THG1_NEUCR
ID THG1_NEUCR Reviewed; 293 AA.
AC Q7SDM8; V5IQ20;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=tRNA(His) guanylyltransferase;
DE EC=2.7.7.79 {ECO:0000250|UniProtKB:P53215};
DE AltName: Full=tRNA-histidine guanylyltransferase;
GN Name=rgt-1; Synonyms=thg1; ORFNames=NCU02105;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002236; ESA43814.1; -; Genomic_DNA.
DR EMBL; CM002236; ESA43815.1; -; Genomic_DNA.
DR RefSeq; XP_011392934.1; XM_011394632.1.
DR RefSeq; XP_011392935.1; XM_011394633.1.
DR AlphaFoldDB; Q7SDM8; -.
DR SMR; Q7SDM8; -.
DR STRING; 5141.EFNCRP00000001295; -.
DR EnsemblFungi; ESA43814; ESA43814; NCU02105.
DR EnsemblFungi; ESA43815; ESA43815; NCU02105.
DR GeneID; 3880248; -.
DR KEGG; ncr:NCU02105; -.
DR VEuPathDB; FungiDB:NCU02105; -.
DR HOGENOM; CLU_044271_1_1_1; -.
DR InParanoid; Q7SDM8; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..293
FT /note="tRNA(His) guanylyltransferase"
FT /id="PRO_0000284992"
FT REGION 226..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 75..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 76
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
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 33604 MW; CEB4DD40B9B600DA CRC64;
MANSKFEYVK QFEQPDSLLP NTWIVVRLDG RGFTKFSTKY AFEKPNDKRA LDLMNAAARS
VMSELPDITI AYGVSDEYSF VFHKSCTLFE RRASKLVSTI VSTFTAYYIH HWPTYFVDGP
PLSPPLPSFD GRAVCYPSVQ NLRDYMSWRQ VDCHINNLYN TTFWALINQG GMDGTAAELM
LKGTFSADKN EILFKKFGIN YNNEPEMFKK GSVVFRNYEL VEPGTKKVSE EEAEEMSSSA
VPEVKSKSQV EKDKKVRTKA KIVVEHLDII RDEFWERRPW LLSGTPGKVP KEP
