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Database: UniProt
Entry: M0DWG2_9EURY
LinkDB: M0DWG2_9EURY
Original site: M0DWG2_9EURY 
ID   M0DWG2_9EURY            Unreviewed;       602 AA.
AC   M0DWG2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
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:ELZ38439.1};
GN   ORFNames=C471_10775 {ECO:0000313|EMBL:ELZ38439.1};
OS   Halorubrum saccharovorum DSM 1137.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=1227484 {ECO:0000313|EMBL:ELZ38439.1, ECO:0000313|Proteomes:UP000011514};
RN   [1] {ECO:0000313|EMBL:ELZ38439.1, ECO:0000313|Proteomes:UP000011514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1137 {ECO:0000313|EMBL:ELZ38439.1,
RC   ECO:0000313|Proteomes:UP000011514};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ38439.1}.
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DR   EMBL; AOJE01000057; ELZ38439.1; -; Genomic_DNA.
DR   RefSeq; WP_004048858.1; NZ_AOJE01000057.1.
DR   AlphaFoldDB; M0DWG2; -.
DR   STRING; 1227484.C471_10775; -.
DR   PATRIC; fig|1227484.4.peg.2118; -.
DR   eggNOG; arCOG00487; Archaea.
DR   OrthoDB; 372102at2157; -.
DR   Proteomes; UP000011514; 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; 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; 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}.
FT   DOMAIN          3..89
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          469..602
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   MOTIF           124..134
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ   SEQUENCE   602 AA;  66109 MW;  3E6E26DE934504C3 CRC64;
     MFRQFRSEVA DALGDALASL DLPTDDLGIE RPPDDMDATL ASSVAFRLAG EVGDAPPNVA
     ATVADAVDAD GYDYLAAVDT AGPYVNFHAG ERYLADTLDA AAPDAGYGAL PDRDTSVVVE
     HTSANPTGPV HVGRARNPIV GDAVANLLEY AGYDVDRHYY VNDAGRQMAV FTWAYERFDE
     SDLDEEPARD RAEYDLVRYY RKGNAYLEEA DPEAVEAAEN EISAILQGLE AGDEETYERV
     GEVVDAVLGG MKECLARLPA EFDEFVKETR FMRDGSTDEI AARLKETDHA VYEEDAWQLE
     LNDWGIDKNL VFLRSDDTSL YTTRDLAHHE WKFDNYDRAV TVLGEDHKLQ ADQLDAALEL
     LGNDTDRLGH VIYSYVNLPE GKMSTRKGTG VMLDDLLDEA IDRAREAVES RMDDRIRDDD
     LTEADVERIA HEVGIGAVRY DIISKQPAKA ITFEWEDALD FEGQSAPFVQ YVHARCCGIL
     DEAADAGIEV PGVTADAGGA VDYGALDVDA AVFETEEARD LLREVARFPA AIEEAANDLE
     PHTIATFTRE FADAYNAFYR ECPVVTAEDE ELRAARVALV AAAKHTMANA LDVLGVEAPE
     SM
//
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