ID A0A2T3AJY7_9PEZI Unreviewed; 641 AA.
AC A0A2T3AJY7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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 ORFNames=BD289DRAFT_450005 {ECO:0000313|EMBL:PSS00898.1};
OS Coniella lustricola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Schizoparmaceae; Coniella.
OX NCBI_TaxID=2025994 {ECO:0000313|EMBL:PSS00898.1, ECO:0000313|Proteomes:UP000241462};
RN [1] {ECO:0000313|EMBL:PSS00898.1, ECO:0000313|Proteomes:UP000241462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B22-T-1 {ECO:0000313|EMBL:PSS00898.1,
RC ECO:0000313|Proteomes:UP000241462};
RA Raudabaugh D.B., Iturriaga T., Carver A., Mondo S., Pangilinan J.,
RA Lipzen A., He G., Amirebrahimi M., Grigoriev I.V., Miller A.N.;
RT "Coniella lustricola, a new species from submerged detritus.";
RL Mycol. Prog. 17:191-203(2018).
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; KZ678380; PSS00898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3AJY7; -.
DR STRING; 2025994.A0A2T3AJY7; -.
DR InParanoid; A0A2T3AJY7; -.
DR Proteomes; UP000241462; 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 HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
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:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000241462}.
FT DOMAIN 37..119
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 524..641
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 239..266
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 641 AA; 72228 MW; 217844405E511372 CRC64;
MAAPAGIDHL VKLTSDLKLD NVRETFPTAY PETNPVDVYR IHLTNVLEKI TGVDRKIIYP
ALQWTQGLDK GDVMMAVPAL RVKGKKPDEL AKEWTDKFPE DDPLISKPVV TAVHMSFFFK
TEPLTKAVIP LIRSLGKTYG NNPAMGLKDP KNPDGERKRI IVEFSSPNIA KPFHAGHLRS
TIIGGFIANL YELAGWDVVR INYLGDWGKQ YGLLALAFER YGDEEALNKD PINHLFNLYV
RINAEIKEEE DKVKALKAEG KDAEAAQLVE SGLDEQARKY FKKMVDGDET ALKQWRRFRD
LSITRYQQTY ARLNIHFDSY SGESQVPESA MEAAAREMEA KGISTESDGA RIVDFTALVP
GKEGKRLERP IIRKKDGTAL YLTRDISELL GRHEKYNYDQ MIYVVASQQD LHLKQLFKIV
ELMGHKDIAA KCQHINFGMV LGMSTRKGTV KFLDDILRDV GDKMHEVMRK NDDKYSQVAN
PEATADTLGI SSVMIQDMTG KRINNYTFNM DAMTSFEGDT GPYLQYAHAR VCSIERRAAI
PAEELAKADL SLLTEPHAIN LVRALSQWPD VVQNTLKTLE PTTVVIYLFK LTHVLSSSYD
GLRIVGAEEE VRKARMALYD AARIVISNGM RLLGLSPVER M
//
