
GIFVNFKRLL EFNQGRLPFA AAQIGNSFRN EISPRSGLLR VREFTMCEIE HFCDVKEHPK
FESVKNTQSL LYSADNQEQG KPADLTTIGD AVCKGIVNNE TLGYFMARIH MYMLAVGIDP
KRLRFRQHMG NEMAHYACDC WDAECLSSYG WIECVGCADR SAYDLTQHTK ATGIRLAAEK
KLPAPKQIEV VEAIANNGRI GKAFKKDSQA INDTLATLDN AALEEMQKEL DSNGEYTLIT
ARGEFKLTPS LVNVKKTQKT IHVEEIIPSV IEPSFGVGRI LYCILEHNFR MREGDEQRTY
FSLPPTVAPM KCVVLPLSGN AEFQPFVRDL SQELITVDVS HKVDDSSGSI GRRYARTDEL
GVPYAVTVDF DTIKEPHTVT LRERDSMRQV RLPMADVPTV VRDLSNSKIL WSDVEQKYPK
FEQQETVKGT SV
