ID A0A0A0KFM2_CUCSA Unreviewed; 1068 AA.
AC A0A0A0KFM2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00012829};
DE EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
GN ORFNames=Csa_6G106190 {ECO:0000313|EMBL:KGN46516.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN46516.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN46516.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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:ARBA00000201};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; CM002927; KGN46516.1; -; Genomic_DNA.
DR RefSeq; XP_004140508.2; XM_004140460.2.
DR RefSeq; XP_011656850.1; XM_011658548.1.
DR AlphaFoldDB; A0A0A0KFM2; -.
DR STRING; 3659.A0A0A0KFM2; -.
DR EnsemblPlants; KGN46516; KGN46516; Csa_6G106190.
DR GeneID; 101209684; -.
DR Gramene; KGN46516; KGN46516; Csa_6G106190.
DR KEGG; csv:101209684; -.
DR eggNOG; ENOG502QS5T; Eukaryota.
DR OMA; LPIPKRM; -.
DR OrthoDB; 3640061at2759; -.
DR Proteomes; UP000029981; Chromosome 6.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; 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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:EnsemblPlants.
DR CDD; cd00733; GlyRS_alpha_core; 1.
DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR NCBIfam; TIGR00388; glyQ; 1.
DR NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02091; tRNA-synt_2e; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 2.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000029981}.
FT DOMAIN 960..1053
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 1068 AA; 119922 MW; F700397B142E3783 CRC64;
MAILALPLFS SFLKHHTYLL SISSRKPLSF TFCKSPYRRQ FNKTCASAIT PSTTLHHSST
GSKTYGSKAS VLTFQQAIQR LQEYWASVGC AVMQCSNTEV GAGTMNPLTF LRVLGPEPWN
VAYVEPSIRP DDSRYGENPN RLQRHTQFQV ILKPDPGNSQ DLFIQSLSAL GIDVAAHDIR
FVEDNWESPV LGAWGLGWEI WMDGMEITQF TYFQQAGSQQ LLPVSVEITY GLERILMLLQ
GVNHFKKIQY ADGITYGELF LENEKEMSAY YLEHANVHQV QKHFNIFEEE AHSLLALGLA
IPAYDQVLKA SHAFNILDSR GFIGVTERAR YFGRMRSLAR QCAQLWLITR ESLGHPLGVA
SDPVDLVCPK ELLDAAIKKV HEDVRWFVFE IGTEEIPPKD VVDASQQLKT YMLQLLEKHR
LSHGNVQAFG TPRRLVVKVE SLCSKQVEKE FEVRGPPVSK AFDDQGNPTK AVEGFCRRYS
ISRESLYKKI DGKTEYLYAS VMESSRHALE IFSENLPGII AKISFPKSMR WNSQVVFSRP
IRWILALHGD VVVPFSYAGV LSGNISYGLR NTSTAIVKVD SAESFMGAMK DAKIDLEVED
RKRKILDQSS MLAQSINGKT VIHEDLLDEV VNLVETPVSI LGKFNDSFLE LPEDLLTMVM
QKHQKYFSIR NADGKLMPYF IAVANGEIDD KVVRKGNEAV LRARYEDAKF FYETDTSKKF
SQFRNQLSGI LFHEKLGSML DKMTRMEAIV VNLSLAIGIS QDLIQIILEA ASLAMSDLAT
AVVTEFTSLA GIMGRHYALR EGFSEEIADA LFEITLPRFS GDILPRSDVG IVLAVADRLD
SLVGLFAAGC QPSSTSDPFG LRRISYGLVQ ILVEKDKNLD LGRALRLAAD NQPVKVDTNV
IDNVKLFVTR RLEQFLVDKG LSPEIVRSVL AERSNFPCLA AKTAHKMNAM SKGDLFPKII
EAYARPTRII SGKDVDNAIE VDEANFESNE ERALWNTFLS IKNKVHPGIE VDEFFEISSK
LIQPLEDFFE HVFVMVEDEK IRKNRLALLK RIADLPSGIA DLSLLSGF
//
