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THG1_ASHGO
ID   THG1_ASHGO              Reviewed;         237 AA.
AC   Q75DJ3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=tRNA(His) guanylyltransferase;
DE            EC=2.7.7.79 {ECO:0000250|UniProtKB:P53215};
DE   AltName: Full=tRNA-histidine guanylyltransferase;
GN   Name=THG1; OrderedLocusNames=ABR031C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and
CC       RNase P cleavage. {ECO:0000250|UniProtKB:P53215}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end ribonucleotide-tRNA(His) + ATP + GTP + H2O = a 5'-end
CC         phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate +
CC         H(+); Xref=Rhea:RHEA:54564, Rhea:RHEA-COMP:14193, Rhea:RHEA-
CC         COMP:14917, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:138282,
CC         ChEBI:CHEBI:141847, ChEBI:CHEBI:456215; EC=2.7.7.79;
CC         Evidence={ECO:0000250|UniProtKB:P53215};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE016815; AAS50801.1; -; Genomic_DNA.
DR   RefSeq; NP_982977.1; NM_208330.1.
DR   AlphaFoldDB; Q75DJ3; -.
DR   SMR; Q75DJ3; -.
DR   STRING; 33169.AAS50801; -.
DR   EnsemblFungi; AAS50801; AAS50801; AGOS_ABR031C.
DR   GeneID; 4619069; -.
DR   KEGG; ago:AGOS_ABR031C; -.
DR   eggNOG; KOG2721; Eukaryota.
DR   HOGENOM; CLU_044271_0_1_1; -.
DR   InParanoid; Q75DJ3; -.
DR   OMA; WKQHTEI; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008193; F:tRNA guanylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR   GO; GO:0008033; P:tRNA processing; ISS:UniProtKB.
DR   Gene3D; 3.30.70.3000; -; 1.
DR   InterPro; IPR025845; Thg1_C_dom.
DR   InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR   InterPro; IPR007537; tRNAHis_GuaTrfase_Thg1.
DR   InterPro; IPR038469; tRNAHis_GuaTrfase_Thg1_sf.
DR   PANTHER; PTHR12729; PTHR12729; 1.
DR   Pfam; PF04446; Thg1; 1.
DR   Pfam; PF14413; Thg1C; 1.
DR   PIRSF; PIRSF028980; tRNAHis_guanylyltransferase; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..237
FT                   /note="tRNA(His) guanylyltransferase"
FT                   /id="PRO_0000284988"
FT   BINDING         29..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..77
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   237 AA;  27938 MW;  0614274B7B94CC9F CRC64;
     MAKSRFEYVR EYEVHDTLLP ETYIVVRIDG KHFHEFSQHY SFEKPNDERA LKLMNASAKN
     VVMAYSGDII LAFGESDEYS FILRKDSTLF RRRRDKLSTL FVSLFTAQYV ALWPKFFPEQ
     PLSHKRLPFF DSRCVCYPNT TVVKDYLCWR YVDTHINNLY NTVFWNLVLK CNLTPREAEQ
     RLSGTLSSDK QEILFSECGV NYNNESEMFK KGSLINRKGE IMHIDVVKQI DELFAGF
 
 
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