ID B1ZTW6_OPITP Unreviewed; 590 AA.
AC B1ZTW6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
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 OrderedLocusNames=Oter_2566 {ECO:0000313|EMBL:ACB75848.1};
OS Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=452637 {ECO:0000313|EMBL:ACB75848.1, ECO:0000313|Proteomes:UP000007013};
RN [1] {ECO:0000313|EMBL:ACB75848.1, ECO:0000313|Proteomes:UP000007013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11246 / JCM 15787 / PB90-1
RC {ECO:0000313|Proteomes:UP000007013};
RX PubMed=21398538; DOI=10.1128/JB.00228-11;
RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT abundant inhabitant of rice paddy soil ecosystems.";
RL J. Bacteriol. 193:2367-2368(2011).
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 -!- SUBUNIT: Monomer. {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; CP001032; ACB75848.1; -; Genomic_DNA.
DR RefSeq; WP_012375383.1; NC_010571.1.
DR AlphaFoldDB; B1ZTW6; -.
DR STRING; 452637.Oter_2566; -.
DR KEGG; ote:Oter_2566; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_0; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000007013; Chromosome.
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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000007013}.
FT DOMAIN 5..92
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 472..590
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 130..140
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 590 AA; 65024 MW; 1DA640BB41325F4D CRC64;
MHVPFSLVDE LDRVLKSAAA AAGFDAAAFS PEVRVADAQH GDYQANGVLG YAKSRKQNPR
ALAEKLVAAL PAEFTQSTRV TIAGPGFINF TLAPGSLLAW LRTYATAEQL AAGAAADHAG
QTWVVDYSSP NTAKQMHVGH LRSAVIGEAI CRLLAFTGAR VIRDNHLGDW GTQFGKLIYG
YKRWADPAAL AADPIEELER LYKLGHHATP EGSPELEEAK RELVKLQSGD PENVALWKKF
SEVSLGAFQQ IYDRLGIHFD HHLGESFYND KVERVYGELT DIGLAENSDG ALVVFHDEHP
RFSRNAERPN PFMVRKADGA SGYASTDLAT ALYRTEHFQA DGIVIVTDFR QSDHFEQLFL
TVKKWFAAKG YRLPQLHHVT FGAVTGEDGK ALKTRDGGTI KLKALLDEAV ERAFAIVSEK
NPELPEDERR AIAEAVGVGA VQYADLSQNR SSNYVFSWEK MLSLEGNTAP YLLYAVARIH
SIFRKAGATP GEPATESAAT EPETPTEIAL ARKLLKFPDA VRLATETLRP HFLSLYLFEL
AGDYSTFNNA DRVLVDDPVI RARRLLLCSR TLLILETGLR LLGLRPLTRM
//
