SYH_UREU1
ID SYH_UREU1 Reviewed; 421 AA.
AC B5ZB96;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=UUR10_0283;
OS Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=565575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33699 / Western;
RA Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL Submitted (OCT-2008) 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; CP001184; ACI60309.1; -; Genomic_DNA.
DR RefSeq; WP_004025545.1; NC_011374.1.
DR AlphaFoldDB; B5ZB96; -.
DR SMR; B5ZB96; -.
DR STRING; 565575.UUR10_0283; -.
DR EnsemblBacteria; ACI60309; ACI60309; UUR10_0283.
DR GeneID; 45015831; -.
DR KEGG; uue:UUR10_0283; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_14; -.
DR OMA; CDFDFIG; -.
DR OrthoDB; 1040215at2; -.
DR Proteomes; UP000002018; 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; 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; 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..421
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000095609"
SQ SEQUENCE 421 AA; 48846 MW; E55F12694E5CB308 CRC64;
MSNYTKPRGT VDLYNEAMNE FKSLENFLLT TTKKYGFQQI KTPIFEFAEL FMKSAGESSD
LVSKEMYLFK DKSDRWLALR PEGTAGVIRA VVENKLLLNN PLPLKLMYFE PCFRYERPQA
GRQRQFHQFG VEVLGTKNIY YDFELIALAN NILKKLAISD YVLEINYIST AHNRSLWVKS
LQEYFNLYRD ELTPLSQERI TTNPLRILDD KLESQKLVVQ QAPKITNFLS NEEKEEFALI
KKMLDEHDIK YRVNEGLVRG LDYYSGLVFE FISTSPRLLG QSTIIGGGRY GQLIKQTGGP
DYEGIGFGIG IERLLIALLD SNKQILNNFE DKYLIAYFDK ELENEAIKLT QSLRINNQLN
VDIILDTIKA DKIFRLAQRL NAKKLIILAK KEWLNKQVIL KDLLSFEQKT LNLDEIKKIK
E