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Database: UniProt
Entry: A0A1L8GX12_XENLA
LinkDB: A0A1L8GX12_XENLA
Original site: A0A1L8GX12_XENLA 
ID   A0A1L8GX12_XENLA        Unreviewed;       509 AA.
AC   A0A1L8GX12;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE            EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
GN   Name=hars1.L {ECO:0000313|RefSeq:XP_018107539.1,
GN   ECO:0000313|Xenbase:XB-GENE-6488084};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018107539.1};
RN   [1] {ECO:0000313|RefSeq:XP_018107539.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018107539.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018107539.1};
RG   RefSeq;
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}.
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DR   RefSeq; XP_018107539.1; XM_018252050.2.
DR   AlphaFoldDB; A0A1L8GX12; -.
DR   STRING; 8355.A0A1L8GX12; -.
DR   PaxDb; 8355-A0A1L8GX12; -.
DR   GeneID; 108710861; -.
DR   KEGG; xla:108710861; -.
DR   AGR; Xenbase:XB-GENE-6488084; -.
DR   CTD; 108710861; -.
DR   Xenbase; XB-GENE-6488084; hars1.L.
DR   OMA; YQIQKVW; -.
DR   OrthoDB; 5476704at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 108710861; Expressed in muscle tissue and 19 other cell types or tissues.
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   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; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 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, ECO:0000313|RefSeq:XP_018107539.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   DOMAIN          63..397
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   509 AA;  57806 MW;  8016CF963C19052F CRC64;
     MGSLRSLSSS CRALLVGRRI LARVTSVPYR LYQPGDQATK DAVEDVIAQK GVQKNFVLKT
     PKGTHDVHPK QMAIRERILS TVVDCFKRHG AETIDTPVFE LKETLTGKYG EDSKLIYDLK
     DQGGELLSLR YDLTVPFARF LAMNKITNIK RYHIGKVYRR DKPARGRYRE FYQCDFDIAG
     HYDPMIPDAE CLKIVHEILT ELQLGNFCIK VNDRRLLIGI LTVCGVPETK FRTVCTSIDK
     LDKIPWDSVR RELIEDKELK AETVEQIGKY IRLNGGLPLL EHLWADSKLS QNNLAMEGLR
     DLKLLNKYSE IFGVTDKIVY DLGLARGLDY YTGVIYEAVL LRNPGGPPVQ QNGHSEEFGS
     VAGGGRYDGL VGMFDPKDRA VPCVGLSIGI ERIFTLLENK YKNSKEKVQT TETQVLVASA
     QKYFLEEKMK LIAALWNSGI KAEMFYKENS KFLSQLNYCE ERGIPLVAII GEQELQAGVV
     KLRNVATREE MDISRENVIE EIRKLTRRQ
//
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