ID A0A024FUS2_9STRA Unreviewed; 644 AA.
AC A0A024FUS2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
GN ORFNames=BN9_097050 {ECO:0000313|EMBL:CCI10394.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI10394.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI10394.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI10394.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) 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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, 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:CCI10394.1}.
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DR EMBL; CAIX01000233; CCI10394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024FUS2; -.
DR STRING; 65357.A0A024FUS2; -.
DR InParanoid; A0A024FUS2; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 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-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; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
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|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 520..644
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 644 AA; 72865 MW; 6F350847EE81B74F CRC64;
MRFLRCDFLS TLRLQKSLFL QTRTLHNKNH RYSVIQAISS LLSEALSSIN DVSISREKLT
AQLGVRRSTQ PKIDFQSNIA LILAHRSPNT SLRPSEIGHT LLQNLPCESS GQRILEAVSV
SSTGFLNFKL CDQFIARFVH EMVLDTHPKS TGESRSILVD FASPNYGKRL HVGHLRSSVI
GDTICNLLEY QGHQVARVSH SGDLGSAIAT LLATFVTEKV PFKSIHNDSQ LAAMYERGKQ
RLAQDETGAF TSIVKQIVII LQHPENPSTD PKFCHEILDM WRHVCALSQH SYQRIFDRLG
VKVQNRPESS YIRDIGPVLA ELEKRGFITK SQGADCIFVS HQLPPLIVCK QDGGYLYATI
DLACLYCRLF GSEVDSTQYD EIIYVTDQSQ NLHFRQLFLA AHRVEWIKEI SEKIGVQKQR
NAKLRHVAFG LVLGPDGSKL SSRNGAFDYL EDLLDAAAIE CQNRSILPLH KAKVQVETEL
FRRIGDAAVR YFELSQQRTR DYKFTWDQAL TFKGNTGVYL LYACARLEGI QRKLQHASDY
DTFLTHSTAE VLTAASMQWQ SSERALALLL AQFEDEVSQA TIHMTPHTLC DYLYRVASHF
HTFYEDCRVV GVPEMNARLC LCALTWNVLT KGLKLLGIEP VDRM
//
