ID A0A1F8TWY9_9CHLR Unreviewed; 356 AA.
AC A0A1F8TWY9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=A3K41_11460 {ECO:0000313|EMBL:OGO76716.1};
OS Chloroflexi bacterium RIFOXYD12_FULL_57_15.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797675 {ECO:0000313|EMBL:OGO76716.1, ECO:0000313|Proteomes:UP000178494};
RN [1] {ECO:0000313|EMBL:OGO76716.1, ECO:0000313|Proteomes:UP000178494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000256|ARBA:ARBA00001766};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
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:OGO76716.1}.
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DR EMBL; MGOQ01000401; OGO76716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8TWY9; -.
DR Proteomes; UP000178494; Unassembled WGS sequence.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07956; Anticodon_Ia_Arg; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00456; argS; 1.
DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363038}.
FT DOMAIN 237..356
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 164..192
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 356 AA; 40217 MW; DB221C029E5EED67 CRC64;
MALWEKTRQW SLNGFDQMYD MLDIKFDKYY FNSEEEQPGK EMVADLVKRG IAVDERPEGP
VIVKLDELLG NKNEKFRVLV VLRSDGTALY ATEDLALVLH KFRDYPDMVR SVYVVDVRQS
LHFTQVFKTM ELAGYEQAKK CVHVAYELVT LPGNVVMSSR EGTVVLLENL IREAIERAKE
EAKKKNPNLS EEQLNAVANA VGLGALKYPL LARENTKIVT FDWQSALDFN GQAAPYIQYA
HVRCNSIIRK SKVESQTSDL GPSTFDYALD PSEIELIETI SRFPAEVQRA AEEYKPLIIA
SLGYEIAKAF ASFYDKCPVI QAEPKVREAR LGLVMAAKQT MANALYLLGI QAPDVM
//
