ID A0A3N6MUN6_9EURY Unreviewed; 609 AA.
AC A0A3N6MUN6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123};
GN ORFNames=EA462_12120 {ECO:0000313|EMBL:RQG89112.1};
OS Natrarchaeobius halalkaliphilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrarchaeobius.
OX NCBI_TaxID=1679091 {ECO:0000313|EMBL:RQG89112.1, ECO:0000313|Proteomes:UP000273828};
RN [1] {ECO:0000313|EMBL:RQG89112.1, ECO:0000313|Proteomes:UP000273828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArcht-Sl {ECO:0000313|EMBL:RQG89112.1,
RC ECO:0000313|Proteomes:UP000273828};
RA Sorokin D.Y., Elcheninov A.G., Kostrikina N.A., Bale N.J.,
RA Sinninghe Damste J.S., Khijniak T.V., Kublanov I.V., Toshchakov S.V.;
RT "Natrarchaeobius chitinivorans gen. nov., sp. nov., and Natrarchaeobius
RT haloalkaliphilus sp. nov., alkaliphilic, chitin-utilizing haloarchaea from
RT hypersaline alkaline lakes.";
RL Submitted (OCT-2018) 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 ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC 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:RQG89112.1}.
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DR EMBL; REFY01000004; RQG89112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6MUN6; -.
DR OrthoDB; 372102at2157; -.
DR Proteomes; UP000273828; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07956; Anticodon_Ia_Arg; 1.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
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; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 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; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Reference proteome {ECO:0000313|Proteomes:UP000273828}.
FT DOMAIN 3..89
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 468..609
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 123..133
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 609 AA; 68264 MW; B483F0858135DD0E CRC64;
MFLSLRTEVE KALGGALSAL EFPTDDLGIE EPPEDVESVL ASSVAFRLAG EAGAPPPQVA
GQLADELDVD DLEYVSEVRS QGPYLNFLPS DAYFAETLGA ATDERYGALE DRGESVVVEH
TSANPTGPVH VGRARNPIIG DAVSNLLEYA GYDVSRHYYV NDAGRQMAVF TWAYETFDES
DLDDDPERDR IEYDLVRYYR HGNAFLENAP ESEVEAAEAE IESIMRGLEA GEETTYERVS
EVVDQVLSGM TACLERLPAE FDEFVKETRF MRDGSTDELV SRLKALDEAV YEEEAWQLDL
SEQGIEKNFV FLRSDDTSLY ATRDLAHHEW KFDNYDRAVT VLGEDHKLQA RQLRTTLELL
GTDTDELRQV LYSYVNLPEG KMSTRRGTGV DLDDLLDEAI DRAREEVEDR MDDRIRDDDL
DDEDVERIAH QVGIGAVRYD IVSKQPTKSI TFEWDQALDF EAQSAPYVQY VHARCCGILE
EGGALQTRDE TDDARPPAEA VETDTATVEI ERDVDADLLE TDAERDLLET IARFPAVVDE
AADDLEPHRV ATYTREFADR FNAFYRECPV LADDVDPEQR EARLALVAAS RHTVSNALSI
LGVAAPRSM
//
