SYH_MESFL
ID SYH_MESFL Reviewed; 457 AA.
AC Q6F199;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=Mfl366;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) 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; AE017263; AAT75724.1; -; Genomic_DNA.
DR RefSeq; YP_053608.1; NC_006055.1.
DR AlphaFoldDB; Q6F199; -.
DR SMR; Q6F199; -.
DR STRING; 265311.Mfl366; -.
DR PRIDE; Q6F199; -.
DR EnsemblBacteria; AAT75724; AAT75724; Mfl366.
DR KEGG; mfl:Mfl366; -.
DR PATRIC; fig|265311.5.peg.365; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_14; -.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000006647; 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..457
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136191"
SQ SEQUENCE 457 AA; 52849 MW; EAF771DF2CCD424F CRC64;
MKTNKNKTNI KMIGFYHFFY FVKPYYLLIN ENVIIFKAKG DFMIQKPRGT QDLFLNNSKE
WNAVEEKFRK VLNLFNYGEI ITPMFESKEL FVRGVGDSSD IVSKEMYEFT DRKGREYVLR
PEGTAPTVRA LIENKLYIQE NLPYKTFYIG PIFRYERPQA GRYRQFNQLG VETFGIDSIS
HDVELISLGQ SFLKELKINK DVIVEMNYLI SGNERKEYEL ELKKYLNLFD DLCSDCEIRI
NKNVLRVLDC KIDGNKFAEA PKMTLFASQE NKERLNKTFD QLKQLGIEAK INFNLVRGLD
YYTGLVFEFK NIKTDQAIIA GGSYNNLVEE LGGPNLPASG FAIGIERIMM ILSDQEIKVA
DEDELDLFII PLSDDAQFLT NKLLLEARTA NLKVDTNWNI KNLKAGFKSA ERLKSKNIVI
IGENSINSDI YAIKDQKSGE TKELKFKDIV KYLKGEK