ID A0A101V2G4_9ACTN Unreviewed; 1006 AA.
AC A0A101V2G4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=AQJ91_10100 {ECO:0000313|EMBL:KUO21309.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO21309.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO21309.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO21309.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO21309.1}.
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DR EMBL; LMXB01000025; KUO21309.1; -; Genomic_DNA.
DR RefSeq; WP_067018624.1; NZ_KQ949078.1.
DR AlphaFoldDB; A0A101V2G4; -.
DR STRING; 909626.AQJ91_10100; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000053260; Unassembled WGS sequence.
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 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; 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:UP000053260}.
SQ SEQUENCE 1006 AA; 108758 MW; D69F41E76E15C097 CRC64;
MNNGHTALTM QDAILTLQNY WSDNGCMITQ PLNTEVGAGT ANPATALRVI GPEPWSVAYV
EPSVRPDDSR YGENPNRLQT HTQFQVILKP DPGNPQELYL GSLQALGVDL RAHDVRFVED
NWASPALGAW GLGWEVWLDG MEITQFTYFQ QVGGVSLSPV SVEITYGLER ILMNLQGVSH
FKDIVYAPGI TYGEVFGQNE YEMSRYYLDD ADVDTNHRLF EAYAAEARRM LDLELPVPAY
TYVLKCSHTF NVLDARGAIS TTERAKAFSL MRGLTHESAK LWARRRTALG HPLGVTAAPA
PAVRAALPSV PGPETLLFEI GLEELPYADV PATTDAVREV ITAKLAATRL RHGAITVLAT
PRRVVVTVEA VQPREPDTEK TVRGPKVAAA YKDGAPTPAL LGFARSQGVD PSALKTVAVG
GVEYVAVTRD EPGRTAVEVL SGVLTEVVSG LRSTRNMRWN DPNLSFSRPV RWLLALLGRS
PLPVTVSALV AGDTTRVHRT APDPEVRVTA AEGYAHFLRM YGIMLDRADR RAAVVRGGQE
LAAEVGGRID VAGQAGLIDE ITDIVEFPHP VRGSFDERYL ELPASVLTTV MRKHQRYLPV
LDGDRLMPHF VTFANGACDD DVVRAGNEGV LRARYEDAAF FWRADLKVAP EEFRRRLDQL
TFEDRLGTVA DRADRIAALA LDLAARAGLA EGALATVRRA GELAKFDLAS QMVVEFSGLA
GVMAEEYARR AGEPDEVALA LAEMELPRSA GGALPTGDAG AVLSLADRFD LVTGMFVIGA
APTGSSDPFG VRRAAIGLLN VLRRVPAAAG VRVGDGLNAA AARYAAQGVE VPAGRLEEAA
ELIARRYEQQ LTDAGHEHRL VQAVRVWADR PAQGDRTLAT LERHVGTEEF GALTAALQRV
VRILPGDAQE NTADAAATDP VDRNLLSAPA ELRLAESAEA VRDALRGRED DLAALIEVSA
PLVAAIDAFF DEVLVMDPDP AIRAARLALL TDVARLARTT LDWSAL
//
