ID A0A0J9E1Z0_9RHOB Unreviewed; 572 AA.
AC A0A0J9E1Z0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=AIOL_001695 {ECO:0000313|EMBL:KMW56740.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW56740.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW56740.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW56740.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-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 -!- 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}.
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:KMW56740.1}.
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DR EMBL; LFTY01000002; KMW56740.1; -; Genomic_DNA.
DR RefSeq; WP_049642580.1; NZ_LFTY01000002.1.
DR AlphaFoldDB; A0A0J9E1Z0; -.
DR STRING; 1675527.AIOL_001695; -.
DR PATRIC; fig|1675527.3.peg.1790; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000037178; 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; 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; 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:UP000037178}.
FT DOMAIN 5..94
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 450..571
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 572 AA; 62610 MW; 47C8E3835AE2F492 CRC64;
MHLFAEIRAL VISTLDDMAE AAELPAGLDT KNVTVEPPRD AAHGDMATNA AMVLAKPAKM
KPRDIAEALA ARLAGDPRVV SAEVAGPGFL NLRLAPGIWA DVVRSVLAAP GFGRSQMGQG
RKVMVEYVSA NPTGPLHVGH TRGAVFGDAL ASLLDYAGFD VTREYYINDG GAQVDVLARS
VYLRYLEAHG QEVAFEDGTY PGDYLIAVGE ALKAKVGDAF VDKGEQFWLT EVREFATEAM
MALIREDLAQ LGIEMDNYFS EKSLYDTGKI EAAIGSLEAK DLIYRGVLEP PKGKAPEDWE
PREQTLFRAT AYGDDVDRPI MKSDGAWTYF APDIAYHYDK VSRGFEAIIN VFGADHGGYV
KRLKAVVAAL SDEKVSLDIK LTQLVKLFKN GQPFKMSKRA GTFVTLRDVV KQVGPDVTRF
VMLTRKNDAP LDFDFDKVLE QSKDNPVFYV QYAHARVRSV LRKAEAAGLA AAAPRIEDAA
EIDLAKKLAE WPRLVEIAAR TNEPHRIAFY LYELAGNFHA LWNKGNDNPD LRFFQEQSPG
ATSEKIALPE AVGVVISAGL GILGVTPVEE MR
//