ID A0A094IFD0_9BACT Unreviewed; 443 AA.
AC A0A094IFD0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ECO:0000313|EMBL:KFZ26405.1};
GN ORFNames=KQ78_01346 {ECO:0000313|EMBL:KFZ26405.1};
OS Candidatus Izimaplasma bacterium HR2.
OC Bacteria; Mycoplasmatota; Candidatus Izimaplasma.
OX NCBI_TaxID=1541960 {ECO:0000313|EMBL:KFZ26405.1, ECO:0000313|Proteomes:UP000029254};
RN [1] {ECO:0000313|EMBL:KFZ26405.1, ECO:0000313|Proteomes:UP000029254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Skennerton C.T., Haroon M.F., Tyson G.W., Orphan V.J.;
RT "Phylogenomic Analysis of Candidatus Izimaplasma species: Representatives
RT from a Novel Mollicute Clade found in Ocean Sediments.";
RL Submitted (SEP-2014) 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:KFZ26405.1}.
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DR EMBL; JRFF01000036; KFZ26405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094IFD0; -.
DR PATRIC; fig|1541960.3.peg.1283; -.
DR eggNOG; COG0124; Bacteria.
DR Proteomes; UP000029254; 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 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 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|ARBA:ARBA00023146,
KW 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029254}.
FT DOMAIN 1..325
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 443 AA; 50758 MW; DDC4EADCBDA94320 CRC64;
MFQKMKGTYD LLPSETGKWQ SLERTIRNVS KLYNYSEIRT PIFENTELFH RGVGEDTDVV
SKETYDFIDR GKRKNTLRPE GTAGVVRSYI ENKLYADKVP VQKLYYIGNM FRYERPQKGR
YRQFVQFGAE AFGSNSPMLD AEIISYAVSV LKALKIDDVE VHINTIGDEE SKALHKEALV
KYLKKDITTL CKDCQTRYIK NPLRILDCKV DKDTELLKNA PKPIDYLNET SKQHFDGVVK
YLNSMGIKYI VDKNLVRGFD YYTHTVFEVN ANLETLGAQN TICGGGRYNN LVKSLGGPDV
PGVGFSFGLE RLMFALESIN FEGDPKFVHL YLMILGEEQK EDGMAILNRC RLGGLSSDID
FLDKAMKGKF KQADFLNARF IAIYGEKEKE EEMINIKDQL TKQEVRINKH KLYNHIITEL
MNPAQEEHDC DEDCENESGA CSC
//
