ID A0A1B8J692_9HELI Unreviewed; 444 AA. AC A0A1B8J692; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 24-JAN-2024, entry version 29. 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; Campylobacterota; 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|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}. 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 AlphaFoldDB; A0A1B8J692; -. DR STRING; 211.BKN38_00550; -. DR OrthoDB; 9800814at2; -. 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; 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 InterPro; IPR033656; HisRS_anticodon. 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|HAMAP-Rule:MF_00127}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00127, ECO:0000313|EMBL:OBV28419.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127}; KW Reference proteome {ECO:0000313|Proteomes:UP000092701}. FT DOMAIN 27..386 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" 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 //