ID A0A0D2E169_9EURO Unreviewed; 516 AA.
AC A0A0D2E169;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
GN ORFNames=Z517_03077 {ECO:0000313|EMBL:KIW83831.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW83831.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW83831.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW83831.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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};
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 EMBL; KN846970; KIW83831.1; -; Genomic_DNA.
DR RefSeq; XP_013287639.1; XM_013432185.1.
DR AlphaFoldDB; A0A0D2E169; -.
DR STRING; 1442368.A0A0D2E169; -.
DR GeneID; 25302567; -.
DR VEuPathDB; FungiDB:Z517_03077; -.
DR HOGENOM; CLU_025113_4_0_1; -.
DR OrthoDB; 5476704at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
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; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR033656; HisRS_anticodon.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT DOMAIN 17..389
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 301..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 58176 MW; DA6B2DD70B503D7C CRC64;
MAKDKKKSKE VVKNPKGTRD WSGEDIDLLK AIRRQIEKVF ENYRGLELDT PVFELQEVLK
GKYGEDSKLI YDLQDQGGEL LSLRYDMTVP FARWLAMNPD IETWRRYAIG KVYRRDQPAI
SKGRMREFWQ CDIDFAGESA PMFNDSEMIS IIVKVFETLE WSGRYTIKIN DRRILDGLFE
VCGVPAEKIR TISSAVDKLD KLPWLEVKKE MVEQKGLEES VADRIQTYVT RKGGKELLEE
LQKDEALMSN PKAQKGIEEM DLLMRYLRRW KALDKISFDL SLARGLDYYT GIIYEVVTEG
SAPTRTPAPA TDSAPPMPPV ATNGGSNGLP RREKKKQISE DDDRSEDPSV GVGSVAAGGR
YDHLVERFRP DANIPCVGVS FGIDRIIAIT KARIAKGEKF SYIARNRTDA YVMAFGGSGF
GGMFEERIDV LVALRDAGIR AETFWKQKAK LQKQFKEADR AGAPIAVILG EDEQARGEVK
VKQMGLAEGD PEKEGVLVKV EDLVARVRGL LAKIDE
//
