ID G4YXG9_PHYSP Unreviewed; 814 AA.
AC G4YXG9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=PHYSODRAFT_556492 {ECO:0000313|EMBL:EGZ23830.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ23830.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ23830.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ23830.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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; JH159152; EGZ23830.1; -; Genomic_DNA.
DR RefSeq; XP_009519118.1; XM_009520823.1.
DR AlphaFoldDB; G4YXG9; -.
DR STRING; 1094619.G4YXG9; -.
DR EnsemblProtists; EGZ23830; EGZ23830; PHYSODRAFT_556492.
DR GeneID; 20663178; -.
DR KEGG; psoj:PHYSODRAFT_556492; -.
DR InParanoid; G4YXG9; -.
DR OMA; CKSMLAW; -.
DR Proteomes; UP000002640; 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; cd00671; ArgRS_core; 1.
DR CDD; cd00299; GST_C_family; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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; IPR036282; Glutathione-S-Trfase_C_sf.
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; SSF47616; GST C-terminal domain-like; 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:UP000002640}.
FT DOMAIN 235..325
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 694..814
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 814 AA; 89715 MW; 8F2F44F4DC5C71B8 CRC64;
MQLLIGKKPG DEELKCFLAL SITATEFTVG AADKKYASCG PQLAVSPDAE LLFSANAVCR
FVAANAGQLQ SDDLAVDEWL EWEANTLAPW LRVAKAASNK NGELDAQLTA MLEAKEEARP
KNGGDLEFLF GSELSLADVV AGVTLRAAFK LIKEQKDEAP VLQTFRKYVA QLFAREDVAK
GVASMKNAGK AAKKGKGGAP AASGAPAAAV KNVVRSTFKL DDKLAQGLTY HNVLGVVESI
FDAAIKAAYP SVNVPVEVAR TTAKNAQFGD YQCNSAMSIF TALKGTPDAA RSPRDVANTI
IAAMPETPVL DRLSVAGAGF INAFLTKEFV SKRLGNVLAN GVKPAPQEKQ TIVVDFSSPN
IAKDMHVGHL RSTIIGDTMC RILEFQDHDV KRINHVGDWG TQFGMLICHL TETYPTWETE
MPNVTDLTLL YKAAKERFDA DADFHERSKA QVVLLQSGDE KSCKVWNTLC EISRIEFQKV
YDRLGVSLKE MGESFYNPII PSVLDILRAK GLMEMSNGAE VIFTKTHKQP FMLVKSDGSY
LYDTTDIAAL WYRLHEMKAN RVIYYTDYSQ KDHFNLLFEV GRMSGIYDPT KQRADHVGFG
TVNDESGKRF KTRSGEVVRL VELLDEAKVR MKAQLVERIE AGQTSLPMDQ VDAAAEKLGY
GAVKYFDLRQ SPTSNYIFSF DRMLSTNGDT AVYLMFAYAR LSSIIRKSGV DMAALVAQQQ
KEGNVLKPEH PTEQALVIEL LQLQDVIVFI NKDLSSNRLC NYLYTISEKV QTFVTACRVL
GSEEQSSRLL LCDATLKVMK TCFSLLGIDP LDQI
//
