ID A0A0Q0WL96_9EURY Unreviewed; 375 AA.
AC A0A0Q0WL96;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00020262};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE Flags: Fragment;
GN ORFNames=APR56_01595 {ECO:0000313|EMBL:KQC15360.1};
OS Methanosaeta sp. SDB.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1735328 {ECO:0000313|EMBL:KQC15360.1, ECO:0000313|Proteomes:UP000051107};
RN [1] {ECO:0000313|EMBL:KQC15360.1, ECO:0000313|Proteomes:UP000051107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC15360.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQC15360.1}.
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DR EMBL; LKUG01000661; KQC15360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0WL96; -.
DR Proteomes; UP000051107; 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 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 PRINTS; PR01038; TRNASYNTHARG.
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|RuleBase:RU363038};
KW Ligase {ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:KQC15360.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363038}.
FT DOMAIN 305..375
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KQC15360.1"
FT NON_TER 375
FT /evidence="ECO:0000313|EMBL:KQC15360.1"
SQ SEQUENCE 375 AA; 42146 MW; CE64A827708BDED7 CRC64;
VRILRRAGCD VEAQYYVNDM GRQIAIVVWG CGRYPLDDSK ADHAIAKVYI QANKDLAAEP
ELKAGVDRLM QLYESDDSET ASKFKSAVDY ALSGIEETLR RLNISHDSYR WEGEFVRDGS
TAGVVKVLES TGLTEWDEGA FQLDLSGEGF EKKLVLKRSD GTSLYTTRDL AYHKWKAENS
DRMIDVLGAD HKLISSQLKA ALRLMGVREP EIVIFEFVSL PTGSMSTRKG KFISTDELLD
EVEAQAYKEV TARRPEEAEE FRRAVAKDVA LGAVRYDVVK VSPDKATVFD WKAALDFEKL
SAPFIQYSHA RACSILDKAG DFGELDPRRL TAPEEIDLIK KISQFDLAVE LAARELKPHQ
LATYARELAE IFNQF
//
