ID   A0A2H3SRH3_FUSOX        Unreviewed;       635 AA.
AC   A0A2H3SRH3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN   ORFNames=FRV6_03255 {ECO:0000313|EMBL:SCO79042.1};
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO79042.1, ECO:0000313|Proteomes:UP000219369};
RN   [1] {ECO:0000313|Proteomes:UP000219369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA   Guldener U.;
RL   Submitted (SEP-2016) 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; FMJY01000002; SCO79042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3SRH3; -.
DR   VEuPathDB; FungiDB:FOC1_g10016399; -.
DR   VEuPathDB; FungiDB:FOC4_g10014346; -.
DR   VEuPathDB; FungiDB:FOIG_13182; -.
DR   VEuPathDB; FungiDB:FOMG_01877; -.
DR   VEuPathDB; FungiDB:FOXG_01089; -.
DR   VEuPathDB; FungiDB:FOZG_01865; -.
DR   VEuPathDB; FungiDB:HZS61_001436; -.
DR   OrthoDB; 67085at2759; -.
DR   Proteomes; UP000219369; 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   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}.
FT   DOMAIN          518..632
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   635 AA;  71893 MW;  337B009FFBF3E804 CRC64;
     MAATTCSVSG IENLLGRVGL DTPIPEFPGA DIVHNPQDIF RVYLADTLEK LLHCDRMVAY
     DAIQTSNVTG MGDLVIVAPR LRLKDVQPED LVKDLLQKLP RTPPFGCPLR DGIRLQVYFS
     PNTLPRLLLS YISDRSTSYG YDTSLGLTDP ASPDGSKKKV IVEYSSPNMA SEFQVSHLRS
     TLIGTYIANI YASMGWDVVK MNYLGDWGKQ IGLLAAGWER FGSEDEFAKQ PLRHLLEVNH
     KIQDLFKPEM EECKIAKAKG QDVTDIESRG LYAERDIFFK KMEDKEPEAI AVWQRFRDAT
     VRDYTDSYAQ LGVTFDEYSG ESQVTVESIT EVEQILKDKG IYEEHEDSWK IDFSKHDAKG
     LSLAVLRYRN GTTSYLLRDL AAVFDRYKKH KFDKMIYVVA MEQEMHFHRV TKTLELMGRH
     DLAERIQHVP FAKINGLPEE LKEAALLSDY LDGCRSMSHA GLDKDDEEAS YVDKSENSVR
     QLSLAGLFIQ DHYHKRTTSY AIDPKKMISL EGETGAAIQN CYARLLAQLG SEPAQFDYTT
     LDHTSLETAD YSELLRILLQ YPDAAHGSFK TLEPSFIVGY LLRLVDQLML TLDDDDEKDW
     AGLEAANEAR LALYENTRQV FENALRLLGV APWSP
//