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Database: UniProt
Entry: A0A0J9E1Z0_9RHOB
LinkDB: A0A0J9E1Z0_9RHOB
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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
//
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