ID A0A0D1Y8D9_9EURO Unreviewed; 684 AA.
AC A0A0D1Y8D9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=PV11_08849 {ECO:0000313|EMBL:KIV77009.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77009.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV77009.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77009.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
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DR EMBL; KN846954; KIV77009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1Y8D9; -.
DR STRING; 1016849.A0A0D1Y8D9; -.
DR HOGENOM; CLU_006406_6_0_1; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000053599; 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; 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: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; 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.
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:UP000053599}.
FT DOMAIN 550..666
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 279..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 76608 MW; 0069BAB4D1906331 CRC64;
MSFSMDLENL AEGLLSRLKG RSFTSSDHIE AVVMASLTLG GVRELLKNLN LEKEVPSFTA
ADIQNNPLDI YQSRLAEILV QITNCEQQAA YDSILLPNEL GDLTVVVPRL RLQNIKPGEV
VADLKQKFPP SPLFANPIDD GINLRLWFSP VTLARLLIPY IRDRGASYGK SQSADLSEAH
ESISVPQKVI VEFSSPNVGK EFDGNHLRST VIGAYIASIY QFMGWDVCRM NFLGDWGRHI
GLLAAGWSRF GSEELLKKNP LRHLLDVFVQ VNDLLRHEQE EAKSRSSQDQ ENVVEHSTTS
TEKDELFRRL EDGDPDALAI WRMFREACVT SYTDLYARLN IKFDHYSGES EVEAKTIVEV
EEILKEKDAY MESDGAWVID FEKHGYKGQR AAIARFSNGT TSYLLRDIAA VLERHNRYSF
DKMIYVVSAK QDTHFHQVFN ALELMGHAQL ASKLQHVSFG KFQGLSPKPD SGGLLLSDIL
DQCQGALEDF LKDSPEDFAE LREELATSKL VDNLTASGLM TQELSIKRGS TFTYDTAKMA
DMNSDAGLTL QYWFTKLDSK LKGVRIVHEE LEHADYSIFT DDAFSDILRI LIQFPGIVKS
SFKNLESSTI LTYLFQLTDA LDGVLGDEEE AECSNLNLAK LAFFECVRQT LENGMQMVGL
VPLRAETGDG SAITVSLEAK VTTD
//