SYH_CHLTR
ID SYH_CHLTR Reviewed; 428 AA.
AC O84547;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Histidine--tRNA ligase;
DE EC=6.1.1.21;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
GN Name=hisS; OrderedLocusNames=CT_543;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE001273; AAC68145.1; -; Genomic_DNA.
DR PIR; H71500; H71500.
DR RefSeq; NP_220058.1; NC_000117.1.
DR RefSeq; WP_009871907.1; NC_000117.1.
DR AlphaFoldDB; O84547; -.
DR SMR; O84547; -.
DR STRING; 813.O172_02985; -.
DR EnsemblBacteria; AAC68145; AAC68145; CT_543.
DR GeneID; 884320; -.
DR KEGG; ctr:CT_543; -.
DR PATRIC; fig|272561.5.peg.588; -.
DR HOGENOM; CLU_025113_1_1_0; -.
DR InParanoid; O84547; -.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000000431; 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; IBA:GO_Central.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00773; HisRS-like_core; 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 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..428
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136136"
SQ SEQUENCE 428 AA; 49189 MW; 9B9F59A096B8D958 CRC64;
MSNALPKGVF DIFPYVTSPK NLWRNSSLWK RVEHAAHRIC NLYGFDEIRT PVFEKTETFL
RVGEYSDIVK KEVYTFLDKK RRSLTLRPEG TAAVVRALLD HSADMRKDNK FYYILPMFRY
ERQQSGRYRQ HHQFGLEAIG VRHPLRDAEV LSLLWDFYAA VGLQHMQIHV NFLGGQKTRA
RYDEALREFF RKDLDRLSPL SQERYHANLL RILDSKEPED QEFIEKAPSI LDYIDDRDLS
YFDAVLAQLK ALGISFAINP RLVRGLDYYT DLVFEAVTVV GEHSYALGGG GRYDELVAQS
GGPSMPAFGF GVGLERVIQT LLEQGNSLST STRRLRLIPM DEQADAFCFS WANRLRNLGI
ATEVDWSHKK PKLSLKDAAD QQVSFVCLLG EQELATKQFI VKDMSLHQSF SGAQQDVEQR
LVYEVQNA