位置:首页 > 蛋白库 > SYH_RHORT
SYH_RHORT
ID   SYH_RHORT               Reviewed;         415 AA.
AC   Q2RWE3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=Rru_A0748;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000230; ABC21552.1; -; Genomic_DNA.
DR   RefSeq; WP_011388506.1; NC_007643.1.
DR   RefSeq; YP_425839.1; NC_007643.1.
DR   AlphaFoldDB; Q2RWE3; -.
DR   SMR; Q2RWE3; -.
DR   STRING; 269796.Rru_A0748; -.
DR   EnsemblBacteria; ABC21552; ABC21552; Rru_A0748.
DR   KEGG; rru:Rru_A0748; -.
DR   PATRIC; fig|269796.9.peg.801; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_1_0_5; -.
DR   OMA; CDFDFIG; -.
DR   OrthoDB; 277998at2; -.
DR   PhylomeDB; Q2RWE3; -.
DR   Proteomes; UP000001929; 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; 3.30.930.10; -; 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   PANTHER; PTHR43707; PTHR43707; 1.
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..415
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_1000016432"
SQ   SEQUENCE   415 AA;  44962 MW;  51F6235CDBD39763 CRC64;
     MAALQPVRGT HDYLPDEARS HRHVEETART VAERFGFGEI ITPIFEFTDV FARTLGDTSD
     VVTKEMYTFT DRSGDSLTLR PENTAGVARA FISGGLAQNV PVKLFYRGPM FRHERPQKGR
     LRQFHQVGVE LIGAENPLAD VEVIALGSQL LGALGVGGRT ILHLNSLGDP ESREAYRAAL
     VSYLSGHRDS LSRDSLERLE RNPLRVLDSK DEGDRAVVAG APRLIDHLNE ASRAFFAGVT
     GGLEALGIPF EIDPLLVRGL DYYGHTAFEF VTTDLGAQGT VMAGGRYDGL IRQMGGSQTP
     GVGWAAGVER LSMLMAADRV GAPRPLAMIP AGPDDEVEAL KLAHALRQGG LFVDFGYSGN
     LGKRMKRANR INARAAIILG GEERANGTVV VRDLDSGEQE TIGLAVLEEF LARFL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024