SYH_RHOBA
ID SYH_RHOBA Reviewed; 442 AA.
AC Q7UZ20;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=RB251;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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:0000255|HAMAP-Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR EMBL; BX294133; CAD71466.1; -; Genomic_DNA.
DR RefSeq; NP_863795.1; NC_005027.1.
DR RefSeq; WP_011117814.1; NC_005027.1.
DR AlphaFoldDB; Q7UZ20; -.
DR SMR; Q7UZ20; -.
DR STRING; 243090.RB251; -.
DR EnsemblBacteria; CAD71466; CAD71466; RB251.
DR KEGG; rba:RB251; -.
DR PATRIC; fig|243090.15.peg.125; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_0_0; -.
DR InParanoid; Q7UZ20; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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 Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..442
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136236"
SQ SEQUENCE 442 AA; 47667 MW; B2CEEB904347EB20 CRC64;
MIQPRTLKGF RDYLPAAMIP REQLMQTARE VFRSFGFAPI DTPTLEHLEI LTGKGSDETD
RQLYSFEDNG GRPVGMRFDL TVPLARFAAQ HIGTLGTPFK RYHIAPVWRG EKPQEGRYRE
FVQCDFDTIG TTSELADIEA VCVIDALLRA IGIDAFTISI NNRAILTGLL ESLGLADKTT
PVLRSLDKLG KIGREKTANE MVESAGVTAE QADAVLRLAE CDGDAESILA SLPEITGGNE
TAAAGIERLT QIYRGALASG VSPDRLKIDV SIARGLDYYT GVIFETTLDE LPGIGSVCSG
GRYDNLAGLY TKQHLPGIGA SLGLDRLLAA LESLGRLSGV SKPCAVFVPF FDKGHRDDYL
KLASQLRDAG IGVEVYPEPK KLGQQLKYAD SQGFAVAIIA GGNEWEAGAV QVKTLATKES
QDVAYSHESP DALIEAIQAA TS