ID I0HCG0_ACTM4 Unreviewed; 985 AA.
AC I0HCG0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|HAMAP-Rule:MF_00255};
DE Includes:
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
DE Includes:
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
GN Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN Synonyms=glyQ {ECO:0000256|HAMAP-Rule:MF_00254};
GN OrderedLocusNames=AMIS_54770 {ECO:0000313|EMBL:BAL90697.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL90697.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL90697.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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DR EMBL; AP012319; BAL90697.1; -; Genomic_DNA.
DR RefSeq; WP_014445585.1; NC_017093.1.
DR AlphaFoldDB; I0HCG0; -.
DR STRING; 512565.AMIS_54770; -.
DR KEGG; ams:AMIS_54770; -.
DR PATRIC; fig|512565.3.peg.5472; -.
DR eggNOG; COG0751; Bacteria.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_007220_0_1_11; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000007882; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; 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; 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 ECO:0000256|HAMAP-Rule:MF_00255};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00255};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000007882}.
SQ SEQUENCE 985 AA; 105765 MW; 1EB93B9BA29B3AFC CRC64;
MLTMQDALAR LTAYWTDQGA LVVQPMNTEV GAGTLNPATF LRVLGPEPWK VVYVEPSVRP
DDSRYGENPN RLQTHTQLQV ILKPDPGNPQ ELYLGSLRAI GIDVAAHDVR FVEDNWASPA
LGAWGLGWEV WLDGLEITQF TYFQQAGGLN LDPVSVEITY GIERIIMALQ DKTHFKEIEY
ATGVSYGEVF GQSEYEMSRY YLDDADIEAN RRLLDLYAGE AQRMIDAGLP VPAHTFVLKC
SQAFNVLDAR GAVSTAERAA EFARMRRLAG DVAKLWVARR AELGLPLGTT PALDPARPAA
STQTSDDART LVFEIGTEEL PPGELRSARA QLLRLVTEGL AGTRLAHGEI RVYGTPRRLI
AVVPGVGARE DDHVRLVKGP KTTAAYGGDG APTKALEGFA RSQGVSVDAV TTVELGGVPH
VVVEKHEAGG AAPAVLATVL AQVVTGLRAA KNMRWNDPKL SFSRPIRWLT ALWGDDVVPV
TVSTLAAGRT TRLLRTAAEP VIAIESAETF LETLGVNGIV ADHEDRRELI VIGAQDLVYP
DGKIDVKGES SLIDQVTDLV EQPLPLLGTF DEGYLDLPDA VLTTVMRKHQ RYLPVRDADG
ALLPMFVTVA NGPVDVELVR AGNEAVLRAR YEDAAFFYRA DLATSPADMR ARLDRLTFTD
KLGSMADRAA RISSLAHALA ADRGISSGVL ERAAALVKFD LGSQLVTEMT SLAGVMARDY
ALRAGEDRAV AQAVYEAELP RNTGDELPRT VAGALLSVAD RLDVIAGLAA TVGLPTGSSD
PFALRRAFLG LIAVHRATPA LAGLDLVEAL RMATAAQPVP VADDVVPACA EFLAKRLEQV
LTEEGQPVDR VRAVLSAESR PARVDLLLAQ LNTAVGDPGF RAVAAAIQRA RRIVPAGTEA
SYPAAALKEP AELALHAAVG EVSAFTDISG FVGATRGLVA PLNTFFDEVF VMADDPELRA
ARLGLLATVR DLGDGLLDWS HLRLQ
//
