ID A1QYT5_BORT9 Unreviewed; 456 AA.
AC A1QYT5;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000256|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000256|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000256|HAMAP-Rule:MF_00127};
GN OrderedLocusNames=BT0135 {ECO:0000313|EMBL:AAX17477.1};
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=314724 {ECO:0000313|EMBL:AAX17477.1, ECO:0000313|Proteomes:UP000001205};
RN [1] {ECO:0000313|Proteomes:UP000001205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135 {ECO:0000313|Proteomes:UP000001205};
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) 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:0000256|ARBA:ARBA00001137, ECO:0000256|HAMAP-
CC Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00127}.
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DR EMBL; CP000049; AAX17477.1; -; Genomic_DNA.
DR RefSeq; WP_011772096.1; NZ_CP073176.1.
DR AlphaFoldDB; A1QYT5; -.
DR KEGG; btu:BT0135; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_0_12; -.
DR Proteomes; UP000001205; 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; 3.40.50.800; Anticodon-binding domain; 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 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 ECO:0000256|HAMAP-Rule:MF_00127};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00127}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00127};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00127}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127}.
FT DOMAIN 1..327
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 456 AA; 53075 MW; 0203BE5D0ACC7E3F CRC64;
MDVRTLKGFR DYLPKEALIR THIIKQIYSV LVSYNFDLID TPILEYSEFL LRKSGDEVEK
QTYRFKDNGD RDVSMRFDLT VPFARFMASN RSKLKFPFRR SQIGKVFRGE NTQRGRYREF
MQFDFDIVGE DTFRSDAEIL SIVYCGLEEI FLNFIEGINR KFVIHFSHIG ILNAYIDKLG
LKDKATFILR NIDKLDKMGI ESVRENLLVQ INEEHVDLIL EFINLEGAFW DKLETLKGVL
ENNDAVKRIE DVFVHLSALG IQDAFNFNLK IVRGLDYYTG IVFEAEMIGI NMGSICSGGR
YDNLLSLFSS SLQKVSGVGG SFGIDRIQDI IEIEKFNYIK LFVVKASSRV LIVNIDDSLQ
DYYYKLADKF RRHDYSKINN IACEVYPKSK EGKNIKVQIE YALNKAIRFL IFVGQDEYRE
DKLKVRDLTK KEELLLSFDE AIKFIKGNDK FLCTPF
//
