SYH_RHILO
ID SYH_RHILO Reviewed; 500 AA.
AC Q987T0;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Histidine--tRNA ligase;
DE EC=6.1.1.21;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
GN Name=hisS; OrderedLocusNames=mlr6928;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BA000012; BAB53120.1; -; Genomic_DNA.
DR RefSeq; WP_010914430.1; NC_002678.2.
DR AlphaFoldDB; Q987T0; -.
DR SMR; Q987T0; -.
DR STRING; 266835.14026523; -.
DR PRIDE; Q987T0; -.
DR EnsemblBacteria; BAB53120; BAB53120; BAB53120.
DR KEGG; mlo:mlr6928; -.
DR PATRIC; fig|266835.9.peg.5510; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_2_5; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000000552; 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.
FT CHAIN 1..500
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136234"
SQ SEQUENCE 500 AA; 54547 MW; 290E8BB18CA2DF84 CRC64;
MADKSEKTKA RLPRGFADRS AEDIRAVEKM MATIRSVYEL YGFEPADQPL IEYTDALGKF
LPDQDRPNEG VFSFQDDDEQ WLSLRYDLTA PTARFVAENY ERLPKPYRSY RSGWVFRNEK
PGPGRFRQFM QFDADTIGTP GVAADAEMAM MMADVMEALG IKRGDYVIRV NNRKVLDGVL
EAIGLGGEEN IGRRLTVLRA IDKLDKLGPE GVKLLLGPGR WDGGKEGEGD FAKGAGLNNG
QAEAVLQATA RNAQAAQDSV VDSNATYQEG VGELATIEAL VRAAGYGEDR IAMDRSVVRG
LEYYTGPVFE AELLAEIPNE DGQIVRFGSV GGGGRYDGLV SRFRGEPVPA TGFSIGVSRL
MTALKNLGKL DNADVIAPVV VLVMDKDTES LGRYQKMVSE LRAAGIRSEM YLGGAGMKAQ
LKYADRRGCP VAIIQGGDER AKGELQIKDL IEGARMSAEI TDNAEWRAAR PAQVTVAESE
LVAEVKKILA AQAEERARGK