ID   SYR_ANAPZ               Reviewed;         580 AA.
AC   Q2GK20;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Arginyl-tRNA synthetase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginine--tRNA ligase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=APH_0700;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000235; ABD43701.1; -; Genomic_DNA.
DR   RefSeq; YP_505281.1; -.
DR   GeneID; 3930454; -.
DR   GenomeReviews; CP000235_GR; APH_0700.
DR   KEGG; aph:APH_0700; -.
DR   NMPDR; fig|212042.5.peg.681; -.
DR   TIGR; APH_0700; -.
DR   HOGENOM; Q2GK20; -.
DR   OMA; Q2GK20; MDFDFAK.
DR   BioCyc; APHA212042:APH_0700-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00123; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-synth_Ic.
DR   InterPro; IPR015945; Arg-tRNA-synth_Ic_core.
DR   InterPro; IPR005148; Arg-tRNA-synth_Ic_N.
DR   InterPro; IPR008909; DALR_anticod_bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.30.1360.70; Arg-tRNA-synth_Ic_N; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11956; Arg_tRNA-synt_1c; 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   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    580       Arginyl-tRNA synthetase.
FT                                /FTId=PRO_0000241977.
FT   MOTIF       137    147       "HIGH" region.
SQ   SEQUENCE   580 AA;  65545 MW;  A5A0216ABAD6C597 CRC64;
     MLLDDKILDI FGFFRNAIEE RIRAVWSGDN IPESLFKRII VGPPAQPKHG DLYTNAALIL
     GKFDKKNPME LASTLCNAFE NIEGIESINV VAPGFINFHC VNSVWHGVVR NINKLGREYG
     RTDLGHNKKV NIEFVSANPT GPLHIGHARG AVFGDVLSNL LKWVGYDVIK EYYVNDAGSQ
     VKTLVSSVFL RYKEALGEEI TIGAGLYPGE YLKPIARDLV EKYGSDLLNA SDKDEIIRSF
     TLSSMLNLIK EDLALLGVEH DVFVSESDLQ NRNVIEECVK YLRERGIIYE GVLEKPKRED
     ELSEWQPRVQ MLFKSTEFGD DSDRALQKED GTWSYFAGDI GYHFHKISRG FDSMIMTLGF
     DHKGYVSRLK AAVAALSNGK ASIDIKLYNL VNFLENGTPV KMSKRKGEFL TVRDVIDEVG
     RDVARFMMLT RRNDVVLDFD FAKAREESKD SQIFYIQYAH ARIRSIVRRC PELLAIEKID
     FSCVITEQEL SLLRLLSRWP SVIKTSAENY EPHTIAFYLI EVAEAFHALW GCGNSDPSMR
     FIVEGDLHTT SARIYIAIAV SHVIASGLDI FSITPSEEMR
//