THG1_BOVIN
ID THG1_BOVIN Reviewed; 298 AA.
AC Q05B50;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC122826; AAI22827.1; -; mRNA.
DR RefSeq; NP_001073702.1; NM_001080233.2.
DR AlphaFoldDB; Q05B50; -.
DR SMR; Q05B50; -.
DR STRING; 9913.ENSBTAP00000013678; -.
DR PaxDb; Q05B50; -.
DR PRIDE; Q05B50; -.
DR Ensembl; ENSBTAT00000013678; ENSBTAP00000013678; ENSBTAG00000010359.
DR GeneID; 507084; -.
DR KEGG; bta:507084; -.
DR CTD; 54974; -.
DR VEuPathDB; HostDB:ENSBTAG00000010359; -.
DR VGNC; VGNC:35837; THG1L.
DR eggNOG; KOG2721; Eukaryota.
DR GeneTree; ENSGT00390000011705; -.
DR HOGENOM; CLU_044271_0_0_1; -.
DR InParanoid; Q05B50; -.
DR OMA; WKQHTEI; -.
DR OrthoDB; 1152974at2759; -.
DR TreeFam; TF325119; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000010359; Expressed in oviduct epithelium and 106 other tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:1990234; C:transferase complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
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_0000284983"
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; 34740 MW; 547FEDEDEF3C8204 CRC64;
MWAAGALKVR DCLAATSVTL RRCLKLGATM AKSKFEYVRD FEADDTCLPH CWVVVRLDGR
NFHRFAEKHS FIKPNDSRAL HLMTKCAQTV MNELEDIVIA YGQSDEYSFV FKRKSNWFKR
RASKFMTHVV SQFASSYVFY WRDYFEDQPL LYPPGFDGRV IVYPSNQTLK DYLSWRQADC
HINNLYNTVF WALVQQSGLT PLQAQERLQG TLAADKNEIL FSEFNINYNN EPLMYRKGTV
LIWQKVEEIT TKEVKLPAEM EGKKMAVTRT RTMVVPLHCN IIGDAFWKEH PEILDEDS
