ID J9FK72_WUCBA Unreviewed; 964 AA.
AC J9FK72;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 13-SEP-2023, entry version 37.
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=WUBG_01338 {ECO:0000313|EMBL:EJW87749.1};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW87749.1, ECO:0000313|Proteomes:UP000004810};
RN [1] {ECO:0000313|Proteomes:UP000004810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA {ECO:0000313|Proteomes:UP000004810};
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Hepburn T.,
RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Wuchereria bancrofti.";
RL Submitted (AUG-2012) 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:EJW87749.1}.
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DR EMBL; ADBV01000301; EJW87749.1; -; Genomic_DNA.
DR AlphaFoldDB; J9FK72; -.
DR Proteomes; UP000004810; 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 Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 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; 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; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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 141..229
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT REGION 83..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..42
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 95..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 109742 MW; 4F7DFB44615E5DA7 CRC64;
MKPEPLDGIS CNSELRQLKQ HLEESEKKLV TYQNLLDAME KGDMNDTVLE HCPDLSKAIM
ENTKLKYRIK ILQASIREQE QLNEKNGIKN SNAEAPMEKK SKTKTSSKND SDKSAGNKKP
SKESKKYNYV IVKDFGSSLL CMLRALFSES VSKLYPEMST IPILITEAQQ VKFGDYQFNS
SMSIAQKLLR NGQKISPQEV ARKILDNLPK CDRIEKMEVS GPGYINIFLN RSWIATSITN
IALKGIEVPV IEKRRALVDF SSPNIAKQMH VGHLRSTIIG DSISRLLTYV GFDVLRLNHI
GDWGTQFGML IAHLQDCFPN FINEVPPISD LQAFYKESKK RFDEDEAFKA RAYQCVTKLQ
SFDPDFVKAW QMICDVSRKD FSQIYDRLDI TIVERGESFY QKHMVELVDE FDKLGVLELD
EGRKILKLGE GVPLTVVKSD GGFTYDTSDL AALKYRLFVD KADWIIYVVD AGQSLHFELL
YAAGQKLGWY SPSEKRVELV TFGLVLGEDK KKFKTRSGDS VRLTDLLDEG VKRAEAKLQE
KERDKVMIPE ELVLARDAVA YGCVKYADLS QTRTQDYVFS FDRMLDDRGN TAVYLLYAFA
RIQSICRNSG VSEEDIHNYL HSLPNGLLPL EHKSEFRLAK TILKFTDCIL NTLDNFLLHQ
KFIASWKCCN LIFSNTEAVP TAYIYLADPH KLPVPAKNAN DNPNRGESDA ENEILQHYFH
CERSNELDQL SEKYEIHDMS ISSDFEETLQ NHFRYTPTPK SEVKSEENND SSIDFSSLKQ
QNMDDGVSLS FAFTENSKSN ISSFREGNFS LQNITENVNI SNNKSPNSEE RKQRIFDDHF
DENSPVEQFR NTSLVASTPL STKSNNGYRR QMVMMKSAVR TKVDELKQRT MLNLSVYSND
SMNTTSSKDE ATMREQCAIA KHIARIRTSS TRLGSSKEAL PSFNNTRYHS MCTSFGSNGS
ASFS
//