ID A0A2U8DZZ8_9BACT Unreviewed; 592 AA.
AC A0A2U8DZZ8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CKA38_01475 {ECO:0000313|EMBL:AWI08105.1};
OS Ereboglobus luteus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Ereboglobus.
OX NCBI_TaxID=1796921 {ECO:0000313|EMBL:AWI08105.1, ECO:0000313|Proteomes:UP000244896};
RN [1] {ECO:0000313|EMBL:AWI08105.1, ECO:0000313|Proteomes:UP000244896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ho45 {ECO:0000313|EMBL:AWI08105.1,
RC ECO:0000313|Proteomes:UP000244896};
RX PubMed=29295750; DOI=10.1016/j.syapm.2017.10.005;
RA Tegtmeier D., Belitz A., Radek R., Heimerl T., Brune A.;
RT "Ereboglobus luteus gen. nov. sp. nov. from cockroach guts, and new
RT insights into the oxygen relationship of the genera Opitutus and
RT Didymococcus (Verrucomicrobia: Opitutaceae).";
RL Syst. Appl. Microbiol. 41:101-112(2018).
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; CP023004; AWI08105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8DZZ8; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000244896; 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:UP000244896}.
FT DOMAIN 5..92
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 473..592
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 592 AA; 66085 MW; CD1F98B81CC8BA91 CRC64;
MHVSFNIAAD IDAAMKTAVA AAGIDAASFA PEVRTADPRN GDFQANGVLA FAKRNKQNPR
ALAEQIIAAL PDEIKARFDT AIAGPGFINF TLKPAALFDW LNTYDSIEKL SSGASSAYAG
QTWVVDYSSP NTAKQMHVGH LRSAVIGEAI CRLLEFSGAK VIRDNHLGDW GTQFGKLIYG
YKRWLDKDAL ARDPISELER LYKLGNEATP DGSPELEEAR QELVKLQRGD YDSLELWKLF
SEVSKKAFDE IYKQLAIKFD HYLGESFYND KLQPVLDELQ KLGLAEESQG ALVVFHPEHP
RFAKQPFIVR KSDGASNYAT TDLATMLYRV EHFHADGIVI LTDFRQSDHF EQLALTAEKW
FAKTGRRMPR FAHVTFGAVL GENNKPLKTR DGDTIKLKEL LGEAEERAYT IVSEKNAGRP
KAEQFTDEEC RAIAHYVGIG AVQYADLSQN RSSDYLFSWD KMLSLDGNTA PYLLYAIARI
HSIFRKAGIE PEALAAIEKE ASPLETPTEL ALARKLVKFP DALRLATDTL RPHFLALYLY
ELAGDYSAFN NADKVLVDDT PVRARRLLLC ARTQLTLNTG LNLLGVRTLK RM
//
