ID C7P2V1_HALMD Unreviewed; 436 AA.
AC C7P2V1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=Hmuk_1302 {ECO:0000313|EMBL:ACV47423.1};
OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB
OS 13541) (Haloarcula mukohataei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV47423.1, ECO:0000313|Proteomes:UP000001746};
RN [1] {ECO:0000313|EMBL:ACV47423.1, ECO:0000313|Proteomes:UP000001746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC {ECO:0000313|Proteomes:UP000001746};
RX PubMed=21304667; DOI=10.4056/sigs.42644;
RA Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K.,
RA Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.,
RA Detter J.C.;
RT "Complete genome sequence of Halomicrobium mukohataei type strain (arg-
RT 2).";
RL Stand. Genomic Sci. 1:270-277(2009).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC 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; CP001688; ACV47423.1; -; Genomic_DNA.
DR RefSeq; WP_015762269.1; NC_013202.1.
DR AlphaFoldDB; C7P2V1; -.
DR STRING; 485914.Hmuk_1302; -.
DR GeneID; 8410822; -.
DR KEGG; hmu:Hmuk_1302; -.
DR eggNOG; arCOG00404; Archaea.
DR HOGENOM; CLU_025113_3_0_2; -.
DR OrthoDB; 8659at2157; -.
DR Proteomes; UP000001746; 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|HAMAP-Rule:MF_00127,
KW ECO:0000313|EMBL:ACV47423.1};
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:UP000001746}.
FT DOMAIN 1..334
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 415..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 48083 MW; D00255F76846B4E1 CRC64;
MYDSLKGFRD VYPAEMAAYR QVIDEIETTA RQYGFREITT PALEATEMYV DKSGEEIVEE
LYHFEDKGGR DVALTPELTP TVARMVVAKQ QELSKPIKWV STRPFWRYEQ VQQGRFREFH
QTNIDIFGSS EPTADAEILA VATDMLTGLG LSADDFDFRV SHRDILTGLL ESFEADVDTQ
DAIRVVDKRA KIDRDEYVEG LTDAGLSLDQ AEQFDEWLRA GDDDLDALAE MSGSEQVADA
VANLEAVLAA AEDFGVREYC TISLTTARGF DYYTGVVFEC FDSTGEVSRA VFGGGRYDDL
IEGFGGEPTP AVGFAPGVMN STLPLLLQRA GVWPEEAVST DYYVLQVGDT RPVAARIARE
LRESGHVVEA DVSDRSFGAQ MGYADSINAE TVVIVGENDL ENDEVTVKDM ASGEQTTAPV
DAFPGDHERP TYGDFA
//
