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Database: UniProt
Entry: G9MIB2_HYPVG
LinkDB: G9MIB2_HYPVG
Original site: G9MIB2_HYPVG 
ID   G9MIB2_HYPVG            Unreviewed;       293 AA.
AC   G9MIB2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   08-NOV-2023, entry version 50.
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=TRIVIDRAFT_219010 {ECO:0000313|EMBL:EHK25229.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK25229.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK25229.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK25229.1}.
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DR   EMBL; ABDF02000003; EHK25229.1; -; Genomic_DNA.
DR   RefSeq; XP_013959440.1; XM_014103965.1.
DR   AlphaFoldDB; G9MIB2; -.
DR   STRING; 413071.G9MIB2; -.
DR   EnsemblFungi; EHK25229; EHK25229; TRIVIDRAFT_219010.
DR   GeneID; 25791380; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_219010; -.
DR   eggNOG; KOG2721; Eukaryota.
DR   HOGENOM; CLU_044271_1_0_1; -.
DR   InParanoid; G9MIB2; -.
DR   OMA; VYFWSTH; -.
DR   OrthoDB; 239198at2759; -.
DR   Proteomes; UP000007115; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
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:UP000007115};
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..136
FT                   /note="tRNAHis guanylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF04446"
FT   DOMAIN          139..266
FT                   /note="Thg1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14413"
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   293 AA;  33468 MW;  F9581C56BCDFBBB6 CRC64;
     MANSKFEYVR NFEQPDPLLP NTWIVVRIDG RGFTKMCAKY EFEKPNDRRA LDLMNAAAKA
     VVTDIPEITI AYGVSDEYSF VFHKSCNLFE RRASKLVTTI VSTFTANYVY LWPTYFPDTP
     LSFPLPTFDG RAVCYPTVQN LRDYMSWRQA DCHINNLYNT AFWKLIQLGG LDNKEAEKTL
     AGTLAADKNE ILFSRFQINY NNEPEIFKKG SIVFRDYELA EPSSHNAAAA ADALAEPVVQ
     SKSQAEKDKK RRAKAKVVVE HLDIIKDEFW DRRPWILSGK PGQPGKASKE IQT
//
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