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Database: UniProt
Entry: A0A1M6YEH5_9BACT
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ID   A0A1M6YEH5_9BACT        Unreviewed;       439 AA.
AC   A0A1M6YEH5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN05720762_104369 {ECO:0000313|EMBL:SHL16523.1};
OS   Fibrobacter sp. UWH4.
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=1896210 {ECO:0000313|EMBL:SHL16523.1, ECO:0000313|Proteomes:UP000184331};
RN   [1] {ECO:0000313|EMBL:SHL16523.1, ECO:0000313|Proteomes:UP000184331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWH4 {ECO:0000313|EMBL:SHL16523.1,
RC   ECO:0000313|Proteomes:UP000184331};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
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; FRAY01000004; SHL16523.1; -; Genomic_DNA.
DR   RefSeq; WP_072978927.1; NZ_FRAY01000004.1.
DR   AlphaFoldDB; A0A1M6YEH5; -.
DR   STRING; 1896210.SAMN05720762_104369; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000184331; 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:SHL16523.1};
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   439 AA;  48901 MW;  0281F6C33AA56D6A CRC64;
     MSISIPQLPK GTRDFYPEAE RIQNYIFDTW RSVAESFAYE EYEGPMFEHL ELYTGKSGEE
     IVSQLYNFKD KGDREIALRP EMTPTLARLV IQKARELKKP FKWFSMPRLF RYEKAQKGRL
     REFFQLNMDI IGTESIYAEA DLMAAIATML RKFGLKDGEF AIGVSSRKLL ATYLEEIGAP
     NPALVYPVLD RRLKIGPEAF AKALADAGLS EDQVKKLDDF MSCKSIEEVK AKVHSENATA
     ALAEIEDLFA TLTAAGYGEC VNLDLSIVRG LAYYTGIVFE VFDKGKSMRA IAGGGRYDSL
     TEKLGGERIP GVGFGMGDVV LADLLAEHKL LPSPKQSVDF YIASFTNDMK KVFETAQVFR
     NAAGNTNAKP FSVAHPLAAM KMGKQLDQAN YQGAKIVVYV DGSKAAEGEF EYKDMRTGEM
     FVGNVDAIVE RLNTEVKKA
//
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