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Database: UniProt
Entry: A0A2I0PVM9_9EURY
LinkDB: A0A2I0PVM9_9EURY
Original site: A0A2I0PVM9_9EURY 
ID   A0A2I0PVM9_9EURY        Unreviewed;       410 AA.
AC   A0A2I0PVM9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=CVV30_02885 {ECO:0000313|EMBL:PKL70320.1};
OS   Methanomicrobiales archaeon HGW-Methanomicrobiales-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales.
OX   NCBI_TaxID=2013817 {ECO:0000313|EMBL:PKL70320.1, ECO:0000313|Proteomes:UP000233367};
RN   [1] {ECO:0000313|EMBL:PKL70320.1, ECO:0000313|Proteomes:UP000233367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGW-Methanomicrobiales-1 {ECO:0000313|EMBL:PKL70320.1};
RX   PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA   Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA   Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT   "Potential for microbial H2 and metal transformations associated with novel
RT   bacteria and archaea in deep terrestrial subsurface sediments.";
RL   ISME J. 11:1915-1929(2017).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       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:PKL70320.1}.
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DR   EMBL; PGYM01000001; PKL70320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0PVM9; -.
DR   Proteomes; UP000233367; 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; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43707; 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|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          6..318
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   410 AA;  45178 MW;  C8111018F7E102F7 CRC64;
     MLQKPRGTRD FLPDEMEARR AVERKLREVA RCYGYREVCT PEFEDLELFT ARSGEGIIDE
     MYVFEDKGGR KLALRPEITA AVIRMYINEA KVAPKPLRWC YFADCFRYER PQKGRYRQFW
     QFGVELIGAD TAAADAETIM LASDMLNATG VTYELKVGHL SFMKNLVKDL EPAMQRKVRA
     HLDKKDFDGL NVTLESLNRT DLAASLAALV GTRDLAEAFE IAGVIPEKER FEKTVGSLDA
     AGVKYSLNFG IARGLDYYTG MVFEGFAQNL GAENQIMGGG TYRLAHLFGG DDVASCGFAI
     GFDRVMVSLG DVQPAVVPIV GLVCTSEGRN RALEVAKALR DAGIRTEMDL MERGLGAQLA
     HAAKTANFAI VIGQREAESG QVTLKNLTTA EQKTVDLAAA VAEVRAFGPR
//
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