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Database: UniProt
Entry: I3CKX4_9GAMM
LinkDB: I3CKX4_9GAMM
Original site: I3CKX4_9GAMM 
ID   I3CKX4_9GAMM            Unreviewed;       428 AA.
AC   I3CKX4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=BegalDRAFT_3453 {ECO:0000313|EMBL:EIJ44267.1};
OS   Beggiatoa alba B18LD.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Beggiatoa.
OX   NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ44267.1, ECO:0000313|Proteomes:UP000005744};
RN   [1] {ECO:0000313|EMBL:EIJ44267.1, ECO:0000313|Proteomes:UP000005744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B18LD {ECO:0000313|EMBL:EIJ44267.1,
RC   ECO:0000313|Proteomes:UP000005744};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA   Mueller J., Woyke T.;
RT   "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; JH600070; EIJ44267.1; -; Genomic_DNA.
DR   RefSeq; WP_002692179.1; NZ_JH600070.1.
DR   AlphaFoldDB; I3CKX4; -.
DR   STRING; 395493.BegalDRAFT_3453; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_1_1_6; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000005744; Unassembled WGS sequence.
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; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43707; 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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00127}; Reference proteome {ECO:0000313|Proteomes:UP000005744}.
FT   DOMAIN          1..360
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   428 AA;  48260 MW;  6471B13024CF1215 CRC64;
     MSKSIQSVRG MNDILPTQTP YWQTVETALR RVFESYGYQE IRTPILEKTE LFSRSIGEVT
     DIVEKEMFTF IDRAEEGDSD AESLSLRPEN TASCVRAGIE HSLFYGQTPR LWYTGPMFRH
     EKPQKGRYRQ FHQLGAEAYG IASADIDAEL IIMSARCFKV LGLKDLSLQL NSLGSSDART
     AYRARLVDYF SAYPTQLDED SQRRLHTNPL RILDSKNPEM QALIQNAPKL IDHLDTESIE
     HFEQLKHRLD LAGISYQVNP RLVRGLDYYN RTVFEWVTTA LGSQGTVCAG GRYDSLVAQI
     GGRATPAIGF AMGLERLLML VEQTGLVPHN ANPHVYLVMM GQTAVEHGIQ LAEQLRDQLP
     ELRIISHCGG GNAKKQFERA DKSGARIALI LGDDEVAQQR VTVKYLRDNQ AQVTLAQTEL
     ADHLQRFL
//
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