SYH_PROMM
ID SYH_PROMM Reviewed; 436 AA.
AC Q7V4P3;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 102.
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=PMT_1905;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE22080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX548175; CAE22080.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011131271.1; NC_005071.1.
DR AlphaFoldDB; Q7V4P3; -.
DR SMR; Q7V4P3; -.
DR STRING; 74547.PMT_1905; -.
DR EnsemblBacteria; CAE22080; CAE22080; PMT_1905.
DR KEGG; pmt:PMT_1905; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_3; -.
DR OrthoDB; 277998at2; -.
DR Proteomes; UP000001423; 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 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..436
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136222"
SQ SEQUENCE 436 AA; 48475 MW; A1093A29E98804BD CRC64;
MTQLQSLRGM VDLLPEQTRC WQAVESVARD HFRRAGLQEI RTPLLEVTEL FARGIGEATD
VVGKEMYTFV DRGDRSCTLR PEGTASVVRA ALQHGLLSQG PQRFWYGGPM FRYERPQAGR
QRQFYQIGVE YLGVGSPRSD AEVIALAWAL LVDLGVQGLV LEINSLGTLQ DRQKYREELV
AWLEARSEEL DDDSRKRLYT NPLRILDSKH PAIKELLQDA PTLFEALSVE SKARFEEVQV
DLEALQIPFQ LNPRLVRGLD YYGHTAFEIT SDQLGAQATV CGGGRYDGLV EQLGGAPTPA
FGWAFGMERL MLLLEAAASI NPSGSAARLR ASTRPDLYVV NRGEQAERVA LVIAHQLRAA
GLVVELDSSG AAFNKQFKRA GRSRATWALV IGDDEAERGE GRLKYLQEAK TQANPTPIDK
LHRLDDVTGL VCLVRE