ID A0A347ZNI4_9CHLR Unreviewed; 1002 AA.
AC A0A347ZNI4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DFR64_1835 {ECO:0000313|EMBL:REG08468.1};
OS Pelolinea submarina.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Pelolinea.
OX NCBI_TaxID=913107 {ECO:0000313|EMBL:REG08468.1, ECO:0000313|Proteomes:UP000256388};
RN [1] {ECO:0000313|EMBL:REG08468.1, ECO:0000313|Proteomes:UP000256388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23923 {ECO:0000313|EMBL:REG08468.1,
RC ECO:0000313|Proteomes:UP000256388};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) 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|ARBA:ARBA00004496,
CC 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:REG08468.1}.
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DR EMBL; QUMS01000002; REG08468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347ZNI4; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000256388; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
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; IPR008909; DALR_anticod-bd.
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; PF05746; DALR_1; 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:UP000256388}.
FT DOMAIN 897..987
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 1002 AA; 111699 MW; 0B828EBDDF23A46B CRC64;
MQDKLNFQTI MMTLQQFWGG KGCLIWQPYY TQVGAGTMNP ATVLRVLGPE PWNVAYVEPS
IRPDDGRYGD NPYRMQQHYQ FQVILKPDPG NPQELYLQSL EALGINPHEH DIRFVEDNWE
SPALGAWGLG WEVWLDGQEI TQFTYFQQAG GVNLDPVSVE ITYGLERIAM ALQGSYNFKK
IQWSPNFTYG DVNYQAEYEH SRYYFEVADV ERLYEMYDLF EKEANLALDQ GLVLPAHDYI
LKCSHTFNVL DTRGAVGVTE RQSLFGRMRE LSRRTAETYI AQREALGFPW LEKPNAVASS
VSAEQPELPE VIKSDQAADF LLEIGTEELP AADLESAWGQ LQTLVPDMLS GLRLDYKDIH
VYATPRRLVV HVSDLAGKQA EVTQEVKGPP AERAYDKDGQ LTPAALGFAR SKGVDVKDLT
VKEVDGGKYL TAVVHQPGLF TLDILPEKLV DLIAHIRFDK SMRWNASGVS FSRPIRWLAA
LFGTAVVPFA YAGLNANRIT RGLRFSEEAE HACKDIPDYF AYLESQGILS DMQARKSVIE
KQVGALLSSL KAADKIDAKL LDEVNNLVEA PTALLGNFNE EHLKLPGEVL IGVMKKHQRY
FPVTEASGAL MPHFITIRNG GKQHLEIVAH GNEEVIQARF SDSAFFINED NKHSLEDFVN
REDTLTFHPK LGSMLDKTKR ILKLTETLCL GMGLDKEETA VAMEAAQFCK ADLVSKMVIE
MTALQGTIGK YYALQRGKSP AVANAIEEHY QPRNAGDQSP ASQAGLVVGI ADRLDSLIGL
FSAGMAPSGT KDPFGLRRAA IGLVQNLINA DISLDLQKYI FKASALLPVE SSPKDCQDCL
DFIVGRLEQI LLEEGYAYDV IKAVLAAQGA NPAKAAASIR ELSEWVKRDD WRGTILPAYS
RCVRITRTEK QRYNVSAEYF QESQEKALYE AVTAAQKNIG DSKNVNDFLT HLLPVVPAIN
AFFDAVLVMD EKQEIRENRL GLLQSVAFLA DGVADLSKLE GF
//
