ID B8LXN5_TALSN Unreviewed; 605 AA.
AC B8LXN5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
GN ORFNames=TSTA_078910 {ECO:0000313|EMBL:EED24536.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED24536.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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 EMBL; EQ962652; EED24536.1; -; Genomic_DNA.
DR RefSeq; XP_002341923.1; XM_002341882.1.
DR AlphaFoldDB; B8LXN5; -.
DR STRING; 441959.B8LXN5; -.
DR GeneID; 8110173; -.
DR VEuPathDB; FungiDB:TSTA_078910; -.
DR eggNOG; KOG1936; Eukaryota.
DR HOGENOM; CLU_025113_4_2_1; -.
DR InParanoid; B8LXN5; -.
DR OMA; CGGGNFK; -.
DR OrthoDB; 5476704at2759; -.
DR PhylomeDB; B8LXN5; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
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; 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 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:0000313|EMBL:EED24536.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EED24536.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 81..539
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 370..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 66645 MW; ECA1462A21663888 CRC64;
MQATPVVCFA RRASPARLVA RFRRGKAVVG LPLTNFGSCK NNIIINNPSY RFLSYLKSPD
SDDMGKDKDN KVTFNLKTPK GTRDWAGADT LIRDRIFSTI TNVFRRHGGT ALDTPVFELR
EILAGKYGED SKLIYDLQDQ GGELCSLRYD LTVPFARWLA MNPEIRSIKR YHIAKVYRRD
QPAVAKGRMR EFYQCDFDIA GANFDPMVPD AEVLKVINEV FEDLGWQGKF TIKINHRKVL
DGMFEVCGVP QDKIRPISSA VDKLDKLPWA DVRKEMVEDK GLDAAAADKI EKYVSRKGRK
DLLEELLKDE DLMANAAAKQ GIEEMGLLMD YLEAFGVLDT ISFDLSLARG LDYYTGVIYE
VVTEGSAPVT ATSAPEAKNL QKSGKKTKSA TGDDDDRSND PTVGVGSIAA GGRYDNLVGM
FYPKAQIPCV GISFGVDRIF SITKARMEKE KAAEMRSSEV DVYVMAFGGK GFTGMLKERM
EICKTLWAAG VKAEFSYKLK PKLPQQFKAA ETSGIPFGVI LGEDELAAGQ VKIKEMGLPE
GHPEKEGVSV DIKNLVEEIK KRISNKNKGI QASATVLPES TTAAVADLTV SSDAASVPKT
EDAGV
//
