SYH_CAMC1
ID SYH_CAMC1 Reviewed; 408 AA.
AC A7ZDK1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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};
GN OrderedLocusNames=Ccon26_09950; ORFNames=CCC13826_1272;
OS Campylobacter concisus (strain 13826).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-2007) 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; CP000792; EAT98631.1; -; Genomic_DNA.
DR RefSeq; WP_012001784.1; NC_009802.2.
DR AlphaFoldDB; A7ZDK1; -.
DR SMR; A7ZDK1; -.
DR STRING; 360104.CCC13826_1272; -.
DR PRIDE; A7ZDK1; -.
DR EnsemblBacteria; EAT98631; EAT98631; CCC13826_1272.
DR KEGG; cco:CCC13826_1272; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_7; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000001121; 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.
FT CHAIN 1..408
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000016333"
SQ SEQUENCE 408 AA; 46381 MW; D20E9386DDFE8E81 CRC64;
MITALRGMKD MLPARAKLYA QIIKTCEEVA KNYGYEQILT PHLEETALFK RSVGESSDIV
GKEMYQFEDK GGNDVCLRPE GTAGVVRAFI EAKLDRANVT KRCFYHGSMF RYERPQKGRL
REFHQFGCEC FGEGSVYEDA SIILMVSEIF NRLNIKTTLK INSLGDESSM KSYKEKLVKF
LDENDDKICE DCKRRKLLNP IRVLDCKIES CQEIYKNAPV ITDSLSDEAQ ADFAKLQEIL
TANGVKFEID TKLVRGLDYY CKTAFEFISN EIGSQSAVAG GGRYDRLVEY LGGRASYGVG
FAMGVERIME ILGEAGDERD GVYLCALDAA NVDFIYNLGS KLRKKYQVEI SYEAKKLQKH
LQNADNKNAK IFLCVGENEM KENKIWYKNL ETKDEKTINL DELEKELG