SYH2_ALKCK
ID SYH2_ALKCK Reviewed; 425 AA.
AC Q5WCR7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Histidine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS 2 {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS2 {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=ABC3310;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD65843.1; -; Genomic_DNA.
DR RefSeq; WP_011248149.1; NC_006582.1.
DR AlphaFoldDB; Q5WCR7; -.
DR SMR; Q5WCR7; -.
DR STRING; 66692.ABC3310; -.
DR EnsemblBacteria; BAD65843; BAD65843; ABC3310.
DR KEGG; bcl:ABC3310; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_0_9; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000001168; 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 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..425
FT /note="Histidine--tRNA ligase 2"
FT /id="PRO_0000136102"
SQ SEQUENCE 425 AA; 48112 MW; 63E0FB026FA7640B CRC64;
MKKWDYQNVR GTQDYLPEDE SVRVWLRREL EEVFQQYGCK PMETPMINYT DLLASKYGGG
AEIKKEMYTL TDRGKRALAL RYDLTIPFAK VMAMNPDIRK PFKRYEIGKV FRDGPIKAGR
FREFTQCDVD VAGVDSPLAE AELLEMATEV FRRIGLNMTI QYNNRKLLTG MLDICGVSKD
QHSAVILILD KREKIGDKQV VNELKEMGVD GKAISKIAQW LKQMSQSGIV DFATDRPTTP
IMAEGIAELQ ELEEALRYLN IDSQCTFNPF LARGLEIYTG TVYELFLTEG AIQSSVGSGG
RYDQAISGLT GEEQPMPTVG ISFGIDVIYT ALKMEGRINQ KPLLDYYVIP LQKQKEALAV
ASSLRKQGFR VDVEFKNKKL TKALDRANKE KIPFVILIGE EEVASGRYKL KNMETGAEQH
VPFSF
