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Database: UniProt
Entry: A0A369JGA5_HYPMA
LinkDB: A0A369JGA5_HYPMA
Original site: A0A369JGA5_HYPMA 
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
//
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