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Database: UniProt
Entry: A0A0S9CNM9_9MICC
LinkDB: A0A0S9CNM9_9MICC
Original site: A0A0S9CNM9_9MICC 
ID   A0A0S9CNM9_9MICC        Unreviewed;       554 AA.
AC   A0A0S9CNM9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=ASE96_03710 {ECO:0000313|EMBL:KQN95289.1};
OS   Arthrobacter sp. Leaf69.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN95289.1, ECO:0000313|Proteomes:UP000051467};
RN   [1] {ECO:0000313|EMBL:KQN95289.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN95289.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN95289.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN95289.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQN95289.1}.
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DR   EMBL; LMLR01000001; KQN95289.1; -; Genomic_DNA.
DR   RefSeq; WP_056426077.1; NZ_LMLR01000001.1.
DR   AlphaFoldDB; A0A0S9CNM9; -.
DR   STRING; 1736232.ASE96_03710; -.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000051467; 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; 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};
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}.
FT   DOMAIN          4..95
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          428..554
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   MOTIF           132..142
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ   SEQUENCE   554 AA;  59812 MW;  F717A0F9D171330F CRC64;
     MTPEELSLAI SACLKDAVAA GEIGLSASDV PDEVRVERPK NRDHGDWATN IALQLAKTAG
     TNPREFASVL SARLKSIDGV SAVDIAGPGF LNITVDAAAA GALAKAIVEA GPAYGTNTAL
     AGHTVNMEFV SANPTGPLHI GHTRWAALGD AIARVLRASG ADVTAEYYIN DAGSQMNVFA
     HSVLSRLHGR GVPEGGYPGE YIADLGHEVL TQHPDIRELT DVAALPVIRG AAYKAQLHDI
     KRTLAEFGVE FDVYFSEQEL HDAGAIEDAV ARLREQGHVY DDGGAVWLRT TDFGDDKDRV
     MIRANGEPTY FAADAAYYLS KKDRGYTEKI YLLGADHHGY INRLKAIAAA AGDDPEVNIE
     VLIGQLVSVN GAKLSKRAGN IIELKDLISW LGKDAVRYSL ARFPADSPLT LDPELLKKHS
     NENPVFYVQY AHARSRGTAR NAVAAGVERR VDGKDCFEAS LLEHATENEL LSHLGSYPSI
     VARAAELREP HRVARHLEVI AGAYHRWYDA CRVAPQGDEP ITDLNRTRLW LNDATSQVLA
     NGLELLGVSA PERM
//
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