ID W7KWL1_9CREN Unreviewed; 620 AA.
AC W7KWL1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ECO:0000313|EMBL:EWG07052.1};
GN ORFNames=ASUL_06013 {ECO:0000313|EMBL:EWG07052.1}, TQ35_02200
GN {ECO:0000313|EMBL:KJR79386.1};
OS Candidatus Aramenus sulfurataquae.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Aramenus.
OX NCBI_TaxID=1326980 {ECO:0000313|EMBL:EWG07052.1, ECO:0000313|Proteomes:UP000054284};
RN [1] {ECO:0000313|EMBL:AHM94042.1}
RP NUCLEOTIDE SEQUENCE.
RA Servin-Garciduenas L.E., Pacheco-Lamas H.R., Peng X., Garrett R.A.,
RA Campos-Garcia J., Martinez-Romero E.;
RT "Phylogenetic diversity of archaeal communities inhabiting Mexican hot
RT springs.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EWG07052.1, ECO:0000313|Proteomes:UP000054284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1-illumnia {ECO:0000313|EMBL:EWG07052.1};
RX PubMed=24604657;
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Draft Genome Sequence of the Sulfolobales Archaeon AZ1, Obtained through
RT Metagenomic Analysis of a Mexican Hot Spring.";
RL Genome Announc. 2:e00164-14(2014).
RN [3] {ECO:0000313|EMBL:KJR79386.1, ECO:0000313|Proteomes:UP000053480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1-454 {ECO:0000313|EMBL:KJR79386.1};
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL Submitted (MAR-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 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}.
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DR EMBL; KC912714; AHM94042.1; -; Genomic_DNA.
DR EMBL; ASRH01000005; EWG07052.1; -; Genomic_DNA.
DR EMBL; JZWS01000009; KJR79386.1; -; Genomic_DNA.
DR AlphaFoldDB; W7KWL1; -.
DR PATRIC; fig|1326980.6.peg.1189; -.
DR Proteomes; UP000053480; Unassembled WGS sequence.
DR Proteomes; UP000054284; 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; cd00671; ArgRS_core; 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; 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; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 2.
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; 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:UP000054284}.
FT DOMAIN 504..620
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 112..122
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 620 AA; 71118 MW; 94901D2ACF746536 CRC64;
MNVIREAKRE MARVISQAIN VEEEKVFNNI EYPSKEGLGD LSLPLPSVTR NLNIDVSGRG
KYVKSFRRDG IFINVELDEV SVFNDVFSSL SEDYGLEKVD KPKRIVVEHT SANPIHPLHI
GHLRNAILGD TLVRLLRARG HLVNSRFYVN DSGRQVAILI YGLSKLNYPE PPAGVKKDEW
LGLIYAMTNV ILEIRQITQE LKNASESEYK EKISKRDELV AVAQGLRERN EEYFDVLSDG
IMKEEDPEKV ILDIIERYER GDERTKQIVR KYVNYALEGF MESLGKLGIS FDVFDYESDL
LWNGDVRKVL EETMDSRARV NYKGTWALDL ENFIDEAVKE ELRIPKGLEL PPLVLMRSDG
TTLYTLRDVA YTFKKFSDFK ADVVINVIAE QQAVPQMQLR ATLYLLGYPE HAKNLLHYSY
GMVSLQGMRM SGRLGRYISF DEVYEKVKEV VEAKVREKKG NLEELDEIVN SAIRYAIVSV
SANKPVTFNV NKITNLEENS GPYLQYTYAR AYNILAKVTD HLDVSNIDPL ELVGEKRKIL
IMIARFPEVF AKAADDMSPE VLTVFLRQFS DLFNAWYDKE RVLQEKDEKK RITRIFLVKG
VEAVLRNGLK SLGIKPLTKM
//
