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Database: UniProt
Entry: J9FK72_WUCBA
LinkDB: J9FK72_WUCBA
Original site: J9FK72_WUCBA 
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
//
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