ID R4PVH4_9BACT Unreviewed; 476 AA.
AC R4PVH4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:AGL61737.1};
GN ORFNames=L336_0025 {ECO:0000313|EMBL:AGL61737.1};
OS Candidatus Saccharimonas aalborgensis.
OC Bacteria; Candidatus Saccharibacteria; Candidatus Saccharimonadia;
OC Candidatus Saccharimonadales; Candidatus Saccharimonadaceae; Saccharimonas.
OX NCBI_TaxID=1332188 {ECO:0000313|EMBL:AGL61737.1, ECO:0000313|Proteomes:UP000013893};
RN [1] {ECO:0000313|EMBL:AGL61737.1, ECO:0000313|Proteomes:UP000013893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM71 {ECO:0000313|EMBL:AGL61737.1};
RX PubMed=23707974; DOI=10.1038/nbt.2579;
RA Albertsen M., Hugenholtz P., Skarshewski A., Nielsen K.L., Tyson G.W.,
RA Nielsen P.H.;
RT "Genome sequences of rare, uncultured bacteria obtained by differential
RT coverage binning of multiple metagenomes.";
RL Nat. Biotechnol. 31:533-538(2013).
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}.
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DR EMBL; CP005957; AGL61737.1; -; Genomic_DNA.
DR AlphaFoldDB; R4PVH4; -.
DR STRING; 1332188.L336_0025; -.
DR KEGG; saal:L336_0025; -.
DR PATRIC; fig|1332188.3.peg.25; -.
DR HOGENOM; CLU_025113_3_1_0; -.
DR Proteomes; UP000013893; Chromosome.
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|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:UP000013893}.
FT DOMAIN 37..362
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 54184 MW; 5E954EDD2314FDC8 CRC64;
MAPTARVELT RFSLRDAGKY ETITDTMTSL SSESYKGARD WYPEDMRVRN YIFRTWRRIV
KSYGYEAYDA PLLEPIEVYA AKSGQELVNE QTYQFVDRGE RRVAIRPEMT PSVSRMIAAR
RQEIAYPARW YNIGQYMRYE RPQRGREREF WQLNCDIFGM DGALPEAEII SMGYDLMKAF
GAADDMFAIR INNRQVINFM MAHYLGLDTI QAQLMIKLFD RKGKIASDAF RDQAIDIFGQ
EAAPTGLQKI AQLLAAKTMA DLPEAIRDSE AVKEIQELFT HLERAGVKNA VFDITLMRGL
DYYTGTVFEF FDTHPENNRA LFGGGRYDGL VSLFGADPVS AVGFAPGLTM TQLFLETHGL
LPTFFSTTDI YMIVVGDSLR GAAKLAKEFR GEGVNVELDF TGRKIDKQLK TAVKKAIPYI
MFIGDEELAS EAYPLKDTTT SNEQKLSFER VVSTVKDRRR KKTSEEDEFD VSDLSS
//
