ID A0A165TKA0_9APHY Unreviewed; 283 AA.
AC A0A165TKA0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 24.
DE RecName: Full=tRNA(His) guanylyltransferase {ECO:0000256|ARBA:ARBA00015443, ECO:0000256|PIRNR:PIRNR028980};
DE EC=2.7.7.79 {ECO:0000256|ARBA:ARBA00012511, ECO:0000256|PIRNR:PIRNR028980};
DE AltName: Full=tRNA-histidine guanylyltransferase {ECO:0000256|ARBA:ARBA00032480, ECO:0000256|PIRNR:PIRNR028980};
GN ORFNames=DAEQUDRAFT_683819 {ECO:0000313|EMBL:KZT73566.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT73566.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT73566.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT73566.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and
CC RNase P cleavage. {ECO:0000256|PIRNR:PIRNR028980}.
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:0000256|PIRNR:PIRNR028980};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR028980-2};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR028980-2};
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010113, ECO:0000256|PIRNR:PIRNR028980}.
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DR EMBL; KV429036; KZT73566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165TKA0; -.
DR STRING; 1314783.A0A165TKA0; -.
DR OrthoDB; 239198at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
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:SF6; TRNA(HIS) GUANYLYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR12729; UNCHARACTERIZED; 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 {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR028980};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR028980};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR028980};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR028980};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR028980};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR028980};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR028980}.
FT DOMAIN 6..135
FT /note="tRNAHis guanylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04446"
FT DOMAIN 138..269
FT /note="Thg1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14413"
FT REGION 227..256
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:0000256|PIRSR:PIRSR028980-1"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR028980-2"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR028980-2"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR028980-2"
FT BINDING 75..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR028980-1"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR028980-2"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR028980-2"
SQ SEQUENCE 283 AA; 32171 MW; A02BBF2038BAC1FD CRC64;
MAGSKYEYVK KFELPDPLLM GTFLVLRIDG HAFHKLSEAH SFNKPNDERA LQLMDHAARD
VMNEFKDILL AFGESDEYSF LFRKSSALYN RRQAKILTTV TSLFTSSYVY NWSKYLPDQE
LKYPPSFDGR IVLYPSSKEV RDYFAWRQAD THINNLYNTI FWALVLQGGE STSQAHATLR
GTVSSKKHEM LHSRFSINYN SLPARFRKGS ILVREKVVPD KTDVQALGAE GATDSPDAVS
SGTPGPTSGK PAKKPKVQFT TELLHCDIIG DEFWEQRPYL LAE
//
