ID A0A2K1QJU4_9PEZI Unreviewed; 538 AA.
AC A0A2K1QJU4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CAC42_656 {ECO:0000313|EMBL:PNS15397.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS15397.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS15397.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS15397.1};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) 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:PNS15397.1}.
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DR EMBL; NKHZ01000070; PNS15397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1QJU4; -.
DR STRING; 2082308.A0A2K1QJU4; -.
DR InParanoid; A0A2K1QJU4; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000243797; 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 CDD; cd07956; Anticodon_Ia_Arg; 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; 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; 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; 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:UP000243797}.
FT DOMAIN 420..538
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 538 AA; 60260 MW; 4465343021C4562C CRC64;
MVAADDRKEI VAHPDCNPVD VAHLVITKQL HRITDIDAKT FHECDTIQLP RAVGISIRFD
FLPSTLPKLV LDRIFKLGEE YGKYPYHGLP SKSTGGPRKK ALVEFSSPNI AKKLHAGHLP
STIIGGFLSN LFTSAGWDVV RMNYLGDWGR QYGLLAVGWQ RYGDETSFSA DPIGHLYDVY
VKISADSKPE DDAYKAASKK GEDTAETYAR LNIHFDEYSG ESQVTPDVMR GAEAVMQKRG
LIHADNSAWV IDFARFAAKK LGVAIVRNRN TTSNYLLRDI GAAIQRYKKY KMDRMIYVVM
AEQEHHLLRL FKILELMGGE YAEISTKMQH VTFGKVNGMS IRKGTAKFLD NILHDVSEAM
HTVMRDNEEK YQQIPEPDLV ADTLGVSAIM VQDMSSKRVH DYDFDMARMT SFKGDTGPYL
QYTHARLCSI ARKAGFTRNQ LLSADWSLLV EKPAIDVLRL MAQFPDVGGQ TLVTLEPATI
LNYLFRLTHQ LSSGYELLRV LGAESKEVAE ARAALYDGAR QVLSNGMALL GISPVERM
//