ID A0A1M5F1P8_9BACT Unreviewed; 434 AA.
AC A0A1M5F1P8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=SAMN05720760_101894 {ECO:0000313|EMBL:SHF85376.1};
OS Fibrobacter sp. UWB8.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1896207 {ECO:0000313|EMBL:SHF85376.1, ECO:0000313|Proteomes:UP000184492};
RN [1] {ECO:0000313|Proteomes:UP000184492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWB8 {ECO:0000313|Proteomes:UP000184492};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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 -!- 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}.
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DR EMBL; FQVZ01000001; SHF85376.1; -; Genomic_DNA.
DR RefSeq; WP_073054613.1; NZ_FQVZ01000001.1.
DR AlphaFoldDB; A0A1M5F1P8; -.
DR Proteomes; UP000184492; 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; 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; 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 ECO:0000313|EMBL:SHF85376.1};
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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127}.
FT DOMAIN 1..332
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 434 AA; 48361 MW; C40AA10D937186E6 CRC64;
MSISIPQLPK GTRDFYPEAE RIQNYIFDTW RSVAESFAYE EYEGPMFEHL ELYTGKSGEE
IVSQLYNFKD KGDREIALRP EMTPTLARLV IQKARELKKP FKWFSMPRLF RYEKAQKGRL
REFFQLNMDI IGTESIYAEA DLMAAIATML RKFGLKDGEF AIGVSSRKLL ATYLEEIGAP
NPALVYPVLD RRLKIGPEAF AKALADAGLS EDQVKKLDDF MSCKSIEEVK TKVHSENATA
ALAEIEDLFA TLTAAGYGEC VNLDLSIVRG LAYYTGIVFE VFDKGKSMRA IAGGGRYDSL
TEKLGGERIP GVGFGMGDVV LADLLAEHNL LPSPKQSVDF YIASFTNDMK KVFETAQVFR
NAAGNTNAKP FSVAHPLAAM KMGKQLDQAN YQGAKIVVYV DGSKAAEGEF EYKDMRTGEM
FVGNVTSIIE RLKA
//
