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Database: UniProt
Entry: A0A171KPV1_9BURK
LinkDB: A0A171KPV1_9BURK
Original site: A0A171KPV1_9BURK 
ID   A0A171KPV1_9BURK        Unreviewed;       561 AA.
AC   A0A171KPV1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, 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   ECO:0000313|EMBL:KKO70918.1};
GN   ORFNames=AAV32_14440 {ECO:0000313|EMBL:KKO70918.1};
OS   Kerstersia gyiorum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Kerstersia.
OX   NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO70918.1, ECO:0000313|Proteomes:UP000078084};
RN   [1] {ECO:0000313|EMBL:KKO70918.1, ECO:0000313|Proteomes:UP000078084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1 {ECO:0000313|EMBL:KKO70918.1,
RC   ECO:0000313|Proteomes:UP000078084};
RA   Greninger A.L., Kozyreva V., Chaturvedi V.;
RT   "Genome sequence of Kerstersia gyiorum CG1.";
RL   Submitted (APR-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:KKO70918.1}.
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DR   EMBL; LBNE01000011; KKO70918.1; -; Genomic_DNA.
DR   RefSeq; WP_068373732.1; NZ_LBNE01000011.1.
DR   AlphaFoldDB; A0A171KPV1; -.
DR   STRING; 206506.AAV32_14440; -.
DR   PATRIC; fig|206506.3.peg.3077; -.
DR   Proteomes; UP000078084; 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:UP000078084}.
FT   DOMAIN          7..93
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          444..561
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   561 AA;  61790 MW;  55173AA6EE7C2456 CRC64;
     MLPEQQNLLI SRIQAAVNAL LPEAQPSIQL ERPKVAAHGD AACNVAMQLA KPARRNPREL
     AQAIVDHLLA DPQAANLLAG AEVAGPGFIN FRLSPAAHQA VLGAIAGQRE QYGRAPRRDE
     KVLVEFVSAN PTGPLHVGHA RQAALGDALC RLFDAHGYDV TREFYYNDAG NQIDNLAISV
     QARGRGISPD DASYPADGYR GDYIVDIAND YLAGKTVQAS DGVPVTGKGD LNDLDAIRRF
     AVTYLRNEQD LDLQAFGLKF DNYYLESSLY TSGRVENTVQ RLVDKGHTYE MDGALWLRTT
     ELGTGDDKDR VMRKAEGGYT YFVPDVAYHE AKWERGFHKA INIQGSDHHG TVARVRAGLQ
     GLDIGIPKDF PAYILHKMVK VVRGGQEVKI SKRAGSYVTL RDLIDWVGRD AVRFFLIQRR
     ADTEFTFDID LARSQSEENP VYYIQYAHAR ICSVLEQAQA DAAALQQADA TPLVAPTEIA
     LLQRLSEFPA LVTLAAQELS PHLVAFWLRD CAADFHAWYN AERVRVDDAA LRDARLRLAD
     ATRQVLANGL ALLGVAAPQR M
//
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