ID A0A1Q4YFU6_9PSEU Unreviewed; 991 AA.
AC A0A1Q4YFU6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=glyQ {ECO:0000256|HAMAP-Rule:MF_00254};
GN Synonyms=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN ORFNames=A6A25_05135 {ECO:0000313|EMBL:OKI33452.1};
OS Saccharothrix sp. CB00851.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI33452.1, ECO:0000313|Proteomes:UP000186828};
RN [1] {ECO:0000313|EMBL:OKI33452.1, ECO:0000313|Proteomes:UP000186828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00851 {ECO:0000313|EMBL:OKI33452.1,
RC ECO:0000313|Proteomes:UP000186828};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI33452.1}.
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DR EMBL; LWLC01000012; OKI33452.1; -; Genomic_DNA.
DR RefSeq; WP_073889982.1; NZ_LWLC01000012.1.
DR AlphaFoldDB; A0A1Q4YFU6; -.
DR STRING; 1835005.A6A25_05135; -.
DR Proteomes; UP000186828; 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:UP000186828}.
SQ SEQUENCE 991 AA; 106321 MW; 0E07F2F22C6589FC CRC64;
MQDALLALTR YWTERGCVVV QPYNTEVGAG TLNPATVLRV LGPEPWRVSY VEPSVRPDDA
RYGENPNRLQ THTQFQVILK PDPGNPQELY LGSLEALGID VRAHDVRFVE DNWASPALGA
WGLGWEVWLD GLEITQFTYF QQAGGMSLDP VSVEITYGIE RIMMALQGVD HFKDIAYAPG
ISYGEAFGQA EYELSRYYLD DADVEANKRL FEEYASEARR MLDARLPVPA HNYVLKCSHT
FNVLDARGAI STTERARAFG RMRGLAREVA GLWAARREEL GHPLGLAEAP AAATTPDTFA
EVTDPATLLF EIGTEELPPA EVTRTVEAVG KAVTDKLGTT RLAHGAVEVH GTPRRIVVLV
PDVAPREPDA EKTVRGPRVS AAFDADGNPT KAVQGFARGQ GVDVDALGRV TENGVEHVAL
VRTDPGRGAV EVLSGLLGEV VSELRAEKNM KWNDPKLSFT RPIRWLLALL GTTPVPVAVS
SLAAEPKTRV HRTAATPVVE VSTADGYLDF LAGHGIDASA RARRDAIVAR AEELAASVGG
VVDFEGVLDE VTNLVERPTP ILGSFEERYL ELPAQILTTV MRKHQRYLPV RAQDGSLLPH
FVAVANGEVD ADLVRAGNEA VLRARYEDAA FFWRADLRTP LADMKAGLEK LTFADKLGSM
ADRAGRIAAL ARRLAEELST GEVGPGKVST ADETLARAGE LAKFDLGSQM VIELSSLAGV
MAREYAERAG EAPEVARALW EMELPRSAGD ALPSSTPGAL LSLADRFDLL AGLFGIGANP
TGSSDPFGLR RAALGAVSVL RAFPDLKDIT LTKALALASQ GLEVSAEALD TAREFTVRRY
EQQLLDAGHD HRFVNAVLPL ADAPAVADAT LAELTGLAGD PDFAALVAAL QRVRRIVPAD
TVGEYDPQAL VEPAEVALHK VLAEVPAGVT GLAAFAAAAN GLTGPVNTFF DEVLVMAEDA
DVRRARLGLL AAIRDLAAPV LDWQALGTAL G
//
