SYH_NOSS1
ID SYH_NOSS1 Reviewed; 462 AA.
AC Q8YMC2;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=all5012;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB76711.1; -; Genomic_DNA.
DR PIR; AD2432; AD2432.
DR RefSeq; WP_010999138.1; NZ_RSCN01000014.1.
DR PDB; 3NET; X-ray; 2.70 A; A/B=1-462.
DR PDBsum; 3NET; -.
DR AlphaFoldDB; Q8YMC2; -.
DR SMR; Q8YMC2; -.
DR STRING; 103690.17134150; -.
DR EnsemblBacteria; BAB76711; BAB76711; BAB76711.
DR KEGG; ana:all5012; -.
DR eggNOG; COG0124; Bacteria.
DR OMA; CDFDFIG; -.
DR OrthoDB; 277998at2; -.
DR EvolutionaryTrace; Q8YMC2; -.
DR Proteomes; UP000002483; 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 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..462
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136089"
FT HELIX 20..39
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 155..172
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 264..282
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 300..312
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 321..331
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 427..431
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:3NET"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:3NET"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:3NET"
FT HELIX 453..459
FT /evidence="ECO:0007829|PDB:3NET"
SQ SEQUENCE 462 AA; 51520 MW; FAD83F2F80B83518 CRC64;
MAKNDKINFS TPSGFPEFLP SEKRLELYLL DTIRRVYESY GFTPIETPAV ERLEVLQAKG
NQGDNIIYGL EPILPPNRQA EKDKSGDTGS EARALKFDQT VPLAAYIARH LNDLTFPFAR
YQMDVVFRGE RAKDGRFRQF RQCDIDVVGR EKLSLLYDAQ MPAIITEIFE AVNIGDFVIR
INNRKVLTGF FQSLNISETQ IKSCISIIDN LEKIGEAKVK LELEKEGINP EQTQKIIDFV
KIDGSVDDVL DKLKHLSQTL PESEQFNLGV SELETVITGV RNLGVPDKRF CIDLAIARGL
NYYTGTVYET TLIGHEALGS ICSGGRYEEL VGTFIGEKMP GVGISIGLTR LISRLLKAGI
LNTLPPTPAQ VVVVNMQDEL MPTYLKVSQQ LRQAGLNVIT NFEKRQLGKQ FQAADKQGIR
FCVIIGADEA AAQKSSLKDL QSGEQVEVAL ADLAEEIKRR LT
