ID SYH_ERYLH Reviewed; 449 AA.
AC Q2N5U7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=ELI_14260;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(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; CP000157; ABC64944.1; -; Genomic_DNA.
DR RefSeq; WP_011415766.1; NC_007722.1.
DR AlphaFoldDB; Q2N5U7; -.
DR SMR; Q2N5U7; -.
DR STRING; 314225.ELI_14260; -.
DR KEGG; eli:ELI_14260; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_5; -.
DR OrthoDB; 9800814at2; -.
DR Proteomes; UP000008808; 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 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; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR NCBIfam; TIGR00442; hisS; 1.
DR PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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..449
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000016359"
SQ SEQUENCE 449 AA; 50263 MW; 7FF60A742074184A CRC64;
MSKKTPQAIR GTQDIFSADA EAFAFVVETF ERVRKLYRFR RVEMPVFEKT EVFSRAIGET
TDVVSKEMYS FEDRGGDSLT LRPEFTAGIA RAFLTNGWQQ HAPLKVATHG PLFRYERPQK
GRYRQFHQID AEIIGAAEPQ ADVELLAMAD QTIRGLGIEG VTLHLNTLGD AESREAWRAA
LVEYFRAVAS ELSEDSQERL EKNPLRILDS KDRRDQQFLA DAPRIDAFLS DTARAFFESV
TTGLDAAGVK WQRAESLVRG LDYYRHTAFE FIPDEGSEAA GKLGSQSTIL GGGRYDGLME
SLGGAPTPAV GWAAGIERLA MLVGGAGFDP PIVVLAEHEH LFDTARLVVQ ALRLSEITAE
AEFRYRRTNK AFDKFKKTGT DVFLVVDQVA NLNGSHQIDI RLSGVLPDEE EELKLLAKRV
ELSLRLFFPD LIPKADPEKQ AISWYLSRK
//
