ID B0WUQ5_CULQU Unreviewed; 736 AA.
AC B0WUQ5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00019404};
DE EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
DE AltName: Full=Diadenosine tetraphosphate synthetase {ECO:0000256|ARBA:ARBA00030057};
GN ORFNames=CpipJ_CPIJ010486 {ECO:0000313|EMBL:EDS35041.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS35041.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS35041.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000713};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34936;
CC Evidence={ECO:0000256|ARBA:ARBA00000713};
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:0000256|ARBA:ARBA00001768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16014;
CC Evidence={ECO:0000256|ARBA:ARBA00001768};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; DS232108; EDS35041.1; -; Genomic_DNA.
DR RefSeq; XP_001859192.1; XM_001859151.1.
DR AlphaFoldDB; B0WUQ5; -.
DR STRING; 7176.B0WUQ5; -.
DR KEGG; cqu:CpipJ_CPIJ010486; -.
DR VEuPathDB; VectorBase:CPIJ010486; -.
DR VEuPathDB; VectorBase:CQUJHB006379; -.
DR eggNOG; KOG2298; Eukaryota.
DR HOGENOM; CLU_015515_1_0_1; -.
DR InParanoid; B0WUQ5; -.
DR OMA; MEMQYFV; -.
DR OrthoDB; 546660at2759; -.
DR PhylomeDB; B0WUQ5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00774; GlyRS-like_core; 1.
DR CDD; cd00858; GlyRS_anticodon; 1.
DR CDD; cd00935; GlyRS_RNA; 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 Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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; IPR002315; tRNA-synt_gly.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
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 Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:EDS35041.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 66..122
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 298..616
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 736 AA; 82360 MW; 95A684A656A041BD CRC64;
MAWVRIPPLS RFFCAHRVRV CSVRQYSQQK PARKPFNWGS NKKHRDFKLK AQILESMAAD
PKIEEQLAPL REAVKEQGDL VRKLKAEGAP EIDVKKAVNE LKARKKILED RELALAPSVA
SFDRARMEDL LKRRFFYDQS FAIYGGITGQ YDFGPMGCAL KANMINVWRQ FFVLEEQMLE
VDCSILTPEP VLKASGHVDR FADLMVKDVK NGECFRLDHL IKNHLEKLAA AKDATKELKD
ECEDIVIKLD GMNKAEMAAI LTKFGMKSPI TGNDLTEPIE FNLMFGTQIG PTGLVKGFLR
PETAQGIFVN FKRLLEFNQG KLPFAAAQIG NSFRNEISPR SGLIRVREFT MCEIEHFCDP
QLKDHPKFEN VRDVVMTLYS ACNQMDGKSA QQIKIGDAVA SGLVANETLG YFMARIQQFM
LKIGILPDRL RFRQHMGNEM AHYACDCWDA ECLTSYGWVE CVGCADRSAY DLTQHTNATG
VKLVAEKKLP APKTIEVTEV VPNKAAIGKV FKKDAKNITE LLAKLSLDEV ETIGKNLAGS
GEHTLDVNGT AVTLKSDMIA VKSSSKTVHV EEITPSVIEP SFGVGRIMYS LLEHSFQMRE
GDEQRCYFSL PPVVAPLKCS VLPLSNNADF TPFVKKISSA LTSVDISHKV DDSSGSIGRR
YARTDEIAIP YGVTIDFDTL KEPHTVTLRE RDSLKQVRIG LDEVAGVVRD LATGRLSWAD
VEAKYPKFEQ QEASSK
//
