ID M7TI93_EUTLA Unreviewed; 559 AA.
AC M7TI93;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=UCREL1_3318 {ECO:0000313|EMBL:EMR69656.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR69656.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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; KB706040; EMR69656.1; -; Genomic_DNA.
DR RefSeq; XP_007791251.1; XM_007793060.1.
DR AlphaFoldDB; M7TI93; -.
DR STRING; 1287681.M7TI93; -.
DR KEGG; ela:UCREL1_3318; -.
DR eggNOG; KOG1195; Eukaryota.
DR HOGENOM; CLU_006406_6_0_1; -.
DR OMA; PNMASEF; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
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; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001278; Arg-tRNA-ligase.
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: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; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363038,
KW ECO:0000313|EMBL:EMR69656.1}; ATP-binding {ECO:0000256|RuleBase:RU363038};
KW Ligase {ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174}.
FT DOMAIN 426..557
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 501..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..523
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 62303 MW; 0C7480FB1FF9CC83 CRC64;
MLICRFQFSP TPLFQLPIPD GVHLRFVFST ATLPRLVLPY IDDRGDKFGR DSWSGFDNAP
SDTTPRKLLV EFSSPNLASE FSPAHFRSTI LGAQIANIHE AMGWDVVRLN YLGDWGKELG
LLAVGWGRFG SEEAFGKNPM EHLLEVYEEI NELFRPEKEA SKKARDEGQD TASIESQGIY
AERDAFFKKM EEGEPDAIDL WKRIRDTSID YYASAYGRLN IRFDEFSGES QVSQDSIEEV
ESILKEKGIY EESGGSWIVD FSKHGPRSLG VSVLRGRTGS TSYLLRDLAA ILDRDKKYSF
DKMIYVVTAD QDAHFNKVLQ AVRYMGRDDL ADKLEHVNFA KTQGLSPQLG KVHLLGEILD
QSISAIQDTL GAEQDKPLPI NNTEAAANTL GITALIAQDG LHKRSTGYSF NTKSLCSFTG
ETGPSLQACY ASLSAKINES RLGQTTLADI DLQYLQEDPW AEVIRLMAQY PDITLTAYKT
HEPSMVLAYL FRLSEELANC LDDDGDDDEE GEATEEPTEP APTDEEPPEA ILAQAMLYKI
ARQVLQNGMT LLGITPIST
//
