SYH_RICCN
ID SYH_RICCN Reviewed; 414 AA.
AC Q92IK8;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 25-MAY-2022, entry version 103.
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=RC0412;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL02950.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006914; AAL02950.1; ALT_INIT; Genomic_DNA.
DR PIR; D97751; D97751.
DR RefSeq; WP_014410545.1; NC_003103.1.
DR AlphaFoldDB; Q92IK8; -.
DR SMR; Q92IK8; -.
DR EnsemblBacteria; AAL02950; AAL02950; RC0412.
DR KEGG; rco:RC0412; -.
DR HOGENOM; CLU_025113_1_0_5; -.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000000816; 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 CDD; cd00859; HisRS_anticodon; 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 InterPro; IPR033656; HisRS_anticodon.
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.
FT CHAIN 1..414
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136238"
SQ SEQUENCE 414 AA; 47455 MW; 44EC0925E8C131E9 CRC64;
MTEKLQPLRG MKDLLPDDYK VHDYIINKAR DVGVLYGYKQ MSTPIVEYTK VFNRSMGESS
DVISKEIYSF LDKSNDFVAL RPEFTACIIR SLISNRLQHK LPLKFFSTGP VFRYDRPQAG
RQRQFHQLNY EYIGAKGAIT DADTLKLAVD ILKALEIEQD TTLELNSLGC NESRSVYQQK
LVEYLNDFKD QLSEESKIRL SKNPMRILDS KSETDQKIIA NAPVLSEYYT DESKEYFEEL
IQYLDILGVK YSINPRLVRG LDYYCHTAFE FTTKKLGSQS TILAGGRYDG LAKIMGNNDD
VPAIGFAAGI ERIALMREYN ISEVKPVFVL PIGKNNICYA LEIVDKLRTE NIAIIIESLG
KIAKRMQRIF NENAQFIIFI GDEEQANNNL KIKDLKKAEE YIVDFAKALE LLKK