ID   A0A1B8J692_9HELI        Unreviewed;       444 AA.
AC   A0A1B8J692;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   11-DEC-2019, entry version 17.
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   ORFNames=BA723_02090 {ECO:0000313|EMBL:OBV28419.1}, BKN38_00550
GN   {ECO:0000313|EMBL:OHU85921.1};
OS   Helicobacter sp. CLO-3.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=211 {ECO:0000313|EMBL:OBV28419.1, ECO:0000313|Proteomes:UP000092701};
RN   [1] {ECO:0000313|EMBL:OBV28419.1, ECO:0000313|Proteomes:UP000092701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMC1 {ECO:0000313|EMBL:OBV28419.1,
RC   ECO:0000313|Proteomes:UP000092701};
RA   Greninger A.L., Bateman A., Jerome K., Fang F.;
RT   "Genome sequence of Helicobacter sp. CLO-3.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OHU85921.1, ECO:0000313|Proteomes:UP000179541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLO-3 {ECO:0000313|EMBL:OHU85921.1,
RC   ECO:0000313|Proteomes:UP000179541};
RA   Greninger A.L., Bateman A.C., Fang F., Jerome K.;
RT   "Genome sequence of Helicobacter sp. CLO-3 Fennel-37 strain.";
RL   Submitted (OCT-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|HAMAP-Rule:MF_00127,
CC         ECO:0000256|SAAS:SAAS01171937};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00127,
CC       ECO:0000256|SAAS:SAAS01206672}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127,
CC       ECO:0000256|SAAS:SAAS01171933}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00127, ECO:0000256|SAAS:SAAS01171943}.
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:OBV28419.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MAMQ01000127; OBV28419.1; -; Genomic_DNA.
DR   EMBL; MLQN01000001; OHU85921.1; -; Genomic_DNA.
DR   RefSeq; WP_066458471.1; NZ_MLQN01000001.1.
DR   EnsemblBacteria; OBV28419; OBV28419; BA723_02090.
DR   Proteomes; UP000092701; Unassembled WGS sequence.
DR   Proteomes; UP000179541; Unassembled WGS sequence.
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   CDD; cd00859; HisRS_anticodon; 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; 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   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS01171946};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS01171941};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127, ECO:0000256|SAAS:SAAS01171950};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00127, ECO:0000256|SAAS:SAAS01171926,
KW   ECO:0000313|EMBL:OBV28419.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS01171939};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS01171928};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092701}.
FT   DOMAIN          27..386
FT                   /note="AA_TRNA_LIGASE_II"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   444 AA;  50336 MW;  D68D66BBE67B5798 CRC64;
     MADKPLITPR TLGGFRDRLP KEAMAKEKLT QNLIAVFESF GFVPIETPHL EYADILVKQG
     SEEIQKELYR FKDHGGRDVV LRFDQTVPLA RFISQYKSEL DLPFKRFVIG NVFRGERAQK
     GRYREFTQCD FDFIGSDSIA CDAEIIQVIY ASLARLGLDE FTIWVNHRSI LNGICHHFGI
     KNERDIQSVL RIIDKLDKIG KEGVSKELES ALGFSQEKTA PLLQAISIKQ CEVSSEFFAK
     IAHMKEWNEE LAKGISELEE MFEILSDLEM DKSITRVNFA IARGLGYYTG IVYETTLNRL
     KNIGSVCSGG RYDDLTRTFS QERLSGVGAS IGLDRLIAAL EELEMLEGKS TSARVLVAVM
     ERKFFAYAHK IAEALRSSGI YTEVYPQDSK LKKQLSYAHN KGHEYCVIIG EDEFATHTMT
     LKNMTTGMQF ENLSLLKTLE IVRG
//