ID A0A1R1LA41_9MICC Unreviewed; 451 AA.
AC A0A1R1LA41;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=BKD30_08755 {ECO:0000313|EMBL:OMH24390.1};
OS Tersicoccus phoenicis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Tersicoccus.
OX NCBI_TaxID=554083 {ECO:0000313|EMBL:OMH24390.1, ECO:0000313|Proteomes:UP000187085};
RN [1] {ECO:0000313|EMBL:OMH24390.1, ECO:0000313|Proteomes:UP000187085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1p05MA {ECO:0000313|EMBL:OMH24390.1,
RC ECO:0000313|Proteomes:UP000187085};
RA Nakajima Y., Yoshizawa S., Nakamura K., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Tersicoccus phoenicis 1P05MA.";
RL Submitted (DEC-2016) 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};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMH24390.1}.
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DR EMBL; MRDE01000058; OMH24390.1; -; Genomic_DNA.
DR RefSeq; WP_076704052.1; NZ_MRDE01000058.1.
DR AlphaFoldDB; A0A1R1LA41; -.
DR STRING; 554083.BKD30_08755; -.
DR OrthoDB; 9800814at2; -.
DR Proteomes; UP000187085; Unassembled WGS sequence.
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; 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.
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:OMH24390.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000187085}.
FT DOMAIN 9..334
FT /note="Class II Histidinyl-tRNA synthetase (HisRS)-like
FT catalytic core"
FT /evidence="ECO:0000259|Pfam:PF13393"
FT DOMAIN 365..412
FT /note="Anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF03129"
FT REGION 419..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49099 MW; 0CFC7D9A173C2F30 CRC64;
MARQASLSGF TELLPAERVV ELHVLDSLRR TFELHGFSSL ETRAVETVGS LLQKGEIDKE
VYAVSRLQGD DDERGGRTDP QQLALHFDLT VPFARFVVEN AGYLQFPFRR YQIQKCWRGE
RPQEGRAREF TQADIDVVGD GELPFVYDVE MALIAAEALD ALPIGDFVIR VNNRKLAEGF
YRGLGLTDPM AVLRSVDKLE KIGADGVVAE LRAEAGATEE QARAALRLAG IRTPDTGFVE
QVRGLGVEHP LLEQGLNELA EVIGLASRRA PGKVVADLSI ARGLDYYTGT VYETVLVGHE
SLGSICSGGR YDALAVKGDR RFPGVGLSVG VTRLLARVLA QKLAVATRPV PTAVLVSLAD
EDGWAAADDV ATALRARGIP TEVAATAAKF GKQIKYADRR GIPFVWFTSI DDGGQARHEV
KDIRSGDQVP ADPRTWTPPA EDRYPRVVPG D
//
