ID W6MRC0_9ASCO Unreviewed; 671 AA.
AC W6MRC0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=KUCA_T00004898001 {ECO:0000313|EMBL:CDK28913.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK28913.1};
RN [1] {ECO:0000313|EMBL:CDK28913.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28913.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK28913.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28913.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) 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; HG793130; CDK28913.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MRC0; -.
DR STRING; 1382522.W6MRC0; -.
DR HOGENOM; CLU_006406_6_2_1; -.
DR OrthoDB; 67085at2759; -.
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; 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 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 68..148
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 528..671
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 671 AA; 75574 MW; C949F2690001EC46 CRC64;
MLKRGLKAVF FTHLPLYRAP ISIYSFSSKR YQRAMSTSVG QVTASLQKLN LEVPPAVEGS
YPDGNIVDLG RNYITKHLAE LTGVDAKIVF PALEWSTTLD KGDLLVALPR LRLKGDLNAL
AEKIASDFPL GGYLSKVVPQ GKFLQFWFDD QMLLSLVTKE ILDKGAQYGS APIGVGKKII
VEFSSPNIAK PFHAGHLRST IIGGFLSNLY EKLGWDVVRL NYLGDWGKQF GVLAVGFAKY
GSEEKLADDP IDHLFQVYVA INNDIKAEKE AGVAEADSID EQARAFFKKL SDGDQDAYKL
WAKFRDLSIE RYIDTYARLN IKFDSYSGES QVPQELMEGA TKTLREKGLI TEDRGALLVD
LAPFDKKLGK VLVQKTDGTS LYLTRDIGAA TDRKAKYNFD KMIYVIASQQ DLHVKQFFKI
LDLMGYEWAN PKKEQLLHVN FGMVLGMSTR AGTVVFLNDI LNTTKEKMLE IMKRNEDKYA
QVEDAENVAD LIGIAAVMIQ DMSAKRVYNY EFSWDRMLSF EGDTGPYLQY AHSRLKSIER
LAGIPEEEYL NAKMDLAVIL GNEPKESDFP AEEYAKELEA YEYRKQKVSY LVKVLSQYPD
SLRFASKNSE PSTVVTYLFK LAHQFSSTYK VLRVVGEEHD VMLARLTLFA CVRQTLSNGL
LLLGITPVDR M
//
