ID   SYH_ANAPZ               Reviewed;         420 AA.
AC   Q2GLK4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Histidyl-tRNA synthetase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidine--tRNA ligase;
DE            Short=HisRS;
GN   Name=hisS; OrderedLocusNames=APH_0120;
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-histidine + tRNA(His) = AMP +
CC       diphosphate + L-histidyl-tRNA(His).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000235; ABD44457.1; -; Genomic_DNA.
DR   RefSeq; YP_504747.1; -.
DR   GeneID; 3930760; -.
DR   GenomeReviews; CP000235_GR; APH_0120.
DR   KEGG; aph:APH_0120; -.
DR   NMPDR; fig|212042.5.peg.117; -.
DR   TIGR; APH_0120; -.
DR   HOGENOM; Q2GLK4; -.
DR   OMA; Q2GLK4; VFEWVTT.
DR   BioCyc; APHA212042:APH_0120-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00127; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR015807; His-tRNA-synth_IIa_sub.
DR   InterPro; IPR004516; His-tRNA_synth_IIA.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   PANTHER; PTHR11476; His-tRNA_synth; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    420       Histidyl-tRNA synthetase.
FT                                /FTId=PRO_1000016309.
SQ   SEQUENCE   420 AA;  47159 MW;  9A81EAC823EF94E0 CRC64;
     MKVGGFQPVR GTKDLLSEEY YKLFHIQNVA QEIGERFGFM PVQTPIFEFQ EVFCKTLGDS
     TDVIGKEMYT FADRGGDVLA LRPEFTAAIV RLLLSEKMQP PARLFTAGPV FRYERPQKCR
     QRQFHQINYE CFGAGGSQAD AEIISLAYCV LEVFGLHCDV TLEINSLGSS ECMNAYRASL
     LSFFEKYRSE LSEDSRRRLQ TNPLRILDSK DATDKEILST APSIEDFYDA ETRASFEGLK
     DHLTNLGIPY AVNRRLVRGL DYYTGTVFEY KTSSLGAQDA IIAGGRYDNL VAAMGGENVP
     AIGFAGGVER LAALMSYSRT RKFCVFILPI SEEVVSHAMR ITYEIRRTLS GVQVICDIVT
     RLKTGIKRAD RQKADIALIL GDEEVNRNAV SCKNMLTGKQ EEISISNITE YLKAMMAERQ
//