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Database: UniProt
Entry: A0A101JNZ7_9ACTN
LinkDB: A0A101JNZ7_9ACTN
Original site: A0A101JNZ7_9ACTN 
ID   A0A101JNZ7_9ACTN        Unreviewed;       982 AA.
AC   A0A101JNZ7;
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=glyQ {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Synonyms=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   ORFNames=ADL15_25705 {ECO:0000313|EMBL:KUL29973.1};
OS   Actinoplanes awajinensis subsp. mycoplanecinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL29973.1, ECO:0000313|Proteomes:UP000053244};
RN   [1] {ECO:0000313|EMBL:KUL29973.1, ECO:0000313|Proteomes:UP000053244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL29973.1,
RC   ECO:0000313|Proteomes:UP000053244};
RA   Gilbert D.G.;
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:KUL29973.1}.
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DR   EMBL; LLZH01000268; KUL29973.1; -; Genomic_DNA.
DR   RefSeq; WP_067696329.1; NZ_LLZH01000268.1.
DR   AlphaFoldDB; A0A101JNZ7; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000053244; 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   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:UP000053244}.
SQ   SEQUENCE   982 AA;  106246 MW;  98DC3A006D573A35 CRC64;
     MLTMQEALTR LTAYWTEQGC LIVQPMNTEV GAGTLNPATF LRVLGPEPWR VVYVEPSVRP
     DDSRYGENPN RLQTHTQMQV ILKPDPGNPQ ELYLGSLAAL GIDVAAHDVR FVEDNWASPA
     LGAWGLGWEV WLDGLEITQF TYFQQAGGLN LDPPSVEITY GIERIIMALQ DKQHFKEIEY
     APGVSYGEVF GQSEYEMSRY YLDDADIDAN RRLLELYAGE AQRMIDAGLP VPAHSYVLKC
     SQAFNVLDSR GAVSTAERAS EFARMRRLAG EVAKLWVARR AELEHPLGLV ADLEPARPAG
     AAQTGDRPRT LLFEIGAEEL PPAELRNARA QLQRLLTEGL AATRLEHGEI RVFGTPRRLI
     AVVQAVAARE EDFVRTVRGP KTSAPAKAIE GFARGHGVTP EELATEEFNG VPHLVLHKQE
     SGGAAPQVLT AVLAKVVGGL RSAKNMRWND PKLAFSRPLR WLTALWGDDV VPVTVSTLAA
     GRQTRLLRTA ATPIVEIASA ETFVETLGVN GIVADHDDRR ELIVVGAQDL VYPDGRIDVT
     GESALIDQIT DLVEQPLPLL GTFDEGYLTL PDAVLTTVMR KHQRYLPVRD EDGKLLPMFV
     TVANGPVDVE LVRTGNEAVL RARYEDARFF YRADLDTAPA DMRAKLTRLT FTDKLGSMAD
     RADRIGTLAG QLGERLGLGS PALTRAAELV KFDLGSQLVT EMTSLAGVMA RDYALRGGES
     RAVAEAVFEA ELPRNTGDAL PRTIPGALLS LADRLDLVTG LAATVGLPTG SSDPFAVRRA
     VLGLLAVHRS TPEFASLSLV EALSLAAAAQ PVPVSAEVLA ATGDFLAKRL EQMLTEEGQP
     VDRVRAVLPH FARPSVADTL LAQLATAVGD ADFASVTAAI QRARRIVPEG TPATYDAGAL
     KEPAELALHD AVTTVRAALD PALIDLPRFV TATGPLVGPV NTFFDDVLVM ADDPAIRAAR
     LGLLATVRDL GDGLLDWPAL RL
//
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