ID M4RFP8_9BIFI Unreviewed; 463 AA.
AC M4RFP8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00017399};
DE EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030619};
GN Name=hisS {ECO:0000313|EMBL:AGH41388.1};
GN ORFNames=D805_1121 {ECO:0000313|EMBL:AGH41388.1};
OS Bifidobacterium thermophilum RBL67.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH41388.1, ECO:0000313|Proteomes:UP000011835};
RN [1] {ECO:0000313|EMBL:AGH41388.1, ECO:0000313|Proteomes:UP000011835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RBL67 {ECO:0000313|EMBL:AGH41388.1,
RC ECO:0000313|Proteomes:UP000011835};
RX PubMed=23640377;
RA Jans C., Lacroix C., Follador R., Stevens M.J.;
RT "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT Strain RBL67.";
RL Genome Announc. 1:E00191-13(2013).
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:0000256|ARBA:ARBA00001137};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; CP004346; AGH41388.1; -; Genomic_DNA.
DR AlphaFoldDB; M4RFP8; -.
DR KEGG; btp:D805_1121; -.
DR PATRIC; fig|1254439.12.peg.1114; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_0_11; -.
DR Proteomes; UP000011835; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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 NCBIfam; TIGR00442; hisS; 1.
DR PANTHER; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11476; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 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 {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AGH41388.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 20..363
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 463 AA; 50412 MW; 10352E59D936999A CRC64;
MAKGASISGF PEWLPSERVV EQRVIDTLRR VFELNGFIGI ETRAVETGAS LLKKGETSKE
IYLLSRLQEV GHESDTPIEE RLGLHFDLTV PLSRYVVEHS GTLAFPFKRW QIQKVWRGER
PQEGRFREFV QADIDVVGNG DLPEHYEVEL PLVMVSALEQ LREFGLPKAT VHANNRKLSE
GFYRGLGLTD IEGVLREIDK LDKIGADEVA RLLIEGCGAN EAQARACLEL AELTAADGKE
LAEKFDALCA KHGIATDSEA YALARQGLDT LAMIVDEAAR IRPGSVIADL KIARGLDYYT
GSVYETFLDG ADSLGSICSG GRYDNLASQG SKRYPGVGLS IGLSRLVSYM LHTAGAHASR
ISPAAVMVAV WNEDDRPAAN AIANQLRSRG IAADVAPTAA KLGKQIKYAD KLGIPYVWFP
AAASEDGEAK GDEVKNIITG DQAPADAKSW EPDTVYARQT VNL
//
