ID F8E8B8_FLESM Unreviewed; 416 AA.
AC F8E8B8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Flexsi_1465 {ECO:0000313|EMBL:AEI15115.1};
OS Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Flexistipitaceae; Flexistipes.
OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI15115.1, ECO:0000313|Proteomes:UP000006621};
RN [1] {ECO:0000313|EMBL:AEI15115.1, ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RX PubMed=22180813; DOI=10.4056/sigs.2235024;
RA Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Genome sequence of the moderately thermophilic halophile Flexistipes
RT sinusarabici strain (MAS10).";
RL Stand. Genomic Sci. 5:86-96(2011).
RN [2] {ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL Submitted (JUN-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; CP002858; AEI15115.1; -; Genomic_DNA.
DR RefSeq; WP_013886596.1; NC_015672.1.
DR AlphaFoldDB; F8E8B8; -.
DR STRING; 717231.Flexsi_1465; -.
DR KEGG; fsi:Flexsi_1465; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_0; -.
DR OrthoDB; 9800814at2; -.
DR Proteomes; UP000006621; 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:UP000006621}.
FT DOMAIN 1..333
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 416 AA; 47362 MW; 47669CCAFB750487 CRC64;
MFRKVRGFRD IYGEEIGYWR KIEEVIYSLS ESFGYSEYKM PVLEKAEVFD RGIGSTTDIV
EKEMFAFEDR NGDLLALRPE GTAGVVRGVV ENKLYAGSGV KKYYYYGPMF RRERPQKGRY
RQFYQYGVEA FGSASPLVDA EVIQLLCSFF DKCGIGEFLR LEINSIGCPE CRPGYKNKLI
EYFSKYEKEL CEDCKRRLST NPLRILDCKV PGCKKVASDA PVMIDYLCSE CRKHFDSVKY
YLEISGIDYD VNPFMVRGLD YYVRTAFEMI TDKFEANSTV GAGGRYDGLV KQLGGPDYPG
IGFAVGIDRL VNLIKEAGLT YEETLDIFMV MFPETVDAGL KLLKSLRDEN WGVDMDFELG
SMKSQLKKAN RSQASYVVIV GEEELGKNAV TLKNMTDGEQ QLVLLDELKN ILSQKL
//
