SYH_PHYAS
ID SYH_PHYAS Reviewed; 415 AA.
AC B1VA46;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=PA0485;
OS Phytoplasma australiense.
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX NCBI_TaxID=59748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18359806; DOI=10.1128/jb.01301-07;
RA Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT and AY-WB.";
RL J. Bacteriol. 190:3979-3991(2008).
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; AM422018; CAM11819.1; -; Genomic_DNA.
DR RefSeq; WP_012358958.1; NC_010544.1.
DR AlphaFoldDB; B1VA46; -.
DR SMR; B1VA46; -.
DR STRING; 59748.PA0485; -.
DR EnsemblBacteria; CAM11819; CAM11819; PA0485.
DR KEGG; pal:PA0485; -.
DR eggNOG; COG0124; Bacteria.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000008323; 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..415
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000199144"
SQ SEQUENCE 415 AA; 48585 MW; 9F55F51067351279 CRC64;
MFYKIKGTHD LLPTQTTSWQ KVENSFHSFF KKHQFQEIRT PIMEYAEVFH RAAQHSEMVS
KETYAFPDKK NRLITLRPEG TAGIVRSYIE NKLDQTNKLQ KFYYYGPYFR YERPQFGRYR
QFHQLGVEVL GKTTPFLDIE VITLIYQFLK SLGLDDITIQ INSLGSKEDH LDYVDIFKQY
LKIYSNYLCG LCHERLNKNP LRIWDCKTCH LQDFLKQAPK IFDSLSPKSK KRFQTVLNGL
EAMKVNFKTC HDLVRGLDYY THTVFEITFN KMVLGGGGCY DHLVAALGGN QLSGIGFALG
MERLMLTLQE NNNFFVSPQP SLKLFLFILD PVFFHHGLTL VHILRNEGFC VEFNYSFTTF
TKGLKEALKC LPNYLLILGH QEFAKKQITI KNIKTHTQTT IDQKDLIFYF QQQRV