ID F1RGD8_PIG Unreviewed; 506 AA.
AC F1RGD8; A0A287A876;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030619};
GN Name=HARS2 {ECO:0000313|Ensembl:ENSSSCP00000040085.2,
GN ECO:0000313|VGNC:VGNC:99755};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000040085.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000040085.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000040085.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000040085.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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 RefSeq; XP_003124096.1; XM_003124048.5.
DR AlphaFoldDB; F1RGD8; -.
DR PaxDb; 9823-ENSSSCP00000015293; -.
DR PeptideAtlas; F1RGD8; -.
DR Ensembl; ENSSSCT00000064703.3; ENSSSCP00000040085.2; ENSSSCG00000014376.5.
DR GeneID; 100521256; -.
DR KEGG; ssc:100521256; -.
DR CTD; 23438; -.
DR VGNC; VGNC:99755; HARS2.
DR GeneTree; ENSGT00390000005922; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 5476704at2759; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000014376; Expressed in hindlimb bud and 45 other cell types or tissues.
DR ExpressionAtlas; F1RGD8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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:SF6; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 62..417
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 506 AA; 56890 MW; 836A4EF9BFEB4CAC CRC64;
MPQLGFLHGR AWAALLGQLR RPPGAVCIGA VRSHSQVAEA TLASQLKPHK EKPNFILKTP
KGTRDFSPQQ MVVREKILDM VVSCFKRHGA KRLDTPAFEL KEMLTERYGE DSGLIYDLKD
QGGELLSLRY DLTVPFARYL AMNKVKKMKR YHVGKVWRRE SPTIVQGRYR EFCQCDFDIA
GHFDPMIPDA ECVKIMCEIL SGLQLGDFLI KVNDRRLLDG IFAVCGVPES KFHAICSSVD
KLDKMSWKDV RHEMVAKRGL APEVADRIGD YVQCHGGVSL VEDMLQDPEL SRNKQALEGL
GDLKLLFDYL TLFGIAEKIS FDLSLARGLD YYTGVIYEAV LLQTPAQAGE EPLNVGSVAA
GGRYDGLVGM FDPKGHTVPC VGLSIGVERI FSIVEQRMKT FGEKIRTTET QVFVATPQKN
FLRERLKLIA ELWDAGIKAE LMYKNNPKLL TQLHYSEDMG IPLVVIIGEQ ELKEGFIKLR
SVASREEVAI KRENLVAEIQ KRLSES
//
