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SYR_CAMJE
ID   SYR_CAMJE               Reviewed;         530 AA.
AC   Q9PNC0; Q0P981;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=Cj1175c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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:0000255|HAMAP-Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR   EMBL; AL111168; CAL35290.1; -; Genomic_DNA.
DR   PIR; A81323; A81323.
DR   RefSeq; WP_010891916.1; NC_002163.1.
DR   RefSeq; YP_002344566.1; NC_002163.1.
DR   PDB; 3FNR; X-ray; 2.20 A; A=77-530.
DR   PDBsum; 3FNR; -.
DR   AlphaFoldDB; Q9PNC0; -.
DR   SMR; Q9PNC0; -.
DR   IntAct; Q9PNC0; 3.
DR   STRING; 192222.Cj1175c; -.
DR   PaxDb; Q9PNC0; -.
DR   PRIDE; Q9PNC0; -.
DR   DNASU; 905465; -.
DR   EnsemblBacteria; CAL35290; CAL35290; Cj1175c.
DR   GeneID; 905465; -.
DR   KEGG; cje:Cj1175c; -.
DR   PATRIC; fig|192222.6.peg.1156; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_7; -.
DR   OMA; NKPLHLG; -.
DR   EvolutionaryTrace; Q9PNC0; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR11956; PTHR11956; 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; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..530
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242001"
FT   MOTIF           113..123
FT                   /note="'HIGH' region"
FT   HELIX           79..91
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           124..139
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          143..150
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           154..171
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           187..200
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           202..204
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           210..231
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           242..245
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           249..258
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          262..265
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          268..271
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           273..276
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          282..285
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           293..305
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          310..317
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           318..323
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           324..332
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   TURN            333..335
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           338..340
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          341..346
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          349..353
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           370..377
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           379..385
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   STRAND          395..398
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           399..403
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           410..427
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           445..455
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           457..467
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           472..490
FT                   /evidence="ECO:0007829|PDB:3FNR"
FT   HELIX           499..519
FT                   /evidence="ECO:0007829|PDB:3FNR"
SQ   SEQUENCE   530 AA;  60190 MW;  D2C9B35AF857B2B8 CRC64;
     MKSIIFNEIK KILECDFALE NPKDKNLAHF ATPLAFSLAK ELKKSPMLIA SDLASKFQNH
     DCFESVEAVN GYLNFRISKT FLNELANQAL TNPNDFTKGE KKQESFLLEY VSANPTGPLH
     IGHARGAVFG DTLTRLARHL GYKFNTEYYV NDAGNQIYLL GLSILLSVKE SILHENVEYP
     EQYYKGEYIV DLAKEAFEKF GKEFFSEENI PSLADWAKDK MLVLIKQNLE QAKIKIDSYV
     SERSYYDALN ATLESLKEHK GIYEQEGKIW LASSQKGDEK DRVIIREDGR GTYLAADIVY
     HKDKMSRGYG KCINIWGADH HGYIPRMKAA MEFLGFDSNN LEIILAQMVS LLKDGEPYKM
     SKRAGNFILM SDVVDEIGSD ALRYIFLSKK CDTHLEFDIS DLQKEDSSNP VYYINYAHAR
     IHQVFAKAGK KIDDVMKADL QSLNQDGVNL LFEALNLKAV LNDAFEARAL QKIPDYLKNL
     AANFHKFYNE NKVVGSANEN DLLKLFSLVA LSIKTAFSLM GIEAKNKMEH
 
 
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