ID A0A369JGA5_HYPMA Unreviewed; 634 AA.
AC A0A369JGA5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JUN-2023, entry version 17.
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_0 {ECO:0000313|EMBL:RDB20230.1};
GN ORFNames=Hypma_012648 {ECO:0000313|EMBL:RDB20230.1};
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:RDB20230.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB20230.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB20230.1,
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:RDB20230.1}.
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DR EMBL; LUEZ02000069; RDB20230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369JGA5; -.
DR STRING; 39966.A0A369JGA5; -.
DR InParanoid; A0A369JGA5; -.
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 PANTHER; PTHR11956:SF11; ARGININE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 2.
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 514..634
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 318..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 71053 MW; 9ECEF1D76F4E76EA CRC64;
MSPPQSDYPV IAGTDISRCV LDQFRVAIAV QLSHSLGISL SACYEGIDVG KKGVDFTVAV
PRFRLKSKPQ ELAARAAKEF IPNEYISSVE AAGIFLHFQV KTSTLSRLVL SQIYELSQPS
PNAPHGTYGQ NLEASGKKVV IEFSSPNIAK PFHAGHLRST IIGTFLANVY ETCGAHVIRM
NYLGDWGKQF GLLAVGFERY GSEEKLSENA IMHLFDVYVR VNQDVKAEAA SGEQAPTDEK
AKDVFRAMED GDANTLALWK RFRDLSIKAY EQAYRRLNVH FDVYAGESLV TSENIQDAIK
ALRAKDLLVE KRKSESVTHK DYNRAEPETT EDDIDASPPE GELGEKPAWA VDLNAWKLGK
PVVQKPDGTT IYMVRDIAGA IQRYEEYKFD KMIYVIGDQQ DLHVAQFFKI LSLMEVPFAS
QLEHVNFGRV NGMSTRNGEV KFLDQILDTA KEAMLDQMNK NQEKMSQIED PDRTADEIGI
TCVKIQDMSA KRIISYDFDW QRMTSFEGDT GAYLQYQHVR LCSVARKVAP SVILRNDPTL
IDTSLLTEPK AHELVMLLAR YPDVVRTALK NSEPNTIASY CFKLSHIVSS AWEILIVKDQ
EIELAQARLL LFTCAKSVLS SAMRLLSLSP LEHM
//