ID A0A1L7FAN6_9PSEU Unreviewed; 1013 AA.
AC A0A1L7FAN6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=UA75_19460 {ECO:0000313|EMBL:APU21882.1};
OS Actinoalloteichus sp. GBA129-24.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU21882.1, ECO:0000313|Proteomes:UP000185506};
RN [1] {ECO:0000313|EMBL:APU21882.1, ECO:0000313|Proteomes:UP000185506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GBA129-24 {ECO:0000313|EMBL:APU21882.1,
RC ECO:0000313|Proteomes:UP000185506};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT (=GBA129-24).";
RL Submitted (JUN-2016) 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; CP016077; APU21882.1; -; Genomic_DNA.
DR RefSeq; WP_075743986.1; NZ_CP016077.1.
DR AlphaFoldDB; A0A1L7FAN6; -.
DR STRING; 1612551.UA75_19460; -.
DR KEGG; acti:UA75_19460; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000185506; 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}.
SQ SEQUENCE 1013 AA; 109066 MW; 7B4D015D197B2CC7 CRC64;
MQDAILALTK YWTDQGCMVV QPLNTEVGAG TLNPATVLRV LGPEPWRTAY VEPSVRPDDS
RYGENPNRLQ THTQFQVILK PDPGNPQELY LGSLAAIGID VEAHDVRFVE DNWDFPALGA
WGLGWEVWLD GLEITQFTYF QQAGGATLDP VSVEITYGLE RILMALQNVS HFKDIAFAPG
ISYGEAFGQA EYEMSRYYLD DADVAMNRRL FDEYAAEARR LLDARLPMPA HYFVLKCSHT
FNVLDARGAV STTERAKAFG RTRALTRDVV RLWAERREEL GHPLGVAEAL PAATVPAELP
SVTEPATLLF EVGTEELPAA EVRRAAEAMR TALTEKLAAT RLGHGEISTY ATPRRIVAVV
EAVEPGEPDA ERTVRGPRVA NAFDATGAPT KAVAGFARGQ GVDVADLGRA VIDGVEFVVA
VKTDVGRGAV TVLSELLSSV VLELRADKNM RWSDSTLSYS RPVRWLLAML GDVGVPVAAS
SLASGVTTRV HRTAATPTVA VPHADGYVDF LAAHGIVVDI DVRRGQIVGA TQRLVSEVGG
TVDFDGEAVL LEEVVNLVEQ PTPILGSFSE HYLELPDEIL TTVMRKHQRY LPVRDGAGAL
MPYFVAVANG ACDHDAVRAG NEGVLRARYE DAAFFWRADL AVEPETMKLG LDRLAFEERL
GSMADRTERI AAVARELGDA TVATPEGVQA SGDRLVPLTG EERQTLDRAA QLVKFDLGSQ
MVVELTSLAG TMAREYALRA GESPSVAGAL YDMEQPRSAG GVLPTTVPGA LLSLADRLDL
LVGLFGIGAS PTGSSDPFGL RRAALGLISV LRAFPQLRQV TVSRALRVAA DVLAAQGIEV
ADSALAEAHE FVIRRYEQQL LDAGHHHAVV AAVLPLADSP ITADETLAEV NRRTGDPTFV
ELAAALQRVR RIVPDDTPAT YDAAHITEPA EVALRTVWEQ VGAALAGTTP DLARFAEEAR
PIVAPIGVFF DDVLVMAEDA QVRAARLGLL ASIRDAAAPV LDWRALGTAL AKD
//
