ID   SYH_PELUB               Reviewed;         465 AA.
AC   Q4FND9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Histidine--tRNA ligase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hisS; OrderedLocusNames=SAR11_0478;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000084; AAZ21300.1; -; Genomic_DNA.
DR   RefSeq; WP_011281738.1; NC_007205.1.
DR   AlphaFoldDB; Q4FND9; -.
DR   SMR; Q4FND9; -.
DR   STRING; 335992.SAR11_0478; -.
DR   EnsemblBacteria; AAZ21300; AAZ21300; SAR11_0478.
DR   GeneID; 66294980; -.
DR   KEGG; pub:SAR11_0478; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_2_5; -.
DR   OMA; CDFDFIG; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000002528; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   CDD; cd00859; HisRS_anticodon; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 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   InterPro; IPR033656; HisRS_anticodon.
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..465
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136217"
SQ   SEQUENCE   465 AA;  52356 MW;  58641B3DB852A0EF CRC64;
     MNKENKLIPG LPSGFEDRWG KKLILKKKLI NTIEANFVKF GFGALETPSF EISENIGSFL
     ADDDSNPMSD VFSFKDGEKN ITLRYDLSSP LARFVAQNNQ ELPLPYKRYQ MGDVWRNEKA
     GNARYRSFLQ CDADIVGNVN PAQANAELCN LIASTLLACG LKKDQFVVNI SNRKIVQGLI
     EDLKISDDKK IKVMRAIDKL DKPGFGLRGV EDLLKEERVD ASGAVTKGAN LTDDQASQII
     NFLKVKDLKE LKENLKNPLS QEGIKELEDL LEIVSYGDYL DQIKTNFTIV RGLAYYDGFC
     VETNLNFKAK NSKGKEVDIG SICSGGQYNK LISRFKGVDI PGTGMSFGVD RLLFAMMQLD
     QIEVDEKKPV IICVMDEKYL KNYYEILKVL RDNNINSEIF LDSKKNLGKQ LTYANKKQCP
     VAVICGENEF KDNTITLKNL LGVKGENNQL TFPKENLINE IKKFI