THG1_RAT
ID THG1_RAT Reviewed; 298 AA.
AC Q5M965;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable tRNA(His) guanylyltransferase;
DE EC=2.7.7.79 {ECO:0000250|UniProtKB:Q9NWX6};
DE AltName: Full=tRNA-histidine guanylyltransferase;
GN Name=Thg1l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and
CC RNase P cleavage. This step is essential for proper recognition of the
CC tRNA and for the fidelity of protein synthesis. Also functions as a
CC guanyl-nucleotide exchange factor/GEF for the MFN1 and MFN2 mitofusins
CC thereby regulating mitochondrial fusion. By regulating both
CC mitochondrial dynamics and bioenergetic function, it contributes to
CC cell survival following oxidative stress.
CC {ECO:0000250|UniProtKB:Q9NWX6}.
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:Q9NWX6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. Interacts with MFN1 and MFN2; functions as a
CC guanyl-nucleotide exchange factor/GEF for MFN2 and also probably MFN1.
CC {ECO:0000250|UniProtKB:Q9NWX6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9NWX6}.
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC {ECO:0000305}.
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; BC087596; AAH87596.1; -; mRNA.
DR RefSeq; NP_001013988.1; NM_001013966.1.
DR AlphaFoldDB; Q5M965; -.
DR SMR; Q5M965; -.
DR STRING; 10116.ENSRNOP00000007917; -.
DR PaxDb; Q5M965; -.
DR PRIDE; Q5M965; -.
DR GeneID; 303067; -.
DR KEGG; rno:303067; -.
DR UCSC; RGD:1359513; rat.
DR CTD; 54974; -.
DR RGD; 1359513; Thg1l.
DR VEuPathDB; HostDB:ENSRNOG00000005539; -.
DR eggNOG; KOG2721; Eukaryota.
DR HOGENOM; CLU_044271_0_0_1; -.
DR InParanoid; Q5M965; -.
DR OMA; WKQHTEI; -.
DR OrthoDB; 1152974at2759; -.
DR PhylomeDB; Q5M965; -.
DR TreeFam; TF325119; -.
DR PRO; PR:Q5M965; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000005539; Expressed in ovary and 19 other tissues.
DR Genevisible; Q5M965; RN.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:1990234; C:transferase complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISO:RGD.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:1990046; P:stress-induced mitochondrial fusion; 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 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..298
FT /note="Probable tRNA(His) guanylyltransferase"
FT /id="PRO_0000284986"
FT BINDING 58..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 104..105
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 34850 MW; 6822E64142F9AE02 CRC64;
MWAFSTARIG SPLAATSVTL RRCLRLGVAM AKSKFEYVRD FEVDDTCLPH CWVVVRLDGR
NFHRFAEKHN FAKPNDSRAL HLMTKCAQTV MQELEDIVIA YGQSDEYSFV FRKRSNWFKR
RASKFMTLVA SQFASSYVFY WRDYFEDQPL LYPPGFDGRV VLYPSNQTLK DYLSWRQADC
HINNLYNTVF WALIQQSGLT PVQAQQRLKG TLTADKNEIL FSEFHINYNN EPHMYRKGTV
LVWQKVNEVR TQEIRLPAEM EGEKMAVTRT RTKLVALNCD LIGDAFWKEH PEILEGED
