ID A0A428P9E4_9HYPO Unreviewed; 662 AA.
AC A0A428P9E4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=CEP54_012324 {ECO:0000313|EMBL:RSL49626.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL49626.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL49626.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL49626.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
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:RSL49626.1}.
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DR EMBL; NKCI01000176; RSL49626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428P9E4; -.
DR STRING; 1325734.A0A428P9E4; -.
DR Proteomes; UP000288168; 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: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; 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:UP000288168}.
FT DOMAIN 519..646
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 662 AA; 74271 MW; A80514273C9E57C8 CRC64;
MASPTNTVAG LNALLYGLSL EPMPESASPI ALTRPVEIWR SYLAEFLSKL TVLNCDATTI
REAIASTTET SLGDLTLILP RLKLKNVDNK ALNRLAFSVA AQLPFSSLFL APRVDDIQLR
MTFSPDTLPR LLLPYIADRK SAYGFDLSQG LRDPKEPNKG KKKVIIEFSS PSLATGFNGN
NLRSTLLGDF IANLYEAMGW EVMRLNYLAD WGKHIALLVD GYRRFGSEKK LQQERSIHLL
DVYTQMEGLF KPVQDLKGKA KQGEKCASPV EDKTIGFERD ETFKKMESRD GETFKLFQHF
RDITIEDLRV QYRRLGIGFD EYSGESQVQP ATITKVENAL KEKGILKESN ESWVIDWAKH
TGKKGLSTQT IRGRDGATRY PLRDVAAALE REEKFTFDKM IYVTSSAQDS HFQQVFSALE
LMGRRDLIEK LQHMSFGAMQ GLEGNSLREI LDNCEARMRD AMNMEHDEED LDGSAAERIT
NNAMVGALLA QELSRKKSHS YTFELKKLTS FGSHSGPMLQ GCHTRLTALI NELRTEGAET
SEIDYAALKD PDCANLLRVM AQFPDIVAAV YKSAEPHSLL GYLYRLMDSL SLVVPHPDEE
DDEDEGGSVC TVQQETSRGE KKARLVLYQN ARQVLENGMK LLGFPLDLQD VVVDFTSDSA
RL
//
