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Database: UniProt
Entry: A0A0D1Y8D9_9EURO
LinkDB: A0A0D1Y8D9_9EURO
Original site: A0A0D1Y8D9_9EURO 
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
//
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