ID K0IM12_NITGG Unreviewed; 634 AA.
AC K0IM12;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:AFU57499.1};
GN OrderedLocusNames=Ngar_c05560 {ECO:0000313|EMBL:AFU57499.1};
OS Nitrososphaera gargensis (strain Ga9.2).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC Nitrososphaeraceae; Nitrososphaera.
OX NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU57499.1, ECO:0000313|Proteomes:UP000008037};
RN [1] {ECO:0000313|EMBL:AFU57499.1, ECO:0000313|Proteomes:UP000008037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA Spieck E., Streit W., Wagner M.;
RT "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT insights into metabolic versatility and environmental adaptations.";
RL Environ. Microbiol. 14:3122-45(2012).
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; CP002408; AFU57499.1; -; Genomic_DNA.
DR AlphaFoldDB; K0IM12; -.
DR STRING; 1237085.Ngar_c05560; -.
DR KEGG; nga:Ngar_c05560; -.
DR PATRIC; fig|1237085.11.peg.531; -.
DR HOGENOM; CLU_006406_6_1_2; -.
DR InParanoid; K0IM12; -.
DR OrthoDB; 372102at2157; -.
DR Proteomes; UP000008037; 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; 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; 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 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; 2.
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}; 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:UP000008037}.
FT DOMAIN 8..91
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 517..634
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 129..139
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 634 AA; 71414 MW; CDB5E24E08C5D060 CRC64;
MTFRLFRNDV RRLVKQALDN AGYPAVEFDV SEPPQKEFGD LSCNVAFLLA RHAKKPPQKI
AAELVEAIRL NIKDTCVLSA ETAGGHINFK ADYSRLSPAT LGQVLKSPEN YGYPDSGQGR
HIVIEHTSVN PNKALHVGHM RNVIIGDTLY RIMKATNHRT TVLNYVDDSG LQVADIVVGF
KFSGFNVEPP KGKKFDHYCG DEVYVKINEM YEKDPLLAEK RKLVLKEIEE GKSEIARFAT
DITLRVLNEQ LKTCWRMKAR YDLLNFESHI VVSKLWSKTF ELLKKERLTH FEEEGKNKGC
WVIEAKDEED KVLVRSDGTA TYIAKDIPYA AWKLGLIEDP FSYREYLGQW DGSMLYATTL
GGSDKPTAAK KFNGGERVIT IIDSRQARLQ RIISQVLSKI GAGTQEYFHL SYEAVTLSSE
TAKAFGIDIG DRQFMHMSGR KGIYVNADYV LDTLHTKAYE EVKTRNPGFT EEQLNAIAEE
IAISAIRYNM IKQDLDKIIT FDVKESLSLE GDTGPYLQYA YARSQRILEK SGQDIAGSNF
AFDRLAHESE IALIKEIAKL DLVVEDAAKS LSPKSLARYA YNLATTFNLF YEKVPVLKEQ
DADIRMARLA LVKAFGVALK NALDVLGITA LDHM
//
