ID C5CDT2_KOSOT Unreviewed; 419 AA.
AC C5CDT2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 OrderedLocusNames=Kole_0376 {ECO:0000313|EMBL:ACR79101.1};
OS Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae;
OC Kosmotoga.
OX NCBI_TaxID=521045 {ECO:0000313|EMBL:ACR79101.1, ECO:0000313|Proteomes:UP000002382};
RN [1] {ECO:0000313|EMBL:ACR79101.1, ECO:0000313|Proteomes:UP000002382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1
RC {ECO:0000313|Proteomes:UP000002382};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Noll K.;
RT "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR79101.1, ECO:0000313|Proteomes:UP000002382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1
RC {ECO:0000313|Proteomes:UP000002382};
RX PubMed=21914881; DOI=10.1128/JB.05828-11;
RA Swithers K.S., Dipippo J.L., Bruce D.C., Detter C., Tapia R., Han S.,
RA Goodwin L.A., Han J., Woyke T., Pitluck S., Pennacchio L., Nolan M.,
RA Mikhailova N., Land M.L., Nesbo C.L., Gogarten J.P., Noll K.M.;
RT "Genome Sequence of Kosmotoga olearia Strain TBF 19.5.1, a Thermophilic
RT Bacterium with a Wide Growth Temperature Range, Isolated from the Troll B
RT Oil Platform in the North Sea.";
RL J. Bacteriol. 193:5566-5567(2011).
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; CP001634; ACR79101.1; -; Genomic_DNA.
DR RefSeq; WP_012744888.1; NC_012785.1.
DR AlphaFoldDB; C5CDT2; -.
DR STRING; 521045.Kole_0376; -.
DR KEGG; kol:Kole_0376; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_0; -.
DR OrthoDB; 9800814at2; -.
DR Proteomes; UP000002382; 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; 3.40.50.800; 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}; 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:UP000002382}.
FT DOMAIN 1..330
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 419 AA; 48303 MW; 7BBC7B01BB9AB5C0 CRC64;
MITRIKGTQD VFFEEIKYWH YIENTIRKIT KLYAFEEIRT PIFEHTELFK RSVGESTDVV
QKEMYTFNDK GGRSLTLRPE GTASVARAYV ENGFINRGSP LKLFYVGPMF RYEKPQAGRL
RQFHQFGIEI LGSHDSTADY EVIELGINFL KELGISGTKL YINSVGCNKC RPKYNEVLKD
YYSDKLSTLC DDCKRRYNTN VLRLLDCKID KEVAEGAPSI HNYLCDDCKI HFEQLQYYLK
SRNLDYEVDH KLVRGLDYYT KTAFEIRSNM LGAQDQVLAG GRYDGLVEYI GGKSVPAVGF
AAGMERMILL LKKMGIEPKV EELNTVAILP MNKEAFVKAF EFAERLRKKG ISTFVDVMER
NLRNKFKHAS RIGAKIAVVI GEEELEKGFV TIKVMEEGSQ YTVDSDWMAD YIFKKLKEL
//
