ID A0A369JR69_HYPMA Unreviewed; 591 AA.
AC A0A369JR69;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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 Name=YDR341C_2 {ECO:0000313|EMBL:RDB21844.1};
GN ORFNames=Hypma_011056 {ECO:0000313|EMBL:RDB21844.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB21844.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB21844.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB21844.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) 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:RDB21844.1}.
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DR EMBL; LUEZ02000053; RDB21844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369JR69; -.
DR STRING; 39966.A0A369JR69; -.
DR InParanoid; A0A369JR69; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000076154; 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 CDD; cd07956; Anticodon_Ia_Arg; 1.
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 InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
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; 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:UP000076154}.
FT DOMAIN 470..591
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 591 AA; 66931 MW; 6FD9A5DEC2CADCAA CRC64;
MASTLPSVPD TDPSTCVFDA FRTAIAKRVS EALPLTLEQA YSGVDYGKKG VDFTIALPRF
RLPGKVDELA NKVISKFEPD EWVESVVHDK AFLHFQLNSQ SLVRKVLDQV HALSHLTPSG
LPEYGTNTSG KGKTAIIEYS SPNIAKSFHV GHLRSTIIGA FLANLYKSCG WNVIRMNYLG
DWGTQFGLIA TGFEKYGSQE ELEKDAIKHL FDVYVKVNKE AEGDPNIKIE AAKWFKRMED
GEEAALVNWR VWRELSIKKY EEQYEILNVH FDVYNGESMV GKEWQDKALA RLDEMGLISD
VDGAKLVDLE KWKLGKAVLR KKDGTSIYLT RDIGGAIERY EKYKFDKMIY VVSSQQDLHL
AQFFKILELM EFPWAKNLQH INYGLVHGMS TRRGNVVFLD QIIKEAAGVM FDQMKQNEEK
FNAVEDPEMV SREIGITGVK IQDMAAKRIN NYTFNWDRML SFEGDTGPYL QYAHVRIASI
GRKNPELLPL PPPSQINTDS LASMSHAREI AFLLGSYPDV IKVALKTQEP SGVVTFAFRL
SHAISSAWET VIVKGEKDLE KARARMFLFE CARDVLAASM RLLSIRPLER M
//
