ID K7WVB4_9NOST Unreviewed; 462 AA.
AC K7WVB4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000256|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000256|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000256|HAMAP-Rule:MF_00127};
GN ORFNames=ANA_C11750 {ECO:0000313|EMBL:AFW94511.1};
OS Anabaena sp. 90.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW94511.1, ECO:0000313|Proteomes:UP000010101};
RN [1] {ECO:0000313|EMBL:AFW94511.1, ECO:0000313|Proteomes:UP000010101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90 {ECO:0000313|EMBL:AFW94511.1};
RX PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT cyanobacterium Anabaena sp. strain 90.";
RL BMC Genomics 13:613-613(2012).
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:0000256|ARBA:ARBA00001137, ECO:0000256|HAMAP-
CC Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|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; CP003284; AFW94511.1; -; Genomic_DNA.
DR RefSeq; WP_015079673.1; NC_019427.1.
DR AlphaFoldDB; K7WVB4; -.
DR STRING; 46234.ANA_C11750; -.
DR KEGG; anb:ANA_C11750; -.
DR PATRIC; fig|46234.3.peg.1956; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_3_0_3; -.
DR OrthoDB; 9800814at2; -.
DR Proteomes; UP000010101; Chromosome chANA01.
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; 3.40.50.800; Anticodon-binding domain; 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 NCBIfam; TIGR00442; hisS; 1.
DR PANTHER; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11476; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00127};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00127}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00127};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00127}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127};
KW Reference proteome {ECO:0000313|Proteomes:UP000010101}.
FT DOMAIN 29..368
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 462 AA; 51377 MW; 7B95B5A1BCAD50C2 CRC64;
MTKSDKINFS TPSGFPEFLP SEKRLEVYLL DIIRKVFESY GFTPIETPAV ERLEVLQAKG
NQGDNIIYSI DPILPPNRQA EKDKSGETGS EARALKFDQT VPFAAYIARH LNELTFPFAR
YQMDMVFRGE RAKDGRFRQF RQCDIDVVAR GKLSLLYDAQ MPAIITEIFE KINIGDFVIR
INNRKILTGF FQSVGVAENQ IKTCISIIDN LEKIGEAKVK QELETEGISS EQTEKIIEFV
KIDGSIDDVL DKLKHLAESL PEAEQFNLGV TELETVINGV RNLGVADKRF CIDLSIARGL
NYYTGTVYET TLLGHAALGS ICSGGRYEEL VGTFIGEKMP GVGISIGLTR LISRLLKAGI
LNTLSATPTQ VVVVNMQEDL MPVYLQVSQQ LRQGGINVVT NFEKRPLGKQ FQAADKQGIR
FCVIIGAEEA AAQKSSLKDL QSGEQIEVAL ADLPEEVKRR LA
//
