SYH_ANAMF
ID SYH_ANAMF Reviewed; 430 AA.
AC B9KHM7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=AMF_101;
OS Anaplasma marginale (strain Florida).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=320483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Florida;
RX PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT "Conservation in the face of diversity: multistrain analysis of an
RT intracellular bacterium.";
RL BMC Genomics 10:16-16(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR EMBL; CP001079; ACM48989.1; -; Genomic_DNA.
DR RefSeq; WP_010262775.1; NZ_AFMS01000025.1.
DR AlphaFoldDB; B9KHM7; -.
DR SMR; B9KHM7; -.
DR STRING; 320483.AMF_101; -.
DR EnsemblBacteria; ACM48989; ACM48989; AMF_101.
DR GeneID; 7398817; -.
DR KEGG; amf:AMF_101; -.
DR PATRIC; fig|320483.3.peg.119; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_0_5; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000007307; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00127; His_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..430
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000199112"
SQ SEQUENCE 430 AA; 47598 MW; 765A7380A09B3094 CRC64;
MNVGKLQPVR GTRDLLPEEC YKFWHIRDVA HDIGERYGFV PVETPIFEFQ DVFLKTLGDS
SDIIGKEMYS FPDRGGDVLV LRPELTAAVA RMLICERLTL PARLFTFGPV FRYERPQKCR
QRQFHQINYE HFGAGCTADA ELMALAYDIL GALNLRSEVQ LEINSLGNQD SVLEYRNSLL
KYFEKHEHAL SEDSRRRLQT NPLRILDSKD RGDIAILCGA PVIADFYDDE SKMTFNGVMQ
QLDNLGIPYT VNPRLVRGLD YYCGTVFEFK TTSLGSQDAV IAGGRYDKLV ASMGGGDVPA
VGFAGGVERL ASLAAYSHST RFSVAFLPLG EEAARCAMRS AYELRGRGIR VLCDGVVEKL
KIGLKHADRS GVDLALILGD EEIAKGEVLC RHMDTGLQQT VSISNLGDYV SGMESNAQGN
NRAALSSAGE